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Serine-threonine kinase receptor-associated protein (MAP activator with WD repeats) (UNR-interacting protein) (WD-40 repeat protein PT-WD)

 STRAP_HUMAN             Reviewed;         350 AA.
Q9Y3F4; B2R5S5; B4DNJ6; Q5TZT4; Q9NTK0; Q9UQC8;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
18-JUL-2018, entry version 178.
RecName: Full=Serine-threonine kinase receptor-associated protein;
AltName: Full=MAP activator with WD repeats;
AltName: Full=UNR-interacting protein;
AltName: Full=WD-40 repeat protein PT-WD;
Name=STRAP; Synonyms=MAWD, UNRIP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CSDE1.
PubMed=10049359; DOI=10.1101/gad.13.4.437;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=10646843;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Blood;
Ye M., Zhang Q.H., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L.,
Fan H.Y., Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z.;
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Liu J., Zhou Y., Peng X., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and Retina;
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).
[11]
PROTEIN SEQUENCE OF 250-262 AND 273-290, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[12]
IDENTIFICATION IN SMN COMPLEX, INTERACTION WITH GEMIN6 AND GEMIN7, AND
SUBCELLULAR LOCATION.
PubMed=15848170; DOI=10.1016/j.febslet.2005.03.034;
Carissimi C., Baccon J., Straccia M., Chiarella P., Maiolica A.,
Sawyer A., Rappsilber J., Pellizzoni L.;
"Unrip is a component of SMN complexes active in snRNP assembly.";
FEBS Lett. 579:2348-2354(2005).
[13]
IDENTIFICATION IN SMN COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=16159890; DOI=10.1093/hmg/ddi343;
Grimmler M., Otter S., Peter C., Mueller 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. Mol. Genet. 14:3099-3111(2005).
[14]
FUNCTION, AND INTERACTION WITH PDPK1.
PubMed=16251192; DOI=10.1074/jbc.M507539200;
Seong H.A., Jung H., Choi H.S., Kim K.T., Ha H.;
"Regulation of transforming growth factor-beta signaling and PDK1
kinase activity by physical interaction between PDK1 and serine-
threonine kinase receptor-associated protein.";
J. Biol. Chem. 280:42897-42908(2005).
[15]
FUNCTION IN SNRNP BIOGENESIS, AND IDENTIFICATION IN SMN-SM COMPLEX.
PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
Englbrecht C., Sickmann A., Stark H., Fischer U.;
"An assembly chaperone collaborates with the SMN complex to generate
spliceosomal SnRNPs.";
Cell 135:497-509(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-338, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-338, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: The SMN complex plays a catalyst role in the assembly of
small nuclear ribonucleoproteins (snRNPs), the building blocks of
the spliceosome. Thereby, plays an important role in the splicing
of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common
set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and
SNRPG that assemble in a heptameric protein ring on the Sm site of
the small nuclear RNA to form the core snRNP. In the cytosol, the
Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in
an inactive 6S pICln-Sm complex by the chaperone CLNS1A that
controls the assembly of the core snRNP. Dissociation by the SMN
complex of CLNS1A from the trapped Sm proteins and their transfer
to an SMN-Sm complex triggers the assembly of core snRNPs and
their transport to the nucleus. STRAP plays a role in the cellular
distribution of the SMN complex. Negatively regulates TGF-beta
signaling but positively regulates the PDPK1 kinase activity by
enhancing its autophosphorylation and by significantly reducing
the association of PDPK1 with 14-3-3 protein.
{ECO:0000269|PubMed:16251192, ECO:0000269|PubMed:18984161}.
-!- SUBUNIT: Part of the core SMN complex that contains SMN1,
GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1,
GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3,
SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN6 and GEMIN7.
Associates with the SMN complex in the cytoplasm but not in the
nucleus. Also interacts with CSDE1/UNR and MAWBP. Interacts with
PDPK1. {ECO:0000269|PubMed:10049359, ECO:0000269|PubMed:15848170,
ECO:0000269|PubMed:16159890, ECO:0000269|PubMed:16251192,
ECO:0000269|PubMed:18984161}.
-!- INTERACTION:
Q8WXD5:GEMIN6; NbExp=3; IntAct=EBI-727414, EBI-752301;
Q9H840:GEMIN7; NbExp=4; IntAct=EBI-727414, EBI-715455;
P15531:NME1; NbExp=9; IntAct=EBI-727414, EBI-741141;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localized
predominantly in the cytoplasm but also found in the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y3F4-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y3F4-2; Sequence=VSP_056873;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the WD repeat STRAP family. {ECO:0000305}.
