CPZIP_HUMAN
ID CPZIP_HUMAN Reviewed; 416 AA.
AC Q6JBY9; B1AK48; Q4G0E7; Q6IN93; Q8IZM2; Q96DX0; Q9NST4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=CapZ-interacting protein;
DE AltName: Full=Protein kinase substrate CapZIP;
DE AltName: Full=RCSD domain-containing protein 1;
GN Name=RCSD1; Synonyms=CAPZIP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CAPZA2
RP AND CAPZB, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT SER-68; SER-83;
RP SER-108; SER-179; SER-216 AND SER-244.
RX PubMed=15850461; DOI=10.1042/bj20050387;
RA Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C., Cuenda A.,
RA Cohen P.;
RT "The phosphorylation of CapZ-interacting protein (CapZIP) by stress-
RT activated protein kinases triggers its dissociation from CapZ.";
RL Biochem. J. 389:127-135(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RA Guo J.H.;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, Brain, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-406 (ISOFORM 1).
RA Rhodes S., Huckle E.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-108; SER-116;
RP SER-120; SER-123; SER-177; SER-179; SER-216; SER-267; SER-268 AND SER-284,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-68; SER-82; SER-83;
RP SER-108; SER-116; SER-120; SER-123; SER-127; SER-177; SER-179; SER-216;
RP SER-268; SER-284; SER-298; SER-333; THR-336 AND SER-351, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Stress-induced phosphorylation of CAPZIP may regulate the
CC ability of F-actin-capping protein to remodel actin filament assembly.
CC {ECO:0000269|PubMed:15850461}.
CC -!- SUBUNIT: Interacts with CAPZA2 and CAPZB.
CC {ECO:0000269|PubMed:15850461}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6JBY9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6JBY9-2; Sequence=VSP_031648;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and more weakly
CC in cardiac muscle. Also expressed in several lymphoid organs, including
CC spleen, thymus, peripheral blood leukocytes, lymph node and bone
CC marrow. {ECO:0000269|PubMed:15850461}.
CC -!- PTM: Dephosphorylation results in its dissociation from CAPZA2.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB70910.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY530954; AAS99235.1; -; mRNA.
DR EMBL; AF545852; AAN52359.1; -; mRNA.
DR EMBL; CH471067; EAW90797.1; -; Genomic_DNA.
DR EMBL; AL031733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC072399; AAH72399.1; -; mRNA.
DR EMBL; BC098426; AAH98426.1; -; mRNA.
DR EMBL; BC101536; AAI01537.1; -; mRNA.
DR EMBL; BC101562; AAI01563.1; -; mRNA.
DR EMBL; BC013186; AAH13186.1; -; mRNA.
DR EMBL; AL137762; CAB70910.1; ALT_INIT; mRNA.
DR CCDS; CCDS1263.1; -. [Q6JBY9-1]
DR RefSeq; NP_443094.3; NM_052862.3. [Q6JBY9-1]
DR AlphaFoldDB; Q6JBY9; -.
DR BioGRID; 124921; 8.
DR IntAct; Q6JBY9; 4.
DR STRING; 9606.ENSP00000356828; -.
DR iPTMnet; Q6JBY9; -.
DR PhosphoSitePlus; Q6JBY9; -.
DR BioMuta; RCSD1; -.
DR DMDM; 74758031; -.
DR CPTAC; CPTAC-998; -.
DR EPD; Q6JBY9; -.
DR jPOST; Q6JBY9; -.
DR MassIVE; Q6JBY9; -.
DR MaxQB; Q6JBY9; -.
DR PaxDb; Q6JBY9; -.
DR PeptideAtlas; Q6JBY9; -.
DR PRIDE; Q6JBY9; -.
DR ProteomicsDB; 66511; -. [Q6JBY9-1]
DR ProteomicsDB; 66512; -. [Q6JBY9-2]
DR Antibodypedia; 34342; 72 antibodies from 17 providers.
DR DNASU; 92241; -.
DR Ensembl; ENST00000367854.8; ENSP00000356828.3; ENSG00000198771.11. [Q6JBY9-1]
DR GeneID; 92241; -.
DR KEGG; hsa:92241; -.
DR MANE-Select; ENST00000367854.8; ENSP00000356828.3; NM_052862.4; NP_443094.3.
DR UCSC; uc001gem.4; human. [Q6JBY9-1]
DR CTD; 92241; -.
DR DisGeNET; 92241; -.
DR GeneCards; RCSD1; -.
