Full text data of USP24
USP24
(KIAA1057)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin carboxyl-terminal hydrolase 24; 3.4.19.12 (Deubiquitinating enzyme 24; Ubiquitin thioesterase 24; Ubiquitin-specific-processing protease 24)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin carboxyl-terminal hydrolase 24; 3.4.19.12 (Deubiquitinating enzyme 24; Ubiquitin thioesterase 24; Ubiquitin-specific-processing protease 24)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UPU5
ID UBP24_HUMAN Reviewed; 2620 AA.
AC Q9UPU5; Q6ZSY2; Q8N2Y4; Q9NXD1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-NOV-2008, sequence version 3.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 24;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 24;
DE AltName: Full=Ubiquitin thioesterase 24;
DE AltName: Full=Ubiquitin-specific-processing protease 24;
GN Name=USP24; Synonyms=KIAA1057;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 751-2082 AND 2256-2620, AND
RP VARIANT ALA-2468.
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 MRNA] OF 2233-2620, AND VARIANT
RP ALA-2468.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1483-2620.
RC TISSUE=Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND MASS
RP SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-1141; SER-2047;
RP THR-2565 AND SER-2604, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2561, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047 AND THR-2565, AND
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047 AND THR-2565, AND
RP MASS 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in the ubiquitin-dependent proteolytic pathway
CC in conjunction with the 26S proteasome (By similarity).
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29660.1; Type=Erroneous initiation;
CC Sequence=BAA91084.1; Type=Erroneous initiation;
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DR EMBL; AC091609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK000321; BAA91084.1; ALT_INIT; mRNA.
DR EMBL; AK127075; BAC86814.1; -; mRNA.
DR EMBL; AB028980; BAA83009.1; -; mRNA.
DR EMBL; BC029660; AAH29660.1; ALT_INIT; mRNA.
DR RefSeq; NP_056121.2; NM_015306.2.
DR UniGene; Hs.477009; -.
DR ProteinModelPortal; Q9UPU5; -.
DR SMR; Q9UPU5; 1677-2043.
DR IntAct; Q9UPU5; 5.
DR MINT; MINT-7945132; -.
DR STRING; 9606.ENSP00000385700; -.
DR MEROPS; C19.047; -.
DR PhosphoSite; Q9UPU5; -.
DR DMDM; 212276491; -.
DR PaxDb; Q9UPU5; -.
DR PRIDE; Q9UPU5; -.
DR Ensembl; ENST00000294383; ENSP00000294383; ENSG00000162402.
DR GeneID; 23358; -.
DR KEGG; hsa:23358; -.
DR UCSC; uc021onw.1; human.
DR CTD; 23358; -.
DR GeneCards; GC01M055536; -.
DR H-InvDB; HIX0000626; -.
DR HGNC; HGNC:12623; USP24.
DR HPA; HPA026723; -.
DR HPA; HPA028428; -.
DR MIM; 610569; gene.
DR neXtProt; NX_Q9UPU5; -.
DR PharmGKB; PA37248; -.
DR eggNOG; COG5077; -.
DR HOGENOM; HOG000068011; -.
DR HOVERGEN; HBG105784; -.
DR InParanoid; Q9UPU5; -.
DR KO; K11840; -.
DR OMA; CMEYFDL; -.
DR OrthoDB; EOG712TV9; -.
DR ChiTaRS; USP24; human.
DR GeneWiki; USP24; -.
DR GenomeRNAi; 23358; -.
DR NextBio; 45380; -.
DR PRO; PR:Q9UPU5; -.
DR ArrayExpress; Q9UPU5; -.
DR Bgee; Q9UPU5; -.
DR CleanEx; HS_USP24; -.
DR Genevestigator; Q9UPU5; -.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR InterPro; IPR001394; Peptidase_C19/C67.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00972; UCH_2_1; 1.
DR PROSITE; PS00973; UCH_2_2; 1.
DR PROSITE; PS50235; UCH_2_3; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Hydrolase; Phosphoprotein; Polymorphism; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1 2620 Ubiquitin carboxyl-terminal hydrolase 24.
FT /FTId=PRO_0000080652.
