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Q13107 (UBP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 4

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 4
Ubiquitin thioesterase 4
Ubiquitin-specific-processing protease 4
Ubiquitous nuclear protein homolog
Gene names
Name:USP4
Synonyms:UNP, UNPH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length963 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolase that deubiquitinates target proteins such as the receptor ADORA2A, PDPK1 and TRIM21. Deubiquitination of ADORA2A increases the amount of functional receptor at the cell surface. Plays a role in the regulation of quality control in the ER. Ref.1 Ref.8 Ref.9 Ref.10

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).

Subunit structure

Interacts with RB1 (both dephosphorylated and hypophosphorylated forms). Interacts with ADORA2A (via cytoplasmic C-terminus); the interaction is direct. Interacts with RB1, RBL1 and RBL2. Ref.7 Ref.10

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The relative amounts found in the nucleus and cytoplasm vary according to the cell type By similarity. Ref.8

Tissue specificity

Overexpressed in small cell tumors and adenocarcinomas of the lung compared to wild-type lung (at protein level). Expressed in the hippocampal neurons. Ref.1 Ref.10

Domain

The Ubiquitin-like domain 2 inserts into the catalytic domain and competes with the ubiquitin substrate, partially inhibiting DUB activity. Ref.13

Post-translational modification

Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated.

Sequence similarities

Belongs to the peptidase C19 family. USP4 subfamily.

Contains 1 DUSP domain.

Contains 2 ubiquitin-like domains.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseProto-oncogene
   DomainRepeat
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of protein ubiquitination

Inferred from mutant phenotype Ref.9. Source: UniProtKB

protein deubiquitination

Inferred from direct assay Ref.8Ref.10Ref.9. Source: UniProtKB

protein localization to cell surface

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of protein stability

Inferred from direct assay Ref.9. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay Ref.8Ref.10. Source: UniProtKB

lysosome

Traceable author statement PubMed 9827704. Source: ProtInc

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionadenosine receptor binding

Inferred from physical interaction Ref.10. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 22001210. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin thiolesterase activity

Inferred from mutant phenotype Ref.8Ref.9. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.8Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13107-1)

Also known as: UnpEL;

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: Q13107-2)

Also known as: UnpES;

The sequence of this isoform differs from the canonical sequence as follows:
     232-279: KSSTAPSRNFTTSPKSSASPYSSVSASLIANGDSTSTCGMHSSGVSRG → N
Isoform 3 (identifier: Q13107-3)

The sequence of this isoform differs from the canonical sequence as follows:
     233-313: SSTAPSRNFT...LGNLGNTCFM → VSFFLPRLEC...LLPQPPEWLG
     314-963: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 963963Ubiquitin carboxyl-terminal hydrolase 4
PRO_0000080621

Regions

Domain11 – 122112DUSP
Domain142 – 22685Ubiquitin-like 1
Domain302 – 923622USP
Domain483 – 57189Ubiquitin-like 2
Region405 – 4073Necessary for interaction with RBL2 By similarity
Region459 – 4635Necessary for interaction with RB1 and RBL2 By similarity
Motif133 – 1419Nuclear export signal By similarity
Motif767 – 7726Nuclear localization signal By similarity

Sites

Active site3111Nucleophile
Active site8811Proton acceptor By similarity
Metal binding4611Zinc
Metal binding4641Zinc
Metal binding7991Zinc
Metal binding8021Zinc

Natural variations

Alternative sequence232 – 27948KSSTA…GVSRG → N in isoform 2.
VSP_005258
Alternative sequence233 – 31381SSTAP…NTCFM → VSFFLPRLECNGAILAHCNF CLPGSSNSPASASRVAPSHL ANFFFFEMESHSVTKLECGG AVSAYSRVQVMLLPQPPEWL G in isoform 3.
VSP_044814
Alternative sequence314 – 963650Missing in isoform 3.
VSP_044815
Natural variant6201Y → C.
Corresponds to variant rs9311440 [ dbSNP | Ensembl ].
VAR_028180

Experimental info

Mutagenesis3111C → A: Loss of activity. Its ubiquitination by TRIM21 is enhanced. Ref.8 Ref.9
Mutagenesis459 – 4635LVCPE → AVRPH: Reduces the interaction with RB1. Ref.7
Mutagenesis4631E → Q: Reduces the interaction with RB1. Ref.7
Sequence conflict3731R → S in AAB72237. Ref.1
Sequence conflict7441S → R in AAB72237. Ref.1

Secondary structure

................................................................. 963
Helix Strand Turn

Details...

