Full text data of UBR4
UBR4
(KIAA0462, KIAA1307, RBAF600, ZUBR1)
[Confidence: high (present in two of the MS resources)]
E3 ubiquitin-protein ligase UBR4; 6.3.2.- (600 kDa retinoblastoma protein-associated factor; N-recognin-4; Retinoblastoma-associated factor of 600 kDa; RBAF600; p600; Zinc finger UBR1-type protein 1)
E3 ubiquitin-protein ligase UBR4; 6.3.2.- (600 kDa retinoblastoma protein-associated factor; N-recognin-4; Retinoblastoma-associated factor of 600 kDa; RBAF600; p600; Zinc finger UBR1-type protein 1)
hRBCD
IPI00180305
IPI00180305 KIAA0462 protein brain soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00180305 KIAA0462 protein brain soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q5T4S7
ID UBR4_HUMAN Reviewed; 5183 AA.
AC Q5T4S7; A8MPT2; A8MQ33; A8MQB1; O60646; O75050; Q4QRK5; Q5T4S8;
read moreAC Q5T4S9; Q5TBN8; Q5TBP2; Q6DKH8; Q6P4A4; Q7L8P7; Q8IXJ4; Q8TDN5;
AC Q8WV67; Q9HA46; Q9P2N9; Q9UG82;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=E3 ubiquitin-protein ligase UBR4;
DE EC=6.3.2.-;
DE AltName: Full=600 kDa retinoblastoma protein-associated factor;
DE AltName: Full=N-recognin-4;
DE AltName: Full=Retinoblastoma-associated factor of 600 kDa;
DE Short=RBAF600;
DE Short=p600;
DE AltName: Full=Zinc finger UBR1-type protein 1;
GN Name=UBR4; Synonyms=KIAA0462, KIAA1307, RBAF600, ZUBR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1 AND CALM,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=16214886; DOI=10.1073/pnas.0507458102;
RA Nakatani Y., Konishi H., Vassilev A., Kurooka H., Ishiguro K.,
RA Sawada J., Ikura T., Korsmeyer S.J., Qin J., Herlitz A.M.;
RT "p600, a unique protein required for membrane morphogenesis and cell
RT survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15093-15098(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP PROTEIN SEQUENCE OF 166-185; 435-443; 850-857; 921-931; 1065-1079;
RP 1131-1141; 1175-1192; 1195-1208; 1286-1293; 1337-1349; 1434-1440;
RP 1464-1470; 1478-1489; 1731-1757; 1838-1850; 1875-1886; 1909-1918;
RP 1921-1931; 2048-2058; 2131-2138; 2211-2218; 2354-2381; 2527-2536;
RP 2564-2572; 2713-2721; 2981-2989; 3046-3065; 3229-3238; 3243-3252;
RP 3589-3606; 3618-3628; 3735-3745; 3809-3816; 3827-3836; 3845-3857;
RP 3889-3915; 4131-4142; 4204-4215; 4320-4334; 4414-4426; 4608-4637;
RP 4686-4696; 4717-4724; 4803-4814; 4852-4860; 5013-5022 AND 5062-5069,
RP PHOSPHORYLATION AT SER-2719, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 779-5183 (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI.
RT The complete sequences of 150 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2908-5183 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries
RT from human brain.";
RL DNA Res. 4:345-349(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4385-5183 (ISOFORMS 1 AND
RP 2), AND VARIANT LEU-4867.
RC TISSUE=Kidney, Liver, Lung, and Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4583-5183 (ISOFORM 1), AND VARIANTS
RP LEU-4867 AND ARG-4924.
RX PubMed=16247014; DOI=10.1073/pnas.0500090102;
RA Lennerz V., Fatho M., Gentilini C., Frye R.A., Lifke A., Ferel D.,
RA Woelfel C., Huber C., Woelfel T.;
RT "The response of autologous T cells to a human melanoma is dominated
RT by mutated neoantigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16013-16018(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4686-5183 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4709-5183 (ISOFORM 1), AND
RP VARIANT LEU-4867.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP INTERACTION WITH HPV-16 E7; HPV-6B E7 AND HPV-11 E7, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=16061792; DOI=10.1073/pnas.0505337102;
RA Huh K.-W., DeMasi J., Ogawa H., Nakatani Y., Howley P.M., Muenger K.;
RT "Association of the human papillomavirus type 16 E7 oncoprotein with
RT the 600-kDa retinoblastoma protein-associated factor, p600.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11492-11497(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181 AND
RP THR-2715, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1084, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181 AND
RP SER-1763, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2719, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP FUNCTION.
RX PubMed=23932781; DOI=10.1016/j.molcel.2013.07.002;
RA Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.;
RT "Acetylation stabilizes ATP-citrate lyase to promote lipid
RT biosynthesis and tumor growth.";
RL Mol. Cell 51:506-518(2013).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-1394.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the
CC N-end rule pathway. Recognizes and binds to proteins bearing
CC specific N-terminal residues that are destabilizing according to
CC the N-end rule, leading to their ubiquitination and subsequent
CC degradation. Together with clathrin, forms meshwork structures
CC involved in membrane morphogenesis and cytoskeletal organization.
CC Regulates integrin-mediated signaling. May play a role in
CC activation of FAK in response to cell-matrix interactions.
CC Mediates ubiquitination of ACLY, leading to its subsequent
CC degradation.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RB1 and calmodulin. Interacts with protein
CC E7 from papilloma virus HPV-16, HPV-6B and HPV-11.
CC -!- INTERACTION:
CC P03129:E7 (xeno); NbExp=4; IntAct=EBI-1995940, EBI-866453;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential). Cytoplasm. Cytoplasm, cytoskeleton. Nucleus.
CC Note=Concentrates at the leading edge of membrane structures
CC involved in actin motility.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q5T4S7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T4S7-2; Sequence=VSP_025209;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q5T4S7-3; Sequence=VSP_025203, VSP_025206;
CC Name=4;
CC IsoId=Q5T4S7-4; Sequence=VSP_025205, VSP_025206;
CC Name=5;
CC IsoId=Q5T4S7-5; Sequence=VSP_025201, VSP_025202, VSP_025204;
CC Name=6;
CC IsoId=Q5T4S7-6; Sequence=VSP_025200, VSP_025207, VSP_025208;
CC -!- SIMILARITY: Belongs to the UBR4 family.
CC -!- SIMILARITY: Contains 1 UBR-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD43719.1; Type=Erroneous initiation;
CC Sequence=CAI19271.1; Type=Erroneous gene model prediction;
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DR EMBL; AF348492; AAL83880.1; -; mRNA.
DR EMBL; AK022322; BAB14011.1; -; mRNA.
DR EMBL; AL137127; CAI19268.1; -; Genomic_DNA.
DR EMBL; AL357564; CAI19268.1; JOINED; Genomic_DNA.
DR EMBL; AL137127; CAI19269.1; -; Genomic_DNA.
DR EMBL; AL357564; CAI19269.1; JOINED; Genomic_DNA.
DR EMBL; AL137127; CAI19271.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL137127; CAI19272.1; -; Genomic_DNA.
DR EMBL; AL357564; CAI19272.1; JOINED; Genomic_DNA.
DR EMBL; AL137127; CAI19273.1; -; Genomic_DNA.
DR EMBL; AL137127; CAI19274.1; -; Genomic_DNA.
DR EMBL; AL357564; CAI20972.1; -; Genomic_DNA.
DR EMBL; AL137127; CAI20972.1; JOINED; Genomic_DNA.
DR EMBL; AL357564; CAI20973.1; -; Genomic_DNA.