FT DOMAIN 3 44 UBA.
FT COMPBIAS 47 94 Gly-rich.
FT COMPBIAS 1035 1062 Ser-rich.
FT COMPBIAS 1132 1164 Ser-rich.
FT ACT_SITE 1698 1698 Nucleophile (By similarity).
FT ACT_SITE 1970 1970 Proton acceptor (By similarity).
FT MOD_RES 63 63 Phosphoserine.
FT MOD_RES 942 942 Phosphotyrosine (By similarity).
FT MOD_RES 1141 1141 Phosphoserine.
FT MOD_RES 2047 2047 Phosphoserine.
FT MOD_RES 2077 2077 Phosphoserine (By similarity).
FT MOD_RES 2561 2561 Phosphoserine.
FT MOD_RES 2565 2565 Phosphothreonine.
FT MOD_RES 2604 2604 Phosphoserine.
FT VARIANT 226 226 T -> I (in dbSNP:rs1165222).
FT /FTId=VAR_047154.
FT VARIANT 1940 1940 G -> S (in dbSNP:rs2274540).
FT /FTId=VAR_047155.
FT VARIANT 2134 2134 Y -> S (in dbSNP:rs12753590).
FT /FTId=VAR_047156.
FT VARIANT 2468 2468 V -> A (in dbSNP:rs487230).
FT /FTId=VAR_047157.
FT CONFLICT 840 840 N -> S (in Ref. 2; BAC86814).
FT CONFLICT 990 990 I -> L (in Ref. 2; BAC86814).
FT CONFLICT 1253 1253 P -> S (in Ref. 2; BAC86814).
FT CONFLICT 1776 1776 E -> G (in Ref. 2; BAC86814).
FT CONFLICT 2576 2576 K -> R (in Ref. 2; BAA91084).
SQ SEQUENCE 2620 AA; 294365 MW; 2773B7857A8B6633 CRC64;
MESEEEQHMT TLLCMGFSDP ATIRKALRLA KNDINEAVAL LTNERPGLDY GGYEPMDSGG
GPSPGPGGGP RGDGGGDGGG GGPSRGGSTG GGGGFDPPPA YHEVVDAEKN DENGNCSGEG
IEFPTTNLYE LESRVLTDHW SIPYKREESL GKCLLASTYL ARLGLSESDE NCRRFMDRCM
PEAFKKLLTS SAVHKWGTEI HEGIYNMLML LIELVAERIK QDPIPTGLLG VLTMAFNPDN
EYHFKNRMKV SQRNWAEVFG EGNMFAVSPV STFQKEPHGW VVDLVNKFGE LGGFAAIQAK
LHSEDIELGA VSALIQPLGV CAEYLNSSVV QPMLDPVILT TIQDVRSVEE KDLKDKRLVS
IPELLSAVKL LCMRFQPDLV TIVDDLRLDI LLRMLKSPHF SAKMNSLKEV TKLIEDSTLS
KSVKNAIDTD RLLDWLVENS VLSIALEGNI DQAQYCDRIK GIIELLGSKL SLDELTKIWK
IQSGQSSTVI ENIHTIIAAA AVKFNSDQLN HLFVLIQKSW ETESDRVRQK LLSLIGRIGR
EARFETTSGK VLDVLWELAH LPTLPSSLIQ QALEEHLTIL SDAYAVKEAI KRSYIIKCIE
DIKRPGEWSG LEKNKKDGFK SSQLNNPQFV WVVPALRQLH EITRSFIKQT YQKQDKSIIQ
DLKKNFEIVK LVTGSLIACH RLAAAVAGPG GLSGSTLVDG RYTYREYLEA HLKFLAFFLQ
EATLYLGWNR AKEIWECLVT GQDVCELDRE MCFEWFTKGQ HDLESDVQQQ LFKEKILKLE
SYEITMNGFN LFKTFFENVN LCDHRLKRQG AQLYVEKLEL IGMDFIWKIA MESPDEEIAN
