STRAP_HUMAN
ID STRAP_HUMAN Reviewed; 350 AA.
AC Q9Y3F4; B2R5S5; B4DNJ6; Q5TZT4; Q9NTK0; Q9UQC8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 205.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CSDE1.
RX PubMed=10049359; DOI=10.1101/gad.13.4.437;
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] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=10646843;
RA Matsuda S., Katsumata R., Okuda T., Yamamoto T., Miyazaki K., Senga T.,
RA 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] (ISOFORM 1).
RC TISSUE=Blood;
RA Ye M., Zhang Q.H., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L., Fan H.Y.,
RA 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] (ISOFORM 1).
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] (ISOFORM 1).
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., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PROTEIN SEQUENCE OF 250-262 AND 273-290, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [12]
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., Sawyer A.,
RA Rappsilber J., Pellizzoni L.;
RT "Unrip is a component of SMN complexes active in snRNP assembly.";
RL FEBS Lett. 579:2348-2354(2005).
RN [13]
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 with
RT the cytosolic SMN complex and influences its intracellular localization.";
RL Hum. Mol. Genet. 14:3099-3111(2005).
RN [14]
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 kinase
RT activity by physical interaction between PDK1 and serine-threonine kinase
RT receptor-associated protein.";
RL J. Biol. Chem. 280:42897-42908(2005).
RN [15]
RP IDENTIFICATION IN THE SMN COMPLEX, AND INTERACTION WITH GEMIN7.
RX PubMed=17178713; DOI=10.1074/jbc.m608528200;
RA Otter S., Grimmler M., Neuenkirchen N., Chari A., Sickmann A., Fischer U.;
RT "A comprehensive interaction map of the human survival of motor neuron
RT (SMN) complex.";
RL J. Biol. Chem. 282:5825-5833(2007).
RN [16]
RP FUNCTION IN SNRNP BIOGENESIS, AND IDENTIFICATION IN SMN-SM COMPLEX.
RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
RA Englbrecht C., Sickmann A., Stark H., Fischer U.;
RT "An assembly chaperone collaborates with the SMN complex to generate
RT spliceosomal SnRNPs.";
RL Cell 135:497-509(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND IDENTIFICATION BY
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-338, AND
RP IDENTIFICATION BY 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).
RN [21]
RP INTERACTION WITH TRIM48.
RX PubMed=29186683; DOI=10.1016/j.celrep.2017.11.007;
RA Hirata Y., Katagiri K., Nagaoka K., Morishita T., Kudoh Y., Hatta T.,
RA Naguro I., Kano K., Udagawa T., Natsume T., Aoki J., Inada T., Noguchi T.,
RA Ichijo H., Matsuzawa A.;
RT "TRIM48 Promotes ASK1 Activation and Cell Death through Ubiquitination-
RT Dependent Degradation of the ASK1-Negative Regulator PRMT1.";
RL Cell Rep. 21:2447-2457(2017).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP plays a
CC role in the cellular distribution of the SMN complex. Negatively
CC regulates TGF-beta signaling but positively regulates the PDPK1 kinase
CC activity by enhancing its autophosphorylation and by significantly
CC reducing the association of PDPK1 with 14-3-3 protein.
CC {ECO:0000269|PubMed:16251192, ECO:0000269|PubMed:18984161}.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP
CC (PubMed:16159890, PubMed:15848170, PubMed:17178713). Part of the SMN-Sm
CC complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5,
CC GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1,
CC SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG (PubMed:18984161). Associates
CC with the SMN complex in the cytoplasm but not in the nucleus
CC (PubMed:16159890). Interacts with GEMIN6; the interaction is direct
CC (PubMed:15848170). Interacts with GEMIN7; the interaction is direct
CC (PubMed:15848170, PubMed:17178713). Interacts with CSDE1/UNR and MAWBP
CC (PubMed:10049359). Interacts with PDPK1 (PubMed:16251192). Interacts
CC with TRIM48 (PubMed:29186683). {ECO:0000269|PubMed:10049359,
CC ECO:0000269|PubMed:15848170, ECO:0000269|PubMed:16159890,
CC ECO:0000269|PubMed:16251192, ECO:0000269|PubMed:17178713,
CC ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:29186683}.
CC -!- INTERACTION:
CC Q9Y3F4; Q8WXD5: GEMIN6; NbExp=4; IntAct=EBI-727414, EBI-752301;
CC Q9Y3F4; Q9H840: GEMIN7; NbExp=5; IntAct=EBI-727414, EBI-715455;
CC Q9Y3F4; P42858: HTT; NbExp=4; IntAct=EBI-727414, EBI-466029;
CC Q9Y3F4; P15531: NME1; NbExp=9; IntAct=EBI-727414, EBI-741141;
CC Q9Y3F4; Q7Z422-4: SZRD1; NbExp=3; IntAct=EBI-727414, EBI-23877111;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localized predominantly
CC in the cytoplasm but also found in the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y3F4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3F4-2; Sequence=VSP_056873;
CC -!- SIMILARITY: Belongs to the WD repeat STRAP family. {ECO:0000305}.
