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Q9UPU5 (UBP24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 24

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 24
Ubiquitin thioesterase 24
Ubiquitin-specific-processing protease 24
Gene names
Name:USP24
Synonyms:KIAA1057
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2620 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the ubiquitin-dependent proteolytic pathway in conjunction with the 26S proteasome By similarity.

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 UBA domain.

Contains 1 USP domain.

Sequence caution

The sequence AAH29660.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA91084.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 26202620Ubiquitin carboxyl-terminal hydrolase 24
PRO_0000080652

Regions

Domain3 – 4442UBA
Domain1689 – 2042354USP
Compositional bias47 – 9448Gly-rich
Compositional bias1035 – 106228Ser-rich
Compositional bias1132 – 116433Ser-rich

Sites

Active site16981Nucleophile By similarity
Active site19701Proton acceptor By similarity

Amino acid modifications

Modified residue631Phosphoserine Ref.6 Ref.9
Modified residue9421Phosphotyrosine By similarity
Modified residue11411Phosphoserine Ref.9
Modified residue20471Phosphoserine Ref.5 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.15
Modified residue20771Phosphoserine By similarity
Modified residue25611Phosphoserine Ref.12
Modified residue25651Phosphothreonine Ref.9 Ref.13 Ref.15
Modified residue26041Phosphoserine Ref.9

Natural variations

Natural variant2261T → I.
Corresponds to variant rs1165222 [ dbSNP | Ensembl ].
VAR_047154
Natural variant19401G → S.
Corresponds to variant rs2274540 [ dbSNP | Ensembl ].
VAR_047155
Natural variant21341Y → S.
Corresponds to variant rs12753590 [ dbSNP | Ensembl ].
VAR_047156
Natural variant24681V → A. Ref.2 Ref.3
Corresponds to variant rs487230 [ dbSNP | Ensembl ].
VAR_047157

Experimental info

Sequence conflict8401N → S in BAC86814. Ref.2
Sequence conflict9901I → L in BAC86814. Ref.2
Sequence conflict12531P → S in BAC86814. Ref.2
Sequence conflict17761E → G in BAC86814. Ref.2
Sequence conflict25761K → R in BAA91084. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9UPU5 [UniParc].

Last modified November 4, 2008. Version 3.
Checksum: 2773B7857A8B6633

FASTA2,620294,365
        10         20         30         40         50         60 
MESEEEQHMT TLLCMGFSDP ATIRKALRLA KNDINEAVAL LTNERPGLDY GGYEPMDSGG 

        70         80         90        100        110        120 
GPSPGPGGGP RGDGGGDGGG GGPSRGGSTG GGGGFDPPPA YHEVVDAEKN DENGNCSGEG 

       130        140        150        160        170        180 
IEFPTTNLYE LESRVLTDHW SIPYKREESL GKCLLASTYL ARLGLSESDE NCRRFMDRCM 

       190        200        210        220        230        240 
PEAFKKLLTS SAVHKWGTEI HEGIYNMLML LIELVAERIK QDPIPTGLLG VLTMAFNPDN 

       250        260        270        280        290        300 
EYHFKNRMKV SQRNWAEVFG EGNMFAVSPV STFQKEPHGW VVDLVNKFGE LGGFAAIQAK 

       310        320        330        340        350        360 
LHSEDIELGA VSALIQPLGV CAEYLNSSVV QPMLDPVILT TIQDVRSVEE KDLKDKRLVS 

       370        380        390        400        410        420 
IPELLSAVKL LCMRFQPDLV TIVDDLRLDI LLRMLKSPHF SAKMNSLKEV TKLIEDSTLS 

       430        440        450        460        470        480 
KSVKNAIDTD RLLDWLVENS VLSIALEGNI DQAQYCDRIK GIIELLGSKL SLDELTKIWK 

       490        500        510        520        530        540 
IQSGQSSTVI ENIHTIIAAA AVKFNSDQLN HLFVLIQKSW ETESDRVRQK LLSLIGRIGR 

       550        560        570        580        590        600 
EARFETTSGK VLDVLWELAH LPTLPSSLIQ QALEEHLTIL SDAYAVKEAI KRSYIIKCIE 

       610        620        630        640        650        660 
DIKRPGEWSG LEKNKKDGFK SSQLNNPQFV WVVPALRQLH EITRSFIKQT YQKQDKSIIQ 

       670        680        690        700        710        720 
DLKKNFEIVK LVTGSLIACH RLAAAVAGPG GLSGSTLVDG RYTYREYLEA HLKFLAFFLQ 