EAIQLIINYS YINLNPRLKK DSVSLHKKFI ADCYTRLEAA SSALGGPTLT HAVTRATKML
TATAMPTVAT SVQSPYRSTK LVIIERLLLL AERYVITIED FYSVPRTILP HGASFHGHLL
TLNVTYESTK DTFTVEAHSN ETIGSVRWKI AKQLCSPVDN IQIFTNDSLL TVNKDQKLLH
QLGFSDEQIL TVKTSGSGTP SGSSADSSTS SSSSSSGVFS SSYAMEQEKS LPGVVMALVC
NVFDMLYQLA NLEEPRITLR VRKLLLLIPT DPAIQEALDQ LDSLGRKKTL LSESSSQSSK
SPSLSSKQQH QPSASSILES LFRSFAPGMS TFRVLYNLEV LSSKLMPTAD DDMARSCAKS
FCENFLKAGG LSLVVNVMQR DSIPSEVDYE TRQGVYSICL QLARFLLVGQ TMPTLLDEDL
TKDGIEALSS RPFRNVSRQT SRQMSLCGTP EKSSYRQLSV SDRSSIRVEE IIPAARVAIQ
TMEVSDFTST VACFMRLSWA AAAGRLDLVG SSQPIKESNS LCPAGIRNRL SSSGSNCSSG
SEGEPVALHA GICVRQQSVS TKDSLIAGEA LSLLVTCLQL RSQQLASFYN LPCVADFIID
ILLGSPSAEI RRVACDQLYT LSQTDTSAHP DVQKPNQFLL GVILTAQLPL WSPTSIMRGV
NQRLLSQCME YFDLRCQLLD DLTTSEMEQL RISPATMLED EITWLDNFEP NRTAECETSE
ADNILLAGHL RLIKTLLSLC GAEKEMLGSS LIKPLLDDFL FRASRIILNS HSPAGSAAIS
QQDFHPKCST ANSRLAAYEV LVMLADSSPS NLQIIIKELL SMHHQPDPAL TKEFDYLPPV
DSRSSSGFVG LRNGGATCYM NAVFQQLYMQ PGLPESLLSV DDDTDNPDDS VFYQVQSLFG
HLMESKLQYY VPENFWKIFK MWNKELYVRE QQDAYEFFTS LIDQMDEYLK KMGRDQIFKN
TFQGIYSDQK ICKDCPHRYE REEAFMALNL GVTSCQSLEI SLDQFVRGEV LEGSNAYYCE
KCKEKRITVK RTCIKSLPSV LVIHLMRFGF DWESGRSIKY DEQIRFPWML NMEPYTVSGM
ARQDSSSEVG ENGRSVDQGG GGSPRKKVAL TENYELVGVI VHSGQAHAGH YYSFIKDRRG
CGKGKWYKFN DTVIEEFDLN DETLEYECFG GEYRPKVYDQ TNPYTDVRRR YWNAYMLFYQ
RVSDQNSPVL PKKSRVSVVR QEAEDLSLSA PSSPEISPQS SPRPHRPNND RLSILTKLVK
KGEKKGLFVE KMPARIYQMV RDENLKFMKN RDVYSSDYFS FVLSLASLNA TKLKHPYYPC
MAKVSLQLAI QFLFQTYLRT KKKLRVDTEE WIATIEALLS KSFDACQWLV EYFISSEGRE
LIKIFLLECN VREVRVAVAT ILEKTLDSAL FYQDKLKSLH QLLEVLLALL DKDVPENCKN
CAQYFFLFNT FVQKQGIRAG DLLLRHSALR HMISFLLGAS RQNNQIRRWS SAQAREFGNL
HNTVALLVLH SDVSSQRNVA PGIFKQRPPI SIAPSSPLLP LHEEVEALLF MSEGKPYLLE
VMFALRELTG SLLALIEMVV YCCFCNEHFS FTMLHFIKNQ LETAPPHELK NTFQLLHEIL
VIEDPIQVER VKFVFETENG LLALMHHSNH VDSSRCYQCV KFLVTLAQKC PAAKEYFKEN
SHHWSWAVQW LQKKMSEHYW TPQSNVSNET STGKTFQRTI SAQDTLAYAT ALLNEKEQSG
SSNGSESSPA NENGDRHLQQ GSESPMMIGE LRSDLDDVDP
//
ID UBP24_HUMAN Reviewed; 2620 AA.