DR EMBL; AL137127; CAI20973.1; JOINED; Genomic_DNA.
DR EMBL; AL357564; CAI20974.1; -; Genomic_DNA.
DR EMBL; AL137127; CAI20974.1; JOINED; Genomic_DNA.
DR EMBL; AB037728; BAA92545.1; -; mRNA.
DR EMBL; AB007931; BAA32307.1; -; mRNA.
DR EMBL; BC018694; AAH18694.2; -; mRNA.
DR EMBL; BC063573; AAH63573.1; -; mRNA.
DR EMBL; BC073905; AAH73905.1; -; mRNA.
DR EMBL; BC096758; AAH96758.1; -; mRNA.
DR EMBL; AJ505016; CAD43719.1; ALT_INIT; mRNA.
DR EMBL; AL049972; CAB43227.1; -; mRNA.
DR EMBL; AF055010; AAC09360.1; -; mRNA.
DR PIR; T00076; T00076.
DR RefSeq; NP_065816.2; NM_020765.2.
DR UniGene; Hs.148078; -.
DR UniGene; Hs.649405; -.
DR ProteinModelPortal; Q5T4S7; -.
DR IntAct; Q5T4S7; 19.
DR MINT; MINT-4715511; -.
DR PhosphoSite; Q5T4S7; -.
DR DMDM; 74744979; -.
DR PaxDb; Q5T4S7; -.
DR PRIDE; Q5T4S7; -.
DR Ensembl; ENST00000375217; ENSP00000364365; ENSG00000127481.
DR Ensembl; ENST00000375218; ENSP00000364366; ENSG00000127481.
DR Ensembl; ENST00000375226; ENSP00000364374; ENSG00000127481.
DR Ensembl; ENST00000375254; ENSP00000364403; ENSG00000127481.
DR Ensembl; ENST00000375267; ENSP00000364416; ENSG00000127481.
DR GeneID; 23352; -.
DR KEGG; hsa:23352; -.
DR UCSC; uc001bbi.3; human.
DR CTD; 23352; -.
DR GeneCards; GC01M019401; -.
DR H-InvDB; HIX0000191; -.
DR HGNC; HGNC:30313; UBR4.
DR HPA; HPA021046; -.
DR MIM; 609890; gene.
DR neXtProt; NX_Q5T4S7; -.
DR PharmGKB; PA162407958; -.
DR eggNOG; NOG236675; -.
DR HOVERGEN; HBG058328; -.
DR InParanoid; Q5T4S7; -.
DR KO; K10691; -.
DR OMA; SNTPMGD; -.
DR OrthoDB; EOG7288QF; -.
DR PhylomeDB; Q5T4S7; -.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR ChiTaRS; UBR4; human.
DR GeneWiki; UBR4; -.
DR GenomeRNAi; 23352; -.
DR NextBio; 45346; -.
DR PRO; PR:Q5T4S7; -.
DR ArrayExpress; Q5T4S7; -.
DR Bgee; Q5T4S7; -.
DR Genevestigator; Q5T4S7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR025704; E3_Ub_ligase_UBR4.
DR InterPro; IPR017986; WD40_repeat_dom.
DR InterPro; IPR003126; Znf_N-recognin.
DR Pfam; PF13764; E3_UbLigase_R4; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SUPFAM; SSF48371; SSF48371; 9.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calmodulin-binding;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Host-virus interaction; Ligase; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 5183 E3 ubiquitin-protein ligase UBR4.
FT /FTId=PRO_0000286861.
FT TRANSMEM 850 870 Helical; (Potential).
FT TRANSMEM 993 1013 Helical; (Potential).
FT ZN_FING 1656 1729 UBR-type.
FT COMPBIAS 9 15 Poly-Ala.
FT COMPBIAS 608 631 Pro-rich.
FT COMPBIAS 2728 2738 Poly-Asp.
FT COMPBIAS 3339 3370 Ser-rich.
FT MOD_RES 178 178 Phosphoserine.
FT MOD_RES 181 181 Phosphoserine.
FT MOD_RES 1084 1084 N6-acetyllysine.
FT MOD_RES 1402 1402 Phosphoserine (By similarity).
FT MOD_RES 1763 1763 Phosphoserine.
FT MOD_RES 2715 2715 Phosphothreonine.
FT MOD_RES 2719 2719 Phosphoserine.
FT VAR_SEQ 1 3585 Missing (in isoform 6).
FT /FTId=VSP_025200.
FT VAR_SEQ 2100 2100 K -> KQ (in isoform 5).
FT /FTId=VSP_025201.
FT VAR_SEQ 2405 2486 IGASVDPAGVTMIDAVKIYGKTKEQFGWPDEPPEEFPSASV
FT SNICPSNLNQSNGTGDSDSAAPTTTSGTVLERLVVSSLEAL
FT -> SESPTPGADSVLIVTAKLGATGLWLSNILGSLHSADFS
FT VLSSGNFELHLMY (in isoform 5).
FT /FTId=VSP_025202.
FT VAR_SEQ 2476 2476 E -> ESSETESLTKLD (in isoform 3).
FT /FTId=VSP_025203.
FT VAR_SEQ 2487 5183 Missing (in isoform 5).
FT /FTId=VSP_025204.
FT VAR_SEQ 2601 2601 T -> TDCFFPRCACWSLGIVGILIGAPLETPSP (in
FT isoform 4).
FT /FTId=VSP_025205.
FT VAR_SEQ 2830 2864 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_025206.
FT VAR_SEQ 3777 3797 DDSGTAGGISSTSASVNRYIL -> VVPRCKGHLDKGLGLD
FT QKTAS (in isoform 6).
FT /FTId=VSP_025207.
FT VAR_SEQ 3798 5183 Missing (in isoform 6).
FT /FTId=VSP_025208.
FT VAR_SEQ 5108 5108 K -> KKQTTPTVGGIDTGSLEPCVCE (in isoform
FT 2).
FT /FTId=VSP_025209.
FT VARIANT 1107 1107 T -> A (in dbSNP:rs16862578).
FT /FTId=VAR_032193.
FT VARIANT 1394 1394 R -> H (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035540.
FT VARIANT 4867 4867 M -> L (in dbSNP:rs12584).
FT /FTId=VAR_032194.
FT VARIANT 4924 4924 G -> R (in a melanoma patient).
FT /FTId=VAR_032195.
FT VARIANT 5084 5084 V -> M (in dbSNP:rs2274010).
FT /FTId=VAR_032196.
FT CONFLICT 2016 2016 A -> S (in Ref. 1; AAL83880).
FT CONFLICT 2410 2410 D -> E (in Ref. 1; AAL83880).
FT CONFLICT 3957 3957 G -> S (in Ref. 1; AAL83880).
FT CONFLICT 4589 4589 G -> V (in Ref. 7; AAH18694).
