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Q9UHJ3

- SMBT1_HUMAN

UniProt

Q9UHJ3 - SMBT1_HUMAN

Protein

Scm-like with four MBT domains protein 1

Gene

SFMBT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic progenitor cells via interaction with MYOD1. Interaction with MYOD1 leads to the recruitment of associated corepressors and silencing of MYOD1 target genes. Part of the SLC complex in germ cells, where it may play a role during spermatogenesis.3 Publications

    GO - Molecular functioni

    1. histone binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. chromatin modification Source: UniProtKB-KW
    3. negative regulation of muscle organ development Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. spermatogenesis Source: UniProtKB-KW
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Differentiation, Spermatogenesis, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Scm-like with four MBT domains protein 1
    Short name:
    hSFMBT
    Alternative name(s):
    Renal ubiquitous protein 1
    Gene namesi
    Name:SFMBT1
    Synonyms:RU1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:20255. SFMBT1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi173 – 1731F → A: Reduced histone-binding. 1 Publication
    Mutagenesisi180 – 1801W → A: Abolishes histone-binding. 1 Publication
    Mutagenesisi196 – 1961Y → A: Reduced histone-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134898464.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 866866Scm-like with four MBT domains protein 1PRO_0000071966Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei775 – 7751Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UHJ3.
    PaxDbiQ9UHJ3.
    PRIDEiQ9UHJ3.

    PTM databases

    PhosphoSiteiQ9UHJ3.

    Expressioni

    Tissue specificityi

    Expressed in all cell lines and normal tissues tested, including the thymus.1 Publication

    Gene expression databases

    ArrayExpressiQ9UHJ3.
    BgeeiQ9UHJ3.
    CleanExiHS_SFMBT1.
    GenevestigatoriQ9UHJ3.

    Organism-specific databases

    HPAiHPA036153.

    Interactioni

    Subunit structurei

    Interacts with MYOD1 By similarity. Component of the SLC (SFMBT1-LSD1-CoREST) corepressor complex, which also contains KDM1A/LSD1 and RCOR1/CoREST. Interacts with KDM1A/LSD1 and RCOR1/CoREST.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST3H3Q166954EBI-747398,EBI-358900

    Protein-protein interaction databases

    BioGridi119553. 8 interactions.
    IntActiQ9UHJ3. 10 interactions.
    MINTiMINT-1448033.
    STRINGi9606.ENSP00000350789.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UHJ3.
    SMRiQ9UHJ3. Positions 14-530, 796-857.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati20 – 120101MBT 1Add
    BLAST
    Repeati128 – 232105MBT 2Add
    BLAST
    Repeati242 – 348107MBT 3Add
    BLAST
    Repeati356 – 45398MBT 4Add
    BLAST
    Domaini796 – 86469SAMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni34 – 429Antigenic epitope

    Domaini

    The MBT repeats mediate binding to histones tails; however, in contrast to other MBT repeats, does not bind specific histone lysine modifications. The MBT repeats lack the conserved Asp and aromatic cage at conserved positions (PubMed:23592795).1 Publication

    Sequence similaritiesi

    Contains 4 MBT repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG316861.
    HOGENOMiHOG000004859.
    HOVERGENiHBG085238.
    InParanoidiQ9UHJ3.
    OMAiKCSENCS.
    OrthoDBiEOG780RKN.
    PhylomeDBiQ9UHJ3.
    TreeFamiTF316498.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    InterProiIPR021987. DUF3588.
    IPR004092. Mbt.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    [Graphical view]
    PfamiPF12140. DUF3588. 1 hit.
    PF02820. MBT. 4 hits.
    PF00536. SAM_1. 1 hit.
    [Graphical view]
    SMARTiSM00561. MBT. 4 hits.
    SM00454. SAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    PROSITEiPS51079. MBT. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UHJ3-1) [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

