Full text data of STRAP
STRAP
(MAWD, UNRIP)
[Confidence: low (only semi-automatic identification from reviews)]
Serine-threonine kinase receptor-associated protein (MAP activator with WD repeats; UNR-interacting protein; WD-40 repeat protein PT-WD)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serine-threonine kinase receptor-associated protein (MAP activator with WD repeats; UNR-interacting protein; WD-40 repeat protein PT-WD)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y3F4
ID STRAP_HUMAN Reviewed; 350 AA.
AC Q9Y3F4; B2R5S5; Q5TZT4; Q9NTK0; Q9UQC8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Serine-threonine kinase receptor-associated protein;
DE AltName: Full=MAP activator with WD repeats;
DE AltName: Full=UNR-interacting protein;
DE AltName: Full=WD-40 repeat protein PT-WD;
GN Name=STRAP; Synonyms=MAWD, UNRIP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CSDE1.
RX PubMed=10049359;
RA Hunt S.L., Hsuan J.J., Totty N., Jackson R.J.;
RT "unr, a cellular cytoplasmic RNA-binding protein with five cold-shock
RT domains, is required for internal initiation of translation of human
RT rhinovirus RNA.";
RL Genes Dev. 13:437-448(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10646843;
RA Matsuda S., Katsumata R., Okuda T., Yamamoto T., Miyazaki K.,
RA Senga T., Machida K., Thant A.A., Nakatsugawa S., Hamaguchi M.;
RT "Molecular cloning and characterization of human MAWD, a novel protein
RT containing WD-40 repeats frequently overexpressed in breast cancer.";
RL Cancer Res. 60:13-17(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RA Ye M., Zhang Q.H., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L.,
RA Fan H.Y., Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu J., Zhou Y., Peng X., Yuan J., Qiang B.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Retina;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 250-262 AND 273-290, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [11]
RP IDENTIFICATION IN SMN COMPLEX, INTERACTION WITH GEMIN6 AND GEMIN7, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15848170; DOI=10.1016/j.febslet.2005.03.034;
RA Carissimi C., Baccon J., Straccia M., Chiarella P., Maiolica A.,
RA Sawyer A., Rappsilber J., Pellizzoni L.;
RT "Unrip is a component of SMN complexes active in snRNP assembly.";
RL FEBS Lett. 579:2348-2354(2005).
RN [12]
RP IDENTIFICATION IN SMN COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=16159890; DOI=10.1093/hmg/ddi343;
RA Grimmler M., Otter S., Peter C., Mueller F., Chari A., Fischer U.;
RT "Unrip, a factor implicated in cap-independent translation, associates
RT with the cytosolic SMN complex and influences its intracellular
RT localization.";
RL Hum. Mol. Genet. 14:3099-3111(2005).
RN [13]
RP FUNCTION, AND INTERACTION WITH PDPK1.
RX PubMed=16251192; DOI=10.1074/jbc.M507539200;
RA Seong H.A., Jung H., Choi H.S., Kim K.T., Ha H.;
RT "Regulation of transforming growth factor-beta signaling and PDK1
RT kinase activity by physical interaction between PDK1 and serine-
RT threonine kinase receptor-associated protein.";
RL J. Biol. Chem. 280:42897-42908(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-338, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: The SMN complex plays an essential role in spliceosomal
CC snRNP assembly in the cytoplasm and is required for pre-mRNA
CC splicing in the nucleus. STRAP may play a role in the cellular
CC distribution of the SMN complex. Negatively regulates TGF-beta
CC signaling but positively regulates the PDPK1 kinase activity by
CC enhancing its autophosphorylation and by significantly reducing
CC the association of PDPK1 with 14-3-3 protein.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
CC and STRAP/UNRIP. Binds directly to GEMIN6 and GEMIN7. Associates
CC with the complex in the cytoplasm but not in the nucleus. Also
CC interacts with CSDE1/UNR and MAWBP. Interacts with PDPK1.
CC -!- INTERACTION:
CC P15531:NME1; NbExp=9; IntAct=EBI-727414, EBI-741141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localized
CC predominantly in the cytoplasm but also found in the nucleus.
CC -!- SIMILARITY: Belongs to the WD repeat STRAP family.
CC -!- SIMILARITY: Contains 7 WD repeats.
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DR EMBL; AJ010025; CAB38041.1; -; mRNA.
DR EMBL; AB024327; BAA75544.1; -; mRNA.
DR EMBL; AF161496; AAF29111.1; -; mRNA.
DR EMBL; AY049776; AAL15433.1; -; mRNA.
DR EMBL; AL136691; CAB66626.1; -; mRNA.
DR EMBL; BT020044; AAV38847.1; -; mRNA.
DR EMBL; BT020045; AAV38848.1; -; mRNA.
DR EMBL; AK312295; BAG35222.1; -; mRNA.
DR EMBL; CH471094; EAW96356.1; -; Genomic_DNA.
DR EMBL; BC000162; AAH00162.1; -; mRNA.
DR EMBL; BC062306; AAH62306.1; -; mRNA.
DR RefSeq; NP_009109.3; NM_007178.3.
DR UniGene; Hs.743971; -.
DR ProteinModelPortal; Q9Y3F4; -.
DR SMR; Q9Y3F4; 9-292.
DR IntAct; Q9Y3F4; 13.
DR MINT; MINT-1346033; -.
DR STRING; 9606.ENSP00000392270; -.
DR PhosphoSite; Q9Y3F4; -.
DR DMDM; 12643951; -.
DR OGP; Q9Y3F4; -.
DR PaxDb; Q9Y3F4; -.
DR PeptideAtlas; Q9Y3F4; -.
DR PRIDE; Q9Y3F4; -.
DR DNASU; 11171; -.
DR Ensembl; ENST00000419869; ENSP00000392270; ENSG00000023734.
DR GeneID; 11171; -.
DR KEGG; hsa:11171; -.
DR UCSC; uc001rdc.4; human.
DR CTD; 11171; -.
DR GeneCards; GC12P016035; -.
DR HGNC; HGNC:30796; STRAP.
DR HPA; HPA027320; -.
DR MIM; 605986; gene.
DR neXtProt; NX_Q9Y3F4; -.
DR PharmGKB; PA134867032; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000174258; -.
DR HOVERGEN; HBG055228; -.
DR InParanoid; Q9Y3F4; -.
DR KO; K13137; -.
DR PhylomeDB; Q9Y3F4; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR SignaLink; Q9Y3F4; -.
DR ChiTaRS; STRAP; human.
DR GeneWiki; STRAP; -.
DR GenomeRNAi; 11171; -.
DR NextBio; 42509; -.
DR PRO; PR:Q9Y3F4; -.
DR ArrayExpress; Q9Y3F4; -.
DR Bgee; Q9Y3F4; -.
DR CleanEx; HS_STRAP; -.
DR Genevestigator; Q9Y3F4; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spliceosome; WD repeat.
FT CHAIN 1 350 Serine-threonine kinase receptor-
FT associated protein.
FT /FTId=PRO_0000051230.
FT REPEAT 12 56 WD 1.
FT REPEAT 57 96 WD 2.
FT REPEAT 98 137 WD 3.
FT REPEAT 141 179 WD 4.
FT REPEAT 180 212 WD 5.
FT REPEAT 221 262 WD 6.
FT REPEAT 263 302 WD 7.
FT MOD_RES 335 335 Phosphoserine.
FT MOD_RES 338 338 Phosphoserine.
FT CONFLICT 24 24 G -> D (in Ref. 2; BAA75544).
FT CONFLICT 332 332 E -> A (in Ref. 6; AAV38848).
FT CONFLICT 339 339 D -> E (in Ref. 5; CAB66626).
