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Q96EN8

- MOCOS_HUMAN

UniProt

Q96EN8 - MOCOS_HUMAN

Protein

Molybdenum cofactor sulfurase

Gene

MOCOS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime.1 PublicationUniRule annotation

    Catalytic activityi

    Molybdenum cofactor + L-cysteine + 2 H+ = thio-molybdenum cofactor + L-alanine + H2O.UniRule annotation

    Cofactori

    Pyridoxal phosphate.UniRule annotation

    Kineticsi

    1. KM=15 µM for benzamidoxime1 Publication

    Vmax=0.24 nmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei424 – 4241UniRule annotation

    GO - Molecular functioni

    1. lyase activity Source: UniProtKB-HAMAP
    2. molybdenum ion binding Source: UniProtKB-HAMAP
    3. Mo-molybdopterin cofactor sulfurase activity Source: UniProtKB
    4. pyridoxal phosphate binding Source: UniProtKB-HAMAP
    5. transferase activity Source: UniProtKB-KW

    GO - Biological processi

    1. molybdopterin cofactor biosynthetic process Source: Reactome
    2. molybdopterin cofactor metabolic process Source: UniProtKB
    3. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP
    4. small molecule metabolic process Source: Reactome
    5. vitamin metabolic process Source: Reactome
    6. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    ReactomeiREACT_25073. Molybdenum cofactor biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Molybdenum cofactor sulfuraseUniRule annotation (EC:2.8.1.9UniRule annotation)
    Short name:
    MCSUniRule annotation
    Short name:
    MOSUniRule annotation
    Short name:
    MoCo sulfuraseUniRule annotation
    Short name:
    hMCS
    Alternative name(s):
    Molybdenum cofactor sulfurtransferaseUniRule annotation
    Gene namesi
    Name:MOCOSUniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:18234. MOCOS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Xanthinuria 2 (XU2) [MIM:603592]: A disorder characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. In addition, patients suffering of xanthinuria 2 cannot metabolize allopurinol into oxypurinol due to dual deficiency of xanthine dehydrogenase and aldehyde oxidase.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571A → P in XU2. 1 Publication
    VAR_027528
    Natural varianti294 – 2941T → I in XU2. 1 Publication
    VAR_027533
    Natural varianti776 – 7761R → C in XU2. 1 Publication
    VAR_045899

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi603592. phenotype.
    Orphaneti93602. Xanthinuria type II.
    PharmGKBiPA134964534.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 888888Molybdenum cofactor sulfurasePRO_0000249952Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei264 – 2641N6-(pyridoxal phosphate)lysineUniRule annotation
    Modified residuei528 – 5281Phosphoserine2 Publications
    Modified residuei530 – 5301Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96EN8.
    PaxDbiQ96EN8.
    PRIDEiQ96EN8.

    PTM databases

    PhosphoSiteiQ96EN8.

    Expressioni

    Gene expression databases

    BgeeiQ96EN8.
    CleanExiHS_MOCOS.
    GenevestigatoriQ96EN8.

    Organism-specific databases

    HPAiHPA039412.
    HPA047958.

    Interactioni

    Protein-protein interaction databases

    BioGridi120363. 2 interactions.
    IntActiQ96EN8. 2 interactions.
    STRINGi9606.ENSP00000261326.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96EN8.
    SMRiQ96EN8. Positions 51-421, 591-706.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini706 – 867162MOSCUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily.UniRule annotation
    Contains 1 MOSC domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3217.
    HOGENOMiHOG000029698.
    HOVERGENiHBG081980.
    InParanoidiQ96EN8.
    KOiK15631.
    OMAiRCGDDHD.
    OrthoDBiEOG7ZKS98.
    PhylomeDBiQ96EN8.
    TreeFamiTF105761.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_03050. MOCOS.
    InterProiIPR000192. Aminotrans_V/Cys_dSase.
    IPR005302. MoCF_Sase_C.
    IPR028886. MoCo_sulfurase.
    IPR005303. MOSC_N.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR011037. Pyrv_Knase-like_insert_dom.
    [Graphical view]
    PfamiPF00266. Aminotran_5. 1 hit.
    PF03473. MOSC. 1 hit.
    PF03476. MOSC_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50800. SSF50800. 1 hit.
    SSF53383. SSF53383. 2 hits.
    PROSITEiPS51340. MOSC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96EN8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGAAAESGR ELWTFAGSRD PSAPRLAYGY GPGSLRELRA REFSRLAGTV    50
    YLDHAGATLF SQSQLESFTS DLMENTYGNP HSQNISSKLT HDTVEQVRYR 100
    ILAHFHTTAE DYTVIFTAGS TAALKLVAEA FPWVSQGPES SGSRFCYLTD 150
    SHTSVVGMRN VTMAINVIST PVRPEDLWSA EERSASASNP DCQLPHLFCY 200
    PAQSNFSGVR YPLSWIEEVK SGRLHPVSTP GKWFVLLDAA SYVSTSPLDL 250
    SAHQADFVPI SFYKIFGFPT GLGALLVHNR AAPLLRKTYF GGGTASAYLA 300
    GEDFYIPRQS VAQRFEDGTI SFLDVIALKH GFDTLERLTG GMENIKQHTF 350
    TLAQYTYVAL SSLQYPNGAP VVRIYSDSEF SSPEVQGPII NFNVLDDKGN 400
    IIGYSQVDKM ASLYNIHLRT GCFCNTGACQ RHLGISNEMV RKHFQAGHVC 450
    GDNMDLIDGQ PTGSVRISFG YMSTLDDVQA FLRFIIDTRL HSSGDWPVPQ 500
    AHADTGETGA PSADSQADVI PAVMGRRSLS PQEDALTGSR VWNNSSTVNA 550
    VPVAPPVCDV ARTQPTPSEK AAGVLEGALG PHVVTNLYLY PIKSCAAFEV 600
    TRWPVGNQGL LYDRSWMVVN HNGVCLSQKQ EPRLCLIQPF IDLRQRIMVI 650
    KAKGMEPIEV PLEENSERTQ IRQSRVCADR VSTYDCGEKI SSWLSTFFGR 700
    PCHLIKQSSN SQRNAKKKHG KDQLPGTMAT LSLVNEAQYL LINTSSILEL 750
    HRQLNTSDEN GKEELFSLKD LSLRFRANII INGKRAFEEE KWDEISIGSL 800
    RFQVLGPCHR CQMICIDQQT GQRNQHVFQK LSESRETKVN FGMYLMHASL 850
    DLSSPCFLSV GSQVLPVLKE NVEGHDLPAS EKHQDVTS 888
    Length:888
    Mass (Da):98,120
    Last modified:May 18, 2010 - v2
    Checksum:i07DB9457516E8C06
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191G → E in BAD96606. (PubMed:14702039)Curated
    Sequence conflicti689 – 6891K → E in BAD96606. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571A → P in XU2. 1 Publication
    VAR_027528
    Natural varianti120 – 1201S → N.
    Corresponds to variant rs3744900 [ dbSNP | Ensembl ].
    VAR_027529
    Natural varianti170 – 1701T → I.2 Publications
    Corresponds to variant rs623053 [ dbSNP | Ensembl ].
    VAR_027530
    Natural varianti184 – 1841S → G.3 Publications
    Corresponds to variant rs540967 [ dbSNP | Ensembl ].
    VAR_027531
    Natural varianti225 – 2251H → R.4 Publications
    Corresponds to variant rs623558 [ dbSNP | Ensembl ].
    VAR_027532
    Natural varianti294 – 2941T → I in XU2. 1 Publication
    VAR_027533
    Natural varianti358 – 3581V → M.3 Publications
    Corresponds to variant rs678560 [ dbSNP | Ensembl ].
    VAR_027534
    Natural varianti495 – 4951D → N.
    Corresponds to variant rs8088347 [ dbSNP | Ensembl ].
    VAR_027535
    Natural varianti541 – 5411V → L.
    Corresponds to variant rs672924 [ dbSNP | Ensembl ].
    VAR_027536
    Natural varianti703 – 7031H → N.2 Publications
    Corresponds to variant rs594445 [ dbSNP | Ensembl ].
    VAR_027537
    Natural varianti776 – 7761R → C in XU2. 1 Publication
    VAR_045899
    Natural varianti867 – 8671V → A.
    Corresponds to variant rs1057251 [ dbSNP | Ensembl ].
    VAR_027538

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000740 mRNA. Translation: BAA91353.1.
    AK222886 mRNA. Translation: BAD96606.1.
    AC023043 Genomic DNA. No translation available.
    BC012079 mRNA. Translation: AAH12079.1.
    AL834481 mRNA. Translation: CAD39140.1.
    CCDSiCCDS11919.1.
    PIRiJC7680.
    RefSeqiNP_060417.2. NM_017947.2.
    UniGeneiHs.405028.

    Genome annotation databases

    EnsembliENST00000261326; ENSP00000261326; ENSG00000075643.
    GeneIDi55034.
    KEGGihsa:55034.
    UCSCiuc002kzq.4. human.

    Polymorphism databases

    DMDMi296438294.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000740 mRNA. Translation: BAA91353.1 .
    AK222886 mRNA. Translation: BAD96606.1 .
    AC023043 Genomic DNA. No translation available.
    BC012079 mRNA. Translation: AAH12079.1 .
    AL834481 mRNA. Translation: CAD39140.1 .
    CCDSi CCDS11919.1.
    PIRi JC7680.
    RefSeqi NP_060417.2. NM_017947.2.
    UniGenei Hs.405028.

    3D structure databases

    ProteinModelPortali Q96EN8.
    SMRi Q96EN8. Positions 51-421, 591-706.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120363. 2 interactions.
    IntActi Q96EN8. 2 interactions.
    STRINGi 9606.ENSP00000261326.

    PTM databases

    PhosphoSitei Q96EN8.

    Polymorphism databases

    DMDMi 296438294.

    Proteomic databases

    MaxQBi Q96EN8.
    PaxDbi Q96EN8.
    PRIDEi Q96EN8.

    Protocols and materials databases

    DNASUi 55034.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261326 ; ENSP00000261326 ; ENSG00000075643 .
    GeneIDi 55034.
    KEGGi hsa:55034.
    UCSCi uc002kzq.4. human.

    Organism-specific databases

    CTDi 55034.
    GeneCardsi GC18P033767.
    H-InvDB HIX0202662.
    HGNCi HGNC:18234. MOCOS.
    HPAi HPA039412.
    HPA047958.
    MIMi 603592. phenotype.
    613274. gene.
    neXtProti NX_Q96EN8.
    Orphaneti 93602. Xanthinuria type II.
    PharmGKBi PA134964534.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3217.
    HOGENOMi HOG000029698.
    HOVERGENi HBG081980.
    InParanoidi Q96EN8.
    KOi K15631.
    OMAi RCGDDHD.
    OrthoDBi EOG7ZKS98.
    PhylomeDBi Q96EN8.
    TreeFami TF105761.

    Enzyme and pathway databases

    Reactomei REACT_25073. Molybdenum cofactor biosynthesis.

    Miscellaneous databases

    GeneWikii MOCOS.
    GenomeRNAii 55034.
    NextBioi 58459.
    PROi Q96EN8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96EN8.
    CleanExi HS_MOCOS.
    Genevestigatori Q96EN8.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPi MF_03050. MOCOS.
    InterProi IPR000192. Aminotrans_V/Cys_dSase.
    IPR005302. MoCF_Sase_C.
    IPR028886. MoCo_sulfurase.
    IPR005303. MOSC_N.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR011037. Pyrv_Knase-like_insert_dom.
    [Graphical view ]
    Pfami PF00266. Aminotran_5. 1 hit.
    PF03473. MOSC. 1 hit.
    PF03476. MOSC_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50800. SSF50800. 1 hit.
    SSF53383. SSF53383. 2 hits.
    PROSITEi PS51340. MOSC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mutation of human molybdenum cofactor sulfurase gene is responsible to classical xanthinuria type II."
      Ichida K., Matsumura T., Sakuma R., Hosoya T., Nishino T.
      Biochem. Biophys. Res. Commun. 282:1194-1200(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN XU2, VARIANTS ARG-225 AND ASN-703.
    2. "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], VARIANTS ILE-170; GLY-184; ARG-225; MET-358 AND ASN-703.
      Tissue: Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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], VARIANTS ILE-170; GLY-184; ARG-225 AND MET-358.
      Tissue: Lung.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-888, VARIANTS ILE-170 GLY-184; ARG-225 AND MET-358.
      Tissue: Melanoma.
    6. "Identification of the missing component in the mitochondrial benzamidoxime prodrug converting system as a novel molybdenum enzyme."
      Havemeyer A., Bittner F., Wollers S., Mendel R., Kunze T., Clement B.
      J. Biol. Chem. 281:34796-34802(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Classical xanthinuria type 2 associated with a missense mutation in HMCS, the gene encoding molybdenum cofactor sulfurase."
      Finckh U., Haddad M., Lukacs Z., Wagener C., Gal A.
      (In) EUREGIO congress of clinical chemistry and laboratory medicine, pp.36-37, Aachen (2003)
      Cited for: VARIANT XU2 ILE-294.
    11. "Identification of a new point mutation in the human molybdenum cofactor sulferase gene that is responsible for xanthinuria type II."
      Yamamoto T., Moriwaki Y., Takahashi S., Tsutsumi Z., Tuneyoshi K., Matsui K., Cheng J., Hada T.
      Metabolism 52:1501-1504(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XU2 PRO-57.
    12. "Identification and characterization of the first mutation (Arg776Cys) in the C-terminal domain of the human molybdenum cofactor sulfurase (HMCS) associated with type II classical xanthinuria."
      Peretz H., Naamati M.S., Levartovsky D., Lagziel A., Shani E., Horn I., Shalev H., Landau D.
      Mol. Genet. Metab. 91:23-29(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XU2 CYS-776.

    Entry informationi

    Entry nameiMOCOS_HUMAN
    AccessioniPrimary (citable) accession number: Q96EN8
    Secondary accession number(s): Q53GP5, Q8N3A4, Q9NWM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 105 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 18
      Human chromosome 18: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3