    MNGEQQLDAD AGSGMEEVEL SWEDYLEETG STAVPYGSFK HVDTRLQNGF    50
    APGMKLEVAV RTDPETYWVA TVITTCEQLL LLRYDGYGED RRADFWCDIR 100
    KADLYPIGWC EQNKKTLEAP EGIRDKVSDW DEFLRQTLIG ACSPPVPLLE 150
    GLRNGRNPLD LIAPGSRLEC QAFQDSLSTW IVTVVENIGG RLKLRYEGLE 200
    SSDNYEHWLY YLDPFLHHVG WAAQQGYELQ PPSAIRHLKN EAEWQEILAK 250
    VKEEEEEPLP SYLFKDKQVI GIHTFSVNMK LEAVDPWSPF GISPATVVKV 300
    FDEKYFLVEM DDLRPENHAR RSFVCHADSP GIFPVQWSLK NGLHISPPPG 350
    YPSQDFDWAD YLKQCGAEAA PQRCFPPLIS EHEFKENMKL EAVNPILPEE 400
    VCVATITAVR GSYLWLQLEG SKKPIPECIV SVESMDIFPL GWCETNGHPL 450
    STPRRARVYK QRKIAVVQPE KQVPSSRTVH EGLRNQELNS TESVMINGKY 500
    CCPKIYFNHR CFSGPYLNKG RIAELPQCVG PGNCVLVLRE VLTLLINAAY 550
    KPSRVLRELQ LDKDSVWHGC GEVLKAKYKG KSYRATVEIV KTADRVTEFC 600
    RQTCIKLECC PNLFGPRMVL DKCSENCSVL TKTKYTHYYG KKKNKRIGRP 650
    PGGHSNLACA LKKASKRRKR RKNVFVHKKK RSSASVDNTP AGSPQGSGGE 700
    DEDDPDEGDD DSLSEGSTSE QQDELQEESE MSEKKSCSSS PTQSEISTSL 750
    PPDRQRRKRE LRTFSFSDDE NKPPSPKEIR IEVAERLHLD SNPLKWSVAD 800
    VVRFIRSTDC APLARIFLDQ EIDGQALLLL TLPTVQECMD LKLGPAIKLC 850
    HHIERIKFAF YEQFAN 866
    Length:866
    Mass (Da):98,141
    Last modified:June 7, 2005 - v2
    Checksum:iDCE67BF35C413EB7
    GO
    Isoform 2 (identifier: Q9UHJ3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         778-820: Missing.

    Show »
    Length:823
    Mass (Da):93,166
    Checksum:i896FEF37B9FCCECF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti642 – 6421K → R in AAF19794. (PubMed:10661410)Curated
    Sequence conflicti767 – 7671S → F in AAF19794. (PubMed:10661410)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei778 – 82043Missing in isoform 2. 1 PublicationVSP_013857Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF168132 mRNA. Translation: AAF19794.1.
    AB189472 mRNA. Translation: BAE43835.1.
    AK313965 mRNA. Translation: BAG36680.1.
    AC099667 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65272.1.
    BC014614 mRNA. Translation: AAH14614.1.
    AL080140 mRNA. Translation: CAB45734.1.
    CCDSiCCDS2867.1. [Q9UHJ3-1]
    PIRiT12525.
    RefSeqiNP_057413.2. NM_016329.3. [Q9UHJ3-1]
    XP_005265278.1. XM_005265221.1. [Q9UHJ3-1]
    XP_006713266.1. XM_006713203.1. [Q9UHJ3-1]
    XP_006713267.1. XM_006713204.1. [Q9UHJ3-1]
    UniGeneiHs.343679.

    Genome annotation databases

    EnsembliENST00000394752; ENSP00000378235; ENSG00000163935. [Q9UHJ3-1]
    GeneIDi51460.
    KEGGihsa:51460.
    UCSCiuc003dgh.3. human. [Q9UHJ3-1]
    uc010hmr.3. human. [Q9UHJ3-2]

    Polymorphism databases

    DMDMi67461585.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF168132 mRNA. Translation: AAF19794.1 .
    AB189472 mRNA. Translation: BAE43835.1 .
    AK313965 mRNA. Translation: BAG36680.1 .
    AC099667 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65272.1 .
    BC014614 mRNA. Translation: AAH14614.1 .
    AL080140 mRNA. Translation: CAB45734.1 .
    CCDSi CCDS2867.1. [Q9UHJ3-1 ]
    PIRi T12525.
    RefSeqi NP_057413.2. NM_016329.3. [Q9UHJ3-1 ]
    XP_005265278.1. XM_005265221.1. [Q9UHJ3-1 ]
    XP_006713266.1. XM_006713203.1. [Q9UHJ3-1 ]
    XP_006713267.1. XM_006713204.1. [Q9UHJ3-1 ]
    UniGenei Hs.343679.

