STRP2_HUMAN
ID STRP2_HUMAN Reviewed; 834 AA.
AC Q9ULQ0; Q8WUZ4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Striatin-interacting protein 2;
DE AltName: Full=Protein FAM40B;
GN Name=STRIP2; Synonyms=FAM40B, KIAA1170;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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 [4]
RP INTERACTION WITH CTTNBP2NL.
RX PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200;
RA Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
RA Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
RA Aebersold R., Raught B., Gingras A.C.;
RT "A PP2A phosphatase high density interaction network identifies a novel
RT striatin-interacting phosphatase and kinase complex linked to the cerebral
RT cavernous malformation 3 (CCM3) protein.";
RL Mol. Cell. Proteomics 8:157-171(2009).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318; SER-329 AND SER-354, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required in the control of cell shape.
CC {ECO:0000269|PubMed:21834987}.
CC -!- SUBUNIT: Component of striatin-interacting phosphatase and kinase
CC (STRIPAK) complex (By similarity). Interacts with CTTNBP2NL.
CC {ECO:0000250, ECO:0000269|PubMed:18782753}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21834987}.
CC Note=Enriched in lamellipodia.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULQ0-2; Sequence=VSP_014867, VSP_014868;
CC -!- SIMILARITY: Belongs to the STRIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86484.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB032996; BAA86484.1; ALT_INIT; mRNA.
DR EMBL; AC009244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019064; AAH19064.1; -; mRNA.
DR CCDS; CCDS34752.1; -. [Q9ULQ0-1]
DR CCDS; CCDS47709.1; -. [Q9ULQ0-2]
DR RefSeq; NP_001127808.1; NM_001134336.1. [Q9ULQ0-2]
DR RefSeq; NP_065755.1; NM_020704.2. [Q9ULQ0-1]
DR AlphaFoldDB; Q9ULQ0; -.
DR SMR; Q9ULQ0; -.
DR BioGRID; 121534; 34.
DR DIP; DIP-51635N; -.
DR IntAct; Q9ULQ0; 24.
DR MINT; Q9ULQ0; -.
DR STRING; 9606.ENSP00000249344; -.
DR iPTMnet; Q9ULQ0; -.
DR PhosphoSitePlus; Q9ULQ0; -.
DR BioMuta; STRIP2; -.
DR DMDM; 71151881; -.
DR EPD; Q9ULQ0; -.
DR jPOST; Q9ULQ0; -.
DR MassIVE; Q9ULQ0; -.
DR MaxQB; Q9ULQ0; -.
DR PaxDb; Q9ULQ0; -.
DR PeptideAtlas; Q9ULQ0; -.
DR PRIDE; Q9ULQ0; -.
DR ProteomicsDB; 85092; -. [Q9ULQ0-1]
DR ProteomicsDB; 85093; -. [Q9ULQ0-2]
DR Antibodypedia; 17893; 59 antibodies from 19 providers.
DR DNASU; 57464; -.
DR Ensembl; ENST00000249344.7; ENSP00000249344.2; ENSG00000128578.10. [Q9ULQ0-1]
DR Ensembl; ENST00000435494.2; ENSP00000392393.2; ENSG00000128578.10. [Q9ULQ0-2]
DR GeneID; 57464; -.
DR KEGG; hsa:57464; -.
DR MANE-Select; ENST00000249344.7; ENSP00000249344.2; NM_020704.3; NP_065755.1.
DR UCSC; uc003vow.5; human. [Q9ULQ0-1]
DR CTD; 57464; -.
DR DisGeNET; 57464; -.
DR GeneCards; STRIP2; -.
DR HGNC; HGNC:22209; STRIP2.
DR HPA; ENSG00000128578; Tissue enhanced (brain, choroid plexus, skeletal muscle).
DR MIM; 617919; gene.
DR neXtProt; NX_Q9ULQ0; -.
DR OpenTargets; ENSG00000128578; -.