AC Q9UPU5; Q6ZSY2; Q8N2Y4; Q9NXD1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-NOV-2008, sequence version 3.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 24;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 24;
DE AltName: Full=Ubiquitin thioesterase 24;
DE AltName: Full=Ubiquitin-specific-processing protease 24;
GN Name=USP24; Synonyms=KIAA1057;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 751-2082 AND 2256-2620, AND
RP VARIANT ALA-2468.
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 MRNA] OF 2233-2620, AND VARIANT
RP ALA-2468.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1483-2620.
RC TISSUE=Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND MASS
RP SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-1141; SER-2047;
RP THR-2565 AND SER-2604, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2561, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047 AND THR-2565, AND
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047 AND THR-2565, AND
RP MASS 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in the ubiquitin-dependent proteolytic pathway
CC in conjunction with the 26S proteasome (By similarity).
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29660.1; Type=Erroneous initiation;
CC Sequence=BAA91084.1; Type=Erroneous initiation;
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DR EMBL; AC091609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK000321; BAA91084.1; ALT_INIT; mRNA.
DR EMBL; AK127075; BAC86814.1; -; mRNA.
DR EMBL; AB028980; BAA83009.1; -; mRNA.
DR EMBL; BC029660; AAH29660.1; ALT_INIT; mRNA.
DR RefSeq; NP_056121.2; NM_015306.2.
DR UniGene; Hs.477009; -.
DR ProteinModelPortal; Q9UPU5; -.
DR SMR; Q9UPU5; 1677-2043.
DR IntAct; Q9UPU5; 5.
DR MINT; MINT-7945132; -.
DR STRING; 9606.ENSP00000385700; -.
DR MEROPS; C19.047; -.
DR PhosphoSite; Q9UPU5; -.
DR DMDM; 212276491; -.
DR PaxDb; Q9UPU5; -.
DR PRIDE; Q9UPU5; -.
DR Ensembl; ENST00000294383; ENSP00000294383; ENSG00000162402.
DR GeneID; 23358; -.
DR KEGG; hsa:23358; -.
DR UCSC; uc021onw.1; human.
DR CTD; 23358; -.
DR GeneCards; GC01M055536; -.
DR H-InvDB; HIX0000626; -.
DR HGNC; HGNC:12623; USP24.
DR HPA; HPA026723; -.
DR HPA; HPA028428; -.
DR MIM; 610569; gene.
DR neXtProt; NX_Q9UPU5; -.
DR PharmGKB; PA37248; -.
DR eggNOG; COG5077; -.
DR HOGENOM; HOG000068011; -.
DR HOVERGEN; HBG105784; -.
DR InParanoid; Q9UPU5; -.
DR KO; K11840; -.
DR OMA; CMEYFDL; -.
DR OrthoDB; EOG712TV9; -.
DR ChiTaRS; USP24; human.
DR GeneWiki; USP24; -.
DR GenomeRNAi; 23358; -.
DR NextBio; 45380; -.
DR PRO; PR:Q9UPU5; -.
DR ArrayExpress; Q9UPU5; -.
DR Bgee; Q9UPU5; -.
DR CleanEx; HS_USP24; -.
DR Genevestigator; Q9UPU5; -.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR InterPro; IPR001394; Peptidase_C19/C67.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00972; UCH_2_1; 1.
DR PROSITE; PS00973; UCH_2_2; 1.
DR PROSITE; PS50235; UCH_2_3; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Hydrolase; Phosphoprotein; Polymorphism; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1 2620 Ubiquitin carboxyl-terminal hydrolase 24.
FT /FTId=PRO_0000080652.
FT DOMAIN 3 44 UBA.
FT COMPBIAS 47 94 Gly-rich.
FT COMPBIAS 1035 1062 Ser-rich.
FT COMPBIAS 1132 1164 Ser-rich.
FT ACT_SITE 1698 1698 Nucleophile (By similarity).
FT ACT_SITE 1970 1970 Proton acceptor (By similarity).
