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P23109

- AMPD1_HUMAN

UniProt

P23109 - AMPD1_HUMAN

Protein

AMP deaminase 1

Gene

AMPD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (18 Apr 2012)
      Previous versions | rss
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    Functioni

    AMP deaminase plays a critical role in energy metabolism.

    Catalytic activityi

    AMP + H2O = IMP + NH3.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi336 – 3361Zinc; catalyticBy similarity
    Metal bindingi338 – 3381Zinc; catalyticBy similarity
    Binding sitei338 – 3381SubstrateBy similarity
    Metal bindingi605 – 6051Zinc; catalyticBy similarity
    Binding sitei608 – 6081SubstrateBy similarity
    Active sitei627 – 6271Proton acceptorPROSITE-ProRule annotation
    Metal bindingi682 – 6821Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. AMP deaminase activity Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. IMP salvage Source: UniProtKB-UniPathway
    2. nucleobase-containing small molecule metabolic process Source: Reactome
    3. purine-containing compound salvage Source: Reactome
    4. purine nucleobase metabolic process Source: Reactome
    5. response to organic substance Source: Ensembl
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_1923. Purine salvage.
    SABIO-RKP23109.
    UniPathwayiUPA00591; UER00663.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AMP deaminase 1 (EC:3.5.4.6)
    Alternative name(s):
    AMP deaminase isoform M
    Myoadenylate deaminase
    Gene namesi
    Name:AMPD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:468. AMPD1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Myopathy due to myoadenylate deaminase deficiency (MMDD) [MIM:615511]: A metabolic disorder resulting in exercise-related myopathy. It is characterized by exercise-induced muscle aches, cramps, and early fatigue.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti421 – 4211R → W in MMDD; loss of activity. 1 Publication
    Corresponds to variant rs35859650 [ dbSNP | Ensembl ].
    VAR_013271
    Natural varianti458 – 4581R → H in MMDD; loss of activity. 1 Publication
    VAR_013272

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615511. phenotype.
    Orphaneti45. Adenosine monophosphate deaminase deficiency.
    PharmGKBiPA24776.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 780780AMP deaminase 1PRO_0000194403Add
    BLAST

    Proteomic databases

    PaxDbiP23109.
    PRIDEiP23109.

    PTM databases

    PhosphoSiteiP23109.

    Expressioni

    Tissue specificityi

    Three isoforms are present in mammals: AMP deaminase 1 is the predominant form in skeletal muscle; AMP deaminase 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; AMP deaminase 3 is found in erythrocytes.

    Gene expression databases

    ArrayExpressiP23109.
    BgeeiP23109.
    CleanExiHS_AMPD1.
    GenevestigatoriP23109.

    Organism-specific databases

    HPAiHPA026478.
    HPA028080.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi106767. 5 interactions.
    IntActiP23109. 5 interactions.
    STRINGi9606.ENSP00000316520.

    Structurei

    3D structure databases

    ProteinModelPortaliP23109.
    SMRiP23109. Positions 225-775.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni407 – 4126Substrate bindingBy similarity
    Regioni683 – 6864Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1816.
    HOGENOMiHOG000092200.
    HOVERGENiHBG050494.
    KOiK01490.
    OMAiNMTWMIQ.
    OrthoDBiEOG70ZZMQ.
    PhylomeDBiP23109.
    TreeFamiTF300439.

    Family and domain databases

    InterProiIPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view]
    PANTHERiPTHR11359. PTHR11359. 1 hit.
    PfamiPF00962. A_deaminase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
    TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
    PROSITEiPS00485. A_DEAMINASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P23109-1) [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

