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Q6JBY9 (CPZIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CapZ-interacting protein
Alternative name(s):
Protein kinase substrate CapZIP
RCSD domain-containing protein 1
Gene names
Name:RCSD1
Synonyms:CAPZIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts with CAPZA2 and CAPZB. Ref.1

Tissue specificity

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. Ref.1

Post-translational modification

Dephosphorylation results in its dissociation from CAPZA2.

Sequence similarities

Contains 1 RCSD domain.

Sequence caution

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

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular hyperosmotic response

Inferred from direct assay Ref.1. Source: BHF-UCL

skeletal muscle contraction

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentactin filament

Inferred by curator Ref.1. Source: BHF-UCL

   Molecular_functionactin filament binding

Inferred from physical interaction Ref.1. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6JBY9-1)

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.
Isoform 2 (identifier: Q6JBY9-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416CapZ-interacting protein
PRO_0000320262

Regions

Domain227 – 330104RCSD

Amino acid modifications

Modified residue681Phosphoserine; by MAPK8; in vitro Ref.1
Modified residue831Phosphoserine; by MAPK8; in vitro Ref.1
Modified residue1051Phosphoserine Ref.9
Modified residue1081Phosphoserine; by MAPK12 and MAPK13 Ref.1 Ref.9
Modified residue1161Phosphoserine Ref.9
Modified residue1201Phosphoserine Ref.9
Modified residue1231Phosphoserine Ref.9
Modified residue1241Phosphothreonine Ref.9
Modified residue1271Phosphoserine Ref.9
Modified residue1771Phosphoserine Ref.9
Modified residue1791Phosphoserine; by MAPKAPK2 and MAPKAPK3 Ref.1 Ref.9
Modified residue2161Phosphoserine; by MAPK8; in vitro Ref.1 Ref.8 Ref.9
Modified residue2441Phosphoserine; by MAPKAPK2 or MAPKAPK3; in vitro Ref.1
Modified residue2671Phosphoserine Ref.9
Modified residue2681Phosphoserine Ref.9
Modified residue2841Phosphoserine Ref.9
Modified residue2981Phosphoserine By similarity

Natural variations

Alternative sequence1 – 310310Missing in isoform 2.
VSP_031648
Natural variant3841Q → R.
Corresponds to variant rs34699420 [ dbSNP | Ensembl ].
VAR_039181

Experimental info

Sequence conflict481P → A in AAN52359. Ref.2
Sequence conflict741H → Q in AAN52359. Ref.2
Sequence conflict961D → E in AAN52359. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E3E617250F965136

FASTA41644,504
        10         20         30         40         50         60 
MEERPAETNA NVDNSASPSV AQLAGRFREQ AAAAKETPAS KPTRRKPPCS LPLFPPKVDL 

        70         80         90        100        110        120 
GQNGEEKSPP NASHPPKFKV KSSPLIEKLQ ANLTFDPAAL LPGASPKSPG LKAMVSPFHS 

       130        140        150        160        170        180 
PPSTPSSPGV RSRPSEAEEV PVSFDQPPEG SHLPCYNKVR TRGSIKRRPP SRRFRRSQSD 

       190        200        210        220        230        240 
CGELGDFRAV ESSQQNGAKE EDGDEVLPSK SKAPGSPLSS EGAAGEGVRT LGPAEKPPLR 

       250        260        270        280        290        300 
RSPSRTEKQE EDRATEEAKN GEKARRSSEE VDGQHPAQEE VPESPQTSGP EAENRCGSPR 

       310        320        330        340        350        360 
EEKPAGEEAE MEKATEVKGE RVQNEEVGPE HDSQETKKLE EGAAVKETPH SPPGGVKGGD 

       370        380        390        400        410 
VPKQEKGKEK QQEGAVLEPG CSPQTGPAQL ETSSEVQSEP AVPKPEDDTP VQDTKM 

« Hide

Isoform 2 [UniParc].

Checksum: EE22246AC4CFF625
Show »

FASTA10611,299

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1263.1. [Q6JBY9-1]
RefSeqNP_443094.3. NM_052862.3. [Q6JBY9-1]
UniGeneHs.493867.

3D structure databases

ProteinModelPortalQ6JBY9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ6JBY9. 1 interaction.
STRING9606.ENSP00000356828.

PTM databases

PhosphoSiteQ6JBY9.

Polymorphism databases

DMDM74758031.

Proteomic databases

MaxQBQ6JBY9.
PaxDbQ6JBY9.
PRIDEQ6JBY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367854; ENSP00000356828; ENSG00000198771. [Q6JBY9-1]
GeneID92241.
KEGGhsa:92241.
UCSCuc001gem.3. human. [Q6JBY9-1]

Organism-specific databases

CTD92241.
GeneCardsGC01P167599.
HGNCHGNC:28310. RCSD1.
HPAHPA016597.
MIM610579. gene.
neXtProtNX_Q6JBY9.
PharmGKBPA142671088.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG78730.
HOVERGENHBG106582.
InParanoidQ6JBY9.
OMAQSDCGEL.
OrthoDBEOG7Z0JX9.
PhylomeDBQ6JBY9.
TreeFamTF334159.

Gene expression databases

ArrayExpressQ6JBY9.
BgeeQ6JBY9.
CleanExHS_RCSD1.
GenevestigatorQ6JBY9.

Family and domain databases

InterProIPR029341. FAM21/CAPZIP.
IPR007850. RCSD.
[Graphical view]
PfamPF15255. CAP-ZIP_m. 1 hit.
PF05177. RCSD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi92241.
NextBio77646.
PMAP-CutDBQ6JBY9.
PROQ6JBY9.
SOURCESearch...

Entry information

Entry nameCPZIP_HUMAN
AccessionPrimary (citable) accession number: Q6JBY9
Secondary accession number(s): B1AK48 expand/collapse secondary AC list , Q4G0E7, Q6IN93, Q8IZM2, Q96DX0, Q9NST4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM