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Q9UHI8

- ATS1_HUMAN

UniProt

Q9UHI8 - ATS1_HUMAN

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Protein
A disintegrin and metalloproteinase with thrombospondin motifs 1
Gene
ADAMTS1, KIAA1346, METH1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover By similarity. Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture.1 Publication

Catalytic activityi

Cleaves aggrecan at the 1938-Glu-|-Leu-1939 site, within the chondroitin sulfate attachment domain.

Cofactori

Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi198 – 1981Zinc; in inhibited form By similarity
Metal bindingi261 – 2611Calcium 1
Metal bindingi261 – 2611Calcium 2
Metal bindingi344 – 3441Calcium 1
Metal bindingi344 – 3441Calcium 2; via carbonyl oxygen
Metal bindingi351 – 3511Calcium 1
Metal bindingi401 – 4011Zinc; catalytic
Active sitei402 – 40211 Publication
Metal bindingi405 – 4051Zinc; catalytic
Metal bindingi411 – 4111Zinc; catalytic
Metal bindingi462 – 4621Calcium 1; via carbonyl oxygen
Metal bindingi465 – 4651Calcium 1
Metal bindingi465 – 4651Calcium 2

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: Ensembl
  3. metallopeptidase activity Source: ProtInc
  4. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. heart trabecula formation Source: Ensembl
  2. integrin-mediated signaling pathway Source: ProtInc
  3. kidney development Source: Ensembl
  4. negative regulation of cell proliferation Source: ProtInc
  5. ovulation from ovarian follicle Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Heparin-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_200626. O-glycosylation of TSR domain-containing proteins.
REACT_201925. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiM12.222.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 1 (EC:3.4.24.-)
Short name:
ADAM-TS 1
Short name:
ADAM-TS1
Short name:
ADAMTS-1
Alternative name(s):
METH-1
Gene namesi
Name:ADAMTS1
Synonyms:KIAA1346, METH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:217. ADAMTS1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. cytoplasm Source: HPA
  3. cytoplasmic vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24536.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4949 Reviewed prediction
Add
BLAST
Propeptidei50 – 252203 By similarity
PRO_0000029150Add
BLAST
Chaini253 – 967715A disintegrin and metalloproteinase with thrombospondin motifs 1
PRO_0000029151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi333 ↔ 3851 Publication
Disulfide bondi362 ↔ 3671 Publication
Disulfide bondi379 ↔ 4621 Publication
Disulfide bondi417 ↔ 4461 Publication
Disulfide bondi488 ↔ 5111 Publication
Disulfide bondi499 ↔ 5211 Publication
Disulfide bondi506 ↔ 5401 Publication
Disulfide bondi534 ↔ 5451 Publication
Glycosylationi547 – 5471N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi571 ↔ 608 By similarity
Disulfide bondi575 ↔ 613 By similarity
Disulfide bondi586 ↔ 598 By similarity
Glycosylationi720 – 7201N-linked (GlcNAc...) Reviewed prediction
Glycosylationi764 – 7641N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase By similarity.
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.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ9UHI8.
PaxDbiQ9UHI8.
PeptideAtlasiQ9UHI8.
PRIDEiQ9UHI8.

PTM databases

PhosphoSiteiQ9UHI8.

Miscellaneous databases

PMAP-CutDBQ9UHI8.

Expressioni

Gene expression databases

ArrayExpressiQ9UHI8.
BgeeiQ9UHI8.
CleanExiHS_ADAMTS1.
GenevestigatoriQ9UHI8.

Organism-specific databases

HPAiCAB016394.
HPA031498.
HPA031499.

Interactioni

Protein-protein interaction databases

BioGridi114888. 4 interactions.
IntActiQ9UHI8. 2 interactions.
STRINGi9606.ENSP00000284984.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi258 – 2669
Helixi268 – 2747
Helixi275 – 2773
Helixi278 – 29316
Helixi296 – 2983
Beta strandi302 – 31110
Helixi315 – 3173
Helixi325 – 33612
Helixi337 – 3393
Beta strandi351 – 3599
Beta strandi371 – 3733
Turni381 – 3833
Beta strandi385 – 3895
Helixi395 – 40612
Helixi415 – 4173
Turni418 – 4203
Helixi445 – 45612
Turni457 – 4604
Helixi461 – 4644
Helixi478 – 4814
Helixi484 – 4929
Beta strandi510 – 5134
Beta strandi520 – 5234
Beta strandi538 – 5414
Beta strandi544 – 5485

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JIHX-ray2.10A/B253-548[»]
2V4BX-ray2.00A/B253-548[»]
3Q2GX-ray2.30A/B256-548[»]
3Q2HX-ray2.33A/B256-548[»]
ProteinModelPortaliQ9UHI8.
SMRiQ9UHI8. Positions 256-844.

