Q6JBY9 (CPZIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CapZ-interacting protein

Alternative name(s):
Protein kinase substrate CapZIP
RCSD domain-containing protein 1

Gene names

Name:	RCSD1
Synonyms:	CAPZIP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Protein existence	Evidence 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 diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular hyperosmotic response Inferred from direct assay Ref.1. Source: BHF-UCL skeletal muscle contraction Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	actin filament Inferred by curator 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 416	416	CapZ-interacting protein		PRO_0000320262
Regions
	Domain	227 – 330	104	RCSD
Amino acid modifications
	Modified residue	68	1	Phosphoserine; by MAPK8; in vitro Ref.1
	Modified residue	83	1	Phosphoserine; by MAPK8; in vitro Ref.1
	Modified residue	105	1	Phosphoserine Ref.9
	Modified residue	108	1	Phosphoserine; by MAPK12 and MAPK13 Ref.1 Ref.9
	Modified residue	116	1	Phosphoserine Ref.9
	Modified residue	120	1	Phosphoserine Ref.9
	Modified residue	123	1	Phosphoserine Ref.9
	Modified residue	124	1	Phosphothreonine Ref.9
	Modified residue	127	1	Phosphoserine Ref.9
	Modified residue	177	1	Phosphoserine Ref.9
	Modified residue	179	1	Phosphoserine; by MAPKAPK2 and MAPKAPK3 Ref.1 Ref.9
	Modified residue	216	1	Phosphoserine; by MAPK8; in vitro Ref.1 Ref.8 Ref.9
	Modified residue	244	1	Phosphoserine; by MAPKAPK2 or MAPKAPK3; in vitro Ref.1
	Modified residue	267	1	Phosphoserine Ref.9
	Modified residue	268	1	Phosphoserine Ref.9
	Modified residue	284	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	1 – 310	310	Missing in isoform 2.		VSP_031648
	Natural variant	384	1	Q → R. Corresponds to variant rs34699420 [ dbSNP | Ensembl ].		VAR_039181
Experimental info
	Sequence conflict	48	1	P → A in AAN52359. Ref.2
	Sequence conflict	74	1	H → Q in AAN52359. Ref.2
	Sequence conflict	96	1	D → E in AAN52359. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: E3E617250F965136	FASTA	416	44,504
	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
	Isoform 2 [UniParc]. Checksum: EE22246AC4CFF625	FASTA	106	11,299
	10 20 30 40 50 60 MEKATEVKGE RVQNEEVGPE HDSQETKKLE EGAAVKETPH SPPGGVKGGD VPKQEKGKEK 70 80 90 100 QQEGAVLEPG CSPQTGPAQL ETSSEVQSEP AVPKPEDDTP VQDTKM

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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.
IPI	IPI00017659. IPI00940120.
RefSeq	NP_443094.3. NM_052862.3.
UniGene	Hs.493867.
3D structure databases
ProteinModelPortal	Q6JBY9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6JBY9. 1 interaction.
STRING	9606.ENSP00000356828.
PTM databases
PhosphoSite	Q6JBY9.
Polymorphism databases
DMDM	74758031.
Proteomic databases
PaxDb	Q6JBY9.
PRIDE	Q6JBY9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367854; ENSP00000356828; ENSG00000198771.
GeneID	92241.
KEGG	hsa:92241.
UCSC	uc001gem.3. human.
Organism-specific databases
CTD	92241.
GeneCards	GC01P167599.
HGNC	HGNC:28310. RCSD1.
HPA	HPA016597.
MIM	610579. gene.
neXtProt	NX_Q6JBY9.
PharmGKB	PA142671088.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG78730.
HOVERGEN	HBG106582.
InParanoid	Q6JBY9.
OMA	QSDCGEL.
OrthoDB	EOG47M1ZQ.
Gene expression databases
ArrayExpress	Q6JBY9.
Bgee	Q6JBY9.
CleanEx	HS_RCSD1.
Genevestigator	Q6JBY9.
Family and domain databases
InterPro	IPR007850. RCSD. [Graphical view]
Pfam	PF05177. RCSD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	92241.
NextBio	77646.
PMAP-CutDB	Q6JBY9.
SOURCE	Search...

Entry information

Entry name

CPZIP_HUMAN

Accession

Primary (citable) accession number: Q6JBY9
Secondary accession number(s): B1AK48 , Q4G0E7, Q6IN93, Q8IZM2, Q96DX0, Q9NST4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.