3BP5_HUMAN
ID 3BP5_HUMAN Reviewed; 455 AA.
AC O60239; B3KQW6; Q5JWV9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=SH3 domain-binding protein 5;
DE Short=SH3BP-5;
DE AltName: Full=SH3 domain-binding protein that preferentially associates with BTK;
GN Name=SH3BP5; Synonyms=SAB;
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=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Adrenal gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-455 (ISOFORM 1), FUNCTION, INTERACTION
RP WITH BTK, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=9571151; DOI=10.1006/bbrc.1998.8420;
RA Matsushita M., Yamadori T., Kato S., Takemoto Y., Inazawa J., Baba Y.,
RA Hashimoto S., Sekine S., Arai S., Kunikata T., Kurimoto M., Kishimoto T.,
RA Tsukada S.;
RT "Identification and characterization of a novel SH3-domain binding protein,
RT Sab, which preferentially associates with Bruton's tyrosine kinase (Btk).";
RL Biochem. Biophys. Res. Commun. 245:337-343(1998).
RN [7]
RP INTERACTION WITH BTK, AND FUNCTION.
RX PubMed=10339589; DOI=10.1073/pnas.96.11.6341;
RA Yamadori T., Baba Y., Mastushita M., Hashimoto S., Kurosaki M.,
RA Kurosaki T., Kishimoto T., Tsukada S.;
RT "Bruton's tyrosine kinase activity is negatively regulated by Sab, the Btk-
RT SH3 domain-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6341-6346(1999).
RN [8]
RP INTERACTION WITH MAPK8; MAPK9 AND MAPK10, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LEU-347; LEU-349; LEU-434 AND LEU-436.
RX PubMed=12167088; DOI=10.1042/bj20020553;
RA Wiltshire C., Matsushita M., Tsukada S., Gillespie D.A., May G.H.;
RT "A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab (SH3BP5),
RT associates with mitochondria.";
RL Biochem. J. 367:577-585(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, 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 [14]
RP INTERACTION WITH RAB11A, AND FUNCTION.
RX PubMed=26506309; DOI=10.1016/j.devcel.2015.09.013;
RA Sakaguchi A., Sato M., Sato K., Gengyo-Ando K., Yorimitsu T., Nakai J.,
RA Hara T., Sato K., Sato K.;
RT "REI-1 is a guanine nucleotide exchange factor regulating RAB-11
RT localization and function in C. elegans embryos.";
RL Dev. Cell 35:211-221(2015).
RN [15] {ECO:0007744|PDB:6DJL}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-265 IN COMPLEX WITH RAB11A,
RP FUNCTION, COILED COIL, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 52-LEU--GLN-54 AND 250-LEU-GLU-251.
RX PubMed=30217979; DOI=10.1038/s41467-018-06196-z;
RA Jenkins M.L., Margaria J.P., Stariha J.T.B., Hoffmann R.M., McPhail J.A.,
RA Hamelin D.J., Boulanger M.J., Hirsch E., Burke J.E.;
RT "Structural determinants of Rab11 activation by the guanine nucleotide
RT exchange factor SH3BP5.";
RL Nat. Commun. 9:3772-3772(2018).
CC -!- FUNCTION: Functions as guanine nucleotide exchange factor (GEF) with
CC specificity for RAB11A and RAB25 (PubMed:26506309, PubMed:30217979).
CC Inhibits the auto- and transphosphorylation activity of BTK. Plays a
CC negative regulatory role in BTK-related cytoplasmic signaling in B-
CC cells. May be involved in BCR-induced apoptotic cell death.
CC {ECO:0000269|PubMed:10339589, ECO:0000269|PubMed:26506309,
CC ECO:0000269|PubMed:30217979, ECO:0000269|PubMed:9571151}.
CC -!- SUBUNIT: Interacts with BTK (PubMed:9571151, PubMed:10339589).
CC Interacts with all isoforms of MAPK8, MAPK9, MAPK10 and MAPK12
CC (PubMed:12167088). Interacts with GDP-bound and nucleotide-free forms
CC of RAB11A (PubMed:26506309, PubMed:30217979).
CC {ECO:0000269|PubMed:10339589, ECO:0000269|PubMed:12167088,
CC ECO:0000269|PubMed:26506309, ECO:0000269|PubMed:30217979,
CC ECO:0000269|PubMed:9571151}.