       730        740        750        760        770        780 
EATLYLGWNR AKEIWECLVT GQDVCELDRE MCFEWFTKGQ HDLESDVQQQ LFKEKILKLE 

       790        800        810        820        830        840 
SYEITMNGFN LFKTFFENVN LCDHRLKRQG AQLYVEKLEL IGMDFIWKIA MESPDEEIAN 

       850        860        870        880        890        900 
EAIQLIINYS YINLNPRLKK DSVSLHKKFI ADCYTRLEAA SSALGGPTLT HAVTRATKML 

       910        920        930        940        950        960 
TATAMPTVAT SVQSPYRSTK LVIIERLLLL AERYVITIED FYSVPRTILP HGASFHGHLL 

       970        980        990       1000       1010       1020 
TLNVTYESTK DTFTVEAHSN ETIGSVRWKI AKQLCSPVDN IQIFTNDSLL TVNKDQKLLH 

      1030       1040       1050       1060       1070       1080 
QLGFSDEQIL TVKTSGSGTP SGSSADSSTS SSSSSSGVFS SSYAMEQEKS LPGVVMALVC 

      1090       1100       1110       1120       1130       1140 
NVFDMLYQLA NLEEPRITLR VRKLLLLIPT DPAIQEALDQ LDSLGRKKTL LSESSSQSSK 

      1150       1160       1170       1180       1190       1200 
SPSLSSKQQH QPSASSILES LFRSFAPGMS TFRVLYNLEV LSSKLMPTAD DDMARSCAKS 

      1210       1220       1230       1240       1250       1260 
FCENFLKAGG LSLVVNVMQR DSIPSEVDYE TRQGVYSICL QLARFLLVGQ TMPTLLDEDL 

      1270       1280       1290       1300       1310       1320 
TKDGIEALSS RPFRNVSRQT SRQMSLCGTP EKSSYRQLSV SDRSSIRVEE IIPAARVAIQ 

      1330       1340       1350       1360       1370       1380 
TMEVSDFTST VACFMRLSWA AAAGRLDLVG SSQPIKESNS LCPAGIRNRL SSSGSNCSSG 

      1390       1400       1410       1420       1430       1440 
SEGEPVALHA GICVRQQSVS TKDSLIAGEA LSLLVTCLQL RSQQLASFYN LPCVADFIID 

      1450       1460       1470       1480       1490       1500 
ILLGSPSAEI RRVACDQLYT LSQTDTSAHP DVQKPNQFLL GVILTAQLPL WSPTSIMRGV 

      1510       1520       1530       1540       1550       1560 
NQRLLSQCME YFDLRCQLLD DLTTSEMEQL RISPATMLED EITWLDNFEP NRTAECETSE 

      1570       1580       1590       1600       1610       1620 
ADNILLAGHL RLIKTLLSLC GAEKEMLGSS LIKPLLDDFL FRASRIILNS HSPAGSAAIS 

      1630       1640       1650       1660       1670       1680 
QQDFHPKCST ANSRLAAYEV LVMLADSSPS NLQIIIKELL SMHHQPDPAL TKEFDYLPPV 

      1690       1700       1710       1720       1730       1740 
DSRSSSGFVG LRNGGATCYM NAVFQQLYMQ PGLPESLLSV DDDTDNPDDS VFYQVQSLFG 

      1750       1760       1770       1780       1790       1800 
HLMESKLQYY VPENFWKIFK MWNKELYVRE QQDAYEFFTS LIDQMDEYLK KMGRDQIFKN 

      1810       1820       1830       1840       1850       1860 
TFQGIYSDQK ICKDCPHRYE REEAFMALNL GVTSCQSLEI SLDQFVRGEV LEGSNAYYCE 

      1870       1880       1890       1900       1910       1920 
KCKEKRITVK RTCIKSLPSV LVIHLMRFGF DWESGRSIKY DEQIRFPWML NMEPYTVSGM 

      1930       1940       1950       1960       1970       1980 
ARQDSSSEVG ENGRSVDQGG GGSPRKKVAL TENYELVGVI VHSGQAHAGH YYSFIKDRRG 

      1990       2000       2010       2020       2030       2040 
CGKGKWYKFN DTVIEEFDLN DETLEYECFG GEYRPKVYDQ TNPYTDVRRR YWNAYMLFYQ 

