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

Q9NZ08 (ERAP1_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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoplasmic reticulum aminopeptidase 1

EC=3.4.11.-
Alternative name(s):
ARTS-1
Adipocyte-derived leucine aminopeptidase
Short name=A-LAP
Aminopeptidase PILS
Puromycin-insensitive leucyl-specific aminopeptidase
Short name=PILS-AP
Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator
Gene names
Name:ERAP1
Synonyms:APPILS, ARTS1, KIAA0525
ORF Names:UNQ584/PRO1154
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length941 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney. Ref.10 Ref.11 Ref.16

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Xbb-, in which Xaa is preferably Leu, but may be other amino acids including Met, Cys and Phe. Ref.16

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Monomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX. Ref.10 Ref.12 Ref.16

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein Probable Ref.10.

Tissue specificity

Ubiquitous.

Induction

By IFNG/IFN-gamma. Ref.10

Post-translational modification

N-glycosylated. Ref.15 Ref.16

Sequence similarities

Belongs to the peptidase M1 family.

Caution

It is uncertain whether Met-1 or Met-13 is the initiator.

Sequence caution

The sequence BAA25451.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Traceable author statement PubMed 15691326. Source: HGNC

antigen processing and presentation of endogenous peptide antigen via MHC class I

Non-traceable author statement PubMed 12748171. Source: UniProtKB

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

fat cell differentiation

Non-traceable author statement Ref.9. Source: UniProtKB

membrane protein ectodomain proteolysis

Inferred from direct assay PubMed 12748171. Source: UniProtKB

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Non-traceable author statement Ref.9. Source: UniProtKB

regulation of innate immune response

Non-traceable author statement PubMed 12748171. Source: UniProtKB

response to bacterium

Inferred from expression pattern PubMed 16034137. Source: BHF-UCL

   Cellular_componentcytosol

Non-traceable author statement Ref.1. Source: UniProtKB

endoplasmic reticulum

Non-traceable author statement PubMed 12748171. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement PubMed 15691326. Source: HGNC

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from direct assay Ref.9. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of membrane

Non-traceable author statement PubMed 12748171. Source: UniProtKB

   Molecular_functionaminopeptidase activity

Inferred from direct assay Ref.1PubMed 12748171. Source: UniProtKB

interleukin-1, Type II receptor binding

Traceable author statement PubMed 15691326. Source: HGNC

interleukin-6 receptor binding

Inferred from physical interaction PubMed 12748171. Source: UniProtKB

metalloexopeptidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

zinc ion binding

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NZ08-1)

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: Q9NZ08-2)

The sequence of this isoform differs from the canonical sequence as follows:
     940-941: RM → HDPEADATG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 941941Endoplasmic reticulum aminopeptidase 1
PRO_0000026751

Regions

Topological domain11Cytoplasmic Potential
Transmembrane2 – 2120Helical; Signal-anchor for type II membrane protein; Potential
Topological domain22 – 941920Lumenal Potential
Region317 – 3215Substrate binding By similarity

Sites

Active site3541Proton acceptor By similarity
Metal binding3531Zinc; catalytic
Metal binding3571Zinc; catalytic
Metal binding3761Zinc; catalytic
Binding site1831Substrate By similarity
Site4381Transition state stabilizer By similarity

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) Ref.15 Ref.16
Glycosylation1541N-linked (GlcNAc...) Ref.15 Ref.16
Glycosylation4141N-linked (GlcNAc...) Ref.13 Ref.15
Glycosylation7601N-linked (GlcNAc...) Ref.16
Glycosylation9011N-linked (GlcNAc...) Potential
Disulfide bond404 ↔ 443 Ref.15 Ref.16
Disulfide bond736 ↔ 743 Ref.15 Ref.16

Natural variations

Alternative sequence940 – 9412RM → HDPEADATG in isoform 2.
VSP_005450
Natural variant561E → K.
Corresponds to variant rs3734016 [ dbSNP | Ensembl ].
VAR_046681
Natural variant1271R → P. Ref.1 Ref.2 Ref.5 Ref.7
Corresponds to variant rs26653 [ dbSNP | Ensembl ].
VAR_012779
Natural variant2761I → M.
Corresponds to variant rs26618 [ dbSNP | Ensembl ].
VAR_012780
Natural variant3461G → D. Ref.3
Corresponds to variant rs27895 [ dbSNP | Ensembl ].
VAR_012781
Natural variant3491M → V. Ref.2 Ref.5 Ref.7
Corresponds to variant rs2287987 [ dbSNP | Ensembl ].
VAR_012782
Natural variant5281K → R. Ref.2 Ref.3 Ref.5 Ref.7
Corresponds to variant rs30187 [ dbSNP | Ensembl ].
VAR_012783
Natural variant5751D → G.
Corresponds to variant rs6863093 [ dbSNP | Ensembl ].
VAR_046682
Natural variant5751D → N. Ref.2 Ref.5 Ref.7
Corresponds to variant rs10050860 [ dbSNP | Ensembl ].
VAR_021555
Natural variant7251R → Q. Ref.2 Ref.5 Ref.7
Corresponds to variant rs17482078 [ dbSNP | Ensembl ].
VAR_021556
Natural variant7301Q → E. Ref.2 Ref.3 Ref.5 Ref.7
Corresponds to variant rs27044 [ dbSNP | Ensembl ].
VAR_012784

