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Q96GM5

- SMRD1_HUMAN

UniProt

Q96GM5 - SMRD1_HUMAN

Protein

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1

Gene

SMARCD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (26 May 2009)
      Previous versions | rss
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    Functioni

    Involved in chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth By similarity. Has a strong influence on the Vitamin D-mediated transcriptional activity from an enhancer Vitamin D receptor element (VDRE). May be a link between mammalian SWI-SNF-like chromatin remodeling complexes and the vitamin D receptor (VDR) heterodimer. Mediates critical interactions between nuclear receptors and the BRG1/SMARCA4 chromatin-remodeling complex for transactivation. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene.By similarity4 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein complex scaffold Source: UniProtKB
    3. transcription coactivator activity Source: BHF-UCL

    GO - Biological processi

    1. chromatin-mediated maintenance of transcription Source: UniProtKB
    2. chromatin remodeling Source: UniProtKB
    3. nervous system development Source: UniProtKB-KW
    4. nucleosome disassembly Source: BHF-UCL
    5. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Neurogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
    Alternative name(s):
    60 kDa BRG-1/Brm-associated factor subunit A
    BRG1-associated factor 60A
    Short name:
    BAF60A
    SWI/SNF complex 60 kDa subunit
    Gene namesi
    Name:SMARCD1Imported
    Synonyms:BAF60A1 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:11106. SMARCD1.

    Subcellular locationi

    Nucleus 1 PublicationCurated

    GO - Cellular componenti

    1. nBAF complex Source: UniProtKB
    2. npBAF complex Source: UniProtKB
    3. SWI/SNF complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35956.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 515515SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1PRO_0000071983Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei223 – 2231N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ96GM5.
    PaxDbiQ96GM5.
    PRIDEiQ96GM5.

    PTM databases

    PhosphoSiteiQ96GM5.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested, including brain, heart, kidney, liver, lung, muscle, pancreas and placenta.1 Publication

    Gene expression databases

    ArrayExpressiQ96GM5.
    BgeeiQ96GM5.
    CleanExiHS_SMARCD1.
    GenevestigatoriQ96GM5.

    Organism-specific databases

    HPAiHPA004101.

    Interactioni

    Subunit structurei

    Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Specifically interacts with the VDR heterodimer complex. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with ESR1, NR3C1, NR1H4, PGR, SMARCA4, SMARCC1 and SMARCC2. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Nr3c1P065362EBI-358489,EBI-1187143From a different organism.
    SMARCA4P515327EBI-358489,EBI-302489
    SMARCC1Q929223EBI-358489,EBI-355653

    Protein-protein interaction databases

    BioGridi112486. 75 interactions.
    DIPiDIP-33390N.
    IntActiQ96GM5. 43 interactions.
    MINTiMINT-1144212.
    STRINGi9606.ENSP00000378414.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96GM5.
    SMRiQ96GM5. Positions 291-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini291 – 390100SWIBAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 167125Interaction with ESR1, NR1H4, NR3C1, PGR and SMARCA4Add
    BLAST
    Regioni168 – 474307Interaction with SMARCC1 and SMARCC2Add
    BLAST
    Regioni180 – 515336Necessary for GR/NR3C1-mediated remodeling and transcription from chromatin; required for GR/NR3C1 interaction with the BRG1/SMARCA4 complex in vivoAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili412 – 44029Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi124 – 1274Poly-Lys

    Sequence similaritiesi

    Belongs to the SMARCD family.Sequence Analysis
    Contains 1 SWIB domain.Sequence Analysis

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5531.
    HOGENOMiHOG000240746.
    HOVERGENiHBG054046.
    InParanoidiQ96GM5.
    KOiK11650.
    OMAiIFETQRM.
    OrthoDBiEOG7PZRXG.
    PhylomeDBiQ96GM5.
    TreeFamiTF106486.

    Family and domain databases

    Gene3Di1.10.245.10. 1 hit.
    InterProiIPR019835. SWIB_domain.
    IPR003121. SWIB_MDM2_domain.
    [Graphical view]
    PfamiPF02201. SWIB. 1 hit.
    [Graphical view]
    SMARTiSM00151. SWIB. 1 hit.
    [Graphical view]
    SUPFAMiSSF47592. SSF47592. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q96GM5-1) [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

    MAARAGFQSV APSGGAGASG GAGAAAALGP GGTPGPPVRM GPAPGQGLYR    50
    SPMPGAAYPR PGMLPGSRMT PQGPSMGPPG YGGNPSVRPG LAQSGMDQSR 100
    KRPAPQQIQQ VQQQAVQNRN HNAKKKKMAD KILPQRIREL VPESQAYMDL 150
    LAFERKLDQT IMRKRLDIQE ALKRPIKQKR KLRIFISNTF NPAKSDAEDG 200
    EGTVASWELR VEGRLLEDSA LSKYDATKQK RKFSSFFKSL VIELDKDLYG 250
    PDNHLVEWHR TATTQETDGF QVKRPGDVNV RCTVLLMLDY QPPQFKLDPR 300
    LARLLGIHTQ TRPVIIQALW QYIKTHKLQD PHEREFVICD KYLQQIFESQ 350
    RMKFSEIPQR LHALLMPPEP IIINHVISVD PNDQKKTACY DIDVEVDDTL 400
    KTQMNSFLLS TASQQEIATL DNKIHETIET INQLKTQREF MLSFARDPQG 450
    FINDWLQSQC RDLKTMTDVV GNPEEERRAE FYFQPWAQEA VCRYFYSKVQ 500
    QRRQELEQAL GIRNT 515
    Length:515
    Mass (Da):58,233
    Last modified:May 26, 2009 - v2
    Checksum:iE683AA1E345DA400
    GO
    Isoform 21 Publication (identifier: Q96GM5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         423-463: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:474
    Mass (Da):53,299
    Checksum:i2DA7AB84B9A3F933
    GO

    Sequence cautioni

    The sequence AAC50695.1 differs from that shown. Reason: Frameshift at position 30.
    The sequence AAD23390.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH09368.3 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti349 – 3491S → T in AAC50695. (PubMed:8804307)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei423 – 46341Missing in isoform 2. 1 PublicationVSP_004179Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF109733 mRNA. Translation: AAD23390.1. Different initiation.
    U66617 mRNA. Translation: AAC50695.1. Frameshift.
    AC025154 Genomic DNA. No translation available.
    BC009368 mRNA. Translation: AAH09368.3. Different initiation.
    CCDSiCCDS8797.2. [Q96GM5-1]
    CCDS8798.2. [Q96GM5-2]
    RefSeqiNP_003067.3. NM_003076.4. [Q96GM5-1]
    NP_620710.2. NM_139071.2. [Q96GM5-2]
    UniGeneiHs.79335.

    Genome annotation databases

    EnsembliENST00000381513; ENSP00000370924; ENSG00000066117. [Q96GM5-2]
    ENST00000394963; ENSP00000378414; ENSG00000066117. [Q96GM5-1]
    GeneIDi6602.
    KEGGihsa:6602.
    UCSCiuc001rvx.4. human. [Q96GM5-1]
    uc001rvy.4. human. [Q96GM5-2]

    Polymorphism databases

    DMDMi238054318.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF109733 mRNA. Translation: AAD23390.1 . Different initiation.
    U66617 mRNA. Translation: AAC50695.1 . Frameshift.
    AC025154 Genomic DNA. No translation available.
    BC009368 mRNA. Translation: AAH09368.3 . Different initiation.
    CCDSi CCDS8797.2. [Q96GM5-1 ]
    CCDS8798.2. [Q96GM5-2 ]
    RefSeqi NP_003067.3. NM_003076.4. [Q96GM5-1 ]
    NP_620710.2. NM_139071.2. [Q96GM5-2 ]
    UniGenei Hs.79335.

    3D structure databases

    ProteinModelPortali Q96GM5.
    SMRi Q96GM5. Positions 291-370.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112486. 75 interactions.
    DIPi DIP-33390N.
    IntActi Q96GM5. 43 interactions.
    MINTi MINT-1144212.
    STRINGi 9606.ENSP00000378414.

    PTM databases

    PhosphoSitei Q96GM5.

    Polymorphism databases

    DMDMi 238054318.

    Proteomic databases

    MaxQBi Q96GM5.
    PaxDbi Q96GM5.
    PRIDEi Q96GM5.

    Protocols and materials databases

    DNASUi 6602.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381513 ; ENSP00000370924 ; ENSG00000066117 . [Q96GM5-2 ]
    ENST00000394963 ; ENSP00000378414 ; ENSG00000066117 . [Q96GM5-1 ]
    GeneIDi 6602.
    KEGGi hsa:6602.
    UCSCi uc001rvx.4. human. [Q96GM5-1 ]
    uc001rvy.4. human. [Q96GM5-2 ]

    Organism-specific databases

    CTDi 6602.
    GeneCardsi GC12P050478.
    HGNCi HGNC:11106. SMARCD1.
    HPAi HPA004101.
    MIMi 601735. gene.
    neXtProti NX_Q96GM5.
    PharmGKBi PA35956.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5531.
    HOGENOMi HOG000240746.
    HOVERGENi HBG054046.
    InParanoidi Q96GM5.
    KOi K11650.
    OMAi IFETQRM.
    OrthoDBi EOG7PZRXG.
    PhylomeDBi Q96GM5.
    TreeFami TF106486.

    Miscellaneous databases

    ChiTaRSi SMARCD1. human.
    GeneWikii SMARCD1.
    GenomeRNAii 6602.
    NextBioi 25683.
    PROi Q96GM5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96GM5.
    Bgeei Q96GM5.
    CleanExi HS_SMARCD1.
    Genevestigatori Q96GM5.

    Family and domain databases

    Gene3Di 1.10.245.10. 1 hit.
    InterProi IPR019835. SWIB_domain.
    IPR003121. SWIB_MDM2_domain.
    [Graphical view ]
    Pfami PF02201. SWIB. 1 hit.
    [Graphical view ]
    SMARTi SM00151. SWIB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47592. SSF47592. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Diversity and specialization of mammalian SWI/SNF complexes."
      Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.
      Genes Dev. 10:2117-2130(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Peripheral blood.
    2. "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].
    3. "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.
    4. "Purification and biochemical heterogeneity of the mammalian SWI-SNF complex."
      Wang W., Cote J., Xue Y., Zhou S., Khavari P.A., Biggar S.R., Muchardt C., Kalpana G.V., Goff S.P., Yaniv M., Workman J.L., Crabtree G.R.
      EMBO J. 15:5370-5382(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    5. "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
      Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
      Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
    6. "Use of a modified yeast one-hybrid screen to identify BAF60a interactions with the Vitamin D receptor heterodimer."
      Koszewski N.J., Henry K.W., Lubert E.J., Gravatte H., Noonan D.J.
      J. Steroid Biochem. Mol. Biol. 87:223-231(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH THE VITAMIN D RECEPTOR HETERODIMER COMPLEX.
    7. "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
      Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
      Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ESR1; NR3C1; NR1H4; PGR; SMARCA4; SMARCC1 AND SMARCC2.
    8. "Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex."
      Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.
      Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiSMRD1_HUMAN
    AccessioniPrimary (citable) accession number: Q96GM5
    Secondary accession number(s): A6NN27, Q92924, Q9Y635
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 17, 2003
    Last sequence update: May 26, 2009
    Last modified: October 1, 2014
    This is version 122 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 12
      Human chromosome 12: 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