SQ SEQUENCE 5183 AA; 573841 MW; 5F6DD7B565E27609 CRC64;
MATSGGEEAA AAAPAPGTPA TGADTTPGWE VAVRPLLSAS YSAFEMKELP QLVASVIESE
SEILHHEKQY EPFYSSFVAL STHYITTVCS LIPRNQLQSV AAACKVLIEF SLLRLENPDE
ACAVSQKHLI LLIKGLCTGC SRLDRTEIIT FTAMMKSAKL PQTVKTLSDV EDQKELASPV
SPELRQKEVQ MNFLNQLTSV FNPRTVASQP ISTQTLVEGE NDEQSSTDQA SAIKTKNVFI
AQNVASLQEL GGSEKLLRVC LNLPYFLRYI NRFQDAVLAN SFFIMPATVA DATAVRNGFH
SLVIDVTMAL DTLSLPVLEP LNPSRLQDVT VLSLSCLYAG VSVATCMAIL HVGSAQQVRT
GSTSSKEDDY ESDAATIVQK CLEIYDMIGQ AISSSRRAGG EHYQNFQLLG AWCLLNSLFL
ILNLSPTALA DKGKEKDPLA ALRVRDILSR TKEGVGSPKL GPGKGHQGFG VLSVILANHA
IKLLTSLFQD LQVEALHKGW ETDGPPAALS IMAQSTSIQR IQRLIDSVPL MNLLLTLLST
SYRKACVLQR QRKGSMSSDA SASTDSNTYY EDDFSSTEED SSQDDDSEPI LGQWFEETIS
PSKEKAAPPP PPPPPPLESS PRVKSPSKQA PGEKGNILAS RKDPELFLGL ASNILNFITS
SMLNSRNNFI RNYLSVSLSE HHMATLASII KEVDKDGLKG SSDEEFAAAL YHFNHSLVTS
DLQSPNLQNT LLQQLGVAPF SEGPWPLYIH PQSLSVLSRL LLIWQHKASA QGDPDVPECL
KVWDRFLSTM KQNALQGVVP SETEDLNVEH LQMLLLIFHN FTETGRRAIL SLFVQIIQEL
SVNMDAQMRF VPLILARLLL IFDYLLHQYS KAPVYLFEQV QHNLLSPPFG WASGSQDSNS
RRATTPLYHG FKEVEENWSK HFSSDAVPHP RFYCVLSPEA SEDDLNRLDS VACDVLFSKL
VKYDELYAAL TALLAAGSQL DTVRRKENKN VTALEACALQ YYFLILWRIL GILPPSKTYI
NQLSMNSPEM SECDILHTLR WSSRLRISSY VNWIKDHLIK QGMKAEHASS LLELASTTKC
SSVKYDVEIV EEYFARQISS FCSIDCTTIL QLHEIPSLQS IYTLDAAISK VQVSLDEHFS
KMAAETDPHK SSEITKNLLP ATLQLIDTYA SFTRAYLLQN FNEEGTTEKP SKEKLQGFAA
VLAIGSSRCK ANTLGPTLVQ NLPSSVQTVC ESWNNINTNE FPNIGSWRNA FANDTIPSES
YISAVQAAHL GTLCSQSLPL AASLKHTLLS LVRLTGDLIV WSDEMNPPQV IRTLLPLLLE
SSTESVAEIS SNSLERILGP AESDEFLARV YEKLITGCYN ILANHADPNS GLDESILEEC
LQYLEKQLES SQARKAMEEF FSDSGELVQI MMATANENLS AKFCNRVLKF FTKLFQLTEK
SPNPSLLHLC GSLAQLACVE PVRLQAWLTR MTTSPPKDSD QLDVIQENRQ LLQLLTTYIV
RENSQVGEGV CAVLLGTLTP MATEMLANGD GTGFPELMVV MATLASAGQG AGHLQLHNAA
VDWLSRCKKY LSQKNVVEKL NANVMHGKHV MILECTCHIM SYLADVTNAL SQSNGQGPSH
LSVDGEERAI EVDSDWVEEL AVEEEDSQAE DSDEDSLCNK LCTFTITQKE FMNQHWYHCH
TCKMVDGVGV CTVCAKVCHK DHEISYAKYG SFFCDCGAKE DGSCLALVKR TPSSGMSSTM
KESAFQSEPR ISESLVRHAS TSSPADKAKV TISDGKVADE EKPKKSSLCR TVEGCREELQ
NQANFSFAPL VLDMLNFLMD AIQTNFQQAS AVGSSSRAQQ ALSELHTVEK AVEMTDQLMV
PTLGSQEGAF ENVRMNYSGD QGQTIRQLIS AHVLRRVAMC VLSSPHGRRQ HLAVSHEKGK
ITVLQLSALL KQADSSKRKL TLTRLASAPV PFTVLSLTGN PCKEDYLAVC GLKDCHVLTF
SSSGSVSDHL VLHPQLATGN FIIKAVWLPG SQTELAIVTA DFVKIYDLCV DALSPTFYFL
LPSSKIRDVT FLFNEEGKNI IVIMSSAGYI YTQLMEEASS AQQGPFYVTN VLEINHEDLK
DSNSQVAGGG VSVYYSHVLQ MLFFSYCQGK SFAATISRTT LEVLQLFPIN IKSSNGGSKT
SPALCQWSEV MNHPGLVCCV QQTTGVPLVV MVKPDTFLIQ EIKTLPAKAK IQDMVAIRHT
ACNEQQRTTM ILLCEDGSLR IYMANVENTS YWLQPSLQPS SVISIMKPVR KRKTATITTR
TSSQVTFPID FFEHNQQLTD VEFGGNDLLQ VYNAQQIKHR LNSTGMYVAN TKPGGFTIEI
SNNNSTMVMT GMRIQIGTQA IERAPSYIEI FGRTMQLNLS RSRWFDFPFT REEALQADKK
LNLFIGASVD PAGVTMIDAV KIYGKTKEQF GWPDEPPEEF PSASVSNICP SNLNQSNGTG
DSDSAAPTTT SGTVLERLVV SSLEALESCF AVGPIIEKER NKNAAQELAT LLLSLPAPAS
VQQQSKSLLA SLHTSRSAYH SHKDQALLSK AVQCLNTSSK EGKDLDPEVF QRLVITARSI
AIMRPNNLVH FTESKLPQME TEGMDEGKEP QKQLEGDCCS FITQLVNHFW KLHASKPKNA
FLAPACLPGL THIEATVNAL VDIIHGYCTC ELDCINTASK IYMQMLLCPD PAVSFSCKQA
LIRVLRPRNK RRHVTLPSSP RSNTPMGDKD DDDDDDADEK MQSSGIPNGG HIRQESQEQS
EVDHGDFEMV SESMVLETAE NVNNGNPSPL EALLAGAEGF PPMLDIPPDA DDETMVELAI
ALSLQQDQQG SSSSALGLQS LGLSGQAPSS SSLDAGTLSD TTASAPASDD EGSTAATDGS
TLRTSPADHG GSVGSESGGS AVDSVAGEHS VSGRSSAYGD ATAEGHPAGP GSVSSSTGAI
STTTGHQEGD GSEGEGEGET EGDVHTSNRL HMVRLMLLER LLQTLPQLRN VGGVRAIPYM
QVILMLTTDL DGEDEKDKGA LDNLLSQLIA ELGMDKKDVS KKNERSALNE VHLVVMRLLS
VFMSRTKSGS KSSICESSSL ISSATAAALL SSGAVDYCLH VLKSLLEYWK SQQNDEEPVA
TSQLLKPHTT SSPPDMSPFF LRQYVKGHAA DVFEAYTQLL TEMVLRLPYQ IKKITDTNSR
IPPPVFDHSW FYFLSEYLMI QQTPFVRRQV RKLLLFICGS KEKYRQLRDL HTLDSHVRGI
KKLLEEQGIF LRASVVTASS GSALQYDTLI SLMEHLKACA EIAAQRTINW QKFCIKDDSV
LYFLLQVSFL VDEGVSPVLL QLLSCALCGS KVLAALAASS GSSSASSSSA PVAASSGQAT
TQSKSSTKKS KKEEKEKEKD GETSGSQEDQ LCTALVNQLN KFADKETLIQ FLRCFLLESN
SSSVRWQAHC LTLHIYRNSS KSQQELLLDL MWSIWPELPA YGRKAAQFVD LLGYFSLKTP
QTEKKLKEYS QKAVEILRTQ NHILTNHPNS NIYNTLSGLV EFDGYYLESD PCLVCNNPEV
PFCYIKLSSI KVDTRYTTTQ QVVKLIGSHT ISKVTVKIGD LKRTKMVRTI NLYYNNRTVQ
AIVELKNKPA RWHKAKKVQL TPGQTEVKID LPLPIVASNL MIEFADFYEN YQASTETLQC
PRCSASVPAN PGVCGNCGEN VYQCHKCRSI NYDEKDPFLC NACGFCKYAR FDFMLYAKPC
CAVDPIENEE DRKKAVSNIN TLLDKADRVY HQLMGHRPQL ENLLCKVNEA APEKPQDDSG
TAGGISSTSA SVNRYILQLA QEYCGDCKNS FDELSKIIQK VFASRKELLE YDLQQREAAT
KSSRTSVQPT FTASQYRALS VLGCGHTSST KCYGCASAVT EHCITLLRAL ATNPALRHIL
VSQGLIRELF DYNLRRGAAA MREEVRQLMC LLTRDNPEAT QQMNDLIIGK VSTALKGHWA
NPDLASSLQY EMLLLTDSIS KEDSCWELRL RCALSLFLMA VNIKTPVVVE NITLMCLRIL
QKLIKPPAPT SKKNKDVPVE ALTTVKPYCN EIHAQAQLWL KRDPKASYDA WKKCLPIRGI
DGNGKAPSKS ELRHLYLTEK YVWRWKQFLS RRGKRTSPLD LKLGHNNWLR QVLFTPATQA
ARQAACTIVE ALATIPSRKQ QVLDLLTSYL DELSIAGECA AEYLALYQKL ITSAHWKVYL