    3D structure databases

    ProteinModelPortali Q9UHJ3.
    SMRi Q9UHJ3. Positions 14-530, 796-857.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119553. 8 interactions.
    IntActi Q9UHJ3. 10 interactions.
    MINTi MINT-1448033.
    STRINGi 9606.ENSP00000350789.

    Chemistry

    ChEMBLi CHEMBL1764944.

    PTM databases

    PhosphoSitei Q9UHJ3.

    Polymorphism databases

    DMDMi 67461585.

    Proteomic databases

    MaxQBi Q9UHJ3.
    PaxDbi Q9UHJ3.
    PRIDEi Q9UHJ3.

    Protocols and materials databases

    DNASUi 51460.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394752 ; ENSP00000378235 ; ENSG00000163935 . [Q9UHJ3-1 ]
    GeneIDi 51460.
    KEGGi hsa:51460.
    UCSCi uc003dgh.3. human. [Q9UHJ3-1 ]
    uc010hmr.3. human. [Q9UHJ3-2 ]

    Organism-specific databases

    CTDi 51460.
    GeneCardsi GC03M052913.
    HGNCi HGNC:20255. SFMBT1.
    HPAi HPA036153.
    MIMi 607319. gene.
    neXtProti NX_Q9UHJ3.
    PharmGKBi PA134898464.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG316861.
    HOGENOMi HOG000004859.
    HOVERGENi HBG085238.
    InParanoidi Q9UHJ3.
    OMAi KCSENCS.
    OrthoDBi EOG780RKN.
    PhylomeDBi Q9UHJ3.
    TreeFami TF316498.

    Miscellaneous databases

    ChiTaRSi SFMBT1. human.
    GenomeRNAii 51460.
    NextBioi 55079.
    PROi Q9UHJ3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHJ3.
    Bgeei Q9UHJ3.
    CleanExi HS_SFMBT1.
    Genevestigatori Q9UHJ3.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    InterProi IPR021987. DUF3588.
    IPR004092. Mbt.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    [Graphical view ]
    Pfami PF12140. DUF3588. 1 hit.
    PF02820. MBT. 4 hits.
    PF00536. SAM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00561. MBT. 4 hits.
    SM00454. SAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    PROSITEi PS51079. MBT. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Processing of some antigens by the standard proteasome but not by the immunoproteasome results in poor presentation by dendritic cells."
      Morel S., Levy F., Burlet-Schiltz O., Brasseur F., Probst-Kepper M., Peitrequin A.L., Monsarrat B., Van Velthoven R., Cerottini J.C., Boon T., Gairin J.E., Van den Eynde B.J.
      Immunity 12:107-117(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    2. "SFMBT and H-L(3)MBT interact with each other and regulate HOX expression and cell proliferation."
      Usui H., Ichikawa T., Kobayashi K., Kumanishi T.
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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] (ISOFORM 1).
      Tissue: Testis.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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).
      Tissue: Muscle.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-866 (ISOFORM 2).
      Tissue: Testis.
    8. "Human SFMBT is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3."
      Wu S., Trievel R.C., Rice J.C.
      FEBS Lett. 581:3289-3296(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HISTONES.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "SFMBT1 functions with LSD1 to regulate expression of canonical histone genes and chromatin-related factors."
      Zhang J., Bonasio R., Strino F., Kluger Y., Holloway J.K., Modzelewski A.J., Cohen P.E., Reinberg D.
      Genes Dev. 27:749-766(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KDM1A AND RCOR1, IDENTIFICATION IN THE SLC COMPLEX, MUTAGENESIS OF PHE-173; TRP-180 AND TYR-196.
    11. "Proteomic and functional analyses reveal the role of chromatin reader SFMBT1 in regulating epigenetic silencing and the myogenic gene program."
      Lin S., Shen H., Li J.L., Tang S., Gu Y., Chen Z., Hu C., Rice J.C., Lu J., Wu L.
      J. Biol. Chem. 288:6238-6247(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN VARIOUS COREPRESSOR COMPLEX.

    Entry informationi

    Entry nameiSMBT1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHJ3
    Secondary accession number(s): Q402F7, Q96C73, Q9Y4Q9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 106 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 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3