SQ SEQUENCE 350 AA; 38438 MW; CFCB34D3946290E2 CRC64;
MAMRQTPLTC SGHTRPVVDL AFSGITPYGY FLISACKDGK PMLRQGDTGD WIGTFLGHKG
AVWGATLNKD ATKAATAAAD FTAKVWDAVS GDELMTLAHK HIVKTVDFTQ DSNYLLTGGQ
DKLLRIYDLN KPEAEPKEIS GHTSGIKKAL WCSEDKQILS ADDKTVRLWD HATMTEVKSL
NFNMSVSSME YIPEGEILVI TYGRSIAFHS AVSLDPIKSF EAPATINSAS LHPEKEFLVA
GGEDFKLYKY DYNSGEELES YKGHFGPIHC VRFSPDGELY ASGSEDGTLR LWQTVVGKTY
GLWKCVLPEE DSGELAKPKI GFPETTEEEL EEIASENSDC IFPSAPDVKA
//
ID STRAP_HUMAN Reviewed; 350 AA.
AC Q9Y3F4; B2R5S5; Q5TZT4; Q9NTK0; Q9UQC8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Serine-threonine kinase receptor-associated protein;
DE AltName: Full=MAP activator with WD repeats;
DE AltName: Full=UNR-interacting protein;
DE AltName: Full=WD-40 repeat protein PT-WD;
GN Name=STRAP; Synonyms=MAWD, UNRIP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CSDE1.
RX PubMed=10049359;
RA Hunt S.L., Hsuan J.J., Totty N., Jackson R.J.;
RT "unr, a cellular cytoplasmic RNA-binding protein with five cold-shock
RT domains, is required for internal initiation of translation of human
RT rhinovirus RNA.";
RL Genes Dev. 13:437-448(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10646843;
RA Matsuda S., Katsumata R., Okuda T., Yamamoto T., Miyazaki K.,
RA Senga T., Machida K., Thant A.A., Nakatsugawa S., Hamaguchi M.;
RT "Molecular cloning and characterization of human MAWD, a novel protein
RT containing WD-40 repeats frequently overexpressed in breast cancer.";
RL Cancer Res. 60:13-17(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RA Ye M., Zhang Q.H., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L.,
RA Fan H.Y., Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu J., Zhou Y., Peng X., Yuan J., Qiang B.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Retina;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 250-262 AND 273-290, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [11]
RP IDENTIFICATION IN SMN COMPLEX, INTERACTION WITH GEMIN6 AND GEMIN7, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15848170; DOI=10.1016/j.febslet.2005.03.034;
RA Carissimi C., Baccon J., Straccia M., Chiarella P., Maiolica A.,
RA Sawyer A., Rappsilber J., Pellizzoni L.;
RT "Unrip is a component of SMN complexes active in snRNP assembly.";
RL FEBS Lett. 579:2348-2354(2005).
RN [12]
RP IDENTIFICATION IN SMN COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=16159890; DOI=10.1093/hmg/ddi343;
RA Grimmler M., Otter S., Peter C., Mueller F., Chari A., Fischer U.;
RT "Unrip, a factor implicated in cap-independent translation, associates
RT with the cytosolic SMN complex and influences its intracellular
RT localization.";
RL Hum. Mol. Genet. 14:3099-3111(2005).
RN [13]
RP FUNCTION, AND INTERACTION WITH PDPK1.