AARGVLPYVG NLITKEIARL LALEEATLST DLQQGYALKS LTGLLSSFVE VESIKRHFKS
RLVGTVLNGY LCLRKLVVQR TKLIDETQDM LLEMLEDMTT GTESETKAFM AVCIETAKRY
NLDDYRTPVF IFERLCSIIY PEENEVTEFF VTLEKDPQQE DFLQGRMPGN PYSSNEPGIG
PLMRDIKNKI CQDCDLVALL EDDSGMELLV NNKIISLDLP VAEVYKKVWC TTNEGEPMRI
VYRMRGLLGD ATEEFIESLD STTDEEEDEE EVYKMAGVMA QCGGLECMLN RLAGIRDFKQ
GRHLLTVLLK LFSYCVKVKV NRQQLVKLEM NTLNVMLGTL NLALVAEQES KDSGGAAVAE
QVLSIMEIIL DESNAEPLSE DKGNLLLTGD KDQLVMLLDQ INSTFVRSNP SVLQGLLRII
PYLSFGEVEK MQILVERFKP YCNFDKYDED HSGDDKVFLD CFCKIAAGIK NNSNGHQLKD
LILQKGITQN ALDYMKKHIP SAKNLDADIW KKFLSRPALP FILRLLRGLA IQHPGTQVLI
GTDSIPNLHK LEQVSSDEGI GTLAENLLEA LREHPDVNKK IDAARRETRA EKKRMAMAMR
QKALGTLGMT TNEKGQVVTK TALLKQMEEL IEEPGLTCCI CREGYKFQPT KVLGIYTFTK
RVALEEMENK PRKQQGYSTV SHFNIVHYDC HLAAVRLARG REEWESAALQ NANTKCNGLL
PVWGPHVPES AFATCLARHN TYLQECTGQR EPTYQLNIHD IKLLFLRFAM EQSFSADTGG
GGRESNIHLI PYIIHTVLYV LNTTRATSRE EKNLQGFLEQ PKEKWVESAF EVDGPYYFTV
LALHILPPEQ WRATRVEILR RLLVTSQARA VAPGGATRLT DKAVKDYSAY RSSLLFWALV
DLIYNMFKKV PTSNTEGGWS CSLAEYIRHN DMPIYEAADK ALKTFQEEFM PVETFSEFLD
VAGLLSEITD PESFLKDLLN SVP
//
ID UBR4_HUMAN Reviewed; 5183 AA.
AC Q5T4S7; A8MPT2; A8MQ33; A8MQB1; O60646; O75050; Q4QRK5; Q5T4S8;
read moreAC Q5T4S9; Q5TBN8; Q5TBP2; Q6DKH8; Q6P4A4; Q7L8P7; Q8IXJ4; Q8TDN5;
AC Q8WV67; Q9HA46; Q9P2N9; Q9UG82;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=E3 ubiquitin-protein ligase UBR4;
DE EC=6.3.2.-;
DE AltName: Full=600 kDa retinoblastoma protein-associated factor;
DE AltName: Full=N-recognin-4;
DE AltName: Full=Retinoblastoma-associated factor of 600 kDa;
DE Short=RBAF600;
DE Short=p600;
DE AltName: Full=Zinc finger UBR1-type protein 1;
GN Name=UBR4; Synonyms=KIAA0462, KIAA1307, RBAF600, ZUBR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1 AND CALM,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=16214886; DOI=10.1073/pnas.0507458102;
RA Nakatani Y., Konishi H., Vassilev A., Kurooka H., Ishiguro K.,
RA Sawada J., Ikura T., Korsmeyer S.J., Qin J., Herlitz A.M.;
RT "p600, a unique protein required for membrane morphogenesis and cell
RT survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15093-15098(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP PROTEIN SEQUENCE OF 166-185; 435-443; 850-857; 921-931; 1065-1079;
RP 1131-1141; 1175-1192; 1195-1208; 1286-1293; 1337-1349; 1434-1440;
RP 1464-1470; 1478-1489; 1731-1757; 1838-1850; 1875-1886; 1909-1918;
RP 1921-1931; 2048-2058; 2131-2138; 2211-2218; 2354-2381; 2527-2536;
RP 2564-2572; 2713-2721; 2981-2989; 3046-3065; 3229-3238; 3243-3252;
RP 3589-3606; 3618-3628; 3735-3745; 3809-3816; 3827-3836; 3845-3857;
RP 3889-3915; 4131-4142; 4204-4215; 4320-4334; 4414-4426; 4608-4637;
RP 4686-4696; 4717-4724; 4803-4814; 4852-4860; 5013-5022 AND 5062-5069,
RP PHOSPHORYLATION AT SER-2719, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 779-5183 (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI.
RT The complete sequences of 150 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2908-5183 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries
RT from human brain.";
RL DNA Res. 4:345-349(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4385-5183 (ISOFORMS 1 AND
RP 2), AND VARIANT LEU-4867.
RC TISSUE=Kidney, Liver, Lung, and Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4583-5183 (ISOFORM 1), AND VARIANTS
RP LEU-4867 AND ARG-4924.
RX PubMed=16247014; DOI=10.1073/pnas.0500090102;
RA Lennerz V., Fatho M., Gentilini C., Frye R.A., Lifke A., Ferel D.,
RA Woelfel C., Huber C., Woelfel T.;
RT "The response of autologous T cells to a human melanoma is dominated
RT by mutated neoantigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16013-16018(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4686-5183 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4709-5183 (ISOFORM 1), AND
RP VARIANT LEU-4867.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP INTERACTION WITH HPV-16 E7; HPV-6B E7 AND HPV-11 E7, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=16061792; DOI=10.1073/pnas.0505337102;
RA Huh K.-W., DeMasi J., Ogawa H., Nakatani Y., Howley P.M., Muenger K.;
RT "Association of the human papillomavirus type 16 E7 oncoprotein with
RT the 600-kDa retinoblastoma protein-associated factor, p600.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11492-11497(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181 AND
RP THR-2715, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1084, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181 AND
RP SER-1763, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2719, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP FUNCTION.
