Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

MTAP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.UniRule annotation1 Publication

Catalytic activityi

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation

Enzyme regulationi

Inhibited by 5'-methylthiotubercin and 5'-chloroformycin.

Kineticsi

  1. KM=5 µM for S-methyl-5'-thioadenosine2 Publications
  2. KM=580 µM for phosphate2 Publications
  3. KM=23 µM for adenine2 Publications
  4. KM=8 µM for S-methyl-5-thio-alpha-D-ribose 1-phosphate2 Publications

    pH dependencei

    Optimum pH is 7.2-7.6.2 Publications

    Pathwayi: L-methionine biosynthesis via salvage pathway

    This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route).UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. S-methyl-5'-thioadenosine phosphorylase (MTAP), S-methyl-5'-thioadenosine phosphorylase (MTAP-ANRIL fusion), S-methyl-5'-thioadenosine phosphorylase (MTAP), S-methyl-5'-thioadenosine phosphorylase (MTAP)
    This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei18Phosphate1
    Sitei178Important for substrate specificity1
    Binding sitei196Substrate; via amide nitrogen1
    Binding sitei197Phosphate1
    Sitei233Important for substrate specificity1

    GO - Molecular functioni

    • phosphorylase activity Source: ProtInc
    • S-methyl-5-thioadenosine phosphorylase activity Source: GO_Central

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01913-MONOMER.
    ZFISH:HS01913-MONOMER.
    BRENDAi2.4.2.28. 2681.
    ReactomeiR-HSA-1237112. Methionine salvage pathway.
    SABIO-RKQ13126.
    SignaLinkiQ13126.
    UniPathwayiUPA00904; UER00873.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-methyl-5'-thioadenosine phosphorylaseUniRule annotation (EC:2.4.2.28UniRule annotation)
    Alternative name(s):
    5'-methylthioadenosine phosphorylaseUniRule annotation
    Short name:
    MTA phosphorylaseUniRule annotation
    Short name:
    MTAPUniRule annotation
    Short name:
    MTAPaseUniRule annotation
    Gene namesi
    Name:MTAPUniRule annotation
    Synonyms:MSAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:7413. MTAP.

    Subcellular locationi

    • Cytoplasm
    • Nucleus UniRule annotation

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry. DMSMFH causing mutations found in MTAP exon 9 result in exon skipping and dysregulated alternative splicing of all MTAP isoforms (PubMed:22464254).1 Publication
    Disease descriptionAn autosomal dominant bone dysplasia characterized by pathologic fractures due to abnormal cortical growth and diaphyseal medullary stenosis. The fractures heal poorly, and there is progressive bowing of the lower extremities. Some patients show a limb-girdle myopathy, with muscle weakness and atrophy. Approximately 35% of affected individuals develop an aggressive form of bone sarcoma consistent with malignant fibrous histiocytoma or osteosarcoma.
    See also OMIM:112250

    Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.

    Organism-specific databases

    DisGeNETi4507.
    MalaCardsiMTAP.
    MIMi112250. phenotype.
    OpenTargetsiENSG00000099810.
    Orphaneti85182. Diaphyseal medullary stenosis - bone malignancy.
    PharmGKBiPA31220.

    Chemistry databases

    ChEMBLiCHEMBL4941.
    DrugBankiDB00173. Adenine.

    Polymorphism and mutation databases

    BioMutaiMTAP.
    DMDMi143811423.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001845451 – 283S-methyl-5'-thioadenosine phosphorylaseAdd BLAST283

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei51N6-acetyllysineBy similarity1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ13126.
    MaxQBiQ13126.
    PaxDbiQ13126.
    PeptideAtlasiQ13126.
    PRIDEiQ13126.

    2D gel databases

    REPRODUCTION-2DPAGEQ13126.
    UCD-2DPAGEQ13126.

    PTM databases

    iPTMnetiQ13126.
    PhosphoSitePlusiQ13126.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.

    Gene expression databases

    BgeeiENSG00000099810.
    CleanExiHS_MTAP.
    ExpressionAtlasiQ13126. baseline and differential.
    GenevisibleiQ13126. HS.

    Organism-specific databases

    HPAiHPA046915.

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CENPHQ9H3R53EBI-2547776,EBI-1003700

    Protein-protein interaction databases

    BioGridi110611. 48 interactors.
    IntActiQ13126. 10 interactors.
    MINTiMINT-268764.
    STRINGi9606.ENSP00000369519.