Experimental info

Mutagenesis4381Y → F: Loss of enzyme activity. Ref.16
Sequence conflict121T → I in AAF07395. Ref.1
Sequence conflict121T → I in AAK37777. Ref.2
Sequence conflict121T → I in AAK37778. Ref.2
Sequence conflict5141G → R in AAF20384. Ref.3

Secondary structure

......................................................................................................................................... 941
Helix Strand Turn

Details...

Sequences

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

Last modified July 24, 2007. Version 3.
Checksum: 22A0795C90155F04

FASTA941107,235
        10         20         30         40         50         60 
MVFLPLKWSL ATMSFLLSSL LALLTVSTPS WCQSTEASPK RSDGTPFPWN KIRLPEYVIP 

        70         80         90        100        110        120 
VHYDLLIHAN LTTLTFWGTT KVEITASQPT STIILHSHHL QISRATLRKG AGERLSEEPL 

       130        140        150        160        170        180 
QVLEHPRQEQ IALLAPEPLL VGLPYTVVIH YAGNLSETFH GFYKSTYRTK EGELRILAST 

       190        200        210        220        230        240 
QFEPTAARMA FPCFDEPAFK ASFSIKIRRE PRHLAISNMP LVKSVTVAEG LIEDHFDVTV 

       250        260        270        280        290        300 
KMSTYLVAFI ISDFESVSKI TKSGVKVSVY AVPDKINQAD YALDAAVTLL EFYEDYFSIP 

       310        320        330        340        350        360 
YPLPKQDLAA IPDFQSGAME NWGLTTYRES ALLFDAEKSS ASSKLGITMT VAHELAHQWF 

       370        380        390        400        410        420 
GNLVTMEWWN DLWLNEGFAK FMEFVSVSVT HPELKVGDYF FGKCFDAMEV DALNSSHPVS 

       430        440        450        460        470        480 
TPVENPAQIR EMFDDVSYDK GACILNMLRE YLSADAFKSG IVQYLQKHSY KNTKNEDLWD 

       490        500        510        520        530        540 
SMASICPTDG VKGMDGFCSR SQHSSSSSHW HQEGVDVKTM MNTWTLQKGF PLITITVRGR 

       550        560        570        580        590        600 
NVHMKQEHYM KGSDGAPDTG YLWHVPLTFI TSKSDMVHRF LLKTKTDVLI LPEEVEWIKF 

       610        620        630        640        650        660 
NVGMNGYYIV HYEDDGWDSL TGLLKGTHTA VSSNDRASLI NNAFQLVSIG KLSIEKALDL 

       670        680        690        700        710        720 
SLYLKHETEI MPVFQGLNEL IPMYKLMEKR DMNEVETQFK AFLIRLLRDL IDKQTWTDEG 

       730        740        750        760        770        780 
SVSERMLRSQ LLLLACVHNY QPCVQRAEGY FRKWKESNGN LSLPVDVTLA VFAVGAQSTE 

       790        800        810        820        830        840 
GWDFLYSKYQ FSLSSTEKSQ IEFALCRTQN KEKLQWLLDE SFKGDKIKTQ EFPQILTLIG 

       850        860        870        880        890        900 
RNPVGYPLAW QFLRKNWNKL VQKFELGSSS IAHMVMGTTN QFSTRTRLEE VKGFFSSLKE 

       910        920        930        940 
NGSQLRCVQQ TIETIEENIG WMDKNFDKIR VWLQSEKLER M 

« Hide

Isoform 2 [UniParc].

Checksum: B7DEE159B1D591EE
Show »