RX PubMed=23932781; DOI=10.1016/j.molcel.2013.07.002;
RA Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.;
RT "Acetylation stabilizes ATP-citrate lyase to promote lipid
RT biosynthesis and tumor growth.";
RL Mol. Cell 51:506-518(2013).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-1394.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the
CC N-end rule pathway. Recognizes and binds to proteins bearing
CC specific N-terminal residues that are destabilizing according to
CC the N-end rule, leading to their ubiquitination and subsequent
CC degradation. Together with clathrin, forms meshwork structures
CC involved in membrane morphogenesis and cytoskeletal organization.
CC Regulates integrin-mediated signaling. May play a role in
CC activation of FAK in response to cell-matrix interactions.
CC Mediates ubiquitination of ACLY, leading to its subsequent
CC degradation.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RB1 and calmodulin. Interacts with protein
CC E7 from papilloma virus HPV-16, HPV-6B and HPV-11.
CC -!- INTERACTION:
CC P03129:E7 (xeno); NbExp=4; IntAct=EBI-1995940, EBI-866453;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential). Cytoplasm. Cytoplasm, cytoskeleton. Nucleus.
CC Note=Concentrates at the leading edge of membrane structures
CC involved in actin motility.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q5T4S7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T4S7-2; Sequence=VSP_025209;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q5T4S7-3; Sequence=VSP_025203, VSP_025206;
CC Name=4;
CC IsoId=Q5T4S7-4; Sequence=VSP_025205, VSP_025206;
CC Name=5;
CC IsoId=Q5T4S7-5; Sequence=VSP_025201, VSP_025202, VSP_025204;
CC Name=6;
CC IsoId=Q5T4S7-6; Sequence=VSP_025200, VSP_025207, VSP_025208;
CC -!- SIMILARITY: Belongs to the UBR4 family.
CC -!- SIMILARITY: Contains 1 UBR-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD43719.1; Type=Erroneous initiation;
CC Sequence=CAI19271.1; Type=Erroneous gene model prediction;
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DR EMBL; AF348492; AAL83880.1; -; mRNA.
DR EMBL; AK022322; BAB14011.1; -; mRNA.
DR EMBL; AL137127; CAI19268.1; -; Genomic_DNA.
DR EMBL; AL357564; CAI19268.1; JOINED; Genomic_DNA.
DR EMBL; AL137127; CAI19269.1; -; Genomic_DNA.
DR EMBL; AL357564; CAI19269.1; JOINED; Genomic_DNA.
DR EMBL; AL137127; CAI19271.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL137127; CAI19272.1; -; Genomic_DNA.
DR EMBL; AL357564; CAI19272.1; JOINED; Genomic_DNA.
DR EMBL; AL137127; CAI19273.1; -; Genomic_DNA.
DR EMBL; AL137127; CAI19274.1; -; Genomic_DNA.
DR EMBL; AL357564; CAI20972.1; -; Genomic_DNA.
DR EMBL; AL137127; CAI20972.1; JOINED; Genomic_DNA.
DR EMBL; AL357564; CAI20973.1; -; Genomic_DNA.
DR EMBL; AL137127; CAI20973.1; JOINED; Genomic_DNA.
DR EMBL; AL357564; CAI20974.1; -; Genomic_DNA.
DR EMBL; AL137127; CAI20974.1; JOINED; Genomic_DNA.
DR EMBL; AB037728; BAA92545.1; -; mRNA.
DR EMBL; AB007931; BAA32307.1; -; mRNA.
DR EMBL; BC018694; AAH18694.2; -; mRNA.
DR EMBL; BC063573; AAH63573.1; -; mRNA.
DR EMBL; BC073905; AAH73905.1; -; mRNA.
DR EMBL; BC096758; AAH96758.1; -; mRNA.
DR EMBL; AJ505016; CAD43719.1; ALT_INIT; mRNA.
DR EMBL; AL049972; CAB43227.1; -; mRNA.
DR EMBL; AF055010; AAC09360.1; -; mRNA.
DR PIR; T00076; T00076.
DR RefSeq; NP_065816.2; NM_020765.2.
DR UniGene; Hs.148078; -.
DR UniGene; Hs.649405; -.
DR ProteinModelPortal; Q5T4S7; -.
DR IntAct; Q5T4S7; 19.
DR MINT; MINT-4715511; -.
DR PhosphoSite; Q5T4S7; -.
DR DMDM; 74744979; -.
DR PaxDb; Q5T4S7; -.
DR PRIDE; Q5T4S7; -.
DR Ensembl; ENST00000375217; ENSP00000364365; ENSG00000127481.
DR Ensembl; ENST00000375218; ENSP00000364366; ENSG00000127481.
DR Ensembl; ENST00000375226; ENSP00000364374; ENSG00000127481.
DR Ensembl; ENST00000375254; ENSP00000364403; ENSG00000127481.
DR Ensembl; ENST00000375267; ENSP00000364416; ENSG00000127481.
DR GeneID; 23352; -.
DR KEGG; hsa:23352; -.
DR UCSC; uc001bbi.3; human.
DR CTD; 23352; -.
DR GeneCards; GC01M019401; -.
DR H-InvDB; HIX0000191; -.
DR HGNC; HGNC:30313; UBR4.
DR HPA; HPA021046; -.
DR MIM; 609890; gene.
DR neXtProt; NX_Q5T4S7; -.
DR PharmGKB; PA162407958; -.
DR eggNOG; NOG236675; -.
DR HOVERGEN; HBG058328; -.
DR InParanoid; Q5T4S7; -.
DR KO; K10691; -.
DR OMA; SNTPMGD; -.
DR OrthoDB; EOG7288QF; -.
DR PhylomeDB; Q5T4S7; -.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR ChiTaRS; UBR4; human.
DR GeneWiki; UBR4; -.
DR GenomeRNAi; 23352; -.
DR NextBio; 45346; -.
DR PRO; PR:Q5T4S7; -.
DR ArrayExpress; Q5T4S7; -.
DR Bgee; Q5T4S7; -.
DR Genevestigator; Q5T4S7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR025704; E3_Ub_ligase_UBR4.
DR InterPro; IPR017986; WD40_repeat_dom.
DR InterPro; IPR003126; Znf_N-recognin.
DR Pfam; PF13764; E3_UbLigase_R4; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SUPFAM; SSF48371; SSF48371; 9.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calmodulin-binding;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Host-virus interaction; Ligase; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 5183 E3 ubiquitin-protein ligase UBR4.
FT /FTId=PRO_0000286861.
FT TRANSMEM 850 870 Helical; (Potential).
FT TRANSMEM 993 1013 Helical; (Potential).
FT ZN_FING 1656 1729 UBR-type.
FT COMPBIAS 9 15 Poly-Ala.
FT COMPBIAS 608 631 Pro-rich.
FT COMPBIAS 2728 2738 Poly-Asp.
FT COMPBIAS 3339 3370 Ser-rich.
FT MOD_RES 178 178 Phosphoserine.
FT MOD_RES 181 181 Phosphoserine.
FT MOD_RES 1084 1084 N6-acetyllysine.
FT MOD_RES 1402 1402 Phosphoserine (By similarity).