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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; AK297942; BAG60258.1; -; mRNA.
DR EMBL; AK312295; BAG35222.1; -; mRNA.
DR EMBL; AC022073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96356.1; -; Genomic_DNA.
DR EMBL; BC000162; AAH00162.1; -; mRNA.
DR EMBL; BC062306; AAH62306.1; -; mRNA.
DR CCDS; CCDS8676.1; -. [Q9Y3F4-1]
DR RefSeq; NP_009109.3; NM_007178.3. [Q9Y3F4-1]
DR AlphaFoldDB; Q9Y3F4; -.
DR SMR; Q9Y3F4; -.
DR BioGRID; 116342; 177.
DR ComplexPortal; CPX-6031; SMN complex.
DR CORUM; Q9Y3F4; -.
DR IntAct; Q9Y3F4; 70.
DR MINT; Q9Y3F4; -.
DR STRING; 9606.ENSP00000392270; -.
DR GlyGen; Q9Y3F4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3F4; -.
DR PhosphoSitePlus; Q9Y3F4; -.
DR SwissPalm; Q9Y3F4; -.
DR BioMuta; STRAP; -.
DR DMDM; 12643951; -.
DR OGP; Q9Y3F4; -.
DR EPD; Q9Y3F4; -.
DR jPOST; Q9Y3F4; -.
DR MassIVE; Q9Y3F4; -.
DR MaxQB; Q9Y3F4; -.
DR PaxDb; Q9Y3F4; -.
DR PeptideAtlas; Q9Y3F4; -.
DR PRIDE; Q9Y3F4; -.
DR ProteomicsDB; 4702; -.
DR ProteomicsDB; 86036; -. [Q9Y3F4-1]
DR TopDownProteomics; Q9Y3F4-1; -. [Q9Y3F4-1]
DR Antibodypedia; 12145; 224 antibodies from 32 providers.
DR DNASU; 11171; -.
DR Ensembl; ENST00000025399.10; ENSP00000025399.6; ENSG00000023734.11. [Q9Y3F4-2]
DR Ensembl; ENST00000419869.7; ENSP00000392270.2; ENSG00000023734.11. [Q9Y3F4-1]
DR GeneID; 11171; -.
DR KEGG; hsa:11171; -.
DR MANE-Select; ENST00000419869.7; ENSP00000392270.2; NM_007178.4; NP_009109.3.
DR UCSC; uc001rdc.5; human. [Q9Y3F4-1]
DR CTD; 11171; -.
DR DisGeNET; 11171; -.
DR GeneCards; STRAP; -.
DR HGNC; HGNC:30796; STRAP.
DR HPA; ENSG00000023734; Low tissue specificity.
DR MIM; 605986; gene.
DR neXtProt; NX_Q9Y3F4; -.
DR OpenTargets; ENSG00000023734; -.
DR PharmGKB; PA134867032; -.
DR VEuPathDB; HostDB:ENSG00000023734; -.
DR eggNOG; KOG0278; Eukaryota.
DR GeneTree; ENSGT00940000155197; -.
DR HOGENOM; CLU_000288_57_6_1; -.
DR InParanoid; Q9Y3F4; -.
DR OMA; FQHNHIV; -.
DR OrthoDB; 1239790at2759; -.
DR PhylomeDB; Q9Y3F4; -.
DR TreeFam; TF323287; -.
DR PathwayCommons; Q9Y3F4; -.
DR Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR SignaLink; Q9Y3F4; -.
DR SIGNOR; Q9Y3F4; -.
DR BioGRID-ORCS; 11171; 605 hits in 1086 CRISPR screens.
DR ChiTaRS; STRAP; human.
DR GeneWiki; STRAP; -.
DR GenomeRNAi; 11171; -.
DR Pharos; Q9Y3F4; Tbio.
DR PRO; PR:Q9Y3F4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y3F4; protein.
DR Bgee; ENSG00000023734; Expressed in secondary oocyte and 212 other tissues.
DR ExpressionAtlas; Q9Y3F4; baseline and differential.
DR Genevisible; Q9Y3F4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:1990447; F:U2 snRNP binding; IEA:Ensembl.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 4.
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 Alternative splicing; Cytoplasm; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..350
FT /note="Serine-threonine kinase receptor-associated protein"
FT /id="PRO_0000051230"
FT REPEAT 12..56
FT /note="WD 1"
FT REPEAT 57..96
FT /note="WD 2"
FT REPEAT 98..137
FT /note="WD 3"
FT REPEAT 141..179
FT /note="WD 4"
FT REPEAT 180..212
FT /note="WD 5"
FT REPEAT 221..262
FT /note="WD 6"
FT REPEAT 263..302
FT /note="WD 7"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 37
FT /note="K -> KGAGQHLPRLSGQH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056873"
FT CONFLICT 24
FT /note="G -> D (in Ref. 2; BAA75544)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="E -> A (in Ref. 6; AAV38848)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="D -> E (in Ref. 5; CAB66626)"
FT /evidence="ECO:0000305"
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