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EMBL; AJ010025; CAB38041.1; -; mRNA.
EMBL; AB024327; BAA75544.1; -; mRNA.
EMBL; AF161496; AAF29111.1; -; mRNA.
EMBL; AY049776; AAL15433.1; -; mRNA.
EMBL; AL136691; CAB66626.1; -; mRNA.
EMBL; BT020044; AAV38847.1; -; mRNA.
EMBL; BT020045; AAV38848.1; -; mRNA.
EMBL; AK297942; BAG60258.1; -; mRNA.
EMBL; AK312295; BAG35222.1; -; mRNA.
EMBL; AC022073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471094; EAW96356.1; -; Genomic_DNA.
EMBL; BC000162; AAH00162.1; -; mRNA.
EMBL; BC062306; AAH62306.1; -; mRNA.
CCDS; CCDS8676.1; -. [Q9Y3F4-1]
RefSeq; NP_009109.3; NM_007178.3. [Q9Y3F4-1]
UniGene; Hs.743971; -.
ProteinModelPortal; Q9Y3F4; -.
SMR; Q9Y3F4; -.
BioGrid; 116342; 94.
CORUM; Q9Y3F4; -.
IntAct; Q9Y3F4; 50.
MINT; Q9Y3F4; -.
STRING; 9606.ENSP00000392270; -.
iPTMnet; Q9Y3F4; -.
PhosphoSitePlus; Q9Y3F4; -.
SwissPalm; Q9Y3F4; -.
BioMuta; STRAP; -.
DMDM; 12643951; -.
OGP; Q9Y3F4; -.
EPD; Q9Y3F4; -.
PaxDb; Q9Y3F4; -.
PeptideAtlas; Q9Y3F4; -.
PRIDE; Q9Y3F4; -.
ProteomicsDB; 86036; -.
TopDownProteomics; Q9Y3F4-1; -. [Q9Y3F4-1]
DNASU; 11171; -.
Ensembl; ENST00000025399; ENSP00000025399; ENSG00000023734. [Q9Y3F4-2]
Ensembl; ENST00000419869; ENSP00000392270; ENSG00000023734. [Q9Y3F4-1]
GeneID; 11171; -.
KEGG; hsa:11171; -.
UCSC; uc001rdc.5; human. [Q9Y3F4-1]
CTD; 11171; -.
DisGeNET; 11171; -.
EuPathDB; HostDB:ENSG00000023734.10; -.
GeneCards; STRAP; -.
HGNC; HGNC:30796; STRAP.
HPA; HPA027320; -.
HPA; HPA055557; -.
HPA; HPA073876; -.
MIM; 605986; gene.
neXtProt; NX_Q9Y3F4; -.
OpenTargets; ENSG00000023734; -.
PharmGKB; PA134867032; -.
eggNOG; KOG0278; Eukaryota.
eggNOG; ENOG410XPJ4; LUCA.
GeneTree; ENSGT00630000089849; -.
HOGENOM; HOG000174258; -.
HOVERGEN; HBG055228; -.
InParanoid; Q9Y3F4; -.
KO; K13137; -.
OMA; MISACKD; -.
OrthoDB; EOG091G0BY5; -.
PhylomeDB; Q9Y3F4; -.
TreeFam; TF323287; -.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
SignaLink; Q9Y3F4; -.
SIGNOR; Q9Y3F4; -.
ChiTaRS; STRAP; human.
GeneWiki; STRAP; -.
GenomeRNAi; 11171; -.
PRO; PR:Q9Y3F4; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000023734; -.
CleanEx; HS_STRAP; -.
ExpressionAtlas; Q9Y3F4; baseline and differential.
Genevisible; Q9Y3F4; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:UniProtKB.
GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:UniProtKB.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00400; WD40; 4.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 4.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Reference proteome; Repeat; WD repeat.
CHAIN 1 350 Serine-threonine kinase receptor-
associated protein.
/FTId=PRO_0000051230.
REPEAT 12 56 WD 1.
REPEAT 57 96 WD 2.
REPEAT 98 137 WD 3.
REPEAT 141 179 WD 4.
REPEAT 180 212 WD 5.
REPEAT 221 262 WD 6.
REPEAT 263 302 WD 7.
MOD_RES 312 312 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 37 37 K -> KGAGQHLPRLSGQH (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056873.
CONFLICT 24 24 G -> D (in Ref. 2; BAA75544).
{ECO:0000305}.
CONFLICT 332 332 E -> A (in Ref. 6; AAV38848).
{ECO:0000305}.
CONFLICT 339 339 D -> E (in Ref. 5; CAB66626).
{ECO:0000305}.
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


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