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P42357

- HUTH_HUMAN

UniProt

P42357 - HUTH_HUMAN

Protein

Histidine ammonia-lyase

Gene

HAL

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 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-histidine = urocanate + NH3.PROSITE-ProRule annotation

    Pathwayi

    GO - Molecular functioni

    1. histidine ammonia-lyase activity Source: UniProtKB-EC

    GO - Biological processi

    1. biosynthetic process Source: InterPro
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. histidine catabolic process Source: Reactome
    4. histidine catabolic process to glutamate and formamide Source: UniProtKB-UniPathway
    5. histidine catabolic process to glutamate and formate Source: UniProtKB-UniPathway
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Histidine metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01466-MONOMER.
    ReactomeiREACT_1249. Histidine catabolism.
    UniPathwayiUPA00379; UER00549.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidine ammonia-lyase (EC:4.3.1.3)
    Short name:
    Histidase
    Gene namesi
    Name:HAL
    Synonyms:HIS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:4806. HAL.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Histidinemia (HISTID) [MIM:235800]: Autosomal recessive disease characterized by increased histidine and histamine as well as decreased urocanic acid in body fluids.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti206 – 2061R → T in HISTID. 1 Publication
    VAR_022915
    Natural varianti208 – 2081R → L in HISTID. 1 Publication
    VAR_022916
    Natural varianti259 – 2591P → L in HISTID. 1 Publication
    VAR_022917
    Natural varianti322 – 3221R → P in HISTID. 1 Publication
    VAR_022918

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi235800. phenotype.
    Orphaneti2157. Histidinemia.
    PharmGKBiPA29181.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 657657Histidine ammonia-lyasePRO_0000161058Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki253 ↔ 2555-imidazolinone (Ala-Gly)By similarity
    Modified residuei254 – 25412,3-didehydroalanine (Ser)PROSITE-ProRule annotation
    Modified residuei396 – 3961PhosphothreonineBy similarity
    Modified residuei648 – 6481PhosphoserineBy similarity

    Post-translational modificationi

    Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP42357.
    PaxDbiP42357.
    PRIDEiP42357.

    PTM databases

    PhosphoSiteiP42357.

    Expressioni

    Gene expression databases

    ArrayExpressiP42357.
    BgeeiP42357.
    CleanExiHS_HAL.
    GenevestigatoriP42357.

    Organism-specific databases

    HPAiHPA038547.
    HPA038548.

    Interactioni

    Protein-protein interaction databases

    BioGridi109284. 1 interaction.
    STRINGi9606.ENSP00000261208.

    Structurei

    3D structure databases

    ProteinModelPortaliP42357.
    SMRiP42357. Positions 114-648.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PAL/histidase family.Curated

    Phylogenomic databases

    eggNOGiCOG2986.
    HOGENOMiHOG000237619.
    HOVERGENiHBG004509.
    InParanoidiP42357.
    KOiK01745.
    OMAiVHIRDEW.
    OrthoDBiEOG73RB9V.
    PhylomeDBiP42357.
    TreeFamiTF313824.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    InterProiIPR001106. Aromatic_Lyase.
    IPR024083. Fumarase/histidase_N.
    IPR005921. HutH.
    IPR008948. L-Aspartase-like.
    IPR022313. Phe/His_NH3-lyase_AS.
    [Graphical view]
    PfamiPF00221. Lyase_aromatic. 1 hit.
    [Graphical view]
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR01225. hutH. 1 hit.
    PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P42357-1) [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

