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 27-MAR-2024, entry version 138. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10. DR IntAct; Q6JBY9; 4. DR STRING; 9606.ENSP00000356828; -. DR GlyGen; Q6JBY9; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000356828; -. DR PeptideAtlas; Q6JBY9; -. DR ProteomicsDB; 66511; -. [Q6JBY9-1] DR ProteomicsDB; 66512; -. [Q6JBY9-2] DR Pumba; Q6JBY9; -. DR Antibodypedia; 34342; 77 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 AGR; HGNC:28310; -. 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; QEGAETH; -. DR OrthoDB; 4640292at2759; -. DR PhylomeDB; Q6JBY9; -. DR TreeFam; TF334159; -. DR PathwayCommons; Q6JBY9; -. DR SignaLink; Q6JBY9; -. DR SIGNOR; Q6JBY9; -. DR BioGRID-ORCS; 92241; 16 hits in 1157 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 171 other cell types or tissues. DR ExpressionAtlas; Q6JBY9; baseline and differential. DR GO; GO:0005884; C:actin filament; IC:BHF-UCL. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0005769; C:early endosome; IBA:GO_Central. DR GO; GO:0071203; C:WASH complex; IBA:GO_Central. DR GO; GO:0051015; F:actin filament binding; IPI:BHF-UCL. DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central. DR GO; GO:1905394; F:retromer complex binding; IBA:GO_Central. DR GO; GO:0071474; P:cellular hyperosmotic response; IDA:BHF-UCL. DR GO; GO:0036010; P:protein localization to endosome; IBA:GO_Central. DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central. 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. DR Genevisible; Q6JBY9; HS. 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 //