DR HGNC; HGNC:28310; RCSD1.
DR HPA; ENSG00000198771; Tissue enhanced (lymphoid tissue, skeletal muscle).
DR MIM; 610579; gene.
DR neXtProt; NX_Q6JBY9; -.
DR OpenTargets; ENSG00000198771; -.
DR PharmGKB; PA142671088; -.
DR VEuPathDB; HostDB:ENSG00000198771; -.
DR eggNOG; ENOG502SRPU; Eukaryota.
DR GeneTree; ENSGT00940000153997; -.
DR HOGENOM; CLU_039301_1_0_1; -.
DR InParanoid; Q6JBY9; -.
DR OMA; SPAGNEQ; -.
DR OrthoDB; 1408738at2759; -.
DR PhylomeDB; Q6JBY9; -.
DR TreeFam; TF334159; -.
DR PathwayCommons; Q6JBY9; -.
DR SignaLink; Q6JBY9; -.
DR SIGNOR; Q6JBY9; -.
DR BioGRID-ORCS; 92241; 16 hits in 1079 CRISPR screens.
DR ChiTaRS; RCSD1; human.
DR GenomeRNAi; 92241; -.
DR Pharos; Q6JBY9; Tbio.
DR PRO; PR:Q6JBY9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6JBY9; protein.
DR Bgee; ENSG00000198771; Expressed in leukocyte and 169 other tissues.
DR ExpressionAtlas; Q6JBY9; baseline and differential.
DR Genevisible; Q6JBY9; HS.
DR GO; GO:0005884; C:actin filament; IC:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IPI:BHF-UCL.
DR GO; GO:0071474; P:cellular hyperosmotic response; IDA:BHF-UCL.
DR GO; GO:0003009; P:skeletal muscle contraction; ISS:BHF-UCL.
DR InterPro; IPR029341; FAM21/CAPZIP.
DR InterPro; IPR007850; RCSD.
DR Pfam; PF15255; CAP-ZIP_m; 1.
DR Pfam; PF05177; RCSD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..416
FT /note="CapZ-interacting protein"
FT /id="PRO_0000320262"
FT DOMAIN 227..330
FT /note="RCSD"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 68
FT /note="Phosphoserine; by MAPK8; in vitro"
FT /evidence="ECO:0000269|PubMed:15850461,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 83
FT /note="Phosphoserine; by MAPK8; in vitro"
FT /evidence="ECO:0000269|PubMed:15850461,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 108
FT /note="Phosphoserine; by MAPK12 and MAPK13"
FT /evidence="ECO:0000269|PubMed:15850461,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZA1"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZA1"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZA1"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZA1"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 179
FT /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
FT /evidence="ECO:0000269|PubMed:15850461,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 216
FT /note="Phosphoserine; by MAPK8; in vitro"
FT /evidence="ECO:0000269|PubMed:15850461,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 244
FT /note="Phosphoserine; by MAPKAPK2 or MAPKAPK3; in vitro"
FT /evidence="ECO:0000269|PubMed:15850461"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..310
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031648"
FT VARIANT 384
FT /note="Q -> R (in dbSNP:rs34699420)"
FT /id="VAR_039181"
FT CONFLICT 48
FT /note="P -> A (in Ref. 2; AAN52359)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="H -> Q (in Ref. 2; AAN52359)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="D -> E (in Ref. 2; AAN52359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 44504 MW; E3E617250F965136 CRC64;
MEERPAETNA NVDNSASPSV AQLAGRFREQ AAAAKETPAS KPTRRKPPCS LPLFPPKVDL
GQNGEEKSPP NASHPPKFKV KSSPLIEKLQ ANLTFDPAAL LPGASPKSPG LKAMVSPFHS
PPSTPSSPGV RSRPSEAEEV PVSFDQPPEG SHLPCYNKVR TRGSIKRRPP SRRFRRSQSD
CGELGDFRAV ESSQQNGAKE EDGDEVLPSK SKAPGSPLSS EGAAGEGVRT LGPAEKPPLR
RSPSRTEKQE EDRATEEAKN GEKARRSSEE VDGQHPAQEE VPESPQTSGP EAENRCGSPR
EEKPAGEEAE MEKATEVKGE RVQNEEVGPE HDSQETKKLE EGAAVKETPH SPPGGVKGGD
VPKQEKGKEK QQEGAVLEPG CSPQTGPAQL ETSSEVQSEP AVPKPEDDTP VQDTKM