    MPRYTVHVRG EWLAVPCQDA QLTVGWLGRE AVRRYIKNKP DNGGFTSVDD    50
    AHFLVRRCKG LGLLDNEDRL EVALENNEFV EVVIEGDAMS PDFIPSQPEG 100
    VYLYSKYREP EKYIELDGDR LTTEDLVNLG KGRYKIKLTP TAEKRVQKSR 150
    EVIDSIIKEK TVVYGITTGF GKFARTVIPI NKLQELQVNL VRSHSSGVGK 200
    PLSPERCRML LALRINVLAK GYSGISLETL KQVIEMFNAS CLPYVPEKGT 250
    VGASGDLAPL SHLALGLVGE GKMWSPKSGW ADAKYVLEAH GLKPVILKPK 300
    EGLALINGTQ MITSLGCEAV ERASAIARQA DIVAALTLEV LKGTTKAFDT 350
    DIHALRPHRG QIEVAFRFRS LLDSDHHPSE IAESHRFCDR VQDAYTLRCC 400
    PQVHGVVNDT IAFVKNIITT ELNSATDNPM VFANRGETVS GGNFHGEYPA 450
    KALDYLAIGI HELAAISERR IERLCNPSLS ELPAFLVAEG GLNSGFMIAH 500
    CTAAALVSEN KALCHPSSVD SLSTSAATED HVSMGGWAAR KALRVIEHVE 550
    QVLAIELLAA CQGIEFLRPL KTTTPLEKVY DLVRSVVRPW IKDRFMAPDI 600
    EAAHRLLLEQ KVWEVAAPYI EKYRMEHIPE SRPLSPTAFS LQFLHKKSTK 650
    IPESEDL 657
    Length:657
    Mass (Da):72,698
    Last modified:November 1, 1995 - v1
    Checksum:i6B9FF97C066FB8F1
    GO
    Isoform 2 (identifier: P42357-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         589-657: PWIKDRFMAPDIEAAHRLLLEQKVWEVAAPYIEKYRMEHIPESRPLSPTAFSLQFLHKKSTKIPESEDL → FGK

    Note: No experimental confirmation available.

    Show »
    Length:591
    Mass (Da):64,888
    Checksum:iDEBBCF642F5BC7DB
    GO
    Isoform 3 (identifier: P42357-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-208: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:449
    Mass (Da):49,123
    Checksum:iDD7DB9B250E4AFDA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti549 – 5491V → M in BAG64570. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti206 – 2061R → T in HISTID. 1 Publication
    VAR_022915
    Natural varianti208 – 2081R → L in HISTID. 1 Publication
    VAR_022916
    Natural varianti259 – 2591P → L in HISTID. 1 Publication
    VAR_022917
    Natural varianti322 – 3221R → P in HISTID. 1 Publication
    VAR_022918
    Natural varianti439 – 4391V → I.4 Publications
    Corresponds to variant rs7297245 [ dbSNP | Ensembl ].
    VAR_006042

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 208208Missing in isoform 3. 1 PublicationVSP_046003Add
    BLAST
    Alternative sequencei589 – 65769PWIKD…ESEDL → FGK in isoform 2. 1 PublicationVSP_044704Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16626 mRNA. Translation: BAA04047.1.
    AB042217 Genomic DNA. Translation: BAB61863.1.
    AK298736 mRNA. Translation: BAG60883.1.
    AK303544 mRNA. Translation: BAG64570.1.
    AC007298 Genomic DNA. No translation available.
    AC126174 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97556.1.
    BC096097 mRNA. Translation: AAH96097.1.
    BC096098 mRNA. Translation: AAH96098.1.
    BC096099 mRNA. Translation: AAH96099.1.
    CCDSiCCDS58264.1. [P42357-3]
    CCDS58265.1. [P42357-2]
    CCDS9058.1. [P42357-1]
    PIRiS43415.
    RefSeqiNP_001245262.1. NM_001258333.1. [P42357-3]
    NP_001245263.1. NM_001258334.1. [P42357-2]
    NP_002099.1. NM_002108.3. [P42357-1]
    UniGeneiHs.190783.
    Hs.742210.

    Genome annotation databases

    EnsembliENST00000261208; ENSP00000261208; ENSG00000084110. [P42357-1]
    ENST00000538703; ENSP00000440861; ENSG00000084110. [P42357-2]
    ENST00000541929; ENSP00000446364; ENSG00000084110. [P42357-3]
    GeneIDi3034.
    KEGGihsa:3034.
    UCSCiuc001tem.2. human. [P42357-1]

    Polymorphism databases

    DMDMi1170423.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16626 mRNA. Translation: BAA04047.1 .
    AB042217 Genomic DNA. Translation: BAB61863.1 .
    AK298736 mRNA. Translation: BAG60883.1 .
    AK303544 mRNA. Translation: BAG64570.1 .
    AC007298 Genomic DNA. No translation available.
    AC126174 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97556.1 .
    BC096097 mRNA. Translation: AAH96097.1 .
    BC096098 mRNA. Translation: AAH96098.1 .
    BC096099 mRNA. Translation: AAH96099.1 .
    CCDSi CCDS58264.1. [P42357-3 ]
    CCDS58265.1. [P42357-2 ]
    CCDS9058.1. [P42357-1 ]
    PIRi S43415.
    RefSeqi NP_001245262.1. NM_001258333.1. [P42357-3 ]
    NP_001245263.1. NM_001258334.1. [P42357-2 ]
    NP_002099.1. NM_002108.3. [P42357-1 ]
    UniGenei Hs.190783.
    Hs.742210.

    3D structure databases

    ProteinModelPortali P42357.
    SMRi P42357. Positions 114-648.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109284. 1 interaction.
    STRINGi 9606.ENSP00000261208.

    Chemistry

    ChEMBLi CHEMBL4003.
    DrugBanki DB00117. L-Histidine.

    PTM databases

    PhosphoSitei P42357.

    Polymorphism databases

    DMDMi 1170423.

    Proteomic databases

    MaxQBi P42357.
    PaxDbi P42357.
    PRIDEi P42357.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261208 ; ENSP00000261208 ; ENSG00000084110 . [P42357-1 ]
    ENST00000538703 ; ENSP00000440861 ; ENSG00000084110 . [P42357-2 ]
    ENST00000541929 ; ENSP00000446364 ; ENSG00000084110 . [P42357-3 ]
    GeneIDi 3034.
    KEGGi hsa:3034.
    UCSCi uc001tem.2. human. [P42357-1 ]

    Organism-specific databases

    CTDi 3034.
    GeneCardsi GC12M096366.
    HGNCi HGNC:4806. HAL.
    HPAi HPA038547.
    HPA038548.
    MIMi 235800. phenotype.
    609457. gene.
    neXtProti NX_P42357.
    Orphaneti 2157. Histidinemia.
    PharmGKBi PA29181.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2986.
    HOGENOMi HOG000237619.
    HOVERGENi HBG004509.
    InParanoidi P42357.
    KOi K01745.
    OMAi VHIRDEW.
    OrthoDBi EOG73RB9V.
    PhylomeDBi P42357.
    TreeFami TF313824.

    Enzyme and pathway databases

    UniPathwayi UPA00379 ; UER00549 .
    BioCyci MetaCyc:HS01466-MONOMER.
    Reactomei REACT_1249. Histidine catabolism.

    Miscellaneous databases

    GeneWikii Histidine_ammonia-lyase.
    GenomeRNAii 3034.
    NextBioi 12010.
    PROi P42357.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42357.
    Bgeei P42357.
    CleanExi HS_HAL.
    Genevestigatori P42357.

    Family and domain databases

    Gene3Di 1.10.275.10. 1 hit.
    InterProi IPR001106. Aromatic_Lyase.
    IPR024083. Fumarase/histidase_N.
    IPR005921. HutH.
    IPR008948. L-Aspartase-like.
    IPR022313. Phe/His_NH3-lyase_AS.
    [Graphical view ]
    Pfami PF00221. Lyase_aromatic. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR01225. hutH. 1 hit.
    PROSITEi PS00488. PAL_HISTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a cDNA encoding human histidase."
      Suchi M., Harada N., Wada Y., Takagi Y.
      Biochim. Biophys. Acta 1216:293-295(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Molecular cloning and structural characterization of the human histidase gene (HAL)."
      Suchi M., Sano H., Mizuno H., Wada Y.
      Genomics 29:98-104(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-439.
    3. "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] (ISOFORMS 2 AND 3), VARIANT ILE-439.
      Tissue: Thymus.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-439.
    6. "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] (ISOFORM 1), VARIANT ILE-439.
    7. "Molecular characterization of histidinemia: identification of four missense mutations in the histidase gene."
      Kawai Y., Moriyama A., Asai K., Coleman-Campbell C.M., Sumi S., Morishita H., Suchi M.
      Hum. Genet. 116:340-346(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HISTID THR-206; LEU-208; LEU-259 AND PRO-322.

    Entry informationi

    Entry nameiHUTH_HUMAN
    AccessioniPrimary (citable) accession number: P42357
    Secondary accession number(s): B4DQC1
    , B4E0V8, F5GXF2, F5H1U5, Q4VB92, Q4VB93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 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 12
      Human chromosome 12: 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