Sequences

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

Last modified October 17, 2006. Version 3.
Checksum: 63055C9ADFE36713

FASTA963108,565
        10         20         30         40         50         60 
MAEGGGCRER PDAETQKSEL GPLMRTTLQR GAQWYLIDSR WFKQWKKYVG FDSWDMYNVG 

        70         80         90        100        110        120 
EHNLFPGPID NSGLFSDPES QTLKEHLIDE LDYVLVPTEA WNKLLNWYGC VEGQQPIVRK 

       130        140        150        160        170        180 
VVEHGLFVKH CKVEVYLLEL KLCENSDPTN VLSCHFSKAD TIATIEKEMR KLFNIPAERE 

       190        200        210        220        230        240 
TRLWNKYMSN TYEQLSKLDN TVQDAGLYQG QVLVIEPQNE DGTWPRQTLQ SKSSTAPSRN 

       250        260        270        280        290        300 
FTTSPKSSAS PYSSVSASLI ANGDSTSTCG MHSSGVSRGG SGFSASYNCQ EPPSSHIQPG 

       310        320        330        340        350        360 
LCGLGNLGNT CFMNSALQCL SNTAPLTDYF LKDEYEAEIN RDNPLGMKGE IAEAYAELIK 

       370        380        390        400        410        420 
QMWSGRDAHV APRMFKTQVG RFAPQFSGYQ QQDSQELLAF LLDGLHEDLN RVKKKPYLEL 

       430        440        450        460        470        480 
KDANGRPDAV VAKEAWENHR LRNDSVIVDT FHGLFKSTLV CPECAKVSVT FDPFCYLTLP 

       490        500        510        520        530        540 
LPLKKDRVME VFLVPADPHC RPTQYRVTVP LMGAVSDLCE ALSRLSGIAA ENMVVADVYN 

       550        560        570        580        590        600 
HRFHKIFQMD EGLNHIMPRD DIFVYEVCST SVDGSECVTL PVYFRERKSR PSSTSSASAL 

       610        620        630        640        650        660 
YGQPLLLSVP KHKLTLESLY QAVCDRISRY VKQPLPDEFG SSPLEPGACN GSRNSCEGED 

       670        680        690        700        710        720 
EEEMEHQEEG KEQLSETEGS GEDEPGNDPS ETTQKKIKGQ PCPKRLFTFS LVNSYGTADI 

       730        740        750        760        770        780 
NSLAADGKLL KLNSRSTLAM DWDSETRRLY YDEQESEAYE KHVSMLQPQK KKKTTVALRD 

       790        800        810        820        830        840 
CIELFTTMET LGEHDPWYCP NCKKHQQATK KFDLWSLPKI LVVHLKRFSY NRYWRDKLDT 

       850        860        870        880        890        900 
VVEFPIRGLN MSEFVCNLSA RPYVYDLIAV SNHYGAMGVG HYTAYAKNKL NGKWYYFDDS 

       910        920        930        940        950        960 
NVSLASEDQI VTKAAYVLFY QRRDDEFYKT PSLSSSGSSD GGTRPSSSQQ GFGDDEACSM 


DTN 

« Hide

Isoform 2 (UnpES) [UniParc].

Checksum: 86CBBDE6AA2AB04E
Show »

FASTA916103,958
Isoform 3 [UniParc].

Checksum: 7B2258A3A64AC0EB
Show »

