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Q6JBY9

- CPZIP_HUMAN

UniProt

Q6JBY9 - CPZIP_HUMAN

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Protein

CapZ-interacting protein

Gene

RCSD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ6JBY9.
CleanExiHS_RCSD1.
ExpressionAtlasiQ6JBY9. baseline and differential.
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.
GeneTreeiENSGT00510000049038.
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

        10         20         30         40         50
MEERPAETNA NVDNSASPSV AQLAGRFREQ AAAAKETPAS KPTRRKPPCS
60 70 80 90 100
LPLFPPKVDL GQNGEEKSPP NASHPPKFKV KSSPLIEKLQ ANLTFDPAAL
110 120 130 140 150
LPGASPKSPG LKAMVSPFHS PPSTPSSPGV RSRPSEAEEV PVSFDQPPEG
160 170 180 190 200
SHLPCYNKVR TRGSIKRRPP SRRFRRSQSD CGELGDFRAV ESSQQNGAKE
210 220 230 240 250
EDGDEVLPSK SKAPGSPLSS EGAAGEGVRT LGPAEKPPLR RSPSRTEKQE
260 270 280 290 300
EDRATEEAKN GEKARRSSEE VDGQHPAQEE VPESPQTSGP EAENRCGSPR
310 320 330 340 350
EEKPAGEEAE MEKATEVKGE RVQNEEVGPE HDSQETKKLE EGAAVKETPH
360 370 380 390 400
SPPGGVKGGD VPKQEKGKEK QQEGAVLEPG CSPQTGPAQL ETSSEVQSEP
410
AVPKPEDDTP VQDTKM
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.
GeneTreei ENSGT00510000049038.
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

Bgeei Q6JBY9.
CleanExi HS_RCSD1.
ExpressionAtlasi Q6JBY9. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 83 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