RX PubMed=16251192; DOI=10.1074/jbc.M507539200;
RA Seong H.A., Jung H., Choi H.S., Kim K.T., Ha H.;
RT "Regulation of transforming growth factor-beta signaling and PDK1
RT kinase activity by physical interaction between PDK1 and serine-
RT threonine kinase receptor-associated protein.";
RL J. Biol. Chem. 280:42897-42908(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-338, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: The SMN complex plays an essential role in spliceosomal
CC snRNP assembly in the cytoplasm and is required for pre-mRNA
CC splicing in the nucleus. STRAP may play a role in the cellular
CC distribution of the SMN complex. Negatively regulates TGF-beta
CC signaling but positively regulates the PDPK1 kinase activity by
CC enhancing its autophosphorylation and by significantly reducing
CC the association of PDPK1 with 14-3-3 protein.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
CC and STRAP/UNRIP. Binds directly to GEMIN6 and GEMIN7. Associates
CC with the complex in the cytoplasm but not in the nucleus. Also
CC interacts with CSDE1/UNR and MAWBP. Interacts with PDPK1.
CC -!- INTERACTION:
CC P15531:NME1; NbExp=9; IntAct=EBI-727414, EBI-741141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localized
CC predominantly in the cytoplasm but also found in the nucleus.
CC -!- SIMILARITY: Belongs to the WD repeat STRAP family.
CC -!- SIMILARITY: Contains 7 WD repeats.
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DR EMBL; AJ010025; CAB38041.1; -; mRNA.
DR EMBL; AB024327; BAA75544.1; -; mRNA.
DR EMBL; AF161496; AAF29111.1; -; mRNA.
DR EMBL; AY049776; AAL15433.1; -; mRNA.
DR EMBL; AL136691; CAB66626.1; -; mRNA.
DR EMBL; BT020044; AAV38847.1; -; mRNA.
DR EMBL; BT020045; AAV38848.1; -; mRNA.
DR EMBL; AK312295; BAG35222.1; -; mRNA.
DR EMBL; CH471094; EAW96356.1; -; Genomic_DNA.
DR EMBL; BC000162; AAH00162.1; -; mRNA.
DR EMBL; BC062306; AAH62306.1; -; mRNA.
DR RefSeq; NP_009109.3; NM_007178.3.
DR UniGene; Hs.743971; -.
DR ProteinModelPortal; Q9Y3F4; -.
DR SMR; Q9Y3F4; 9-292.
DR IntAct; Q9Y3F4; 13.
DR MINT; MINT-1346033; -.
DR STRING; 9606.ENSP00000392270; -.
DR PhosphoSite; Q9Y3F4; -.
DR DMDM; 12643951; -.
DR OGP; Q9Y3F4; -.
DR PaxDb; Q9Y3F4; -.
DR PeptideAtlas; Q9Y3F4; -.
DR PRIDE; Q9Y3F4; -.
DR DNASU; 11171; -.
DR Ensembl; ENST00000419869; ENSP00000392270; ENSG00000023734.
DR GeneID; 11171; -.
DR KEGG; hsa:11171; -.
DR UCSC; uc001rdc.4; human.
DR CTD; 11171; -.
DR GeneCards; GC12P016035; -.
DR HGNC; HGNC:30796; STRAP.
DR HPA; HPA027320; -.
DR MIM; 605986; gene.
DR neXtProt; NX_Q9Y3F4; -.
DR PharmGKB; PA134867032; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000174258; -.
DR HOVERGEN; HBG055228; -.
DR InParanoid; Q9Y3F4; -.
DR KO; K13137; -.
DR PhylomeDB; Q9Y3F4; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR SignaLink; Q9Y3F4; -.
DR ChiTaRS; STRAP; human.
DR GeneWiki; STRAP; -.
DR GenomeRNAi; 11171; -.
DR NextBio; 42509; -.
DR PRO; PR:Q9Y3F4; -.
DR ArrayExpress; Q9Y3F4; -.
DR Bgee; Q9Y3F4; -.
DR CleanEx; HS_STRAP; -.
DR Genevestigator; Q9Y3F4; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spliceosome; WD repeat.
FT CHAIN 1 350 Serine-threonine kinase receptor-
FT associated protein.
FT /FTId=PRO_0000051230.
FT REPEAT 12 56 WD 1.
FT REPEAT 57 96 WD 2.
FT REPEAT 98 137 WD 3.