FASTA31335,661

References

« Hide 'large scale' references
[1]"Elevated expression of Unph, a proto-oncogene at 3p21.3, in human lung tumors."
Gray D.A., Inazawa J., Gupta K., Wong A., Ueda R., Takahashi T.
Oncogene 10:2179-2183(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Tissue: Brain cortex.
[2]Gray D.A.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The human UNP locus at 3p21.31 encodes two tissue-selective, cytoplasmic isoforms with deubiquitinating activity that have reduced expression in small cell lung carcinoma cell lines."
Frederick A., Rolfe M., Chiu M.I.
Oncogene 16:153-165(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
Tissue: B-cell and T-cell.
[4]"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] (ISOFORM 1).
Tissue: Placenta.
[5]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 3).
Tissue: Leukocyte.
[7]"The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein."
DeSalle L.M., Latres E., Lin D., Graner E., Montagnoli A., Baker R.T., Pagano M., Loda M.
Oncogene 20:5538-5542(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RB1, MUTAGENESIS OF GLU-463 AND 459-LEU--GLU-463.
[8]"Oncogenic protein UnpEL/Usp4 deubiquitinates Ro52 by its isopeptidase activity."
Wada K., Tanji K., Kamitani T.
Biochem. Biophys. Res. Commun. 339:731-736(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-311.
[9]"UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself."
Wada K., Kamitani T.
Biochem. Biophys. Res. Commun. 342:253-258(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTODEUBIQUITINATION, UBIQUITINATION BY TRIM21, MUTAGENESIS OF CYS-311.
[10]"The ubiquitin-specific protease Usp4 regulates the cell surface level of the A2A receptor."
Milojevic T., Reiterer V., Stefan E., Korkhov V.M., Dorostkar M.M., Ducza E., Ogris E., Boehm S., Freissmuth M., Nanoff C.
Mol. Pharmacol. 69:1083-1094(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ADORA2A, TISSUE SPECIFICITY.
[11]"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].
[12]"Ubiquitin-specific protease 4 inhibits mono-ubiquitination of the master growth factor signaling kinase PDK1."
Uras I.Z., List T., Nijman S.M.
PLoS ONE 7:E31003-E31003(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DEUBIQUITINATION OF PDPK1.
[13]"Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain."
Luna-Vargas M.P., Faesen A.C., van Dijk W.J., Rape M., Fish A., Sixma T.K.
EMBO Rep. 12:365-372(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 296-932, DOMAINS UBIQUITIN-LIKE, ZINC-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20657 mRNA. Translation: AAB72237.1.
AF017305 mRNA. Translation: AAC27355.1.
AF017306 mRNA. Translation: AAC27356.1.
AK291795 mRNA. Translation: BAF84484.1.
AC121247 Genomic DNA. No translation available.
BC068017 mRNA. No translation available.
BC125130 mRNA. Translation: AAI25131.1.
PIRT09478.
RefSeqNP_001238806.1. NM_001251877.1.
NP_003354.2. NM_003363.3.
NP_955475.1. NM_199443.2.
UniGeneHs.403828.
Hs.77500.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y6EX-ray2.40A/B/C/D/E/F296-932[»]
ProteinModelPortalQ13107.
SMRQ13107. Positions 8-226, 297-483, 740-930.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113221. 73 interactions.
IntActQ13107. 32 interactions.
MINTMINT-3027027.
STRING9606.ENSP00000265560.

Protein family/group databases

MEROPSC19.010.

PTM databases

PhosphoSiteQ13107.

Polymorphism databases

DMDM116242839.

Proteomic databases

PaxDbQ13107.
PRIDEQ13107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265560; ENSP00000265560; ENSG00000114316. [Q13107-1]
ENST00000351842; ENSP00000341028; ENSG00000114316. [Q13107-2]
ENST00000416417; ENSP00000400623; ENSG00000114316. [Q13107-3]
GeneID7375.
KEGGhsa:7375.
UCSCuc003cwp.2. human. [Q13107-1]
uc003cwr.2. human. [Q13107-2]

Organism-specific databases

CTD7375.
GeneCardsGC03M049315.
HGNCHGNC:12627. USP4.
HPAHPA018499.
MIM603486. gene.
neXtProtNX_Q13107.
PharmGKBPA37252.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5560.
HOGENOMHOG000264375.
HOVERGENHBG000864.
InParanoidQ13107.
KOK11835.
OMACERISRY.
PhylomeDBQ13107.
TreeFamTF106276.

Gene expression databases

ArrayExpressQ13107.
BgeeQ13107.
CleanExHS_USP4.
GenevestigatorQ13107.

Family and domain databases

Gene3D3.30.2230.10. 1 hit.
InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028135. Ub_USP-typ.
IPR028889. UCH/PAN2.
IPR028134. USP.
[Graphical view]
PANTHERPTHR24006:SF34. PTHR24006:SF34. 1 hit.
PfamPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMSSF143791. SSF143791. 1 hit.
PROSITEPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP4. human.
EvolutionaryTraceQ13107.
GeneWikiUSP4.
GenomeRNAi7375.
NextBio28880.
PROQ13107.
SOURCESearch...

Entry information

Entry nameUBP4_HUMAN
AccessionPrimary (citable) accession number: Q13107
Secondary accession number(s): A8K6Y0 expand/collapse secondary AC list , C9IY91, O43452, O43453, Q08AK8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 135 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 3

Human chromosome 3: entries, gene names and cross-references to MIM