FT MOD_RES 1763 1763 Phosphoserine.
FT MOD_RES 2715 2715 Phosphothreonine.
FT MOD_RES 2719 2719 Phosphoserine.
FT VAR_SEQ 1 3585 Missing (in isoform 6).
FT /FTId=VSP_025200.
FT VAR_SEQ 2100 2100 K -> KQ (in isoform 5).
FT /FTId=VSP_025201.
FT VAR_SEQ 2405 2486 IGASVDPAGVTMIDAVKIYGKTKEQFGWPDEPPEEFPSASV
FT SNICPSNLNQSNGTGDSDSAAPTTTSGTVLERLVVSSLEAL
FT -> SESPTPGADSVLIVTAKLGATGLWLSNILGSLHSADFS
FT VLSSGNFELHLMY (in isoform 5).
FT /FTId=VSP_025202.
FT VAR_SEQ 2476 2476 E -> ESSETESLTKLD (in isoform 3).
FT /FTId=VSP_025203.
FT VAR_SEQ 2487 5183 Missing (in isoform 5).
FT /FTId=VSP_025204.
FT VAR_SEQ 2601 2601 T -> TDCFFPRCACWSLGIVGILIGAPLETPSP (in
FT isoform 4).
FT /FTId=VSP_025205.
FT VAR_SEQ 2830 2864 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_025206.
FT VAR_SEQ 3777 3797 DDSGTAGGISSTSASVNRYIL -> VVPRCKGHLDKGLGLD
FT QKTAS (in isoform 6).
FT /FTId=VSP_025207.
FT VAR_SEQ 3798 5183 Missing (in isoform 6).
FT /FTId=VSP_025208.
FT VAR_SEQ 5108 5108 K -> KKQTTPTVGGIDTGSLEPCVCE (in isoform
FT 2).
FT /FTId=VSP_025209.
FT VARIANT 1107 1107 T -> A (in dbSNP:rs16862578).
FT /FTId=VAR_032193.
FT VARIANT 1394 1394 R -> H (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035540.
FT VARIANT 4867 4867 M -> L (in dbSNP:rs12584).
FT /FTId=VAR_032194.
FT VARIANT 4924 4924 G -> R (in a melanoma patient).
FT /FTId=VAR_032195.
FT VARIANT 5084 5084 V -> M (in dbSNP:rs2274010).
FT /FTId=VAR_032196.
FT CONFLICT 2016 2016 A -> S (in Ref. 1; AAL83880).
FT CONFLICT 2410 2410 D -> E (in Ref. 1; AAL83880).
FT CONFLICT 3957 3957 G -> S (in Ref. 1; AAL83880).
FT CONFLICT 4589 4589 G -> V (in Ref. 7; AAH18694).
SQ SEQUENCE 5183 AA; 573841 MW; 5F6DD7B565E27609 CRC64;
MATSGGEEAA AAAPAPGTPA TGADTTPGWE VAVRPLLSAS YSAFEMKELP QLVASVIESE
SEILHHEKQY EPFYSSFVAL STHYITTVCS LIPRNQLQSV AAACKVLIEF SLLRLENPDE
ACAVSQKHLI LLIKGLCTGC SRLDRTEIIT FTAMMKSAKL PQTVKTLSDV EDQKELASPV
SPELRQKEVQ MNFLNQLTSV FNPRTVASQP ISTQTLVEGE NDEQSSTDQA SAIKTKNVFI
AQNVASLQEL GGSEKLLRVC LNLPYFLRYI NRFQDAVLAN SFFIMPATVA DATAVRNGFH
SLVIDVTMAL DTLSLPVLEP LNPSRLQDVT VLSLSCLYAG VSVATCMAIL HVGSAQQVRT
GSTSSKEDDY ESDAATIVQK CLEIYDMIGQ AISSSRRAGG EHYQNFQLLG AWCLLNSLFL
ILNLSPTALA DKGKEKDPLA ALRVRDILSR TKEGVGSPKL GPGKGHQGFG VLSVILANHA
IKLLTSLFQD LQVEALHKGW ETDGPPAALS IMAQSTSIQR IQRLIDSVPL MNLLLTLLST
SYRKACVLQR QRKGSMSSDA SASTDSNTYY EDDFSSTEED SSQDDDSEPI LGQWFEETIS
PSKEKAAPPP PPPPPPLESS PRVKSPSKQA PGEKGNILAS RKDPELFLGL ASNILNFITS
SMLNSRNNFI RNYLSVSLSE HHMATLASII KEVDKDGLKG SSDEEFAAAL YHFNHSLVTS
DLQSPNLQNT LLQQLGVAPF SEGPWPLYIH PQSLSVLSRL LLIWQHKASA QGDPDVPECL
KVWDRFLSTM KQNALQGVVP SETEDLNVEH LQMLLLIFHN FTETGRRAIL SLFVQIIQEL
SVNMDAQMRF VPLILARLLL IFDYLLHQYS KAPVYLFEQV QHNLLSPPFG WASGSQDSNS
RRATTPLYHG FKEVEENWSK HFSSDAVPHP RFYCVLSPEA SEDDLNRLDS VACDVLFSKL
VKYDELYAAL TALLAAGSQL DTVRRKENKN VTALEACALQ YYFLILWRIL GILPPSKTYI
NQLSMNSPEM SECDILHTLR WSSRLRISSY VNWIKDHLIK QGMKAEHASS LLELASTTKC
SSVKYDVEIV EEYFARQISS FCSIDCTTIL QLHEIPSLQS IYTLDAAISK VQVSLDEHFS
KMAAETDPHK SSEITKNLLP ATLQLIDTYA SFTRAYLLQN FNEEGTTEKP SKEKLQGFAA
VLAIGSSRCK ANTLGPTLVQ NLPSSVQTVC ESWNNINTNE FPNIGSWRNA FANDTIPSES
YISAVQAAHL GTLCSQSLPL AASLKHTLLS LVRLTGDLIV WSDEMNPPQV IRTLLPLLLE
SSTESVAEIS SNSLERILGP AESDEFLARV YEKLITGCYN ILANHADPNS GLDESILEEC
LQYLEKQLES SQARKAMEEF FSDSGELVQI MMATANENLS AKFCNRVLKF FTKLFQLTEK
SPNPSLLHLC GSLAQLACVE PVRLQAWLTR MTTSPPKDSD QLDVIQENRQ LLQLLTTYIV
RENSQVGEGV CAVLLGTLTP MATEMLANGD GTGFPELMVV MATLASAGQG AGHLQLHNAA
VDWLSRCKKY LSQKNVVEKL NANVMHGKHV MILECTCHIM SYLADVTNAL SQSNGQGPSH
LSVDGEERAI EVDSDWVEEL AVEEEDSQAE DSDEDSLCNK LCTFTITQKE FMNQHWYHCH
TCKMVDGVGV CTVCAKVCHK DHEISYAKYG SFFCDCGAKE DGSCLALVKR TPSSGMSSTM
KESAFQSEPR ISESLVRHAS TSSPADKAKV TISDGKVADE EKPKKSSLCR TVEGCREELQ
NQANFSFAPL VLDMLNFLMD AIQTNFQQAS AVGSSSRAQQ ALSELHTVEK AVEMTDQLMV
PTLGSQEGAF ENVRMNYSGD QGQTIRQLIS AHVLRRVAMC VLSSPHGRRQ HLAVSHEKGK
ITVLQLSALL KQADSSKRKL TLTRLASAPV PFTVLSLTGN PCKEDYLAVC GLKDCHVLTF
SSSGSVSDHL VLHPQLATGN FIIKAVWLPG SQTELAIVTA DFVKIYDLCV DALSPTFYFL
LPSSKIRDVT FLFNEEGKNI IVIMSSAGYI YTQLMEEASS AQQGPFYVTN VLEINHEDLK
DSNSQVAGGG VSVYYSHVLQ MLFFSYCQGK SFAATISRTT LEVLQLFPIN IKSSNGGSKT
SPALCQWSEV MNHPGLVCCV QQTTGVPLVV MVKPDTFLIQ EIKTLPAKAK IQDMVAIRHT
ACNEQQRTTM ILLCEDGSLR IYMANVENTS YWLQPSLQPS SVISIMKPVR KRKTATITTR
TSSQVTFPID FFEHNQQLTD VEFGGNDLLQ VYNAQQIKHR LNSTGMYVAN TKPGGFTIEI
SNNNSTMVMT GMRIQIGTQA IERAPSYIEI FGRTMQLNLS RSRWFDFPFT REEALQADKK
LNLFIGASVD PAGVTMIDAV KIYGKTKEQF GWPDEPPEEF PSASVSNICP SNLNQSNGTG
DSDSAAPTTT SGTVLERLVV SSLEALESCF AVGPIIEKER NKNAAQELAT LLLSLPAPAS
VQQQSKSLLA SLHTSRSAYH SHKDQALLSK AVQCLNTSSK EGKDLDPEVF QRLVITARSI
AIMRPNNLVH FTESKLPQME TEGMDEGKEP QKQLEGDCCS FITQLVNHFW KLHASKPKNA
FLAPACLPGL THIEATVNAL VDIIHGYCTC ELDCINTASK IYMQMLLCPD PAVSFSCKQA
LIRVLRPRNK RRHVTLPSSP RSNTPMGDKD DDDDDDADEK MQSSGIPNGG HIRQESQEQS
EVDHGDFEMV SESMVLETAE NVNNGNPSPL EALLAGAEGF PPMLDIPPDA DDETMVELAI
ALSLQQDQQG SSSSALGLQS LGLSGQAPSS SSLDAGTLSD TTASAPASDD EGSTAATDGS
TLRTSPADHG GSVGSESGGS AVDSVAGEHS VSGRSSAYGD ATAEGHPAGP GSVSSSTGAI
STTTGHQEGD GSEGEGEGET EGDVHTSNRL HMVRLMLLER LLQTLPQLRN VGGVRAIPYM
QVILMLTTDL DGEDEKDKGA LDNLLSQLIA ELGMDKKDVS KKNERSALNE VHLVVMRLLS
VFMSRTKSGS KSSICESSSL ISSATAAALL SSGAVDYCLH VLKSLLEYWK SQQNDEEPVA
TSQLLKPHTT SSPPDMSPFF LRQYVKGHAA DVFEAYTQLL TEMVLRLPYQ IKKITDTNSR
IPPPVFDHSW FYFLSEYLMI QQTPFVRRQV RKLLLFICGS KEKYRQLRDL HTLDSHVRGI
KKLLEEQGIF LRASVVTASS GSALQYDTLI SLMEHLKACA EIAAQRTINW QKFCIKDDSV
LYFLLQVSFL VDEGVSPVLL QLLSCALCGS KVLAALAASS GSSSASSSSA PVAASSGQAT
TQSKSSTKKS KKEEKEKEKD GETSGSQEDQ LCTALVNQLN KFADKETLIQ FLRCFLLESN
SSSVRWQAHC LTLHIYRNSS KSQQELLLDL MWSIWPELPA YGRKAAQFVD LLGYFSLKTP
QTEKKLKEYS QKAVEILRTQ NHILTNHPNS NIYNTLSGLV EFDGYYLESD PCLVCNNPEV
PFCYIKLSSI KVDTRYTTTQ QVVKLIGSHT ISKVTVKIGD LKRTKMVRTI NLYYNNRTVQ
AIVELKNKPA RWHKAKKVQL TPGQTEVKID LPLPIVASNL MIEFADFYEN YQASTETLQC
PRCSASVPAN PGVCGNCGEN VYQCHKCRSI NYDEKDPFLC NACGFCKYAR FDFMLYAKPC
CAVDPIENEE DRKKAVSNIN TLLDKADRVY HQLMGHRPQL ENLLCKVNEA APEKPQDDSG
TAGGISSTSA SVNRYILQLA QEYCGDCKNS FDELSKIIQK VFASRKELLE YDLQQREAAT
KSSRTSVQPT FTASQYRALS VLGCGHTSST KCYGCASAVT EHCITLLRAL ATNPALRHIL
VSQGLIRELF DYNLRRGAAA MREEVRQLMC LLTRDNPEAT QQMNDLIIGK VSTALKGHWA
NPDLASSLQY EMLLLTDSIS KEDSCWELRL RCALSLFLMA VNIKTPVVVE NITLMCLRIL
QKLIKPPAPT SKKNKDVPVE ALTTVKPYCN EIHAQAQLWL KRDPKASYDA WKKCLPIRGI
DGNGKAPSKS ELRHLYLTEK YVWRWKQFLS RRGKRTSPLD LKLGHNNWLR QVLFTPATQA
ARQAACTIVE ALATIPSRKQ QVLDLLTSYL DELSIAGECA AEYLALYQKL ITSAHWKVYL
AARGVLPYVG NLITKEIARL LALEEATLST DLQQGYALKS LTGLLSSFVE VESIKRHFKS
RLVGTVLNGY LCLRKLVVQR TKLIDETQDM LLEMLEDMTT GTESETKAFM AVCIETAKRY
NLDDYRTPVF IFERLCSIIY PEENEVTEFF VTLEKDPQQE DFLQGRMPGN PYSSNEPGIG
PLMRDIKNKI CQDCDLVALL EDDSGMELLV NNKIISLDLP VAEVYKKVWC TTNEGEPMRI
VYRMRGLLGD ATEEFIESLD STTDEEEDEE EVYKMAGVMA QCGGLECMLN RLAGIRDFKQ
GRHLLTVLLK LFSYCVKVKV NRQQLVKLEM NTLNVMLGTL NLALVAEQES KDSGGAAVAE
QVLSIMEIIL DESNAEPLSE DKGNLLLTGD KDQLVMLLDQ INSTFVRSNP SVLQGLLRII
PYLSFGEVEK MQILVERFKP YCNFDKYDED HSGDDKVFLD CFCKIAAGIK NNSNGHQLKD
LILQKGITQN ALDYMKKHIP SAKNLDADIW KKFLSRPALP FILRLLRGLA IQHPGTQVLI
GTDSIPNLHK LEQVSSDEGI GTLAENLLEA LREHPDVNKK IDAARRETRA EKKRMAMAMR
QKALGTLGMT TNEKGQVVTK TALLKQMEEL IEEPGLTCCI CREGYKFQPT KVLGIYTFTK
RVALEEMENK PRKQQGYSTV SHFNIVHYDC HLAAVRLARG REEWESAALQ NANTKCNGLL
PVWGPHVPES AFATCLARHN TYLQECTGQR EPTYQLNIHD IKLLFLRFAM EQSFSADTGG
GGRESNIHLI PYIIHTVLYV LNTTRATSRE EKNLQGFLEQ PKEKWVESAF EVDGPYYFTV
LALHILPPEQ WRATRVEILR RLLVTSQARA VAPGGATRLT DKAVKDYSAY RSSLLFWALV
DLIYNMFKKV PTSNTEGGWS CSLAEYIRHN DMPIYEAADK ALKTFQEEFM PVETFSEFLD
VAGLLSEITD PESFLKDLLN SVP
//
MIM
609890
*RECORD*
*FIELD* NO
609890
*FIELD* TI
*609890 RETINOBLASTOMA-ASSOCIATED FACTOR 600
;;RBAF600;;
KIAA1307;;
p600
*FIELD* TX
read more
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Nagase et al. (2000) cloned RBAF600, which they designated
KIAA1307. RT-PCR ELISA detected BBAF600 in all adult and fetal tissues
and specific brain regions examined. Highest expression was in
cerebellum and caudate nucleus.
