Full text data of UBXN7
UBXN7
(KIAA0794, UBXD7)
[Confidence: low (only semi-automatic identification from reviews)]
UBX domain-containing protein 7
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UBX domain-containing protein 7
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O94888
ID UBXN7_HUMAN Reviewed; 489 AA.
AC O94888; D3DXB3; Q6ZP77; Q86X20; Q8N327;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2005, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=UBX domain-containing protein 7;
GN Name=UBXN7; Synonyms=KIAA0794, UBXD7;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-489.
RC TISSUE=Testis;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-288, AND
RP 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-288, AND
RP MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, 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 [15]
RP STRUCTURE BY NMR OF 376-487.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the UBX domain of KIAA0794 protein.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [16]
RP STRUCTURE BY NMR OF 5-54.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the novel identified UBA-like domain in the N-
RT terminal of human FAS associated factor 1 protein.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [17]
RP STRUCTURE BY NMR OF 131-270.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the UAS domain of human UBX domain-containing
RT protein 7.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- INTERACTION:
CC Q16665:HIF1A; NbExp=3; IntAct=EBI-1993627, EBI-447269;
CC -!- SIMILARITY: Contains 1 UBX domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34514.1; Type=Erroneous initiation;
CC Sequence=BAC85247.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites;
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DR EMBL; AB018337; BAA34514.1; ALT_INIT; mRNA.
DR EMBL; AK129880; BAC85247.1; ALT_SEQ; mRNA.
DR EMBL; CH471191; EAW53652.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53654.1; -; Genomic_DNA.
DR EMBL; BC028986; AAH28986.1; -; mRNA.
DR RefSeq; NP_056377.1; NM_015562.1.
DR UniGene; Hs.518524; -.
DR PDB; 1WJ4; NMR; -; A=378-487.
DR PDB; 2DAL; NMR; -; A=6-54.
DR PDB; 2DLX; NMR; -; A=131-270.
DR PDBsum; 1WJ4; -.
DR PDBsum; 2DAL; -.
DR PDBsum; 2DLX; -.
DR ProteinModelPortal; O94888; -.
DR SMR; O94888; 13-51, 130-265, 376-487.
DR DIP; DIP-47029N; -.
DR IntAct; O94888; 37.
DR STRING; 9606.ENSP00000296328; -.
DR PhosphoSite; O94888; -.
DR PaxDb; O94888; -.
DR PRIDE; O94888; -.
DR DNASU; 26043; -.
DR Ensembl; ENST00000296328; ENSP00000296328; ENSG00000163960.
DR GeneID; 26043; -.
DR KEGG; hsa:26043; -.
DR UCSC; uc003fwm.4; human.
DR CTD; 26043; -.
DR GeneCards; GC03M196074; -.
DR HGNC; HGNC:29119; UBXN7.
DR HPA; HPA048441; -.
DR HPA; HPA049442; -.
DR neXtProt; NX_O94888; -.
DR PharmGKB; PA162408447; -.
DR eggNOG; NOG322646; -.
DR HOGENOM; HOG000143398; -.
DR HOVERGEN; HBG057394; -.
DR InParanoid; O94888; -.
DR OMA; PEKSDGI; -.
DR ChiTaRS; UBXN7; human.
DR EvolutionaryTrace; O94888; -.
DR GenomeRNAi; 26043; -.
DR NextBio; 47875; -.
DR PMAP-CutDB; O94888; -.
DR PRO; PR:O94888; -.
DR ArrayExpress; O94888; -.
DR Bgee; O94888; -.
DR CleanEx; HS_UBXN7; -.
DR Genevestigator; O94888; -.
DR GO; GO:0034098; C:Cdc48p-Npl4p-Ufd1p AAA ATPase complex; IDA:BHF-UCL.
DR GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR001012; UBX.
DR InterPro; IPR017346; UCP037991_UAS/UBX.
DR Pfam; PF00789; UBX; 1.
DR PIRSF; PIRSF037991; UCP037991_UBX7/2; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 489 UBX domain-containing protein 7.
FT /FTId=PRO_0000211035.
FT DOMAIN 408 485 UBX.
FT COMPBIAS 337 342 Poly-Glu.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 278 278 Phosphoserine.
