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O95450

- ATS2_HUMAN

UniProt

O95450 - ATS2_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 2

Gene

ADAMTS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    Cleaves the propeptides of type I and II collagen prior to fibril assembly. Does not act on type III collagen. May also play a role in development that is independent of its role in collagen biosynthesis.

    Catalytic activityi

    Cleaves the N-propeptide of collagen chain alpha-1(I) at Pro-|-Gln and of alpha-1(II) and alpha-2(I) at Ala-|-Gln.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi408 – 4081Zinc; catalyticPROSITE-ProRule annotation
    Active sitei409 – 4091PROSITE-ProRule annotation
    Metal bindingi412 – 4121Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi418 – 4181Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: ProtInc
    2. metallopeptidase activity Source: ProtInc
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. collagen catabolic process Source: UniProtKB-KW
    2. collagen fibril organization Source: Ensembl
    3. extracellular matrix organization Source: Reactome
    4. lung development Source: Ensembl
    5. protein processing Source: Ensembl
    6. skin development Source: Ensembl
    7. spermatogenesis Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.

    Protein family/group databases

    MEROPSiM12.301.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 2 (EC:3.4.24.14)
    Short name:
    ADAM-TS 2
    Short name:
    ADAM-TS2
    Short name:
    ADAMTS-2
    Alternative name(s):
    Procollagen I N-proteinase
    Short name:
    PC I-NP
    Procollagen I/II amino propeptide-processing enzyme
    Procollagen N-endopeptidase
    Short name:
    pNPI
    Gene namesi
    Name:ADAMTS2
    Synonyms:PCINP, PCPNI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:218. ADAMTS2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ehlers-Danlos syndrome 7C (EDS7C) [MIM:225410]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Marked by extremely fragile tissues, hyperextensible skin and easy bruising. Facial skin contains numerous folds, as in the cutis laxa syndrome.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Ehlers-Danlos syndrome

    Organism-specific databases

    MIMi225410. phenotype.
    Orphaneti1901. Ehlers-Danlos syndrome, dermatosparaxis type.
    PharmGKBiPA24546.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Propeptidei30 – 253224By similarityPRO_0000029158Add
    BLAST
    Chaini254 – 1211958A disintegrin and metalloproteinase with thrombospondin motifs 2PRO_0000029159Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi343 ↔ 392By similarity
    Disulfide bondi386 ↔ 465By similarity
    Disulfide bondi425 ↔ 451By similarity
    Disulfide bondi492 ↔ 517By similarity
    Disulfide bondi503 ↔ 526By similarity
    Disulfide bondi512 ↔ 545By similarity
    Disulfide bondi539 ↔ 550By similarity
    Disulfide bondi573 ↔ 610By similarity
    Disulfide bondi577 ↔ 615By similarity
    Disulfide bondi588 ↔ 600By similarity
    Glycosylationi949 – 9491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi987 ↔ 1023By similarity
    Disulfide bondi991 ↔ 1028By similarity
    Glycosylationi993 – 9931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1002 ↔ 1012By similarity
    Glycosylationi1031 – 10311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1098 – 10981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1145 – 11451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1150 – 11501N-linked (GlcNAc...)Sequence Analysis

    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.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiO95450.
    PRIDEiO95450.

    PTM databases

    PhosphoSiteiO95450.

    Expressioni

    Tissue specificityi

    Expressed at high level in skin, bone, tendon and aorta and at low levels in thymus and brain.

    Gene expression databases

    BgeeiO95450.
    CleanExiHS_ADAMTS2.
    GenevestigatoriO95450.

    Organism-specific databases

    HPAiHPA028444.

    Interactioni

    Subunit structurei

    May belong to a multimeric complex. Binds specifically to collagen type XIV By similarity.By similarity

    Protein-protein interaction databases

    BioGridi114887. 1 interaction.
    IntActiO95450. 1 interaction.
    STRINGi9606.ENSP00000251582.