FT REPEAT 141 179 WD 4.
FT REPEAT 180 212 WD 5.
FT REPEAT 221 262 WD 6.
FT REPEAT 263 302 WD 7.
FT MOD_RES 335 335 Phosphoserine.
FT MOD_RES 338 338 Phosphoserine.
FT CONFLICT 24 24 G -> D (in Ref. 2; BAA75544).
FT CONFLICT 332 332 E -> A (in Ref. 6; AAV38848).
FT CONFLICT 339 339 D -> E (in Ref. 5; CAB66626).
SQ SEQUENCE 350 AA; 38438 MW; CFCB34D3946290E2 CRC64;
MAMRQTPLTC SGHTRPVVDL AFSGITPYGY FLISACKDGK PMLRQGDTGD WIGTFLGHKG
AVWGATLNKD ATKAATAAAD FTAKVWDAVS GDELMTLAHK HIVKTVDFTQ DSNYLLTGGQ
DKLLRIYDLN KPEAEPKEIS GHTSGIKKAL WCSEDKQILS ADDKTVRLWD HATMTEVKSL
NFNMSVSSME YIPEGEILVI TYGRSIAFHS AVSLDPIKSF EAPATINSAS LHPEKEFLVA
GGEDFKLYKY DYNSGEELES YKGHFGPIHC VRFSPDGELY ASGSEDGTLR LWQTVVGKTY
GLWKCVLPEE DSGELAKPKI GFPETTEEEL EEIASENSDC IFPSAPDVKA
//
MIM
605986
*RECORD*
*FIELD* NO
605986
*FIELD* TI
*605986 SERINE/THREONINE KINASE RECEPTOR-ASSOCIATED PROTEIN; STRAP
;;UNR-INTERACTING PROTEIN; UNRIP;;
read moreMITOGEN-ACTIVATED PROTEIN KINASE ACTIVATOR WITH WD REPEATS; MAWD;;
MAPK ACTIVATOR WITH WD REPEATS
*FIELD* TX
CLONING
Hunt et al. (1999) stated that a number of viral and some cellular mRNAs
are translated by an unusual mechanism involving internal ribosome entry
sites (IRES). Some viruses require cellular factors (e.g., PTB; 600693)
to stimulate the activity of viral IRES. By biochemical purification of
rhinovirus IRES-stimulating activity from HeLa cells, micropeptide
sequence analysis, EST database searching, and PCR analysis, Hunt et al.
(1999) identified cDNAs encoding UNR (CSDE1; 191510) and STRAP, which
they called UNRIP (UNR-interacting protein). Sequence analysis predicted
that the 350-amino acid UNRIP protein, which is 25% identical to EIF3S2
(603911), contains 6 WD repeats. Coimmunoprecipitation analysis
indicated that UNRIP interacts with UNR, which acts synergistically with
PTB to stimulate translation dependent on the rhinovirus IRES.
By searching EST databases for proteins resembling EIF3S2 and by RT-PCR
of a placenta cDNA library, Matsuda et al. (2000) isolated cDNAs
encoding STRAP, which they termed mitogen-activated protein kinase
(MAPK) activator with WD repeats, or MAWD. Northern blot and RT-PCR
analyses revealed ubiquitous expression of a 2.0-kb MAWD transcript.
Western blot analysis showed that overexpression of MAWD induces
expression of activated MAPK and correlates with anchorage-independent
growth in vitro. PCR and immunoblot analyses detected expression of MAWD
as a 39-kD protein in breast cancer but not normal tissue.
Immunohistochemical analysis demonstrated cytoplasmic expression in
tumor cells. Matsuda et al. (2000) proposed that the MAWD gene may be a
frequent target for alteration in breast cancer.
