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Q6JBY9

- CPZIP_HUMAN

UniProt

Q6JBY9 - CPZIP_HUMAN

Protein

CapZ-interacting protein

Gene

RCSD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Stress-induced phosphorylation of CAPZIP may regulate the ability of F-actin-capping protein to remodel actin filament assembly.1 Publication

    GO - Molecular functioni

    1. actin filament binding Source: BHF-UCL

    GO - Biological processi

    1. cellular hyperosmotic response Source: BHF-UCL
    2. skeletal muscle contraction Source: BHF-UCL

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CapZ-interacting protein
    Alternative name(s):
    Protein kinase substrate CapZIP
    RCSD domain-containing protein 1
    Gene namesi
    Name:RCSD1
    Synonyms:CAPZIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:28310. RCSD1.

    Subcellular locationi

    GO - Cellular componenti

    1. actin filament Source: BHF-UCL

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671088.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416CapZ-interacting proteinPRO_0000320262Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681Phosphoserine; by MAPK8; in vitro1 Publication
    Modified residuei83 – 831Phosphoserine; by MAPK8; in vitro1 Publication
    Modified residuei105 – 1051Phosphoserine1 Publication
    Modified residuei108 – 1081Phosphoserine; by MAPK12 and MAPK132 Publications
    Modified residuei116 – 1161Phosphoserine1 Publication
    Modified residuei120 – 1201Phosphoserine1 Publication
    Modified residuei123 – 1231Phosphoserine1 Publication
    Modified residuei124 – 1241Phosphothreonine1 Publication
    Modified residuei127 – 1271Phosphoserine1 Publication
    Modified residuei177 – 1771Phosphoserine1 Publication
    Modified residuei179 – 1791Phosphoserine; by MAPKAPK2 and MAPKAPK32 Publications
    Modified residuei216 – 2161Phosphoserine; by MAPK8; in vitro3 Publications
    Modified residuei244 – 2441Phosphoserine; by MAPKAPK2 or MAPKAPK3; in vitro1 Publication
    Modified residuei267 – 2671Phosphoserine1 Publication
    Modified residuei268 – 2681Phosphoserine1 Publication
    Modified residuei284 – 2841Phosphoserine1 Publication
    Modified residuei298 – 2981PhosphoserineBy similarity

    Post-translational modificationi

    Dephosphorylation results in its dissociation from CAPZA2.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6JBY9.
    PaxDbiQ6JBY9.
    PRIDEiQ6JBY9.

    PTM databases

    PhosphoSiteiQ6JBY9.

    Miscellaneous databases

    PMAP-CutDBQ6JBY9.

    Expressioni

    Tissue specificityi

    Highly expressed in skeletal muscle and more weakly in cardiac muscle. Also expressed in several lymphoid organs, including spleen, thymus, peripheral blood leukocytes, lymph node and bone marrow.1 Publication

    Gene expression databases

    ArrayExpressiQ6JBY9.
    BgeeiQ6JBY9.
    CleanExiHS_RCSD1.
    GenevestigatoriQ6JBY9.

    Organism-specific databases

    HPAiHPA016597.

    Interactioni

    Subunit structurei

    Interacts with CAPZA2 and CAPZB.1 Publication

    Protein-protein interaction databases

    BioGridi124921. 1 interaction.
    IntActiQ6JBY9. 1 interaction.
    STRINGi9606.ENSP00000356828.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6JBY9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini227 – 330104RCSDAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RCSD domain.Curated

    Phylogenomic databases

    eggNOGiNOG78730.
    HOVERGENiHBG106582.
    InParanoidiQ6JBY9.
    OMAiQSDCGEL.
    OrthoDBiEOG7Z0JX9.
    PhylomeDBiQ6JBY9.
    TreeFamiTF334159.

    Family and domain databases

    InterProiIPR029341. FAM21/CAPZIP.
    IPR007850. RCSD.
    [Graphical view]
    PfamiPF15255. CAP-ZIP_m. 1 hit.
    PF05177. RCSD. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6JBY9-1) [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

    MEERPAETNA NVDNSASPSV AQLAGRFREQ AAAAKETPAS KPTRRKPPCS    50
    LPLFPPKVDL GQNGEEKSPP NASHPPKFKV KSSPLIEKLQ ANLTFDPAAL 100
    LPGASPKSPG LKAMVSPFHS PPSTPSSPGV RSRPSEAEEV PVSFDQPPEG 150
    SHLPCYNKVR TRGSIKRRPP SRRFRRSQSD CGELGDFRAV ESSQQNGAKE 200
    EDGDEVLPSK SKAPGSPLSS EGAAGEGVRT LGPAEKPPLR RSPSRTEKQE 250
    EDRATEEAKN GEKARRSSEE VDGQHPAQEE VPESPQTSGP EAENRCGSPR 300
    EEKPAGEEAE MEKATEVKGE RVQNEEVGPE HDSQETKKLE EGAAVKETPH 350
    SPPGGVKGGD VPKQEKGKEK QQEGAVLEPG CSPQTGPAQL ETSSEVQSEP 400
    AVPKPEDDTP VQDTKM 416
    Length:416
    Mass (Da):44,504
    Last modified:July 5, 2004 - v1
    Checksum:iE3E617250F965136
    GO
    Isoform 2 (identifier: Q6JBY9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-310: Missing.

    Show »
    Length:106
    Mass (Da):11,299
    Checksum:iEE22246AC4CFF625
    GO

    Sequence cautioni

    The sequence CAB70910.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481P → A in AAN52359. 1 PublicationCurated
    Sequence conflicti74 – 741H → Q in AAN52359. 1 PublicationCurated
    Sequence conflicti96 – 961D → E in AAN52359. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti384 – 3841Q → R.
    Corresponds to variant rs34699420 [ dbSNP | Ensembl ].
    VAR_039181

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 310310Missing in isoform 2. 1 PublicationVSP_031648Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY530954 mRNA. Translation: AAS99235.1.
    AF545852 mRNA. Translation: AAN52359.1.
    CH471067 Genomic DNA. Translation: EAW90797.1.
    AL031733, AL356532 Genomic DNA. Translation: CAI21377.1.
    AL356532, AL031733 Genomic DNA. Translation: CAI21595.1.
    BC072399 mRNA. Translation: AAH72399.1.
    BC098426 mRNA. Translation: AAH98426.1.
    BC101536 mRNA. Translation: AAI01537.1.
    BC101562 mRNA. Translation: AAI01563.1.
    BC013186 mRNA. Translation: AAH13186.1.
    AL137762 mRNA. Translation: CAB70910.1. Different initiation.
    CCDSiCCDS1263.1. [Q6JBY9-1]
    RefSeqiNP_443094.3. NM_052862.3. [Q6JBY9-1]
    UniGeneiHs.493867.

    Genome annotation databases

    EnsembliENST00000367854; ENSP00000356828; ENSG00000198771. [Q6JBY9-1]
    GeneIDi92241.
    KEGGihsa:92241.
    UCSCiuc001gem.3. human. [Q6JBY9-1]

    Polymorphism databases

    DMDMi74758031.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY530954 mRNA. Translation: AAS99235.1 .
    AF545852 mRNA. Translation: AAN52359.1 .
    CH471067 Genomic DNA. Translation: EAW90797.1 .
    AL031733 , AL356532 Genomic DNA. Translation: CAI21377.1 .
    AL356532 , AL031733 Genomic DNA. Translation: CAI21595.1 .
    BC072399 mRNA. Translation: AAH72399.1 .
    BC098426 mRNA. Translation: AAH98426.1 .
    BC101536 mRNA. Translation: AAI01537.1 .
    BC101562 mRNA. Translation: AAI01563.1 .
    BC013186 mRNA. Translation: AAH13186.1 .
    AL137762 mRNA. Translation: CAB70910.1 . Different initiation.
    CCDSi CCDS1263.1. [Q6JBY9-1 ]
    RefSeqi NP_443094.3. NM_052862.3. [Q6JBY9-1 ]
    UniGenei Hs.493867.

    3D structure databases

    ProteinModelPortali Q6JBY9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124921. 1 interaction.
    IntActi Q6JBY9. 1 interaction.
    STRINGi 9606.ENSP00000356828.

    PTM databases

    PhosphoSitei Q6JBY9.

    Polymorphism databases

    DMDMi 74758031.

    Proteomic databases

    MaxQBi Q6JBY9.
    PaxDbi Q6JBY9.
    PRIDEi Q6JBY9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367854 ; ENSP00000356828 ; ENSG00000198771 . [Q6JBY9-1 ]
    GeneIDi 92241.
    KEGGi hsa:92241.
    UCSCi uc001gem.3. human. [Q6JBY9-1 ]

    Organism-specific databases

    CTDi 92241.
    GeneCardsi GC01P167599.
    HGNCi HGNC:28310. RCSD1.
    HPAi HPA016597.
    MIMi 610579. gene.
    neXtProti NX_Q6JBY9.
    PharmGKBi PA142671088.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG78730.
    HOVERGENi HBG106582.
    InParanoidi Q6JBY9.
    OMAi QSDCGEL.
    OrthoDBi EOG7Z0JX9.
    PhylomeDBi Q6JBY9.
    TreeFami TF334159.

    Miscellaneous databases

    GenomeRNAii 92241.
    NextBioi 77646.
    PMAP-CutDB Q6JBY9.
    PROi Q6JBY9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6JBY9.
    Bgeei Q6JBY9.
    CleanExi HS_RCSD1.
    Genevestigatori Q6JBY9.

    Family and domain databases

    InterProi IPR029341. FAM21/CAPZIP.
    IPR007850. RCSD.
    [Graphical view ]
    Pfami PF15255. CAP-ZIP_m. 1 hit.
    PF05177. RCSD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ."
      Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C., Cuenda A., Cohen P.
      Biochem. J. 389:127-135(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CAPZA2 AND CAPZB, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-68; SER-83; SER-108; SER-179; SER-216 AND SER-244.
    2. Guo J.H.
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Blood.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "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] (ISOFORMS 1 AND 2).
      Tissue: Blood, Brain and Lymph.
    6. Rhodes S., Huckle E.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-406 (ISOFORM 1).
    7. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-108; SER-116; SER-120; SER-123; THR-124; SER-127; SER-177; SER-179; SER-216; SER-267; SER-268 AND SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCPZIP_HUMAN
    AccessioniPrimary (citable) accession number: Q6JBY9
    Secondary accession number(s): B1AK48
    , Q4G0E7, Q6IN93, Q8IZM2, Q96DX0, Q9NST4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 82 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 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3