    Structurei

    3D structure databases

    ProteinModelPortaliO95450.
    SMRiO95450. Positions 268-766, 923-1010.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini266 – 470205Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini480 – 56081DisintegrinAdd
    BLAST
    Domaini561 – 61656TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini854 – 91259TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini914 – 97158TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini975 – 102955TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1059 – 109739PLACPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni723 – 851129SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi691 – 6933Cell attachment siteSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi40 – 434Poly-Ala
    Compositional biasi185 – 1884Poly-Glu
    Compositional biasi618 – 722105Cys-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 disintegrin domain.Curated
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 1 PLAC domain.PROSITE-ProRule annotation
    Contains 4 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG307411.
    HOGENOMiHOG000034222.
    HOVERGENiHBG004314.
    InParanoidiO95450.
    KOiK08618.
    OMAiIHEDSLN.
    OrthoDBiEOG76HQ0N.
    PhylomeDBiO95450.
    TreeFamiTF313537.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013275. Pept_M12B_ADAM-TS2.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR010909. PLAC.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 4 hits.
    [Graphical view]
    PRINTSiPR01859. ADAMTS2.
    PR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 4 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 4 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform LpNPI (identifier: O95450-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MDPPAGAARR LLCPALLLLL LLLPPPLLPP PPPPANARLA AAADPPGGPL     50
    GHGAERILAV PVRTDAQGRL VSHVVSAATS RAGVRARRAA PVRTPSFPGG 100
    NEEEPGSHLF YNVTVFGRDL HLRLRPNARL VAPGATMEWQ GEKGTTRVEP 150
    LLGSCLYVGD VAGLAEASSV ALSNCDGLAG LIRMEEEEFF IEPLEKGLAA 200
    QEAEQGRVHV VYRRPPTSPP LGGPQALDTG ASLDSLDSLS RALGVLEEHA 250
    NSSRRRARRH AADDDYNIEV LLGVDDSVVQ FHGKEHVQKY LLTLMNIVNE 300
    IYHDESLGAH INVVLVRIIL LSYGKSMSLI EIGNPSQSLE NVCRWAYLQQ 350
    KPDTGHDEYH DHAIFLTRQD FGPSGMQGYA PVTGMCHPVR SCTLNHEDGF 400
    SSAFVVAHET GHVLGMEHDG QGNRCGDEVR LGSIMAPLVQ AAFHRFHWSR 450
    CSQQELSRYL HSYDCLLDDP FAHDWPALPQ LPGLHYSMNE QCRFDFGLGY 500
    MMCTAFRTFD PCKQLWCSHP DNPYFCKTKK GPPLDGTMCA PGKHCFKGHC 550
    IWLTPDILKR DGSWGAWSPF GSCSRTCGTG VKFRTRQCDN PHPANGGRTC 600
    SGLAYDFQLC SRQDCPDSLA DFREEQCRQW DLYFEHGDAQ HHWLPHEHRD 650
    AKERCHLYCE SRETGEVVSM KRMVHDGTRC SYKDAFSLCV RGDCRKVGCD 700
    GVIGSSKQED KCGVCGGDNS HCKVVKGTFT RSPKKHGYIK MFEIPAGARH 750
    LLIQEVDATS HHLAVKNLET GKFILNEEND VDASSKTFIA MGVEWEYRDE 800
    DGRETLQTMG PLHGTITVLV IPVGDTRVSL TYKYMIHEDS LNVDDNNVLE 850
    EDSVVYEWAL KKWSPCSKPC GGGSQFTKYG CRRRLDHKMV HRGFCAALSK 900
    PKAIRRACNP QECSQPVWVT GEWEPCSQTC GRTGMQVRSV RCIQPLHDNT 950
    TRSVHAKHCN DARPESRRAC SRELCPGRWR AGPWSQCSVT CGNGTQERPV 1000
    LCRTADDSFG ICQEERPETA RTCRLGPCPR NISDPSKKSY VVQWLSRPDP 1050
    DSPIRKISSK GHCQGDKSIF CRMEVLSRYC SIPGYNKLCC KSCNLYNNLT 1100
    NVEGRIEPPP GKHNDIDVFM PTLPVPTVAM EVRPSPSTPL EVPLNASSTN 1150
    ATEDHPETNA VDEPYKIHGL EDEVQPPNLI PRRPSPYEKT RNQRIQELID 1200
    EMRKKEMLGK F 1211
    Length:1,211
    Mass (Da):134,755
    Last modified:December 16, 2008 - v2
    Checksum:i6C4F2C2D46A1F925
    GO
    Isoform SpNPI (identifier: O95450-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         544-566: HCFKGHCIWLTPDILKRDGSWGA → FRPGAVAHACYPSTLGGQGRWIA
         567-1211: Missing.

    Note: Has no significant N-procollagen peptidase activity.

    Show »
    Length:566
    Mass (Da):61,756
    Checksum:i4D0D641B94307BA2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1001 – 10011L → P in CAA05880. (PubMed:10417273)Curated
    Sequence conflicti1089 – 10891C → S in CAA05880. (PubMed:10417273)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti74 – 741V → M.
    Corresponds to variant rs2271211 [ dbSNP | Ensembl ].
    VAR_047927
    Natural varianti241 – 2411R → H.
    Corresponds to variant rs11750821 [ dbSNP | Ensembl ].
    VAR_047928
    Natural varianti245 – 2451V → I.
    Corresponds to variant rs398829 [ dbSNP | Ensembl ].
    VAR_020058
    Natural varianti331 – 3311E → K.
    Corresponds to variant rs17667857 [ dbSNP | Ensembl ].
    VAR_047929
    Natural varianti665 – 6651G → R.
    Corresponds to variant rs35372714 [ dbSNP | Ensembl ].
    VAR_047930
    Natural varianti827 – 8271R → Q.
    Corresponds to variant rs35445112 [ dbSNP | Ensembl ].
    VAR_047931
    Natural varianti1177 – 11771P → S.
    Corresponds to variant rs1054480 [ dbSNP | Ensembl ].
    VAR_020059