    Chemistry databases

    BindingDBiQ13126.

    Structurei

    Secondary structure

    1283
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi11 – 16Combined sources6
    Helixi23 – 25Combined sources3
    Beta strandi26 – 32Combined sources7
    Beta strandi45 – 50Combined sources6
    Beta strandi53 – 59Combined sources7
    Turni60 – 65Combined sources6
    Helixi69 – 71Combined sources3
    Helixi74 – 83Combined sources10
    Beta strandi87 – 97Combined sources11
    Beta strandi107 – 109Combined sources3
    Beta strandi112 – 116Combined sources5
    Beta strandi126 – 128Combined sources3
    Beta strandi134 – 136Combined sources3
    Beta strandi140 – 142Combined sources3
    Helixi146 – 158Combined sources13
    Beta strandi163 – 165Combined sources3
    Beta strandi168 – 172Combined sources5
    Helixi180 – 188Combined sources9
    Beta strandi193 – 197Combined sources5
    Helixi198 – 207Combined sources10
    Beta strandi211 – 220Combined sources10
    Turni222 – 224Combined sources3
    Beta strandi225 – 228Combined sources4
    Helixi233 – 258Combined sources26
    Helixi264 – 275Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CB0X-ray1.70A1-283[»]
    1CG6X-ray1.70A1-283[»]
    1K27X-ray1.95A1-283[»]
    1SD1X-ray2.03A1-283[»]
    1SD2X-ray2.10A1-283[»]
    3LN5X-ray1.90C227-237[»]
    3OZCX-ray1.93A1-283[»]
    3OZDX-ray2.10A/B1-283[»]
    3OZEX-ray2.00A/B/C/D/E/F1-283[»]
    ProteinModelPortaliQ13126.
    SMRiQ13126.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13126.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni60 – 61Phosphate binding2
    Regioni93 – 94Phosphate binding2
    Regioni220 – 222Substrate binding3

    Sequence similaritiesi

    Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiKOG3985. Eukaryota.
    COG0005. LUCA.
    GeneTreeiENSGT00550000074874.
    HOGENOMiHOG000228986.
    HOVERGENiHBG002487.
    KOiK00772.
    OrthoDBiEOG091G0CQI.
    PhylomeDBiQ13126.
    TreeFamiTF312883.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    HAMAPiMF_01963. MTAP. 1 hit.
    InterProiIPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01694. MTAP. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q13126-1) [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

            10         20         30         40         50
    MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI
    60 70 80 90 100
    KNVDCVLLAR HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE
    110 120 130 140 150
    EIQPGDIVII DQFIDRTTMR PQSFYDGSHS CARGVCHIPM AEPFCPKTRE
    160 170 180 190 200
    VLIETAKKLG LRCHSKGTMV TIEGPRFSSR AESFMFRTWG ADVINMTTVP
    210 220 230 240 250
    EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL KENANKAKSL
    260 270 280
    LLTTIPQIGS TEWSETLHNL KNMAQFSVLL PRH
    Length:283
    Mass (Da):31,236
    Last modified:April 3, 2007 - v2
    Checksum:i3B34C565EB5B99DA
    GO
    Isoform 2 (identifier: Q13126-2) [UniParc]FASTAAdd to basket
    Also known as: MTAP_v1

    The sequence of this isoform differs from the canonical sequence as follows:
         272-283: NMAQFSVLLPRH → MIKFQMILSE...KDQTYICMKS

    Show »
    Length:346
    Mass (Da):38,356
    Checksum:i1681DA9B0DFB66EE
    GO
    Isoform 3 (identifier: Q13126-3) [UniParc]FASTAAdd to basket
    Also known as: MTAP_v2

    The sequence of this isoform differs from the canonical sequence as follows:
         272-283: NMAQFSVLLPRH → MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGEILPLSPLDLAGYCFQQPMQPPCPDS

    Show »
    Length:334
    Mass (Da):36,936
    Checksum:i3CD3E1A173FC3465
    GO
    Isoform 4 (identifier: Q13126-4) [UniParc]FASTAAdd to basket
    Also known as: MTAP_v3

    The sequence of this isoform differs from the canonical sequence as follows:
         272-283: NMAQFSVLLPRH → VRSAFQLPP

    Show »
    Length:280
    Mass (Da):30,838
    Checksum:i68C30E7ABA7B8AB6
    GO
    Isoform 5 (identifier: Q13126-5) [UniParc]FASTAAdd to basket
    Also known as: MTAP_v4

