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P58397 (ATS12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 12

Short name=ADAM-TS 12
Short name=ADAM-TS12
Short name=ADAMTS-12
EC=3.4.24.-
Gene names
Name:ADAMTS12
ORF Names:UNQ1918/PRO4389
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1594 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties. Ref.5 Ref.6 Ref.7

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by alpha-2 macroglobulin. Ref.7

Subunit structure

Interacts with COMP. Ref.5

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Expressed in skeletal muscle and fat. Detected at significant levels in fetal lung. Widely expressed in gastric carcinomas and in cancer cells of diverse origin. Ref.1 Ref.5

Induction

By IFN-alpha and by IL1B/interleukin-1 beta. Up-regulated in articular cartilage and synovium from arthritis patients. Up-regulared in chondrocytes. Ref.5 Ref.7

Domain

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix By similarity.

The C-terminal four TSP1-like repeats are necessary and sufficient for binding COMP.

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Post-translational modification

The precursor is cleaved by a furin endopeptidase.

Subjected to an intracellular maturation process yielding a 120 kDa N-terminal fragment containing the metalloproteinase, disintegrin, one TSP type-1 and the Cys-rich domains and a 83 kDa C-terminal fragment containing the spacer 2 and four TSP type-1 domains.

Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion By similarity.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 1 PLAC domain.

Contains 8 TSP type-1 domains.

Biophysicochemical properties

pH dependence:

Optimum pH is between 7.5 and 9.5 with COMP for substrate.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell migration

Inferred from mutant phenotype PubMed 21494557. Source: BHF-UCL

cell-matrix adhesion

Inferred from mutant phenotype PubMed 21494557. Source: BHF-UCL

cellular response to BMP stimulus

Inferred from direct assay PubMed 22247065. Source: BHF-UCL

cellular response to interleukin-1

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

cellular response to tumor necrosis factor

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

negative regulation of cellular response to hepatocyte growth factor stimulus

Inferred from direct assay Ref.6. Source: BHF-UCL

negative regulation of cellular response to vascular endothelial growth factor stimulus

Inferred from direct assay Ref.6. Source: BHF-UCL

negative regulation of chondrocyte differentiation

Inferred from direct assay PubMed 22247065. Source: BHF-UCL

negative regulation of hepatocyte growth factor receptor signaling pathway

Inferred from direct assay Ref.6. Source: BHF-UCL

proteoglycan catabolic process

Inferred from direct assay Ref.6. Source: BHF-UCL

proteolysis involved in cellular protein catabolic process

Inferred from direct assay Ref.5. Source: BHF-UCL

regulation of endothelial tube morphogenesis

Inferred from direct assay Ref.6. Source: BHF-UCL

regulation of inflammatory response

Inferred from direct assay PubMed 23019333. Source: BHF-UCL

   Cellular_componentextracellular matrix

Inferred from direct assay Ref.1. Source: BHF-UCL

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetalloendopeptidase activity

Inferred from direct assay Ref.5Ref.6Ref.7. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

COMPP497473EBI-9028051,EBI-2531022
CompQ9R0G63EBI-9028051,EBI-9028018From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P58397-1)

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: P58397-2)

The sequence of this isoform differs from the canonical sequence as follows:
     212-229: DSVNISQKQELWREKWER → GIVTHMSSWVEESVLFFW
     230-1594: Missing.
Isoform 3 (identifier: P58397-3)

The sequence of this isoform differs from the canonical sequence as follows:
     630-714: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 240215 By similarity
PRO_0000029186
Chain241 – 15941354A disintegrin and metalloproteinase with thrombospondin motifs 12
PRO_0000029187