FT MOD_RES 63 63 Phosphoserine.
FT MOD_RES 942 942 Phosphotyrosine (By similarity).
FT MOD_RES 1141 1141 Phosphoserine.
FT MOD_RES 2047 2047 Phosphoserine.
FT MOD_RES 2077 2077 Phosphoserine (By similarity).
FT MOD_RES 2561 2561 Phosphoserine.
FT MOD_RES 2565 2565 Phosphothreonine.
FT MOD_RES 2604 2604 Phosphoserine.
FT VARIANT 226 226 T -> I (in dbSNP:rs1165222).
FT /FTId=VAR_047154.
FT VARIANT 1940 1940 G -> S (in dbSNP:rs2274540).
FT /FTId=VAR_047155.
FT VARIANT 2134 2134 Y -> S (in dbSNP:rs12753590).
FT /FTId=VAR_047156.
FT VARIANT 2468 2468 V -> A (in dbSNP:rs487230).
FT /FTId=VAR_047157.
FT CONFLICT 840 840 N -> S (in Ref. 2; BAC86814).
FT CONFLICT 990 990 I -> L (in Ref. 2; BAC86814).
FT CONFLICT 1253 1253 P -> S (in Ref. 2; BAC86814).
FT CONFLICT 1776 1776 E -> G (in Ref. 2; BAC86814).
FT CONFLICT 2576 2576 K -> R (in Ref. 2; BAA91084).
SQ SEQUENCE 2620 AA; 294365 MW; 2773B7857A8B6633 CRC64;
MESEEEQHMT TLLCMGFSDP ATIRKALRLA KNDINEAVAL LTNERPGLDY GGYEPMDSGG
GPSPGPGGGP RGDGGGDGGG GGPSRGGSTG GGGGFDPPPA YHEVVDAEKN DENGNCSGEG
IEFPTTNLYE LESRVLTDHW SIPYKREESL GKCLLASTYL ARLGLSESDE NCRRFMDRCM
PEAFKKLLTS SAVHKWGTEI HEGIYNMLML LIELVAERIK QDPIPTGLLG VLTMAFNPDN
EYHFKNRMKV SQRNWAEVFG EGNMFAVSPV STFQKEPHGW VVDLVNKFGE LGGFAAIQAK
LHSEDIELGA VSALIQPLGV CAEYLNSSVV QPMLDPVILT TIQDVRSVEE KDLKDKRLVS
IPELLSAVKL LCMRFQPDLV TIVDDLRLDI LLRMLKSPHF SAKMNSLKEV TKLIEDSTLS
KSVKNAIDTD RLLDWLVENS VLSIALEGNI DQAQYCDRIK GIIELLGSKL SLDELTKIWK
IQSGQSSTVI ENIHTIIAAA AVKFNSDQLN HLFVLIQKSW ETESDRVRQK LLSLIGRIGR
EARFETTSGK VLDVLWELAH LPTLPSSLIQ QALEEHLTIL SDAYAVKEAI KRSYIIKCIE
DIKRPGEWSG LEKNKKDGFK SSQLNNPQFV WVVPALRQLH EITRSFIKQT YQKQDKSIIQ
DLKKNFEIVK LVTGSLIACH RLAAAVAGPG GLSGSTLVDG RYTYREYLEA HLKFLAFFLQ
EATLYLGWNR AKEIWECLVT GQDVCELDRE MCFEWFTKGQ HDLESDVQQQ LFKEKILKLE
SYEITMNGFN LFKTFFENVN LCDHRLKRQG AQLYVEKLEL IGMDFIWKIA MESPDEEIAN
EAIQLIINYS YINLNPRLKK DSVSLHKKFI ADCYTRLEAA SSALGGPTLT HAVTRATKML
TATAMPTVAT SVQSPYRSTK LVIIERLLLL AERYVITIED FYSVPRTILP HGASFHGHLL
TLNVTYESTK DTFTVEAHSN ETIGSVRWKI AKQLCSPVDN IQIFTNDSLL TVNKDQKLLH
QLGFSDEQIL TVKTSGSGTP SGSSADSSTS SSSSSSGVFS SSYAMEQEKS LPGVVMALVC