FT MOD_RES 285 285 Phosphoserine.
FT MOD_RES 288 288 Phosphoserine.
FT CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT HELIX 11 23
FT HELIX 28 36
FT TURN 37 39
FT HELIX 42 51
FT TURN 146 148
FT HELIX 154 164
FT STRAND 167 173
FT TURN 177 179
FT HELIX 180 186
FT TURN 187 189
FT HELIX 191 199
FT STRAND 201 210
FT HELIX 211 220
FT STRAND 224 231
FT TURN 233 235
FT STRAND 240 244
FT HELIX 247 260
FT STRAND 412 418
FT STRAND 424 430
FT HELIX 435 446
FT TURN 449 451
FT STRAND 452 455
FT STRAND 457 459
FT STRAND 468 470
FT TURN 472 476
FT STRAND 479 481
FT STRAND 484 487
SQ SEQUENCE 489 AA; 54862 MW; 3C894533B1A2C41A CRC64;
MAAHGGSAAS SALKGLIQQF TTITGASESV GKHMLEACNN NLEMAVTMFL DGGGIAEEPS
TSSASVSTVR PHTEEEVRAP IPQKQEILVE PEPLFGAPKR RRPARSIFDG FRDFQTETIR
QEQELRNGGA IDKKLTTLAD LFRPPIDLMH KGSFETAKEC GQMQNKWLMI NIQNVQDFAC
QCLNRDVWSN EAVKNIIREH FIFWQVYHDS EEGQRYIQFY KLGDFPYVSI LDPRTGQKLV
EWHQLDVSSF LDQVTGFLGE HGQLDGLSSS PPKKCARSES LIDASEDSQL EAAIRASLQE
THFDSTQTKQ DSRSDEESES ELFSGSEEFI SVCGSDEEEE VENLAKSRKS PHKDLGHRKE
ENRRPLTEPP VRTDPGTATN HQGLPAVDSE ILEMPPEKAD GVVEGIDVNG PKAQLMLRYP
DGKREQITLP EQAKLLALVK HVQSKGYPNE RFELLTNFPR RKLSHLDYDI TLQEAGLCPQ
ETVFVQERN
//
ID UBXN7_HUMAN Reviewed; 489 AA.
AC O94888; D3DXB3; Q6ZP77; Q86X20; Q8N327;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2005, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=UBX domain-containing protein 7;
GN Name=UBXN7; Synonyms=KIAA0794, UBXD7;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-489.
RC TISSUE=Testis;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-288, AND
RP 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-288, AND
RP MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, 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 [15]
RP STRUCTURE BY NMR OF 376-487.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the UBX domain of KIAA0794 protein.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [16]
RP STRUCTURE BY NMR OF 5-54.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the novel identified UBA-like domain in the N-
RT terminal of human FAS associated factor 1 protein.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [17]
RP STRUCTURE BY NMR OF 131-270.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the UAS domain of human UBX domain-containing
RT protein 7.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- INTERACTION:
CC Q16665:HIF1A; NbExp=3; IntAct=EBI-1993627, EBI-447269;
CC -!- SIMILARITY: Contains 1 UBX domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34514.1; Type=Erroneous initiation;
CC Sequence=BAC85247.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites;
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DR EMBL; AB018337; BAA34514.1; ALT_INIT; mRNA.
DR EMBL; AK129880; BAC85247.1; ALT_SEQ; mRNA.
DR EMBL; CH471191; EAW53652.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53654.1; -; Genomic_DNA.
DR EMBL; BC028986; AAH28986.1; -; mRNA.
DR RefSeq; NP_056377.1; NM_015562.1.
DR UniGene; Hs.518524; -.
DR PDB; 1WJ4; NMR; -; A=378-487.
DR PDB; 2DAL; NMR; -; A=6-54.
DR PDB; 2DLX; NMR; -; A=131-270.
DR PDBsum; 1WJ4; -.
DR PDBsum; 2DAL; -.
DR PDBsum; 2DLX; -.
DR ProteinModelPortal; O94888; -.
DR SMR; O94888; 13-51, 130-265, 376-487.
DR DIP; DIP-47029N; -.