Regions

Domain246 – 456211Peptidase M12B
Domain465 – 54480Disintegrin
Domain542 – 59756TSP type-1 1
Domain823 – 88361TSP type-1 2
Domain887 – 94357TSP type-1 3
Domain944 – 99754TSP type-1 4
Domain1313 – 136654TSP type-1 5
Domain1368 – 142255TSP type-1 6
Domain1423 – 147149TSP type-1 7
Domain1472 – 153261TSP type-1 8
Domain1535 – 157541PLAC
Region701 – 827127Spacer 1
Region997 – 1316320Spacer 2
Motif208 – 2136Cysteine switch By similarity
Compositional bias302 – 3054Poly-Glu
Compositional bias597 – 700104Cys-rich

Sites

Active site3931 By similarity
Metal binding2081Zinc; in inhibited form By similarity
Metal binding3921Zinc; catalytic By similarity
Metal binding3961Zinc; catalytic By similarity
Metal binding4021Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1251N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation6851N-linked (GlcNAc...) Potential
Glycosylation7901N-linked (GlcNAc...) Potential
Glycosylation9521N-linked (GlcNAc...) Potential
Glycosylation11051N-linked (GlcNAc...) Potential
Glycosylation12761N-linked (GlcNAc...) Potential
Glycosylation13011N-linked (GlcNAc...) Potential
Glycosylation13211N-linked (GlcNAc...) Potential
Glycosylation13721N-linked (GlcNAc...) Potential
Glycosylation13791N-linked (GlcNAc...) Potential
Glycosylation15041N-linked (GlcNAc...) Potential
Disulfide bond322 ↔ 376 By similarity
Disulfide bond351 ↔ 358 By similarity
Disulfide bond370 ↔ 451 By similarity
Disulfide bond409 ↔ 435 By similarity
Disulfide bond478 ↔ 501 By similarity
Disulfide bond489 ↔ 507 By similarity
Disulfide bond496 ↔ 526 By similarity
Disulfide bond520 ↔ 531 By similarity
Disulfide bond554 ↔ 591 By similarity
Disulfide bond558 ↔ 596 By similarity
Disulfide bond569 ↔ 581 By similarity

Natural variations

Alternative sequence212 – 22918DSVNI…EKWER → GIVTHMSSWVEESVLFFW in isoform 2.
VSP_013141
Alternative sequence230 – 15941365Missing in isoform 2.
VSP_013142
Alternative sequence630 – 71485Missing in isoform 3.
VSP_038151
Natural variant1101Q → E.
Corresponds to variant rs16891862 [ dbSNP | Ensembl ].
VAR_057074
Natural variant10001R → Q.
Corresponds to variant rs13362345 [ dbSNP | Ensembl ].
VAR_057075
Natural variant11771W → R.
Corresponds to variant rs3813474 [ dbSNP | Ensembl ].
VAR_059761
Natural variant14951T → I. Ref.1
Corresponds to variant rs25754 [ dbSNP | Ensembl ].
VAR_058972
Natural variant15911S → P.
Corresponds to variant rs16891281 [ dbSNP | Ensembl ].
VAR_059762

Experimental info

Sequence conflict8241Missing in CAC20419. Ref.1
Sequence conflict13361R → K in CAC20419. Ref.1
Sequence conflict13411S → T in CAC20419. Ref.1
Sequence conflict15781H → R in AAI31734. Ref.4

Sequences

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

Last modified September 22, 2009. Version 2.
Checksum: C88563125F0F90D8

FASTA1,594177,676
        10         20         30         40         50         60 
MPCAQRSWLA NLSVVAQLLN FGALCYGRQP QPGPVRFPDR RQEHFIKGLP EYHVVGPVRV 

        70         80         90        100        110        120 
DASGHFLSYG LHYPITSSRR KRDLDGSEDW VYYRISHEEK DLFFNLTVNQ GFLSNSYIME 

       130        140        150        160        170        180 
KRYGNLSHVK MMASSAPLCH LSGTVLQQGT RVGTAALSAC HGLTGFFQLP HGDFFIEPVK 

       190        200        210        220        230        240 
KHPLVEGGYH PHIVYRRQKV PETKEPTCGL KDSVNISQKQ ELWREKWERH NLPSRSLSRR 