GENE FUNCTION
Spliceosomal uridine-rich small nuclear ribonucleoprotein (snRNP)
assembly is an active process mediated by the macromolecular SMN complex
(see SMN1, 600354). This complex contains the SMN1 protein and 6
additional proteins named GEMIN2 (SIP1; 602595) to GEMIN7 (607419),
according to their localization to nuclear structures termed gems.
Grimmler et al. (2005) showed that UNRIP is integrated into a complex
with UNR or with the SMN complex in vivo in a mutually exclusive manner.
In the latter case, UNRIP is recruited to the active SMN complex via a
stable interaction with GEMIN7. However, unlike SMN and the gemins,
UNRIP localized predominantly to the cytoplasm and was absent from
gems/Cajal bodies. RNAi-induced reduction of UNRIP protein levels led to
enhanced accumulation of SMN in the nucleus as evident by the increased
formation of nuclear gems/Cajal bodies. Grimmler et al. (2005) concluded
that UNRIP is the first component of the uridine-rich snRNP assembly
machinery that associates with the SMN complex in a compartment-specific
way, and it may play a crucial role in the intracellular distribution of
the SMN complex.
MAPPING
Matsuda et al. (2000) mapped the STRAP gene to chromosome 12q11-q12 by
radiation hybrid analysis. However, Gross (2010) mapped the STRAP gene
to chromosome 12p12.3 based on an alignment of the STRAP sequence
(GenBank GENBANK BC000162) with the genomic sequence (GRCh37).
*FIELD* RF
1. Grimmler, M.; Otter, S.; Peter, C.; Muller, F.; Chari, A.; Fischer,
U.: Unrip, a factor implicated in cap-independent translation, associates
with the cytosolic SMN complex and influences its intracellular localization. Hum.
Molec. Genet. 14: 3099-3111, 2005.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 5/18/2010.
3. Hunt, S. L.; Hsuan, J. J.; Totty, N.; Jackson, R. J.: unr, a cellular
cytoplasmic RNA-binding protein with five cold-shock domains, is required
for internal initiation of translation of human rhinovirus RNA. Genes
Dev. 13: 437-448, 1999.
4. Matsuda, S.; Katsumata, R.; Okuda, T.; Yamamoto, T.; Miyazaki,
K.; Senga, T.; Machida, K.; Thant, A. A.; Nakatsugawa, S.; Hamaguchi,
M.: Molecular cloning and characterization of human MAWD, a novel
protein containing WD-40 repeats frequently overexpressed in breast
cancer. Cancer Res. 60: 13-17, 2000.
*FIELD* CN
Matthew B. Gross - updated: 05/18/2010
George E. Tiller - updated: 5/13/2009
*FIELD* CD
Paul J. Converse: 6/5/2001
*FIELD* ED
mgross: 05/18/2010
wwang: 6/25/2009
terry: 5/13/2009
mgross: 6/5/2001
*RECORD*
*FIELD* NO
605986
*FIELD* TI
*605986 SERINE/THREONINE KINASE RECEPTOR-ASSOCIATED PROTEIN; STRAP
;;UNR-INTERACTING PROTEIN; UNRIP;;
read moreMITOGEN-ACTIVATED PROTEIN KINASE ACTIVATOR WITH WD REPEATS; MAWD;;
MAPK ACTIVATOR WITH WD REPEATS
*FIELD* TX
CLONING
Hunt et al. (1999) stated that a number of viral and some cellular mRNAs
are translated by an unusual mechanism involving internal ribosome entry
sites (IRES). Some viruses require cellular factors (e.g., PTB; 600693)
to stimulate the activity of viral IRES. By biochemical purification of
rhinovirus IRES-stimulating activity from HeLa cells, micropeptide
sequence analysis, EST database searching, and PCR analysis, Hunt et al.
(1999) identified cDNAs encoding UNR (CSDE1; 191510) and STRAP, which
they called UNRIP (UNR-interacting protein). Sequence analysis predicted
that the 350-amino acid UNRIP protein, which is 25% identical to EIF3S2
(603911), contains 6 WD repeats. Coimmunoprecipitation analysis
indicated that UNRIP interacts with UNR, which acts synergistically with
PTB to stimulate translation dependent on the rhinovirus IRES.