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei544 – 56623HCFKG…GSWGA → FRPGAVAHACYPSTLGGQGR WIA in isoform SpNPI. 1 PublicationVSP_005497Add
    BLAST
    Alternative sequencei567 – 1211645Missing in isoform SpNPI. 1 PublicationVSP_005498Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ003125 mRNA. Translation: CAA05880.1.
    AC008544 Genomic DNA. No translation available.
    AC010216 Genomic DNA. No translation available.
    AC109479 Genomic DNA. No translation available.
    CCDSiCCDS34311.1. [O95450-2]
    CCDS4444.1. [O95450-1]
    RefSeqiNP_055059.2. NM_014244.4. [O95450-1]
    NP_067610.1. NM_021599.2. [O95450-2]
    UniGeneiHs.23871.

    Genome annotation databases

    EnsembliENST00000251582; ENSP00000251582; ENSG00000087116. [O95450-1]
    ENST00000274609; ENSP00000274609; ENSG00000087116. [O95450-2]
    GeneIDi9509.
    KEGGihsa:9509.
    UCSCiuc003mjw.3. human. [O95450-1]
    uc011dgm.2. human. [O95450-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ003125 mRNA. Translation: CAA05880.1 .
    AC008544 Genomic DNA. No translation available.
    AC010216 Genomic DNA. No translation available.
    AC109479 Genomic DNA. No translation available.
    CCDSi CCDS34311.1. [O95450-2 ]
    CCDS4444.1. [O95450-1 ]
    RefSeqi NP_055059.2. NM_014244.4. [O95450-1 ]
    NP_067610.1. NM_021599.2. [O95450-2 ]
    UniGenei Hs.23871.

    3D structure databases

    ProteinModelPortali O95450.
    SMRi O95450. Positions 268-766, 923-1010.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114887. 1 interaction.
    IntActi O95450. 1 interaction.
    STRINGi 9606.ENSP00000251582.

    Protein family/group databases

    MEROPSi M12.301.

    PTM databases

    PhosphoSitei O95450.

    Proteomic databases

    PaxDbi O95450.
    PRIDEi O95450.

    Protocols and materials databases

    DNASUi 9509.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251582 ; ENSP00000251582 ; ENSG00000087116 . [O95450-1 ]
    ENST00000274609 ; ENSP00000274609 ; ENSG00000087116 . [O95450-2 ]
    GeneIDi 9509.
    KEGGi hsa:9509.
    UCSCi uc003mjw.3. human. [O95450-1 ]
    uc011dgm.2. human. [O95450-2 ]

    Organism-specific databases

    CTDi 9509.
    GeneCardsi GC05M178537.
    HGNCi HGNC:218. ADAMTS2.
    HPAi HPA028444.
    MIMi 225410. phenotype.
    604539. gene.
    neXtProti NX_O95450.
    Orphaneti 1901. Ehlers-Danlos syndrome, dermatosparaxis type.
    PharmGKBi PA24546.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307411.
    HOGENOMi HOG000034222.
    HOVERGENi HBG004314.
    InParanoidi O95450.
    KOi K08618.
    OMAi IHEDSLN.
    OrthoDBi EOG76HQ0N.
    PhylomeDBi O95450.
    TreeFami TF313537.

    Enzyme and pathway databases

    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    ChiTaRSi ADAMTS2. human.
    GeneWikii ADAMTS2.
    GenomeRNAii 9509.
    NextBioi 35632.
    PROi O95450.
    SOURCEi Search...

    Gene expression databases

    Bgeei O95450.
    CleanExi HS_ADAMTS2.
    Genevestigatori O95450.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013275. Pept_M12B_ADAM-TS2.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR010909. PLAC.
    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. 4 hits.
    [Graphical view ]
    PRINTSi PR01859. ADAMTS2.
    PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 4 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 4 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene."
      Colige A., Sieron A.L., Li S.-W., Schwarze U., Petty E., Wertelecki W., Wilcox W., Krakow D., Cohn D.H., Reardon W., Byers P.H., Lapiere C.M., Prockop D.J., Nusgens B.V.
      Am. J. Hum. Genet. 65:308-317(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LPNPI AND SPNPI), INVOLVEMENT IN EDS7C.
      Tissue: Skin.
    2. "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.
      , 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].

    Entry informationi

    Entry nameiATS2_HUMAN
    AccessioniPrimary (citable) accession number: O95450
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3