       250        260        270        280        290        300 
SISKERWVET LVVADTKMIE YHGSENVESY ILTIMNMVTG LFHNPSIGNA IHIVVVRLIL 

       310        320        330        340        350        360 
LEEEEQGLKI VHHAEKTLSS FCKWQKSINP KSDLNPVHHD VAVLLTRKDI CAGFNRPCET 

       370        380        390        400        410        420 
LGLSHLSGMC QPHRSCNINE DSGLPLAFTI AHELGHSFGI QHDGKENDCE PVGRHPYIMS 

       430        440        450        460        470        480 
RQLQYDPTPL TWSKCSEEYI TRFLDRGWGF CLDDIPKKKG LKSKVIAPGV IYDVHHQCQL 

       490        500        510        520        530        540 
QYGPNATFCQ EVENVCQTLW CSVKGFCRSK LDAAADGTQC GEKKWCMAGK CITVGKKPES 

       550        560        570        580        590        600 
IPGGWGRWSP WSHCSRTCGA GVQSAERLCN NPEPKFGGKY CTGERKRYRL CNVHPCRSEA 

       610        620        630        640        650        660 
PTFRQMQCSE FDTVPYKNEL YHWFPIFNPA HPCELYCRPI DGQFSEKMLD AVIDGTPCFE 

       670        680        690        700        710        720 
GGNSRNVCIN GICKMVGCDY EIDSNATEDR CGVCLGDGSS CQTVRKMFKQ KEGSGYVDIG 

       730        740        750        760        770        780 
LIPKGARDIR VMEIEGAGNF LAIRSEDPEK YYLNGGFIIQ WNGNYKLAGT VFQYDRKGDL 

       790        800        810        820        830        840 
EKLMATGPTN ESVWIQLLFQ VTNPGIKYEY TIQKDGLDND VEQQMYFWQY GHWTECSVTC 

       850        860        870        880        890        900 
GTGIRRQTAH CIKKGRGMVK ATFCDPETQP NGRQKKCHEK ACPPRWWAGE WEACSATCGP 

       910        920        930        940        950        960 
HGEKKRTVLC IQTMVSDEQA LPPTDCQHLL KPKTLLSCNR DILCPSDWTV GNWSECSVSC 

       970        980        990       1000       1010       1020 
GGGVRIRSVT CAKNHDEPCD VTRKPNSRAL CGLQQCPSSR RVLKPNKGTI SNGKNPPTLK 

      1030       1040       1050       1060       1070       1080 
PVPPPTSRPR MLTTPTGPES MSTSTPAISS PSPTTASKEG DLGGKQWQDS STQPELSSRY 

      1090       1100       1110       1120       1130       1140 
LISTGSTSQP ILTSQSLSIQ PSEENVSSSD TGPTSEGGLV ATTTSGSGLS SSRNPITWPV 

      1150       1160       1170       1180       1190       1200 
TPFYNTLTKG PEMEIHSGSG EEREQPEDKD ESNPVIWTKI RVPGNDAPVE STEMPLAPPL 

      1210       1220       1230       1240       1250       1260 
TPDLSRESWW PPFSTVMEGL LPSQRPTTSE TGTPRVEGMV TEKPANTLLP LGGDHQPEPS 

      1270       1280       1290       1300       1310       1320 
GKTANRNHLK LPNNMNQTKS SEPVLTEEDA TSLITEGFLL NASNYKQLTN GHGSAHWIVG 

      1330       1340       1350       1360       1370       1380 
NWSECSTTCG LGAYWRRVEC STQMDSDCAA IQRPDPAKRC HLRPCAGWKV GNWSKCSRNC 

      1390       1400       1410       1420       1430       1440 
SGGFKIREIQ CVDSRDHRNL RPFHCQFLAG IPPPLSMSCN PEPCEAWQVE PWSQCSRSCG 

      1450       1460       1470       1480       1490       1500 
GGVQERGVFC PGGLCDWTKR PTSTMSCNEH LCCHWATGNW DLCSTSCGGG FQKRTVQCVP 

      1510       1520       1530       1540       1550       1560 
SEGNKTEDQD QCLCDHKPRP PEFKKCNQQA CKKSADLLCT KDKLSASFCQ TLKAMKKCSV 

      1570       1580       1590 
PTVRAECCFS CPQTHITHTQ RQRRQRLLQK SKEL 

« Hide

Isoform 2 [UniParc].