Miscellaneous databases

EvolutionaryTraceiQ9UHI8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini258 – 467210Peptidase M12B
Add
BLAST
Domaini476 – 55984Disintegrin
Add
BLAST
Domaini559 – 61456TSP type-1 1
Add
BLAST
Domaini854 – 90552TSP type-1 2
Add
BLAST
Domaini908 – 96760TSP type-1 3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni725 – 849125Spacer
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi196 – 2038Cysteine switch By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi617 – 724108Cys-rich
Add
BLAST
Compositional biasi843 – 8464Poly-Lys

Domaini

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

Sequence similaritiesi

Contains 1 disintegrin domain.
Contains 3 TSP type-1 domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG291688.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiQ9UHI8.
KOiK08617.
OMAiCPDNNGK.
OrthoDBiEOG7WDN1M.
PhylomeDBiQ9UHI8.
TreeFamiTF331949.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013274. Pept_M12B_ADAM-TS1.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 3 hits.
[Graphical view]
PRINTSiPR01858. ADAMTS1.
PR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 3 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UHI8-1 [UniParc]FASTAAdd to Basket

« Hide

MQRAVPEGFG RRKLGSDMGN AERAPGSRSF GPVPTLLLLA AALLAVSDAL    50
GRPSEEDEEL VVPELERAPG HGTTRLRLHA FDQQLDLELR PDSSFLAPGF 100
TLQNVGRKSG SETPLPETDL AHCFYSGTVN GDPSSAAALS LCEGVRGAFY 150
LLGEAYFIQP LPAASERLAT AAPGEKPPAP LQFHLLRRNR QGDVGGTCGV 200
VDDEPRPTGK AETEDEDEGT EGEDEGAQWS PQDPALQGVG QPTGTGSIRK 250
KRFVSSHRYV ETMLVADQSM AEFHGSGLKH YLLTLFSVAA RLYKHPSIRN 300
SVSLVVVKIL VIHDEQKGPE VTSNAALTLR NFCNWQKQHN PPSDRDAEHY 350
DTAILFTRQD LCGSQTCDTL GMADVGTVCD PSRSCSVIED DGLQAAFTTA 400
HELGHVFNMP HDDAKQCASL NGVNQDSHMM ASMLSNLDHS QPWSPCSAYM 450
ITSFLDNGHG ECLMDKPQNP IQLPGDLPGT SYDANRQCQF TFGEDSKHCP 500
DAASTCSTLW CTGTSGGVLV CQTKHFPWAD GTSCGEGKWC INGKCVNKTD 550
RKHFDTPFHG SWGMWGPWGD CSRTCGGGVQ YTMRECDNPV PKNGGKYCEG 600
KRVRYRSCNL EDCPDNNGKT FREEQCEAHN EFSKASFGSG PAVEWIPKYA 650
GVSPKDRCKL ICQAKGIGYF FVLQPKVVDG TPCSPDSTSV CVQGQCVKAG 700
CDRIIDSKKK FDKCGVCGGN GSTCKKISGS VTSAKPGYHD IITIPTGATN 750
IEVKQRNQRG SRNNGSFLAI KAADGTYILN GDYTLSTLEQ DIMYKGVVLR 800
YSGSSAALER IRSFSPLKEP LTIQVLTVGN ALRPKIKYTY FVKKKKESFN 850
AIPTFSAWVI EEWGECSKSC ELGWQRRLVE CRDINGQPAS ECAKEVKPAS 900
TRPCADHPCP QWQLGEWSSC SKTCGKGYKK RSLKCLSHDG GVLSHESCDP 950
LKKPKHFIDF CTMAECS 967
Length:967
Mass (Da):105,358
Last modified:January 23, 2007 - v4
Checksum:i334119D6310A05A7
GO

Sequence cautioni

The sequence AAD48080.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA92584.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti227 – 2271A → P.3 Publications
Corresponds to variant rs428785 [ dbSNP | Ensembl ].
VAR_030001

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti468 – 4681Q → H in AAF15317. 1 Publication
Sequence conflicti561 – 5611S → N in AAF15317. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF170084 mRNA. Translation: AAF15317.1.
AF060152 mRNA. Translation: AAD48080.1. Different initiation.
AF207664 mRNA. Translation: AAF23772.1.
AB037767 mRNA. Translation: BAA92584.1. Different initiation.
AP001697 Genomic DNA. Translation: BAA95502.1.
CH471079 Genomic DNA. Translation: EAX09951.1.
CH471079 Genomic DNA. Translation: EAX09952.1.
AL162080 mRNA. Translation: CAB82413.1.
CCDSiCCDS33524.1.
PIRiT47158.
RefSeqiNP_008919.3. NM_006988.3.
UniGeneiHs.643357.

Genome annotation databases

EnsembliENST00000284984; ENSP00000284984; ENSG00000154734.
GeneIDi9510.
KEGGihsa:9510.
UCSCiuc002ymf.3. human.