    MNVRIFYSVS QSPHSLLSLL FYCAILESRI SATMPLFKLP AEEKQIDDAM    50
    RNFAEKVFAS EVKDEGGRQE ISPFDVDEIC PISHHEMQAH IFHLETLSTS 100
    TEARRKKRFQ GRKTVNLSIP LSETSSTKLS HIDEYISSSP TYQTVPDFQR 150
    VQITGDYASG VTVEDFEIVC KGLYRALCIR EKYMQKSFQR FPKTPSKYLR 200
    NIDGEAWVAN ESFYPVFTPP VKKGEDPFRT DNLPENLGYH LKMKDGVVYV 250
    YPNEAAVSKD EPKPLPYPNL DTFLDDMNFL LALIAQGPVK TYTHRRLKFL 300
    SSKFQVHQML NEMDELKELK NNPHRDFYNC RKVDTHIHAA ACMNQKHLLR 350
    FIKKSYQIDA DRVVYSTKEK NLTLKELFAK LKMHPYDLTV DSLDVHAGRQ 400
    TFQRFDKFND KYNPVGASEL RDLYLKTDNY INGEYFATII KEVGADLVEA 450
    KYQHAEPRLS IYGRSPDEWS KLSSWFVCNR IHCPNMTWMI QVPRIYDVFR 500
    SKNFLPHFGK MLENIFMPVF EATINPQADP ELSVFLKHIT GFDSVDDESK 550
    HSGHMFSSKS PKPQEWTLEK NPSYTYYAYY MYANIMVLNS LRKERGMNTF 600
    LFRPHCGEAG ALTHLMTAFM IADDISHGLN LKKSPVLQYL FFLAQIPIAM 650
    SPLSNNSLFL EYAKNPFLDF LQKGLMISLS TDDPMQFHFT KEPLMEEYAI 700
    AAQVFKLSTC DMCEVARNSV LQCGISHEEK VKFLGDNYLE EGPAGNDIRR 750
    TNVAQIRMAY RYETWCYELN LIAEGLKSTE 780
    Length:780
    Mass (Da):90,219
    Last modified:April 18, 2012 - v2
    Checksum:i2449E96D00312629
    GO
    Isoform 2 (identifier: P23109-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         41-45: AEEKQ → E

    Show »
    Length:776
    Mass (Da):89,763
    Checksum:iB831F57E1D7AA491
    GO

    Sequence cautioni

    The sequence AAA57281.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAG24258.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAF84038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAG36918.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAI18828.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti234 – 2341P → S in BAF84038. (PubMed:14702039)Curated
    Sequence conflicti306 – 3061V → A in BAF84038. (PubMed:14702039)Curated
    Sequence conflicti467 – 4671D → G in BAG36918. (PubMed:14702039)Curated
    Sequence conflicti475 – 4751W → R in BAF84038. (PubMed:14702039)Curated
    Sequence conflicti659 – 6591F → S in BAF84038. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551E → K.
    Corresponds to variant rs2273268 [ dbSNP | Ensembl ].
    VAR_048860
    Natural varianti81 – 811P → L Polymorphism; activity comparable to wild-type. 1 Publication
    Corresponds to variant rs61752479 [ dbSNP | Ensembl ].
    VAR_013270
    Natural varianti421 – 4211R → W in MMDD; loss of activity. 1 Publication
    Corresponds to variant rs35859650 [ dbSNP | Ensembl ].
    VAR_013271
    Natural varianti458 – 4581R → H in MMDD; loss of activity. 1 Publication
    VAR_013272
    Natural varianti666 – 6661P → H in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035801

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei41 – 455AEEKQ → E in isoform 2. CuratedVSP_042638

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37931
    , M37920, M37921, M37922, M37923, M37924, M37927, M37928, M37929, M37930 Genomic DNA. Translation: AAG24258.1. Different initiation.
    AL096773 Genomic DNA. Translation: CAI18828.1. Different initiation.
    AL096773 Genomic DNA. Translation: CAI18830.1.
    CH471122 Genomic DNA. Translation: EAW56607.1.
    M60092 mRNA. Translation: AAA57281.1. Different initiation.
    AK314252 mRNA. Translation: BAG36918.1. Different initiation.
    AK291349 mRNA. Translation: BAF84038.1. Different initiation.
    CCDSiCCDS53349.1. [P23109-2]
    CCDS876.2. [P23109-1]
    PIRiI39444.
    RefSeqiNP_000027.2. NM_000036.2. [P23109-1]
    NP_001166097.1. NM_001172626.1. [P23109-2]
    UniGeneiHs.89570.