Checksum: 11FBCB40E82091F6
Show »

FASTA22926,003
Isoform 3 [UniParc].

Checksum: 5BF525F456FC8EE5
Show »

FASTA1,509168,460

References

« Hide 'large scale' references
[1]"Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats."
Cal S., Argueelles J.M., Fernandez P.L., Lopez-Otin C.
J. Biol. Chem. 276:17932-17940(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT ILE-1495.
Tissue: Fetal lung.
[2]"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 2).
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 2 AND 3).
[5]"ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein."
Liu C.-J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E.
J. Biol. Chem. 281:15800-15808(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH COMP, PH DEPENDENCE, TISSUE SPECIFICITY, INDUCTION.
[6]"The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway."
Llamazares M., Obaya A.J., Moncada-Pazos A., Heljasvaara R., Espada J., Lopez-Otin C., Cal S.
J. Cell Sci. 120:3544-3552(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin."
Luan Y., Kong L., Howell D.R., Ilalov K., Fajardo M., Bai X.-H., Di Cesare P.E., Goldring M.B., Abramson S.B., Liu C.-J.
Osteoarthritis Cartilage 16:1413-1420(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ250725 mRNA. Translation: CAC20419.1.
AY358745 mRNA. Translation: AAQ89105.1.
AC008880 Genomic DNA. No translation available.
AC034232 Genomic DNA. No translation available.
AC109491 Genomic DNA. No translation available.
AC139777 Genomic DNA. No translation available.
BC058841 mRNA. Translation: AAH58841.1.
BC131733 mRNA. Translation: AAI31734.1.
BC139900 mRNA. Translation: AAI39901.1.
RefSeqNP_112217.2. NM_030955.2.
UniGeneHs.12680.

3D structure databases

ProteinModelPortalP58397.
SMRP58397. Positions 246-810, 824-997, 1318-1532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP58397. 3 interactions.
STRING9606.ENSP00000344847.

Protein family/group databases

MEROPSM12.237.

PTM databases

PhosphoSiteP58397.

Polymorphism databases

DMDM259016182.

Proteomic databases

PaxDbP58397.
PRIDEP58397.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000352040; ENSP00000344847; ENSG00000151388. [P58397-3]
ENST00000504830; ENSP00000422554; ENSG00000151388. [P58397-1]
GeneID81792.
KEGGhsa:81792.
UCSCuc003jia.1. human. [P58397-1]
uc010iuq.1. human. [P58397-3]

Organism-specific databases

CTD81792.
GeneCardsGC05M033495.
HGNCHGNC:14605. ADAMTS12.
HPAHPA035973.
MIM606184. gene.
neXtProtNX_P58397.
PharmGKBPA24538.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237764.
HOGENOMHOG000015092.
HOVERGENHBG050620.
InParanoidP58397.
KOK08626.
OMALLCTKDK.
OrthoDBEOG7V765X.
PhylomeDBP58397.
TreeFamTF313537.

Gene expression databases

ArrayExpressP58397.
BgeeP58397.
CleanExHS_ADAMTS12.
GenevestigatorP58397.

Family and domain databases

Gene3D3.40.390.10. 2 hits.
InterProIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 8 hits.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 8 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 8 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 6 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSADAMTS12. human.
GeneWikiADAMTS12.
GenomeRNAi81792.
NextBio72100.
PROP58397.
SOURCESearch...

Entry information

Entry nameATS12_HUMAN
AccessionPrimary (citable) accession number: P58397
Secondary accession number(s): A2RRN9, A5D6V6, Q6UWL3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 128 of the entry and version 2 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 5

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