    The sequence of this isoform differs from the canonical sequence as follows:
         231-283: VSVDRVLKTL...AQFSVLLPRH → MIKFQMILSE...KDQTYICMKS

    Show »
    Length:305
    Mass (Da):33,797
    Checksum:iD50D41EC7E7123EB
    GO
    Isoform 6 (identifier: Q13126-6) [UniParc]FASTAAdd to basket
    Also known as: MTAP_v5

    The sequence of this isoform differs from the canonical sequence as follows:
         231-283: VSVDRVLKTL...AQFSVLLPRH → MIKFQMILSE...QPMQPPCPDS

    Show »
    Length:293
    Mass (Da):32,376
    Checksum:i3968FB0DFD63A981
    GO
    Isoform 7 (identifier: Q13126-7) [UniParc]FASTAAdd to basket
    Also known as: MTAP_v6

    The sequence of this isoform differs from the canonical sequence as follows:
         232-283: SVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH → RSAFQLPP

    Show »
    Length:239
    Mass (Da):26,278
    Checksum:iDD08ECE4DF322F02
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti218A → G in AAG38871 (PubMed:8650244).Curated1
    Sequence conflicti218A → G in AAR24607 (PubMed:8650244).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_03147056V → I.3 PublicationsCorresponds to variant rs7023954dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_044071231 – 283VSVDR…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGKKC LSAPAIILRPPQPRGTVTTF KVSWSKDQTYICMKS in isoform 5. 1 PublicationAdd BLAST53
    Alternative sequenceiVSP_044072231 – 283VSVDR…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGEIL PLSPLDLAGYCFQQPMQPPC PDS in isoform 6. 1 PublicationAdd BLAST53
    Alternative sequenceiVSP_044073232 – 283SVDRV…LLPRH → RSAFQLPP in isoform 7. 1 PublicationAdd BLAST52
    Alternative sequenceiVSP_044074272 – 283NMAQF…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGKKC LSAPAIILRPPQPRGTVTTF KVSWSKDQTYICMKS in isoform 2. 1 PublicationAdd BLAST12
    Alternative sequenceiVSP_044075272 – 283NMAQF…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGEIL PLSPLDLAGYCFQQPMQPPC PDS in isoform 3. 1 PublicationAdd BLAST12
    Alternative sequenceiVSP_044076272 – 283NMAQF…LLPRH → VRSAFQLPP in isoform 4. 1 PublicationAdd BLAST12

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U22233 mRNA. Translation: AAA81646.1.
    L40432 mRNA. Translation: AAG38871.1.
    L42634
    , L42627, L42628, L42629, L42630, L42631, L42632, L42633 Genomic DNA. Translation: AAR24607.2.
    HE654772 mRNA. Translation: CCF77345.1.
    HE654773 mRNA. Translation: CCF77346.1.
    HE654774 mRNA. Translation: CCF77347.1.
    HE654775 mRNA. Translation: CCF77348.1.
    HE654776 mRNA. Translation: CCF77349.1.
    HE654777 mRNA. Translation: CCF77350.1.
    AY712791 mRNA. Translation: AAU04442.1.
    AL359922 Genomic DNA. Translation: CAI16481.1.
    CH471071 Genomic DNA. Translation: EAW58606.1.
    BC026106 mRNA. Translation: AAH26106.1.
    CCDSiCCDS6509.1. [Q13126-1]
    PIRiI38969.
    RefSeqiNP_002442.2. NM_002451.3. [Q13126-1]
    UniGeneiHs.193268.

