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P40818 (UBP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 8

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 8
Ubiquitin isopeptidase Y
Short name=hUBPy
Ubiquitin thioesterase 8
Ubiquitin-specific-processing protease 8
Gene names
Name:USP8
Synonyms:KIAA0055, UBPY
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1118 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Ref.4 Ref.5 Ref.7 Ref.8

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

Forms a ternary complex with RNF128 and OTUB1. Interacts (via C-terminal UCH catalytic domain) with OTUB1 isoform 1 Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3, EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ By similarity. Interacts with NBR1, RASGRF1, RNF41 and IST1. Associates with the ESCRT-0 complex and with microtubules By similarity. Interacts with BIRC6/bruce and KIF23/MKLP1. Ref.7 Ref.8 Ref.11 Ref.12

Subcellular location

Cytoplasm. Nucleus By similarity. Endosome membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein Ref.5 Ref.7 Ref.11.

Induction

Upon growth stimulation in starved human fibroblasts. Decreases in response to growth arrest induced by cell-cell contact. Ref.4

Domain

The MIT domain is required for endosomal localization, CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR degradation. Ref.7

The rhodanese domain is sufficent for RNF41-binding By similarity. Ref.7

Post-translational modification

Phosphorylation of Ser-718 is essential for interaction with YWHAE and for cytosol localization By similarity. Undergoes dephosphorylation at Ser-718 in the M phase By similarity. Tyrosine-phosphorylated in its N-terminal half in an EGFR-dependent manner By similarity.

Ubiquitinated. Inactive form is mostly monoubiquitinated, but polyubiquitination happens too. Ubiquitination is increased in EGF-stimulated cells. Ubiquitination of active form is undetectable, suggesting a possibility that USP8 deubiquitinates itself, thereby regulating its own function By similarity.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 MIT domain.

Contains 1 rhodanese domain.

Contains 1 USP domain.

Sequence caution

The sequence AAH38801.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH51345.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processCell cycle
Ubl conjugation pathway
   Cellular componentCell membrane
Cytoplasm
Endosome
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainSH3-binding
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRas protein signal transduction

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement Ref.4. Source: ProtInc

endosome organization

Inferred from mutant phenotype Ref.5. Source: UniProtKB

mitotic cytokinesis

Inferred from mutant phenotype PubMed 18388320. Source: MGI

protein K48-linked deubiquitination

Inferred from direct assay Ref.5. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from direct assay Ref.5. Source: UniProtKB

protein deubiquitination

Inferred from mutant phenotype PubMed 18388320. Source: MGI

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 18388320. Source: MGI

cytosol

Inferred from direct assay Ref.5. Source: UniProtKB

early endosome

Inferred from direct assay Ref.5. Source: UniProtKB

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of plasma membrane

Inferred from direct assay Ref.5. Source: UniProtKB

midbody

Inferred from direct assay PubMed 18388320. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type endopeptidase activity

Traceable author statement PubMed 9827704. Source: ProtInc

ubiquitin-specific protease activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11181118Ubiquitin carboxyl-terminal hydrolase 8
PRO_0000080627

Regions

Domain33 – 11684MIT
Domain195 – 313119Rhodanese
Domain777 – 1109333USP
Motif405 – 4139SH3-binding By similarity

Sites

Active site7861Nucleophile By similarity
Active site10671Proton acceptor By similarity

Amino acid modifications

Modified residue1601Phosphoserine Ref.14
Modified residue4521Phosphoserine Ref.9
Modified residue5771Phosphothreonine Ref.16
Modified residue7181Phosphoserine Ref.9 Ref.14 Ref.16
Modified residue7191Phosphoserine Ref.9
Modified residue9451Phosphothreonine By similarity

Natural variations

Natural variant4431D → G.
Corresponds to variant rs3743044 [ dbSNP | Ensembl ].
VAR_017796
Natural variant7391T → A.
Corresponds to variant rs11638390 [ dbSNP | Ensembl ].
VAR_051525
Natural variant8271A → G.
Corresponds to variant rs1056577 [ dbSNP | Ensembl ].
VAR_017797

Experimental info

Mutagenesis7861C → S: Impairs deubiquitination activity and leads to endosome membrane accumulation. Ref.5
Sequence conflict5261E → G in CAD97662. Ref.2
Sequence conflict7171Y → H in CAD97662. Ref.2
Sequence conflict9451T → A in CAD97662. Ref.2