      2050       2060       2070       2080       2090       2100 
RVSDQNSPVL PKKSRVSVVR QEAEDLSLSA PSSPEISPQS SPRPHRPNND RLSILTKLVK 

      2110       2120       2130       2140       2150       2160 
KGEKKGLFVE KMPARIYQMV RDENLKFMKN RDVYSSDYFS FVLSLASLNA TKLKHPYYPC 

      2170       2180       2190       2200       2210       2220 
MAKVSLQLAI QFLFQTYLRT KKKLRVDTEE WIATIEALLS KSFDACQWLV EYFISSEGRE 

      2230       2240       2250       2260       2270       2280 
LIKIFLLECN VREVRVAVAT ILEKTLDSAL FYQDKLKSLH QLLEVLLALL DKDVPENCKN 

      2290       2300       2310       2320       2330       2340 
CAQYFFLFNT FVQKQGIRAG DLLLRHSALR HMISFLLGAS RQNNQIRRWS SAQAREFGNL 

      2350       2360       2370       2380       2390       2400 
HNTVALLVLH SDVSSQRNVA PGIFKQRPPI SIAPSSPLLP LHEEVEALLF MSEGKPYLLE 

      2410       2420       2430       2440       2450       2460 
VMFALRELTG SLLALIEMVV YCCFCNEHFS FTMLHFIKNQ LETAPPHELK NTFQLLHEIL 

      2470       2480       2490       2500       2510       2520 
VIEDPIQVER VKFVFETENG LLALMHHSNH VDSSRCYQCV KFLVTLAQKC PAAKEYFKEN 

      2530       2540       2550       2560       2570       2580 
SHHWSWAVQW LQKKMSEHYW TPQSNVSNET STGKTFQRTI SAQDTLAYAT ALLNEKEQSG 

      2590       2600       2610       2620 
SSNGSESSPA NENGDRHLQQ GSESPMMIGE LRSDLDDVDP 

« Hide

References

[1]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 751-2082 AND 2256-2620, VARIANT ALA-2468.
[3]"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."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2233-2620, VARIANT ALA-2468.
Tissue: Brain.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1483-2620.
Tissue: Placenta.
[5]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[6]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-1141; SER-2047; THR-2565 AND SER-2604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2561, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047 AND THR-2565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047 AND THR-2565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC091609 Genomic DNA. No translation available.
AK000321 mRNA. Translation: BAA91084.1. Different initiation.
AK127075 mRNA. Translation: BAC86814.1.
AB028980 mRNA. Translation: BAA83009.1.
BC029660 mRNA. Translation: AAH29660.1. Different initiation.
RefSeqNP_056121.2. NM_015306.2.
UniGeneHs.477009.

3D structure databases

ProteinModelPortalQ9UPU5.
SMRQ9UPU5. Positions 2-44, 958-1034, 1677-2043.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116939. 9 interactions.
IntActQ9UPU5. 5 interactions.
MINTMINT-7945132.
STRING9606.ENSP00000385700.

Protein family/group databases

MEROPSC19.047.

PTM databases

PhosphoSiteQ9UPU5.

Polymorphism databases

DMDM212276491.

Proteomic databases

PaxDbQ9UPU5.
PRIDEQ9UPU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294383; ENSP00000294383; ENSG00000162402.
GeneID23358.
KEGGhsa:23358.
UCSCuc021onw.1. human.

Organism-specific databases

CTD23358.
GeneCardsGC01M055536.
H-InvDBHIX0000626.
HGNCHGNC:12623. USP24.
HPAHPA026723.
HPA028428.
MIM610569. gene.
neXtProtNX_Q9UPU5.
PharmGKBPA37248.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5077.
HOGENOMHOG000068011.
HOVERGENHBG105784.
InParanoidQ9UPU5.
KOK11840.
OMACMEYFDL.
OrthoDBEOG712TV9.
PhylomeDBQ9UPU5.
TreeFamTF323966.

Gene expression databases

ArrayExpressQ9UPU5.
BgeeQ9UPU5.
CleanExHS_USP24.
GenevestigatorQ9UPU5.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF48371. SSF48371. 2 hits.
PROSITEPS50030. UBA. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP24. human.
GeneWikiUSP24.
GenomeRNAi23358.
NextBio45380.
PROQ9UPU5.
SOURCESearch...

Entry information

Entry nameUBP24_HUMAN
AccessionPrimary (citable) accession number: Q9UPU5
Secondary accession number(s): Q6ZSY2, Q8N2Y4, Q9NXD1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 4, 2008
Last modified: April 16, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM