Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96K76 (UBP47_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 47

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 47
Ubiquitin thioesterase 47
Ubiquitin-specific-processing protease 47
Gene names
Name:USP47
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER). Acts as a regulator of cell growth and genome integrity. May also indirectly regulates CDC25A expression at a transcriptional level. Ref.11 Ref.14

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). Ref.14

Subunit structure

Interacts with BTRC and FBXW11. Interacts with POLB. Ref.11 Ref.14

Subcellular location

Cytoplasm Ref.14.

Tissue specificity

Expressed in skeletal muscle, heart and testis. Ref.6

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Caution

Was initially thought to catalytically inactive (Ref.6). However, it was later shown that it is active (Ref.14).

Sequence caution

The sequence BAA91348.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbase-excision repair

Inferred from mutant phenotype Ref.14. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.14. Source: UniProtKB

cellular response to UV

Inferred from sequence or structural similarity Ref.11. Source: UniProtKB

monoubiquitinated protein deubiquitination

Inferred from direct assay Ref.14. Source: UniProtKB

negative regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of cell growth

Inferred from mutant phenotype Ref.11. Source: UniProtKB

response to drug

Inferred from mutant phenotype Ref.11. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentSCF ubiquitin ligase complex

Inferred from direct assay Ref.11. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionWD40-repeat domain binding

Inferred from physical interaction Ref.11. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96K76-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96K76-2)

The sequence of this isoform differs from the canonical sequence as follows:
     14-101: Missing.
Isoform 3 (identifier: Q96K76-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1218: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13751375Ubiquitin carboxyl-terminal hydrolase 47
PRO_0000080676

Regions

Domain188 – 564377USP

Sites

Active site1971Nucleophile By similarity
Active site5031Proton acceptor By similarity

Amino acid modifications

Modified residue1221N6-acetyllysine Ref.10
Modified residue8321Phosphoserine Ref.7 Ref.8 Ref.12
Modified residue9101Phosphoserine Ref.8 Ref.9 Ref.12
Modified residue10151Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 12181218Missing in isoform 3.
VSP_014414
Alternative sequence14 – 10188Missing in isoform 2.
VSP_014415
Natural variant1631G → V. Ref.1 Ref.8 Ref.9
Corresponds to variant rs11022079 [ dbSNP | Ensembl ].
VAR_022787

Experimental info

Sequence conflict3401F → L in BAG54467. Ref.1
Sequence conflict4941V → A in BAB55063. Ref.1
Sequence conflict4941V → A in BAG54467. Ref.1
Sequence conflict5201N → D in BAB55063. Ref.1
Sequence conflict5761D → G in BAB55063. Ref.1
Sequence conflict6041R → G in BAB84902. Ref.4
Sequence conflict9111P → S in BAG54467. Ref.1
Sequence conflict11571E → G in BAA91348. Ref.1
Sequence conflict13131A → G in BAA91348. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 1EDEAA9B5AFC97FE

FASTA1,375157,311
        10         20         30         40         50         60 
MVPGEENQLV PKEDVFWRCR QNIFDEMKKK FLQIENAAEE PRVLCIIQDT TNSKTVNERI 

        70         80         90        100        110        120 
TLNLPASTPV RKLFEDVANK VGYINGTFDL VWGNGINTAD MAPLDHTSDK SLLDANFEPG 

       130        140        150        160        170        180 
KKNFLHLTDK DGEQPQILLE DSSAGEDSVH DRFIGPLPRE GSGGSTSDYV SQSYSYSSIL 

       190        200        210        220        230        240 
NKSETGYVGL VNQAMTCYLN SLLQTLFMTP EFRNALYKWE FEESEEDPVT SIPYQLQRLF 

       250        260        270        280        290        300 
VLLQTSKKRA IETTDVTRSF GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINEL 

       310        320        330        340        350        360 
YQGKLKDYVR CLECGYEGWR IDTYLDIPLV IRPYGSSQAF ASVEEALHAF IQPEILDGPN 

       370        380        390        400        410        420 
QYFCERCKKK CDARKGLRFL HFPYLLTLQL KRFDFDYTTM HRIKLNDRMT FPEELDMSTF 

       430        440        450        460        470        480 
IDVEDEKSPQ TESCTDSGAE NEGSCHSDQM SNDFSNDDGV DEGICLETNS GTEKISKSGL 

       490        500        510        520        530        540 
EKNSLIYELF SVMVHSGSAA GGHYYACIKS FSDEQWYSFN DQHVSRITQE DIKKTHGGSS 

       550        560        570        580        590        600 
GSRGYYSSAF ASSTNAYMLI YRLKDPARNA KFLEVDEYPE HIKNLVQKER ELEEQEKRQR 

       610        620        630        640        650        660 
EIERNTCKIK LFCLHPTKQV MMENKLEVHK DKTLKEAVEM AYKMMDLEEV IPLDCCRLVK 

       670        680        690        700        710        720 
YDEFHDYLER SYEGEEDTPM GLLLGGVKST YMFDLLLETR KPDQVFQSYK PGEVMVKVHV 

       730        740        750        760        770        780 
VDLKAESVAA PITVRAYLNQ TVTEFKQLIS KAIHLPAETM RIVLERCYND LRLLSVSSKT 

       790        800        810        820        830        840 
LKAEGFFRSN KVFVESSETL DYQMAFADSH LWKLLDRHAN TIRLFVLLPE QSPVSYSKRT 

       850        860        870        880        890        900 
AYQKAGGDSG NVDDDCERVK GPVGSLKSVE AILEESTEKL KSLSLQQQQD GDNGDSSKST 

       910        920        930        940        950        960 
ETSDFENIES PLNERDSSAS VDNRELEQHI QTSDPENFQS EERSDSDVNN DRSTSSVDSD 

       970        980        990       1000       1010       1020 
ILSSSHSSDT LCNADNAQIP LANGLDSHSI TSSRRTKANE GKKETWDTAE EDSGTDSEYD 

      1030       1040       1050       1060       1070       1080 
ESGKSRGEMQ YMYFKAEPYA ADEGSGEGHK WLMVHVDKRI TLAAFKQHLE PFVGVLSSHF 

      1090       1100       1110       1120       1130       1140 
KVFRVYASNQ EFESVRLNET LSSFSDDNKI TIRLGRALKK GEYRVKVYQL LVNEQEPCKF 

      1150       1160       1170       1180       1190       1200 
LLDAVFAKGM TVRQSKEELI PQLREQCGLE LSIDRFRLRK KTWKNPGTVF LDYHIYEEDI 

      1210       1220       1230       1240       1250       1260 
NISSNWEVFL EVLDGVEKMK SMSQLAVLSR RWKPSEMKLD PFQEVVLESS SVDELREKLS 

      1270       1280       1290       1300       1310       1320 
EISGIPLDDI EFAKGRGTFP CDISVLDIHQ DLDWNPKVST LNVWPLYICD DGAVIFYRDK 

      1330       1340       1350       1360       1370 
TEELMELTDE QRNELMKKES SRLQKTGHRV TYSPRKEKAL KIYLDGAPNK DLTQD 

« Hide

Isoform 2 [UniParc].

Checksum: 2A332C63E843B074
Show »

FASTA1,287147,223
Isoform 3 [UniParc].

Checksum: 95A4D6BB8090CD30
Show »

FASTA15718,150

References

« Hide 'large scale' references
[1]"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] (ISOFORMS 1 AND 2), VARIANT VAL-163.
Tissue: Embryo, Hepatoma and Spleen.
[2]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 940-1375 (ISOFORMS 1/2).
Tissue: Eye and Testis.
[4]"The nucleotide sequence of a long cDNA clone isolated from human spleen."
Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-1375 (ISOFORMS 1/2).
Tissue: Spleen.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 630-1375 (ISOFORMS 1/2).
Tissue: Stomach.
[6]"Cloning and enzymatic analysis of 22 novel human ubiquitin-specific proteases."
Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S., Lopez-Otin C.
Biochem. Biophys. Res. Commun. 314:54-62(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-832 AND SER-910, VARIANT [LARGE SCALE ANALYSIS] VAL-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-910, VARIANT [LARGE SCALE ANALYSIS] VAL-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor regulating cell survival."
Peschiaroli A., Skaar J.R., Pagano M., Melino G.
Oncogene 29:1384-1393(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BTRC AND FBXW11.
[12]"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-832 AND SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"USP47 is a deubiquitylating enzyme that regulates base excision repair by controlling steady-state levels of DNA Polymerase beta."
Parsons J.L., Dianova I.I., Khoronenkova S.V., Edelmann M.J., Kessler B.M., Dianov G.L.
Mol. Cell 41:609-615(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH POLB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000734 mRNA. Translation: BAA91348.1. Different initiation.
AK027362 mRNA. Translation: BAB55063.1.
AK092290 mRNA. No translation available.
AK127264 mRNA. Translation: BAG54467.1.
AC104383 Genomic DNA. No translation available.
AC124276 Genomic DNA. No translation available.
BC000226 mRNA. Translation: AAH00226.2.
BC047044 mRNA. Translation: AAH47044.2.
AK074076 mRNA. Translation: BAB84902.1.
AL832991 mRNA. Translation: CAH56337.1.
RefSeqNP_001269588.1. NM_001282659.1.
NP_060414.3. NM_017944.3.
XP_005253054.1. XM_005252997.1.
UniGeneHs.577256.

3D structure databases

ProteinModelPortalQ96K76.
SMRQ96K76. Positions 182-596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120360. 14 interactions.
DIPDIP-53629N.
IntActQ96K76. 3 interactions.
STRING9606.ENSP00000339957.

Chemistry

ChEMBLCHEMBL2157851.

Protein family/group databases

MEROPSC19.055.

PTM databases

PhosphoSiteQ96K76.

Polymorphism databases

DMDM313104266.

Proteomic databases

PaxDbQ96K76.
PRIDEQ96K76.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339865; ENSP00000339957; ENSG00000170242. [Q96K76-2]
ENST00000399455; ENSP00000382382; ENSG00000170242. [Q96K76-1]
ENST00000539466; ENSP00000440405; ENSG00000170242. [Q96K76-3]
GeneID55031.
KEGGhsa:55031.
UCSCuc001mjq.1. human. [Q96K76-1]
uc001mjr.3. human. [Q96K76-2]
uc009ygi.3. human. [Q96K76-3]

Organism-specific databases

CTD55031.
GeneCardsGC11P011819.
HGNCHGNC:20076. USP47.
HPAHPA029286.
HPA029289.
MIM614460. gene.
neXtProtNX_Q96K76.
PharmGKBPA134880952.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5077.
HOVERGENHBG058854.
InParanoidQ96K76.
KOK11857.
OMALCEISGI.
OrthoDBEOG7M3HZD.
PhylomeDBQ96K76.
TreeFamTF314142.

Gene expression databases

ArrayExpressQ96K76.
BgeeQ96K76.
CleanExHS_USP47.
GenevestigatorQ96K76.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP47. human.
GeneWikiUSP47.
GenomeRNAi55031.
NextBio58447.
PROQ96K76.
SOURCESearch...

Entry information

Entry nameUBP47_HUMAN
AccessionPrimary (citable) accession number: Q96K76
Secondary accession number(s): B3KXF5 expand/collapse secondary AC list , Q658U0, Q86Y73, Q8TEP6, Q9BWI0, Q9NWN1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 108 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 11

Human chromosome 11: entries, gene names and cross-references to MIM