FASTA948107,841

References

« Hide 'large scale' references
[1]"Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine aminopeptidase/oxytocinase."
Hattori A., Matsumoto H., Mizutani S., Tsujimoto M.
J. Biochem. 125:931-938(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-127.
Tissue: White adipose tissue.
[2]"Genomic organization of the human adipocyte-derived leucine aminopeptidase gene and its relationship to the placental leucine aminopeptidase/oxytocinase gene."
Hattori A., Matsumoto K., Mizutani S., Tsujimoto M.
J. Biochem. 130:235-241(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730.
Tissue: Leukocyte.
[3]"Molecular characterization of human aminopeptidase PILS."
Schomburg L.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-346; ARG-528 AND GLU-730.
[4]"Identification of an aminopeptidase regulator of type I tumor necrosis factor receptor shedding."
Cui X., Alsaaty S., Lawrence M., Combs C.A., Rouhani F.N., Levine S.J.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730.
Tissue: Brain.
[6]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[7]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730.
[8]"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 1).
Tissue: Testis.
[9]"Characterization of recombinant human adipocyte-derived leucine aminopeptidase expressed in Chinese hamster ovary cells."
Hattori A., Kitatani K., Matsumoto H., Miyazawa S., Rogi T., Tsuruoka N., Mizutani S., Natori Y., Tsujimoto M.
J. Biochem. 128:755-762(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 37-49, CHARACTERIZATION.
[10]"Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum."
Saveanu L., Carroll O., Lindo V., Del Val M., Lopez D., Lepelletier Y., Greer F., Schomburg L., Fruci D., Niedermann G., van Endert P.M.
Nat. Immunol. 6:689-697(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INDUCTION BY IFNG.
[11]"The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a 'molecular ruler' mechanism."
Chang S.-C., Momburg F., Bhutani N., Goldberg A.L.
Proc. Natl. Acad. Sci. U.S.A. 102:17107-17112(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"An association between RBMX, a heterogeneous nuclear ribonucleoprotein, and ARTS-1 regulates extracellular TNFR1 release."
Adamik B., Islam A., Rouhani F.N., Hawari F.I., Zhang J., Levine S.J.
Biochem. Biophys. Res. Commun. 371:505-509(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBMX.
[13]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-414.
Tissue: Liver.
[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]"Crystal structure of the soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1."
Structural genomics consortium (SGC)
Submitted (MAY-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 46-940 IN COMPLEX WITH ZINC IONS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-70; ASN-154 AND ASN-414.
[16]"Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1."
Nguyen T.T., Chang S.C., Evnouchidou I., York I.A., Zikos C., Rock K.L., Goldberg A.L., Stratikos E., Stern L.J.
Nat. Struct. Mol. Biol. 18:604-613(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 37-939 IN COMPLEX WITH ZINC IONS AND BESTATIN, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-70; ASN-154 AND ASN-760, ACTIVE SITE, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF TYR-438.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF106037 mRNA. Translation: AAF07395.1.
AY028806 mRNA. Translation: AAK37777.1.
AY028807 mRNA. Translation: AAK37778.1.
AF183569 mRNA. Translation: AAF20384.1.
AF222340 mRNA. Translation: AAF34664.1.
AB011097 mRNA. Translation: BAA25451.2. Different initiation.
AY358590 mRNA. Translation: AAQ88953.1.
BC030775 mRNA. Translation: AAH30775.1.
RefSeqNP_001035548.1. NM_001040458.1.
NP_001185470.1. NM_001198541.1.
NP_057526.3. NM_016442.3.
UniGeneHs.666524.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YD0X-ray2.70A46-940[»]
3MDJX-ray2.95A/B/C37-939[»]
3QNFX-ray3.00A/B/C1-941[»]
3RJOX-ray2.30A529-941[»]
ProteinModelPortalQ9NZ08.
SMRQ9NZ08. Positions 46-941.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119713. 3 interactions.
IntActQ9NZ08. 3 interactions.
STRING9606.ENSP00000296754.

Chemistry

ChEMBLCHEMBL5939.

Protein family/group databases

MEROPSM01.018.

PTM databases

PhosphoSiteQ9NZ08.

Polymorphism databases

DMDM158937334.

Proteomic databases

PaxDbQ9NZ08.
PRIDEQ9NZ08.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296754; ENSP00000296754; ENSG00000164307. [Q9NZ08-2]
ENST00000443439; ENSP00000406304; ENSG00000164307. [Q9NZ08-1]
GeneID51752.
KEGGhsa:51752.
UCSCuc003kml.3. human. [Q9NZ08-2]
uc003kmm.3. human. [Q9NZ08-1]

Organism-specific databases

CTD51752.
GeneCardsGC05M096124.
H-InvDBHIX0164377.
HGNCHGNC:18173. ERAP1.
HPACAB025095.
HPA042317.
MIM606832. gene.
neXtProtNX_Q9NZ08.
PharmGKBPA162385163.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0308.
HOVERGENHBG108296.
InParanoidQ9NZ08.
KOK09604.
OMALIHANLT.
OrthoDBEOG754HNR.
PhylomeDBQ9NZ08.
TreeFamTF300395.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9NZ08.
BgeeQ9NZ08.
CleanExHS_ERAP1.
GenevestigatorQ9NZ08.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NZ08.
GeneWikiARTS-1.
GenomeRNAi51752.
NextBio55845.
PROQ9NZ08.
SOURCESearch...

Entry information

Entry nameERAP1_HUMAN
AccessionPrimary (citable) accession number: Q9NZ08
Secondary accession number(s): O60278 expand/collapse secondary AC list , Q6UWY6, Q8NEL4, Q8TAD0, Q9UHF8, Q9UKY2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: July 24, 2007
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 5

Human chromosome 5: entries, gene names and cross-references to MIM