NVFDMLYQLA NLEEPRITLR VRKLLLLIPT DPAIQEALDQ LDSLGRKKTL LSESSSQSSK
SPSLSSKQQH QPSASSILES LFRSFAPGMS TFRVLYNLEV LSSKLMPTAD DDMARSCAKS
FCENFLKAGG LSLVVNVMQR DSIPSEVDYE TRQGVYSICL QLARFLLVGQ TMPTLLDEDL
TKDGIEALSS RPFRNVSRQT SRQMSLCGTP EKSSYRQLSV SDRSSIRVEE IIPAARVAIQ
TMEVSDFTST VACFMRLSWA AAAGRLDLVG SSQPIKESNS LCPAGIRNRL SSSGSNCSSG
SEGEPVALHA GICVRQQSVS TKDSLIAGEA LSLLVTCLQL RSQQLASFYN LPCVADFIID
ILLGSPSAEI RRVACDQLYT LSQTDTSAHP DVQKPNQFLL GVILTAQLPL WSPTSIMRGV
NQRLLSQCME YFDLRCQLLD DLTTSEMEQL RISPATMLED EITWLDNFEP NRTAECETSE
ADNILLAGHL RLIKTLLSLC GAEKEMLGSS LIKPLLDDFL FRASRIILNS HSPAGSAAIS
QQDFHPKCST ANSRLAAYEV LVMLADSSPS NLQIIIKELL SMHHQPDPAL TKEFDYLPPV
DSRSSSGFVG LRNGGATCYM NAVFQQLYMQ PGLPESLLSV DDDTDNPDDS VFYQVQSLFG
HLMESKLQYY VPENFWKIFK MWNKELYVRE QQDAYEFFTS LIDQMDEYLK KMGRDQIFKN
TFQGIYSDQK ICKDCPHRYE REEAFMALNL GVTSCQSLEI SLDQFVRGEV LEGSNAYYCE
KCKEKRITVK RTCIKSLPSV LVIHLMRFGF DWESGRSIKY DEQIRFPWML NMEPYTVSGM
ARQDSSSEVG ENGRSVDQGG GGSPRKKVAL TENYELVGVI VHSGQAHAGH YYSFIKDRRG
CGKGKWYKFN DTVIEEFDLN DETLEYECFG GEYRPKVYDQ TNPYTDVRRR YWNAYMLFYQ
RVSDQNSPVL PKKSRVSVVR QEAEDLSLSA PSSPEISPQS SPRPHRPNND RLSILTKLVK
KGEKKGLFVE KMPARIYQMV RDENLKFMKN RDVYSSDYFS FVLSLASLNA TKLKHPYYPC
MAKVSLQLAI QFLFQTYLRT KKKLRVDTEE WIATIEALLS KSFDACQWLV EYFISSEGRE
LIKIFLLECN VREVRVAVAT ILEKTLDSAL FYQDKLKSLH QLLEVLLALL DKDVPENCKN
CAQYFFLFNT FVQKQGIRAG DLLLRHSALR HMISFLLGAS RQNNQIRRWS SAQAREFGNL
HNTVALLVLH SDVSSQRNVA PGIFKQRPPI SIAPSSPLLP LHEEVEALLF MSEGKPYLLE
VMFALRELTG SLLALIEMVV YCCFCNEHFS FTMLHFIKNQ LETAPPHELK NTFQLLHEIL
VIEDPIQVER VKFVFETENG LLALMHHSNH VDSSRCYQCV KFLVTLAQKC PAAKEYFKEN
SHHWSWAVQW LQKKMSEHYW TPQSNVSNET STGKTFQRTI SAQDTLAYAT ALLNEKEQSG
SSNGSESSPA NENGDRHLQQ GSESPMMIGE LRSDLDDVDP
//
MIM
610569
*RECORD*
*FIELD* NO
610569
*FIELD* TI
*610569 UBIQUITIN-SPECIFIC PROTEASE 24; USP24
;;KIAA1057
*FIELD* TX
DESCRIPTION
Modification of cellular proteins by ubiquitin is an essential
read moreregulatory mechanism controlled by the coordinated action of multiple
ubiquitin-conjugating and deubiquitinating enzymes. USP24 belongs to a
large family of cysteine proteases that function as deubiquitinating
enzymes (Quesada et al., 2004).