Polymorphism databases

DMDMi124053460.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF170084 mRNA. Translation: AAF15317.1 .
AF060152 mRNA. Translation: AAD48080.1 . Different initiation.
AF207664 mRNA. Translation: AAF23772.1 .
AB037767 mRNA. Translation: BAA92584.1 . Different initiation.
AP001697 Genomic DNA. Translation: BAA95502.1 .
CH471079 Genomic DNA. Translation: EAX09951.1 .
CH471079 Genomic DNA. Translation: EAX09952.1 .
AL162080 mRNA. Translation: CAB82413.1 .
CCDSi CCDS33524.1.
PIRi T47158.
RefSeqi NP_008919.3. NM_006988.3.
UniGenei Hs.643357.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JIH X-ray 2.10 A/B 253-548 [» ]
2V4B X-ray 2.00 A/B 253-548 [» ]
3Q2G X-ray 2.30 A/B 256-548 [» ]
3Q2H X-ray 2.33 A/B 256-548 [» ]
ProteinModelPortali Q9UHI8.
SMRi Q9UHI8. Positions 256-844.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114888. 4 interactions.
IntActi Q9UHI8. 2 interactions.
STRINGi 9606.ENSP00000284984.

Chemistry

BindingDBi Q9UHI8.
ChEMBLi CHEMBL5133.

Protein family/group databases

MEROPSi M12.222.

PTM databases

PhosphoSitei Q9UHI8.

Polymorphism databases

DMDMi 124053460.

Proteomic databases

MaxQBi Q9UHI8.
PaxDbi Q9UHI8.
PeptideAtlasi Q9UHI8.
PRIDEi Q9UHI8.

Protocols and materials databases

DNASUi 9510.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284984 ; ENSP00000284984 ; ENSG00000154734 .
GeneIDi 9510.
KEGGi hsa:9510.
UCSCi uc002ymf.3. human.

Organism-specific databases

CTDi 9510.
GeneCardsi GC21M028208.
HGNCi HGNC:217. ADAMTS1.
HPAi CAB016394.
HPA031498.
HPA031499.
MIMi 605174. gene.
neXtProti NX_Q9UHI8.
PharmGKBi PA24536.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG291688.
HOGENOMi HOG000004799.
HOVERGENi HBG004313.
InParanoidi Q9UHI8.
KOi K08617.
OMAi CPDNNGK.
OrthoDBi EOG7WDN1M.
PhylomeDBi Q9UHI8.
TreeFami TF331949.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_200626. O-glycosylation of TSR domain-containing proteins.
REACT_201925. Degradation of the extracellular matrix.

Miscellaneous databases

ChiTaRSi ADAMTS1. human.
EvolutionaryTracei Q9UHI8.
GeneWikii ADAMTS1.
GenomeRNAii 9510.
NextBioi 35638.
PMAP-CutDB Q9UHI8.
PROi Q9UHI8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UHI8.
Bgeei Q9UHI8.
CleanExi HS_ADAMTS1.
Genevestigatori Q9UHI8.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013274. Pept_M12B_ADAM-TS1.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 3 hits.
[Graphical view ]
PRINTSi PR01858. ADAMTS1.
PR01857. ADAMTSFAMILY.
SMARTi SM00608. ACR. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 3 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, characterization and mapping on human chromosome 21 of the orthologue of murine Adamts-1."
    Casas C., Pritchard M.A., Estivill X., Arbones M.L.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-227.
  2. "METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity."
    Vazquez F., Hastings G., Ortega M.-A., Lane T.F., Oikemus S., Lombardo M., Iruela-Arispe M.L.
    J. Biol. Chem. 274:23349-23357(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-227, FUNCTION.
    Tissue: Heart.
  3. "Differential gene expression by endothelial cells in distinct angiogenic states."
    Glienke J., Schmitt A.O., Pilarsky C., Hinzmann B., Weiss B., Rosenthal A., Thierauch K.H.
    Eur. J. Biochem. 267:2820-2830(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-227.
    Tissue: Endothelial cell.
  4. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 418-967.
    Tissue: Melanoma.
  8. "Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains."
    Gerhardt S., Hassall G., Hawtin P., McCall E., Flavell L., Minshull C., Hargreaves D., Ting A., Pauptit R.A., Parker A.E., Abbott W.M.
    J. Mol. Biol. 373:891-902(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 253-548 ALONE AND IN COMPLEX WITH INHIBITOR, ACTIVE SITE, COFACTOR, ZINC-BINDING SITES, CALCIUM-BINDING SITES, DISULFIDE BONDS.

Entry informationi

Entry nameiATS1_HUMAN
AccessioniPrimary (citable) accession number: Q9UHI8
Secondary accession number(s): D3DSD5
, Q9NSJ8, Q9P2K0, Q9UH83, Q9UP80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 145 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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