By searching EST databases for proteins resembling EIF3S2 and by RT-PCR
of a placenta cDNA library, Matsuda et al. (2000) isolated cDNAs
encoding STRAP, which they termed mitogen-activated protein kinase
(MAPK) activator with WD repeats, or MAWD. Northern blot and RT-PCR
analyses revealed ubiquitous expression of a 2.0-kb MAWD transcript.
Western blot analysis showed that overexpression of MAWD induces
expression of activated MAPK and correlates with anchorage-independent
growth in vitro. PCR and immunoblot analyses detected expression of MAWD
as a 39-kD protein in breast cancer but not normal tissue.
Immunohistochemical analysis demonstrated cytoplasmic expression in
tumor cells. Matsuda et al. (2000) proposed that the MAWD gene may be a
frequent target for alteration in breast cancer.
GENE FUNCTION
Spliceosomal uridine-rich small nuclear ribonucleoprotein (snRNP)
assembly is an active process mediated by the macromolecular SMN complex
(see SMN1, 600354). This complex contains the SMN1 protein and 6
additional proteins named GEMIN2 (SIP1; 602595) to GEMIN7 (607419),
according to their localization to nuclear structures termed gems.
Grimmler et al. (2005) showed that UNRIP is integrated into a complex
with UNR or with the SMN complex in vivo in a mutually exclusive manner.
In the latter case, UNRIP is recruited to the active SMN complex via a
stable interaction with GEMIN7. However, unlike SMN and the gemins,
UNRIP localized predominantly to the cytoplasm and was absent from
gems/Cajal bodies. RNAi-induced reduction of UNRIP protein levels led to
enhanced accumulation of SMN in the nucleus as evident by the increased
formation of nuclear gems/Cajal bodies. Grimmler et al. (2005) concluded
that UNRIP is the first component of the uridine-rich snRNP assembly
machinery that associates with the SMN complex in a compartment-specific
way, and it may play a crucial role in the intracellular distribution of
the SMN complex.
MAPPING
Matsuda et al. (2000) mapped the STRAP gene to chromosome 12q11-q12 by
radiation hybrid analysis. However, Gross (2010) mapped the STRAP gene
to chromosome 12p12.3 based on an alignment of the STRAP sequence
(GenBank GENBANK BC000162) with the genomic sequence (GRCh37).
*FIELD* RF
1. Grimmler, M.; Otter, S.; Peter, C.; Muller, F.; Chari, A.; Fischer,
U.: Unrip, a factor implicated in cap-independent translation, associates
with the cytosolic SMN complex and influences its intracellular localization. Hum.
Molec. Genet. 14: 3099-3111, 2005.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 5/18/2010.
3. Hunt, S. L.; Hsuan, J. J.; Totty, N.; Jackson, R. J.: unr, a cellular
cytoplasmic RNA-binding protein with five cold-shock domains, is required
for internal initiation of translation of human rhinovirus RNA. Genes
Dev. 13: 437-448, 1999.
4. Matsuda, S.; Katsumata, R.; Okuda, T.; Yamamoto, T.; Miyazaki,
K.; Senga, T.; Machida, K.; Thant, A. A.; Nakatsugawa, S.; Hamaguchi,
M.: Molecular cloning and characterization of human MAWD, a novel
protein containing WD-40 repeats frequently overexpressed in breast
cancer. Cancer Res. 60: 13-17, 2000.
*FIELD* CN
Matthew B. Gross - updated: 05/18/2010
George E. Tiller - updated: 5/13/2009
*FIELD* CD
Paul J. Converse: 6/5/2001
*FIELD* ED
mgross: 05/18/2010
wwang: 6/25/2009
terry: 5/13/2009
mgross: 6/5/2001