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Striatin-interacting protein 2 (Protein FAM40B)

 STRP2_HUMAN             Reviewed;         834 AA.
Q9ULQ0; Q8WUZ4;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 2.
12-SEP-2018, entry version 114.
RecName: Full=Striatin-interacting protein 2;
AltName: Full=Protein FAM40B;
Name=STRIP2; Synonyms=FAM40B, KIAA1170;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10574461; DOI=10.1093/dnares/6.5.329;
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
"Characterization of cDNA clones selected by the GeneMark analysis
from size-fractionated cDNA libraries from human brain.";
DNA Res. 6:329-336(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH CTTNBP2NL.
PubMed=18782753; DOI=10.1074/mcp.M800266-MCP200;
Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
Aebersold R., Raught B., Gingras A.C.;
"A PP2A phosphatase high density interaction network identifies a
novel striatin-interacting phosphatase and kinase complex linked to
the cerebral cavernous malformation 3 (CCM3) protein.";
Mol. Cell. Proteomics 8:157-171(2009).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21834987; DOI=10.1186/1741-7007-9-54;
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
"Identification and characterization of a set of conserved and new
regulators of cytoskeletal organisation, cell morphology and
migration.";
BMC Biol. 9:54-54(2011).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318; SER-329 AND
SER-354, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Plays a role in the regulation of cell morphology and
cytoskeletal organization. Required in the control of cell shape.
{ECO:0000269|PubMed:21834987}.
-!- SUBUNIT: Component of striatin-interacting phosphatase and kinase
(STRIPAK) complex (By similarity). Interacts with CTTNBP2NL.
{ECO:0000250, ECO:0000269|PubMed:18782753}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21834987}.
Note=Enriched in lamellipodia.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9ULQ0-1; Sequence=Displayed;
Name=2;
IsoId=Q9ULQ0-2; Sequence=VSP_014867, VSP_014868;
-!- SIMILARITY: Belongs to the STRIP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA86484.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB032996; BAA86484.1; ALT_INIT; mRNA.
EMBL; AC009244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC019064; AAH19064.1; -; mRNA.
CCDS; CCDS34752.1; -. [Q9ULQ0-1]
CCDS; CCDS47709.1; -. [Q9ULQ0-2]
RefSeq; NP_001127808.1; NM_001134336.1. [Q9ULQ0-2]
RefSeq; NP_065755.1; NM_020704.2. [Q9ULQ0-1]
UniGene; Hs.489988; -.
ProteinModelPortal; Q9ULQ0; -.
BioGrid; 121534; 28.
DIP; DIP-51635N; -.
IntAct; Q9ULQ0; 20.
STRING; 9606.ENSP00000249344; -.
iPTMnet; Q9ULQ0; -.
PhosphoSitePlus; Q9ULQ0; -.
BioMuta; STRIP2; -.
DMDM; 71151881; -.
EPD; Q9ULQ0; -.
PaxDb; Q9ULQ0; -.
PeptideAtlas; Q9ULQ0; -.
PRIDE; Q9ULQ0; -.
ProteomicsDB; 85092; -.
ProteomicsDB; 85093; -. [Q9ULQ0-2]
DNASU; 57464; -.
Ensembl; ENST00000249344; ENSP00000249344; ENSG00000128578. [Q9ULQ0-1]
Ensembl; ENST00000435494; ENSP00000392393; ENSG00000128578. [Q9ULQ0-2]
GeneID; 57464; -.
KEGG; hsa:57464; -.
UCSC; uc003vow.5; human. [Q9ULQ0-1]
CTD; 57464; -.
EuPathDB; HostDB:ENSG00000128578.9; -.
GeneCards; STRIP2; -.
H-InvDB; HIX0007066; -.
HGNC; HGNC:22209; STRIP2.
HPA; HPA019657; -.
MIM; 617919; gene.
neXtProt; NX_Q9ULQ0; -.
OpenTargets; ENSG00000128578; -.
PharmGKB; PA134923427; -.
eggNOG; KOG3680; Eukaryota.
eggNOG; ENOG410XRAB; LUCA.
GeneTree; ENSGT00400000022095; -.
HOGENOM; HOG000252963; -.
HOVERGEN; HBG081506; -.
InParanoid; Q9ULQ0; -.
OMA; RRYDKPQ; -.
OrthoDB; EOG091G02GC; -.
PhylomeDB; Q9ULQ0; -.
TreeFam; TF314205; -.
ChiTaRS; STRIP2; human.
GenomeRNAi; 57464; -.
PRO; PR:Q9ULQ0; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000128578; Expressed in 150 organ(s), highest expression level in pigmented layer of retina.
CleanEx; HS_FAM40B; -.
Genevisible; Q9ULQ0; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
InterPro; IPR021819; Far11/STRP_C.
InterPro; IPR012486; Far11/STRP_N.
Pfam; PF11882; DUF3402; 2.
Pfam; PF07923; N1221; 1.
SMART; SM01293; DUF3402; 1.
SMART; SM01292; N1221; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 834 Striatin-interacting protein 2.
/FTId=PRO_0000187022.
COMPBIAS 577 582 Poly-Leu.
MOD_RES 318 318 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 752 758 DIDARPW -> GESSQSS (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014867.
VAR_SEQ 759 834 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014868.
VARIANT 383 383 R -> Q (in dbSNP:rs2242030).
/FTId=VAR_049021.
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


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