CC -!- INTERACTION:
CC O60239; Q06187: BTK; NbExp=4; IntAct=EBI-624860, EBI-624835;
CC O60239; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-624860, EBI-9091197;
CC O60239; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-624860, EBI-3911716;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:30217979}; Peripheral membrane protein
CC {ECO:0000269|PubMed:30217979}. Mitochondrion
CC {ECO:0000269|PubMed:12167088}. Note=Colocalizes with RAB11A on
CC cytoplasmic vesicle membranes. {ECO:0000269|PubMed:30217979}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60239-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60239-2; Sequence=VSP_042854;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and ovaries. It is also
CC expressed in a variety of tissues including spleen, lymph node, thymus,
CC bone marrow, fetal liver, colon, small intestine and prostate.
CC {ECO:0000269|PubMed:9571151}.
CC -!- DOMAIN: The N-terminal half of the protein mediates interaction with
CC RAB11A and functions as guanine nucleotide exchange factor. Four long
CC alpha-helices (interrupted by a central kink) assemble into coiled
CC coils, giving rise to a 'V' shape. {ECO:0000269|PubMed:30217979}.
CC -!- SIMILARITY: Belongs to the SH3BP5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25922.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK090524; BAG52178.1; -; mRNA.
DR EMBL; AC087590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117422; CAI46220.1; -; mRNA.
DR EMBL; CH471055; EAW64225.1; -; Genomic_DNA.
DR EMBL; BC010123; AAH10123.2; -; mRNA.
DR EMBL; AB005047; BAA25922.1; ALT_INIT; mRNA.
DR CCDS; CCDS2625.2; -. [O60239-1]
DR CCDS; CCDS43055.1; -. [O60239-2]
DR PIR; JE0086; JE0086.
DR RefSeq; NP_001018009.2; NM_001018009.3. [O60239-2]
DR RefSeq; NP_004835.2; NM_004844.4. [O60239-1]
DR RefSeq; XP_016863011.1; XM_017007522.1. [O60239-2]
DR RefSeq; XP_016863012.1; XM_017007523.1. [O60239-2]
DR RefSeq; XP_016863013.1; XM_017007524.1. [O60239-2]
DR RefSeq; XP_016863014.1; XM_017007525.1. [O60239-2]
DR PDB; 4H3B; X-ray; 2.08 A; B/D=341-350.
DR PDB; 6DJL; X-ray; 3.10 A; B/C/D/E=1-265.
DR PDB; 6IXE; X-ray; 3.35 A; A=41-266.
DR PDB; 6IXF; X-ray; 3.60 A; A/B=41-266.
DR PDB; 6IXG; X-ray; 3.80 A; A/B=41-266.
DR PDB; 6IXV; X-ray; 3.80 A; A/B/C/D=10-276.
DR PDBsum; 4H3B; -.
DR PDBsum; 6DJL; -.
DR PDBsum; 6IXE; -.
DR PDBsum; 6IXF; -.
DR PDBsum; 6IXG; -.
DR PDBsum; 6IXV; -.
DR AlphaFoldDB; O60239; -.
DR SMR; O60239; -.
DR BioGRID; 114853; 25.
DR ELM; O60239; -.
DR IntAct; O60239; 22.
DR STRING; 9606.ENSP00000373301; -.
DR iPTMnet; O60239; -.
DR PhosphoSitePlus; O60239; -.
DR BioMuta; SH3BP5; -.
DR EPD; O60239; -.
DR jPOST; O60239; -.
DR MassIVE; O60239; -.
DR MaxQB; O60239; -.
DR PaxDb; O60239; -.
DR PeptideAtlas; O60239; -.
DR PRIDE; O60239; -.
DR ProteomicsDB; 49268; -. [O60239-1]
DR ProteomicsDB; 49269; -. [O60239-2]
DR TopDownProteomics; O60239-1; -. [O60239-1]
DR Antibodypedia; 26718; 168 antibodies from 27 providers.
DR DNASU; 9467; -.
DR Ensembl; ENST00000383791.8; ENSP00000373301.3; ENSG00000131370.16. [O60239-1]
DR Ensembl; ENST00000408919.7; ENSP00000386231.3; ENSG00000131370.16. [O60239-2]
DR Ensembl; ENST00000426925.5; ENSP00000388553.1; ENSG00000131370.16. [O60239-2]
DR GeneID; 9467; -.
DR KEGG; hsa:9467; -.
DR MANE-Select; ENST00000383791.8; ENSP00000373301.3; NM_004844.5; NP_004835.2.
DR UCSC; uc003bzp.3; human. [O60239-1]
DR CTD; 9467; -.
DR DisGeNET; 9467; -.
DR GeneCards; SH3BP5; -.
DR HGNC; HGNC:10827; SH3BP5.
DR HPA; ENSG00000131370; Tissue enhanced (adrenal).
DR MIM; 605612; gene.
DR neXtProt; NX_O60239; -.
DR OpenTargets; ENSG00000131370; -.
DR PharmGKB; PA35735; -.
DR VEuPathDB; HostDB:ENSG00000131370; -.
DR eggNOG; KOG2008; Eukaryota.
DR GeneTree; ENSGT00390000018500; -.
DR HOGENOM; CLU_048895_1_0_1; -.
DR InParanoid; O60239; -.
DR OMA; QFPPATR; -.
DR PhylomeDB; O60239; -.
DR TreeFam; TF105573; -.
DR PathwayCommons; O60239; -.
DR SignaLink; O60239; -.
DR SIGNOR; O60239; -.
DR BioGRID-ORCS; 9467; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; SH3BP5; human.
DR GeneWiki; SH3BP5; -.
DR GenomeRNAi; 9467; -.
DR Pharos; O60239; Tbio.
DR PRO; PR:O60239; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O60239; protein.
DR Bgee; ENSG00000131370; Expressed in adrenal tissue and 211 other tissues.
DR ExpressionAtlas; O60239; baseline and differential.
DR Genevisible; O60239; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR DisProt; DP02850; -.
DR IDEAL; IID00507; -.
DR InterPro; IPR007940; SH3BP5.
DR PANTHER; PTHR19423; PTHR19423; 2.
DR Pfam; PF05276; SH3BP5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasmic vesicle;
KW Guanine-nucleotide releasing factor; Membrane; Mitochondrion;
KW Phosphoprotein; Reference proteome; SH3-binding.
FT CHAIN 1..455
FT /note="SH3 domain-binding protein 5"
FT /id="PRO_0000064368"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..265
FT /note="Sufficient for interaction with RAB11A and for
FT guanine nucleotide exchange activity"
FT /evidence="ECO:0000269|PubMed:30217979"
FT REGION 259..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..90
FT /evidence="ECO:0000269|PubMed:30217979"
FT COILED 97..145
FT /evidence="ECO:0000269|PubMed:30217979"
FT COILED 154..200
FT /evidence="ECO:0000269|PubMed:30217979"
FT COILED 211..255
FT /evidence="ECO:0000269|PubMed:30217979"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 351
FT /note="Phosphoserine; by MAPK12 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:Q91Y80"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z131"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z131"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y80"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042854"
FT MUTAGEN 52..54
FT /note="LNQ->AAA: Loss of guanine nucleotide exchange factor
FT activity."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 250..251
FT /note="LE->AK: Loss of guanine nucleotide exchange factor
FT activity."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 347
FT /note="L->A: Loss of phosphorylation and binding by
FT phospho-JNK; when associated with A-349."
FT /evidence="ECO:0000269|PubMed:12167088"
FT MUTAGEN 349
FT /note="L->A: Loss of phosphorylation and binding by
FT phospho-JNK; when associated with A-347."
FT /evidence="ECO:0000269|PubMed:12167088"
FT MUTAGEN 434
FT /note="L->A: No change of phosphorylation or binding by
FT phospho-JNK; when associated with A-436."
FT /evidence="ECO:0000269|PubMed:12167088"
FT MUTAGEN 436
FT /note="L->A: No change of phosphorylation or binding by
FT phospho-JNK; when associated with A-434."
FT /evidence="ECO:0000269|PubMed:12167088"
FT HELIX 44..91
FT /evidence="ECO:0007829|PDB:6DJL"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6DJL"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6DJL"
FT HELIX 99..145
FT /evidence="ECO:0007829|PDB:6DJL"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:6DJL"
FT HELIX 153..200
FT /evidence="ECO:0007829|PDB:6DJL"
FT HELIX 202..260
FT /evidence="ECO:0007829|PDB:6DJL"
SQ SEQUENCE 455 AA; 50425 MW; 5C8CA4861D66346B CRC64;
MDAALKRSRS EEPAEILPPA RDEEEEEEEG MEQGLEEEEE VDPRIQGELE KLNQSTDDIN
RRETELEDAR QKFRSVLVEA TVKLDELVKK IGKAVEDSKP YWEARRVARQ AQLEAQKATQ
DFQRATEVLR AAKETISLAE QRLLEDDKRQ FDSAWQEMLN HATQRVMEAE QTKTRSELVH
KETAARYNAA MGRMRQLEKK LKRAINKSKP YFELKAKYYV QLEQLKKTVD DLQAKLTLAK
GEYKMALKNL EMISDEIHER RRSSAMGPRG CGVGAEGSST SVEDLPGSKP EPDAISVASE
AFEDDSCSNF VSEDDSETQS VSSFSSGPTS PSEMPDQFPA VVRPGSLDLP SPVSLSEFGM
MFPVLGPRSE CSGASSPECE VERGDRAEGA ENKTSDKANN NRGLSSSSGS GGSSKSQSST
SPEGQALENR MKQLSLQCSK GRDGIIADIK MVQIG