    Genome annotation databases

    EnsembliENST00000369538; ENSP00000358551; ENSG00000116748. [P23109-2]
    ENST00000520113; ENSP00000430075; ENSG00000116748. [P23109-1]
    GeneIDi270.
    KEGGihsa:270.
    UCSCiuc001efe.2. human. [P23109-1]
    uc001eff.2. human. [P23109-2]

    Polymorphism databases

    DMDMi384872309.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37931
    , M37920 , M37921 , M37922 , M37923 , M37924 , M37927 , M37928 , M37929 , M37930 Genomic DNA. Translation: AAG24258.1 . Different initiation.
    AL096773 Genomic DNA. Translation: CAI18828.1 . Different initiation.
    AL096773 Genomic DNA. Translation: CAI18830.1 .
    CH471122 Genomic DNA. Translation: EAW56607.1 .
    M60092 mRNA. Translation: AAA57281.1 . Different initiation.
    AK314252 mRNA. Translation: BAG36918.1 . Different initiation.
    AK291349 mRNA. Translation: BAF84038.1 . Different initiation.
    CCDSi CCDS53349.1. [P23109-2 ]
    CCDS876.2. [P23109-1 ]
    PIRi I39444.
    RefSeqi NP_000027.2. NM_000036.2. [P23109-1 ]
    NP_001166097.1. NM_001172626.1. [P23109-2 ]
    UniGenei Hs.89570.

    3D structure databases

    ProteinModelPortali P23109.
    SMRi P23109. Positions 225-775.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106767. 5 interactions.
    IntActi P23109. 5 interactions.
    STRINGi 9606.ENSP00000316520.

    Chemistry

    BindingDBi P23109.
    ChEMBLi CHEMBL2869.
    DrugBanki DB00131. Adenosine monophosphate.

    PTM databases

    PhosphoSitei P23109.

    Polymorphism databases

    DMDMi 384872309.

    Proteomic databases

    PaxDbi P23109.
    PRIDEi P23109.

    Protocols and materials databases

    DNASUi 270.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369538 ; ENSP00000358551 ; ENSG00000116748 . [P23109-2 ]
    ENST00000520113 ; ENSP00000430075 ; ENSG00000116748 . [P23109-1 ]
    GeneIDi 270.
    KEGGi hsa:270.
    UCSCi uc001efe.2. human. [P23109-1 ]
    uc001eff.2. human. [P23109-2 ]

    Organism-specific databases

    CTDi 270.
    GeneCardsi GC01M115215.
    H-InvDB HIX0199913.
    HGNCi HGNC:468. AMPD1.
    HPAi HPA026478.
    HPA028080.
    MIMi 102770. gene.
    615511. phenotype.
    neXtProti NX_P23109.
    Orphaneti 45. Adenosine monophosphate deaminase deficiency.
    PharmGKBi PA24776.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1816.
    HOGENOMi HOG000092200.
    HOVERGENi HBG050494.
    KOi K01490.
    OMAi NMTWMIQ.
    OrthoDBi EOG70ZZMQ.
    PhylomeDBi P23109.
    TreeFami TF300439.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00663 .
    Reactomei REACT_1923. Purine salvage.
    SABIO-RK P23109.

    Miscellaneous databases

    ChiTaRSi AMPD1. human.
    GeneWikii AMP_deaminase.
    GenomeRNAii 270.
    NextBioi 1061.
    PROi P23109.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23109.
    Bgeei P23109.
    CleanExi HS_AMPD1.
    Genevestigatori P23109.

    Family and domain databases

    InterProi IPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view ]
    PANTHERi PTHR11359. PTHR11359. 1 hit.
    Pfami PF00962. A_deaminase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001251. AMP_deaminase_met. 1 hit.
    TIGRFAMsi TIGR01429. AMP_deaminase. 1 hit.
    PROSITEi PS00485. A_DEAMINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the human and rat myoadenylate deaminase genes."
      Sabina R.L., Morisaki T., Clarke P., Eddy R., Shows T.B., Morton C.C., Holmes E.W.
      J. Biol. Chem. 265:9423-9433(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Molecular analysis of the myoadenylate deaminase deficiencies."
      Sabina R.L., Fishbein W.N., Pezeshkpour G., Clarke P.R., Holmes E.W.
      Neurology 42:170-179(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-780 (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-780 (ISOFORM 1).
      Tissue: Pericardium and Tongue.
    6. Cited for: VARIANT LEU-81.
    7. "First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient."
      Morisaki H., Higuchi I., Abe M., Osame M., Morisaki T.
      Hum. Mutat. 16:467-472(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MMDD TRP-421 AND HIS-458.
    8. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-666.

    Entry informationi

    Entry nameiAMPD1_HUMAN
    AccessioniPrimary (citable) accession number: P23109
    Secondary accession number(s): A8K5N4
    , B2RAM1, F2Z3B3, Q5TF00, Q5TF02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: April 18, 2012
    Last modified: October 1, 2014
    This is version 137 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

    Caution

    It is uncertain whether Met-1 or Met-34 is the initiator.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3