CLONING
By sequencing clones obtained from a brain cDNA library, Kikuno et al.
(1999) cloned USP24, which they designated KIAA1057. The deduced
977-amino acid protein shares significant similarity with USP9X
(300072). RT-PCR ELISA detected highest expression in skeletal muscle
followed by ovary, with moderate expression in heart, brain, lung,
liver, and kidney, and low expression in pancreas, spleen, and testis.
Fetal tissues and specific brain regions examined showed either low or
moderate expression.
Quesada et al. (2004) showed that the catalytic domain of USP24 contains
the cys box, QQD box, and his box characteristic of USP enzymes.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the USP24
gene to chromosome 1 (TMAP SHGC-74876).
MOLECULAR GENETICS
For a discussion of a possible association between variation in the
USP24 gene and susceptibility to Parkinson disease, see PARK10 (606852).
*FIELD* RF
1. Kikuno, R.; Nagase, T.; Ishikawa, K.; Hirosawa, M.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XIV. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 6: 197-205, 1999.
2. Quesada, V.; Diaz-Perales, A.; Gutierrez-Fernandez, A.; Garabaya,
C.; Cal, S.; Lopez-Otin, C.: Cloning and enzymatic analysis of 22
novel human ubiquitin-specific proteases. Biochem. Biophys. Res.
Commun. 314: 54-62, 2004.
*FIELD* CN
Cassandra L. Kniffin - updated: 9/29/2008
*FIELD* CD
Patricia A. Hartz: 11/15/2006
*FIELD* ED
ckniffin: 09/24/2009
carol: 9/30/2008
ckniffin: 9/29/2008
mgross: 5/3/2007
wwang: 11/15/2006
*RECORD*
*FIELD* NO
610569
*FIELD* TI
*610569 UBIQUITIN-SPECIFIC PROTEASE 24; USP24
;;KIAA1057
*FIELD* TX
DESCRIPTION
Modification of cellular proteins by ubiquitin is an essential
read moreregulatory mechanism controlled by the coordinated action of multiple
ubiquitin-conjugating and deubiquitinating enzymes. USP24 belongs to a
large family of cysteine proteases that function as deubiquitinating
enzymes (Quesada et al., 2004).
CLONING
By sequencing clones obtained from a brain cDNA library, Kikuno et al.
(1999) cloned USP24, which they designated KIAA1057. The deduced
977-amino acid protein shares significant similarity with USP9X
(300072). RT-PCR ELISA detected highest expression in skeletal muscle
followed by ovary, with moderate expression in heart, brain, lung,
liver, and kidney, and low expression in pancreas, spleen, and testis.
Fetal tissues and specific brain regions examined showed either low or
moderate expression.
Quesada et al. (2004) showed that the catalytic domain of USP24 contains
the cys box, QQD box, and his box characteristic of USP enzymes.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the USP24
gene to chromosome 1 (TMAP SHGC-74876).
MOLECULAR GENETICS
For a discussion of a possible association between variation in the
USP24 gene and susceptibility to Parkinson disease, see PARK10 (606852).
*FIELD* RF
1. Kikuno, R.; Nagase, T.; Ishikawa, K.; Hirosawa, M.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XIV. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 6: 197-205, 1999.
2. Quesada, V.; Diaz-Perales, A.; Gutierrez-Fernandez, A.; Garabaya,
C.; Cal, S.; Lopez-Otin, C.: Cloning and enzymatic analysis of 22
novel human ubiquitin-specific proteases. Biochem. Biophys. Res.
Commun. 314: 54-62, 2004.
*FIELD* CN
Cassandra L. Kniffin - updated: 9/29/2008
*FIELD* CD
Patricia A. Hartz: 11/15/2006
*FIELD* ED
ckniffin: 09/24/2009
carol: 9/30/2008
ckniffin: 9/29/2008
mgross: 5/3/2007
wwang: 11/15/2006