Secondary structure

................................................................................................................. 1118
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40818 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 8B884B7A842F9A9A

FASTA1,118127,523
        10         20         30         40         50         60 
MPAVASVPKE LYLSSSLKDL NKKTEVKPEK ISTKSYVHSA LKIFKTAEEC RLDRDEERAY 

        70         80         90        100        110        120 
VLYMKYVTVY NLIKKRPDFK QQQDYFHSIL GPGNIKKAVE EAERLSESLK LRYEEAEVRK 

       130        140        150        160        170        180 
KLEEKDRQEE AQRLQQKRQE TGREDGGTLA KGSLENVLDS KDKTQKSNGE KNEKCETKEK 

       190        200        210        220        230        240 
GAITAKELYT MMTDKNISLI IMDARRMQDY QDSCILHSLS VPEEAISPGV TASWIEAHLP 

       250        260        270        280        290        300 
DDSKDTWKKR GNVEYVVLLD WFSSAKDLQI GTTLRSLKDA LFKWESKTVL RNEPLVLEGG 

       310        320        330        340        350        360 
YENWLLCYPQ YTTNAKVTPP PRRQNEEVSI SLDFTYPSLE ESIPSKPAAQ TPPASIEVDE 

       370        380        390        400        410        420 
NIELISGQNE RMGPLNISTP VEPVAASKSD VSPIIQPVPS IKNVPQIDRT KKPAVKLPEE 

       430        440        450        460        470        480 
HRIKSESTNH EQQSPQSGKV IPDRSTKPVV FSPTLMLTDE EKARIHAETA LLMEKNKQEK 

       490        500        510        520        530        540 
ELRERQQEEQ KEKLRKEEQE QKAKKKQEAE ENEITEKQQK AKEEMEKKES EQAKKEDKET 

       550        560        570        580        590        600 
SAKRGKEITG VKRQSKSEHE TSDAKKSVED RGKRCPTPEI QKKSTGDVPH TSVTGDSGSG 

       610        620        630        640        650        660 
KPFKIKGQPE SGILRTGTFR EDTDDTERNK AQREPLTRAR SEEMGRIVPG LPSGWAKFLD 

       670        680        690        700        710        720 
PITGTFRYYH SPTNTVHMYP PEMAPSSAPP STPPTHKAKP QIPAERDREP SKLKRSYSSP 

       730        740        750        760        770        780 
DITQAIQEEE KRKPTVTPTV NRENKPTCYP KAEISRLSAS QIRNLNPVFG GSGPALTGLR 

       790        800        810        820        830        840 
NLGNTCYMNS ILQCLCNAPH LADYFNRNCY QDDINRSNLL GHKGEVAEEF GIIMKALWTG 

       850        860        870        880        890        900 
QYRYISPKDF KITIGKINDQ FAGYSQQDSQ ELLLFLMDGL HEDLNKADNR KRYKEENNDH 

       910        920        930        940        950        960 
LDDFKAAEHA WQKHKQLNES IIVALFQGQF KSTVQCLTCH KKSRTFEAFM YLSLPLASTS 

       970        980        990       1000       1010       1020 
KCTLQDCLRL FSKEEKLTDN NRFYCSHCRA RRDSLKKIEI WKLPPVLLVH LKRFSYDGRW 

      1030       1040       1050       1060       1070       1080 
KQKLQTSVDF PLENLDLSQY VIGPKNNLKK YNLFSVSNHY GGLDGGHYTA YCKNAARQRW 