DR IntAct; O94888; 37.
DR STRING; 9606.ENSP00000296328; -.
DR PhosphoSite; O94888; -.
DR PaxDb; O94888; -.
DR PRIDE; O94888; -.
DR DNASU; 26043; -.
DR Ensembl; ENST00000296328; ENSP00000296328; ENSG00000163960.
DR GeneID; 26043; -.
DR KEGG; hsa:26043; -.
DR UCSC; uc003fwm.4; human.
DR CTD; 26043; -.
DR GeneCards; GC03M196074; -.
DR HGNC; HGNC:29119; UBXN7.
DR HPA; HPA048441; -.
DR HPA; HPA049442; -.
DR neXtProt; NX_O94888; -.
DR PharmGKB; PA162408447; -.
DR eggNOG; NOG322646; -.
DR HOGENOM; HOG000143398; -.
DR HOVERGEN; HBG057394; -.
DR InParanoid; O94888; -.
DR OMA; PEKSDGI; -.
DR ChiTaRS; UBXN7; human.
DR EvolutionaryTrace; O94888; -.
DR GenomeRNAi; 26043; -.
DR NextBio; 47875; -.
DR PMAP-CutDB; O94888; -.
DR PRO; PR:O94888; -.
DR ArrayExpress; O94888; -.
DR Bgee; O94888; -.
DR CleanEx; HS_UBXN7; -.
DR Genevestigator; O94888; -.
DR GO; GO:0034098; C:Cdc48p-Npl4p-Ufd1p AAA ATPase complex; IDA:BHF-UCL.
DR GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR001012; UBX.
DR InterPro; IPR017346; UCP037991_UAS/UBX.
DR Pfam; PF00789; UBX; 1.
DR PIRSF; PIRSF037991; UCP037991_UBX7/2; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 489 UBX domain-containing protein 7.
FT /FTId=PRO_0000211035.
FT DOMAIN 408 485 UBX.
FT COMPBIAS 337 342 Poly-Glu.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 278 278 Phosphoserine.
FT MOD_RES 285 285 Phosphoserine.
FT MOD_RES 288 288 Phosphoserine.
FT CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT HELIX 11 23
FT HELIX 28 36
FT TURN 37 39
FT HELIX 42 51
FT TURN 146 148
FT HELIX 154 164
FT STRAND 167 173
FT TURN 177 179
FT HELIX 180 186
FT TURN 187 189
FT HELIX 191 199
FT STRAND 201 210
FT HELIX 211 220
FT STRAND 224 231
FT TURN 233 235
FT STRAND 240 244
FT HELIX 247 260
FT STRAND 412 418
FT STRAND 424 430
FT HELIX 435 446
FT TURN 449 451
FT STRAND 452 455
FT STRAND 457 459
FT STRAND 468 470
FT TURN 472 476
FT STRAND 479 481
FT STRAND 484 487
SQ SEQUENCE 489 AA; 54862 MW; 3C894533B1A2C41A CRC64;
MAAHGGSAAS SALKGLIQQF TTITGASESV GKHMLEACNN NLEMAVTMFL DGGGIAEEPS
TSSASVSTVR PHTEEEVRAP IPQKQEILVE PEPLFGAPKR RRPARSIFDG FRDFQTETIR
QEQELRNGGA IDKKLTTLAD LFRPPIDLMH KGSFETAKEC GQMQNKWLMI NIQNVQDFAC
QCLNRDVWSN EAVKNIIREH FIFWQVYHDS EEGQRYIQFY KLGDFPYVSI LDPRTGQKLV
EWHQLDVSSF LDQVTGFLGE HGQLDGLSSS PPKKCARSES LIDASEDSQL EAAIRASLQE
THFDSTQTKQ DSRSDEESES ELFSGSEEFI SVCGSDEEEE VENLAKSRKS PHKDLGHRKE
ENRRPLTEPP VRTDPGTATN HQGLPAVDSE ILEMPPEKAD GVVEGIDVNG PKAQLMLRYP
DGKREQITLP EQAKLLALVK HVQSKGYPNE RFELLTNFPR RKLSHLDYDI TLQEAGLCPQ
ETVFVQERN
//