DR PharmGKB; PA134923427; -.
DR VEuPathDB; HostDB:ENSG00000128578; -.
DR eggNOG; KOG3680; Eukaryota.
DR GeneTree; ENSGT00400000022095; -.
DR HOGENOM; CLU_011008_1_0_1; -.
DR InParanoid; Q9ULQ0; -.
DR OMA; RHNNFLL; -.
DR OrthoDB; 1095402at2759; -.
DR PhylomeDB; Q9ULQ0; -.
DR TreeFam; TF314205; -.
DR PathwayCommons; Q9ULQ0; -.
DR SignaLink; Q9ULQ0; -.
DR BioGRID-ORCS; 57464; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; STRIP2; human.
DR GenomeRNAi; 57464; -.
DR Pharos; Q9ULQ0; Tbio.
DR PRO; PR:Q9ULQ0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9ULQ0; protein.
DR Bgee; ENSG00000128578; Expressed in pigmented layer of retina and 141 other tissues.
DR Genevisible; Q9ULQ0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR InterPro; IPR040185; Far11/STRP.
DR InterPro; IPR021819; Far11/STRP_C.
DR InterPro; IPR012486; Far11/STRP_N.
DR PANTHER; PTHR13239; PTHR13239; 1.
DR Pfam; PF11882; DUF3402; 2.
DR Pfam; PF07923; N1221; 1.
DR SMART; SM01293; DUF3402; 1.
DR SMART; SM01292; N1221; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..834
FT /note="Striatin-interacting protein 2"
FT /id="PRO_0000187022"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 752..758
FT /note="DIDARPW -> GESSQSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014867"
FT VAR_SEQ 759..834
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014868"
FT VARIANT 383
FT /note="R -> Q (in dbSNP:rs2242030)"
FT /id="VAR_049021"
SQ SEQUENCE 834 AA; 95360 MW; 3DAF1DA8FD6E4C4D CRC64;
MEDPAAPGTG GPPANGNGNG GGKGKQAAPK GREAFRSQRR ESEGSVDCPT LEFEYGDADG
HAAELSELYS YTENLEFTNN RRCFEEDFKT QVQGKEWLEL EEDAQKAYIM GLLDRLEVVS
RERRLKVARA VLYLAQGTFG ECDSEVDVLH WSRYNCFLLY QMGTFSTFLE LLHMEIDNSQ
ACSSALRKPA VSIADSTELR VLLSVMYLMV ENIRLERETD PCGWRTARET FRTELSFSMH
NEEPFALLLF SMVTKFCSGL APHFPIKKVL LLLWKVVMFT LGGFEHLQTL KVQKRAELGL
PPLAEDSIQV VKSMRAASPP SYTLDLGESQ LAPPPSKLRG RRGSRRQLLT KQDSLDIYNE
RDLFKTEEPA TEEEEESAGD GERTLDGELD LLEQDPLVPP PPSQAPLSAE RVAFPKGLPW
APKVRQKDIE HFLEMSRNKF IGFTLGQDTD TLVGLPRPIH ESVKTLKQHK YISIADVQIK
NEEELEKCPM SLGEEVVPET PCEILYQGML YSLPQYMIAL LKILLAAAPT SKAKTDSINI
LADVLPEEMP ITVLQSMKLG IDVNRHKEII VKSISTLLLL LLKHFKLNHI YQFEYVSQHL
VFANCIPLIL KFFNQNILSY ITAKNSISVL DYPCCTIQDL PELTTESLEA GDNSQFCWRN
LFSCINLLRL LNKLTKWKHS RTMMLVVFKS APILKRALKV KQAMLQLYVL KLLKLQTKYL
GRQWRKSNMK TMSAIYQKVR HRMNDDWAYG NDIDARPWDF QAEECTLRAN IEAFNSRRYD
RPQDSEFSPV DNCLQSVLGQ RLDLPEDFHY SYELWLEREV FSQPICWEEL LQNH