      1090       1100       1110 
FKFDDHEVSD ISVSSVKSSA AYILFYTSLG PRVTDVAT 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[2]"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].
Tissue: Testis.
[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].
Tissue: Lung and Lymph.
[4]"UBPY: a growth-regulated human ubiquitin isopeptidase."
Naviglio S., Mattecucci C., Matoskova B., Nagase T., Nomura N., Di Fiore P.P., Draetta G.F.
EMBO J. 17:3241-3250(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[5]"The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation."
Row P.E., Prior I.A., McCullough J., Clague M.J., Urbe S.
J. Biol. Chem. 281:12618-12624(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-786.
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation."
Row P.E., Liu H., Hayes S., Welchman R., Charalabous P., Hofmann K., Clague M.J., Sanderson C.M., Urbe S.
J. Biol. Chem. 282:30929-30937(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, INTERACTION WITH CHMP1A; CHMP1B AND CHMP7, FUNCTION, SUBCELLULAR LOCATION.
[8]"Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
Pohl C., Jentsch S.
Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BIRC6/BRUCE AND KIF23/MKLP1.
[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-452; SER-718 AND SER-719, 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]"Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover."
Waters S., Marchbank K., Solomon E., Whitehouse C., Gautel M.
FEBS Lett. 583:1846-1852(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NBR1, SUBCELLULAR LOCATION.
[12]"Essential role of hIST1 in cytokinesis."
Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M., Ameer-Beg S., Bowers K., Martin-Serrano J.
Mol. Biol. Cell 20:1374-1387(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IST1.
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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-160 AND SER-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"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 THR-577 AND SER-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Solution structure of the rhodanese-like domain in human ubiquitin specific protease 8 (UBP8)."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 174-317.
[18]"Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)."
Avvakumov G.V., Walker J.R., Xue S., Finerty P.J. Jr., Mackenzie F., Newman E.M., Dhe-Paganon S.
J. Biol. Chem. 281:38061-38070(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-318 IN COMPLEX WITH RNF41.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D29956 mRNA. Translation: BAA06225.2.
BX537420 mRNA. Translation: CAD97662.1.
BC038801 mRNA. Translation: AAH38801.1. Sequence problems.
BC051345 mRNA. Translation: AAH51345.1. Sequence problems.
BC110590 mRNA. Translation: AAI10591.1.
RefSeqNP_001122082.1. NM_001128610.2.
NP_001269978.1. NM_001283049.1.
NP_005145.3. NM_005154.4.
UniGeneHs.443731.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WHBNMR-A176-317[»]
2A9UX-ray2.10A/B1-142[»]
2GFOX-ray2.00A734-1110[»]
2GWFX-ray2.30A/C/E181-318[»]
3N3KX-ray2.60A734-1110[»]
ProteinModelPortalP40818.
SMRP40818. Positions 6-139, 181-316, 756-1110.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114555. 54 interactions.
DIPDIP-40365N.
IntActP40818. 19 interactions.
MINTMINT-244406.
STRING9606.ENSP00000302239.

Chemistry

ChEMBLCHEMBL2157854.

Protein family/group databases

MEROPSC19.011.

PTM databases

PhosphoSiteP40818.

Polymorphism databases

DMDM731046.

Proteomic databases

PaxDbP40818.
PeptideAtlasP40818.
PRIDEP40818.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307179; ENSP00000302239; ENSG00000138592.
ENST00000396444; ENSP00000379721; ENSG00000138592.
ENST00000433963; ENSP00000405537; ENSG00000138592.
GeneID9101.
KEGGhsa:9101.
UCSCuc001zyl.4. human.

Organism-specific databases

CTD9101.
GeneCardsGC15P050716.
H-InvDBHIX0172812.
HGNCHGNC:12631. USP8.
HPAHPA004869.
MIM603158. gene.
neXtProtNX_P40818.
PharmGKBPA37256.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000231497.
HOVERGENHBG012631.
InParanoidP40818.
KOK11839.
OMAQIDRTKK.
OrthoDBEOG7FR7GN.
PhylomeDBP40818.
TreeFamTF106277.

Enzyme and pathway databases

BRENDA3.1.2.15. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkP40818.

Gene expression databases

ArrayExpressP40818.
BgeeP40818.
CleanExHS_USP8.
GenevestigatorP40818.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR001763. Rhodanese-like_dom.
IPR028889. UCH/PAN2.
IPR015063. USP8_dimer.
[Graphical view]
PfamPF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
PF08969. USP8_dimer. 1 hit.
[Graphical view]
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP8. human.
EvolutionaryTraceP40818.
GeneWikiUSP8.
GenomeRNAi9101.
NextBio34117.
PROP40818.
SOURCESearch...

Entry information

Entry nameUBP8_HUMAN
AccessionPrimary (citable) accession number: P40818
Secondary accession number(s): Q2TB31 expand/collapse secondary AC list , Q7Z3U2, Q86VA0, Q8IWI7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 152 of the entry and version 1 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 15

Human chromosome 15: entries, gene names and cross-references to MIM