    Genome annotation databases

    EnsembliENST00000380172; ENSP00000369519; ENSG00000099810. [Q13126-1]
    ENST00000580900; ENSP00000463424; ENSG00000099810. [Q13126-3]
    GeneIDi4507.
    KEGGihsa:4507.
    UCSCiuc003zph.4. human. [Q13126-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U22233 mRNA. Translation: AAA81646.1.
    L40432 mRNA. Translation: AAG38871.1.
    L42634
    , L42627, L42628, L42629, L42630, L42631, L42632, L42633 Genomic DNA. Translation: AAR24607.2.
    HE654772 mRNA. Translation: CCF77345.1.
    HE654773 mRNA. Translation: CCF77346.1.
    HE654774 mRNA. Translation: CCF77347.1.
    HE654775 mRNA. Translation: CCF77348.1.
    HE654776 mRNA. Translation: CCF77349.1.
    HE654777 mRNA. Translation: CCF77350.1.
    AY712791 mRNA. Translation: AAU04442.1.
    AL359922 Genomic DNA. Translation: CAI16481.1.
    CH471071 Genomic DNA. Translation: EAW58606.1.
    BC026106 mRNA. Translation: AAH26106.1.
    CCDSiCCDS6509.1. [Q13126-1]
    PIRiI38969.
    RefSeqiNP_002442.2. NM_002451.3. [Q13126-1]
    UniGeneiHs.193268.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CB0X-ray1.70A1-283[»]
    1CG6X-ray1.70A1-283[»]
    1K27X-ray1.95A1-283[»]
    1SD1X-ray2.03A1-283[»]
    1SD2X-ray2.10A1-283[»]
    3LN5X-ray1.90C227-237[»]
    3OZCX-ray1.93A1-283[»]
    3OZDX-ray2.10A/B1-283[»]
    3OZEX-ray2.00A/B/C/D/E/F1-283[»]
    ProteinModelPortaliQ13126.
    SMRiQ13126.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110611. 48 interactors.
    IntActiQ13126. 10 interactors.
    MINTiMINT-268764.
    STRINGi9606.ENSP00000369519.

    Chemistry databases

    BindingDBiQ13126.
    ChEMBLiCHEMBL4941.
    DrugBankiDB00173. Adenine.

    PTM databases

    iPTMnetiQ13126.
    PhosphoSitePlusiQ13126.

    Polymorphism and mutation databases

    BioMutaiMTAP.
    DMDMi143811423.

    2D gel databases

    REPRODUCTION-2DPAGEQ13126.
    UCD-2DPAGEQ13126.

    Proteomic databases

    EPDiQ13126.
    MaxQBiQ13126.
    PaxDbiQ13126.
    PeptideAtlasiQ13126.
    PRIDEiQ13126.

    Protocols and materials databases

    DNASUi4507.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000380172; ENSP00000369519; ENSG00000099810. [Q13126-1]
    ENST00000580900; ENSP00000463424; ENSG00000099810. [Q13126-3]
    GeneIDi4507.
    KEGGihsa:4507.
    UCSCiuc003zph.4. human. [Q13126-1]

    Organism-specific databases

    CTDi4507.
    DisGeNETi4507.
    GeneCardsiMTAP.
    H-InvDBHIX0007954.
    HIX0025895.
    HGNCiHGNC:7413. MTAP.
    HPAiHPA046915.
    MalaCardsiMTAP.
    MIMi112250. phenotype.
    156540. gene.
    neXtProtiNX_Q13126.
    OpenTargetsiENSG00000099810.
    Orphaneti85182. Diaphyseal medullary stenosis - bone malignancy.
    PharmGKBiPA31220.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3985. Eukaryota.
    COG0005. LUCA.
    GeneTreeiENSGT00550000074874.
    HOGENOMiHOG000228986.
    HOVERGENiHBG002487.
    KOiK00772.
    OrthoDBiEOG091G0CQI.
    PhylomeDBiQ13126.
    TreeFamiTF312883.

    Enzyme and pathway databases

    UniPathwayiUPA00904; UER00873.
    BioCyciMetaCyc:HS01913-MONOMER.
    ZFISH:HS01913-MONOMER.
    BRENDAi2.4.2.28. 2681.
    ReactomeiR-HSA-1237112. Methionine salvage pathway.
    SABIO-RKQ13126.
    SignaLinkiQ13126.

    Miscellaneous databases

    ChiTaRSiMTAP. human.
    EvolutionaryTraceiQ13126.
    GeneWikiiMTAP.
    GenomeRNAii4507.
    PROiQ13126.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000099810.
    CleanExiHS_MTAP.
    ExpressionAtlasiQ13126. baseline and differential.
    GenevisibleiQ13126. HS.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    HAMAPiMF_01963. MTAP. 1 hit.
    InterProiIPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01694. MTAP. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMTAP_HUMAN
    AccessioniPrimary (citable) accession number: Q13126
    Secondary accession number(s): I2G7M5
    , I2G7M6, I2G7M7, I2G7M8, I2G7M9, I2G7N0, Q5T3P3, Q9H010
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 3, 2007
    Last modified: November 30, 2016
    This is version 175 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.