By mass spectrometric analysis of proteins associated with
retinoblastoma protein (RB1; 614041) in HeLa cells, followed by peptide
sequencing, EST database analysis, and screening a cDNA library,
Nakatani et al. (2005) cloned RBAF600, which they designated p600. The
deduced 5,183-amino acid protein has a calculated molecular mass of
573.5 kD. Immunostaining of human foreskin fibroblasts localized p600 in
a continuous meshwork pattern from the nucleus to the cytoplasm, passing
through the nuclear envelope. In the cytoplasm, p600 was concentrated at
the leading edge of membrane structures.
GENE FUNCTION
The human papillomavirus (HPV) type 16 E7 gene encodes a multifunctional
oncoprotein that can subvert multiple cellular regulatory pathways. E7
targets RB and the related pocket proteins p107 (RBL1; 116957) and p130
(RBL2; 180203). By tandem affinity purification in the HPV-positive HeLa
cell cervical carcinoma cell line and mass spectrometry, Huh et al.
(2005) found that p600 is a cellular target of E7. The association of E7
with p600 was independent of the pocket proteins and was mediated
through the N-terminal E7 domain. Huh et al. (2005) observed that
depletion of p600 by RNA interference substantially decreased
anchorage-independent growth in HPV-positive and -negative human cancer
cells. They concluded that p600 is a cellular target of E7 that
regulates cellular pathways that contribute to anchorage-independent
growth and cellular transformation.
Nakatani et al. (2005) found that RBAF600 associates with RB in the
nucleus and with Ca(2+)-bound calmodulin (see CALM1, 114180) in the
cytoplasm. They noted that in the nucleus, p600 and RB appears to act as
a chromatin scaffold, and in the cytoplasm p600 and clathrin (see CLTC,
118955) form a meshwork structure which could contribute to cytoskeletal
organization and membrane morphogenesis. Reduced expression of p600 with
interfering RNA abrogated integrin (see ITGB1, 135630)-mediated ruffled
membrane formation and prevented activation of integrin-mediated
survival pathways. Knockdown of p600 sensitized cells to apoptosis
induced by cell detachment.
MAPPING
By radiation hybrid analysis, Nagase et al. (2000) mapped the RBAF600
gene to chromosome 1.
*FIELD* RF
1. Huh, K.-W.; DeMasi, J.; Ogawa, H.; Nakatani, Y.; Howley, P. M.;
Munger, K.: Association of the human papillomavirus type 16 E7 oncoprotein
with the 600-kDa retinoblastoma protein-associated factor, p600. Proc.
Nat. Acad. Sci. 102: 11492-11497, 2005.
2. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 65-73, 2000.
3. Nakatani, Y.; Konishi, H.; Vassilev, A.; Kurooka, H.; Ishiguro,
K.; Sawada, J.; Ikura, T.; Korsmeyer, S. J.; Qin, J.; Herlitz, A.
M.: p600, a unique protein required for membrane morphogenesis and
cell survival. Proc. Nat. Acad. Sci. 102: 15093-15098, 2005. Note:
Erratum: Proc. Nat. Acad. Sci. 102: 17882 only, 2005.
*FIELD* CD
Patricia A. Hartz: 2/16/2006
*FIELD* ED
alopez: 06/17/2011
alopez: 2/16/2006
*RECORD*
*FIELD* NO
609890
*FIELD* TI
*609890 RETINOBLASTOMA-ASSOCIATED FACTOR 600
;;RBAF600;;
KIAA1307;;
p600
*FIELD* TX
read more
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Nagase et al. (2000) cloned RBAF600, which they designated
KIAA1307. RT-PCR ELISA detected BBAF600 in all adult and fetal tissues
and specific brain regions examined. Highest expression was in
cerebellum and caudate nucleus.
By mass spectrometric analysis of proteins associated with
retinoblastoma protein (RB1; 614041) in HeLa cells, followed by peptide
sequencing, EST database analysis, and screening a cDNA library,
Nakatani et al. (2005) cloned RBAF600, which they designated p600. The
deduced 5,183-amino acid protein has a calculated molecular mass of
573.5 kD. Immunostaining of human foreskin fibroblasts localized p600 in
a continuous meshwork pattern from the nucleus to the cytoplasm, passing
through the nuclear envelope. In the cytoplasm, p600 was concentrated at
the leading edge of membrane structures.
GENE FUNCTION
The human papillomavirus (HPV) type 16 E7 gene encodes a multifunctional
oncoprotein that can subvert multiple cellular regulatory pathways. E7
targets RB and the related pocket proteins p107 (RBL1; 116957) and p130
(RBL2; 180203). By tandem affinity purification in the HPV-positive HeLa
cell cervical carcinoma cell line and mass spectrometry, Huh et al.
(2005) found that p600 is a cellular target of E7. The association of E7
with p600 was independent of the pocket proteins and was mediated
through the N-terminal E7 domain. Huh et al. (2005) observed that
depletion of p600 by RNA interference substantially decreased
anchorage-independent growth in HPV-positive and -negative human cancer
cells. They concluded that p600 is a cellular target of E7 that
regulates cellular pathways that contribute to anchorage-independent
growth and cellular transformation.
Nakatani et al. (2005) found that RBAF600 associates with RB in the
nucleus and with Ca(2+)-bound calmodulin (see CALM1, 114180) in the
cytoplasm. They noted that in the nucleus, p600 and RB appears to act as
a chromatin scaffold, and in the cytoplasm p600 and clathrin (see CLTC,
118955) form a meshwork structure which could contribute to cytoskeletal
organization and membrane morphogenesis. Reduced expression of p600 with
interfering RNA abrogated integrin (see ITGB1, 135630)-mediated ruffled
membrane formation and prevented activation of integrin-mediated
survival pathways. Knockdown of p600 sensitized cells to apoptosis
induced by cell detachment.
MAPPING
By radiation hybrid analysis, Nagase et al. (2000) mapped the RBAF600
gene to chromosome 1.
*FIELD* RF
1. Huh, K.-W.; DeMasi, J.; Ogawa, H.; Nakatani, Y.; Howley, P. M.;
Munger, K.: Association of the human papillomavirus type 16 E7 oncoprotein
with the 600-kDa retinoblastoma protein-associated factor, p600. Proc.
Nat. Acad. Sci. 102: 11492-11497, 2005.
2. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 65-73, 2000.
3. Nakatani, Y.; Konishi, H.; Vassilev, A.; Kurooka, H.; Ishiguro,
K.; Sawada, J.; Ikura, T.; Korsmeyer, S. J.; Qin, J.; Herlitz, A.
M.: p600, a unique protein required for membrane morphogenesis and
cell survival. Proc. Nat. Acad. Sci. 102: 15093-15098, 2005. Note:
Erratum: Proc. Nat. Acad. Sci. 102: 17882 only, 2005.
*FIELD* CD
Patricia A. Hartz: 2/16/2006
*FIELD* ED
alopez: 06/17/2011
alopez: 2/16/2006