IQEC2_HUMAN
ID IQEC2_HUMAN Reviewed; 1488 AA.
AC Q5JU85; A0A1W2PQN3; B3KT97; C7SDG1; O60275; Q5JUX1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=IQ motif and SEC7 domain-containing protein 2;
GN Name=IQSEC2; Synonyms=KIAA0522;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-494 (ISOFORM 2).
RA Shapovalova Z., Lasell T.K., Smith C., Melancon P.;
RT "PH domain targets the Arf-GEF BRAG1 to the plasma membrane.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344; SER-393; SER-412;
RP SER-1107 AND SER-1143, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [7]
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 [8]
RP FUNCTION, VARIANT XLID1 VAL-789, AND CHARACTERIZATION OF VARIANT XLID1
RP VAL-789.
RX PubMed=26793055; DOI=10.3389/fnmol.2015.00085;
RA Kalscheuer V.M., James V.M., Himelright M.L., Long P., Oegema R.,
RA Jensen C., Bienek M., Hu H., Haas S.A., Topf M., Hoogeboom A.J., Harvey K.,
RA Walikonis R., Harvey R.J.;
RT "Novel missense mutation A789V in IQSEC2 underlies X-linked intellectual
RT disability in the MRX78 family.";
RL Front. Mol. Neurosci. 8:85-85(2015).
RN [9]
RP VARIANTS XLID1 CYS-359; GLN-758; PRO-801 AND TRP-863.
RX PubMed=20473311; DOI=10.1038/ng.588;
RA Shoubridge C., Tarpey P.S., Abidi F., Ramsden S.L., Rujirabanjerd S.,
RA Murphy J.A., Boyle J., Shaw M., Gardner A., Proos A., Puusepp H.,
RA Raymond F.L., Schwartz C.E., Stevenson R.E., Turner G., Field M.,
RA Walikonis R.S., Harvey R.J., Hackett A., Futreal P.A., Stratton M.R.,
RA Gecz J.;
RT "Mutations in the guanine nucleotide exchange factor gene IQSEC2 cause
RT nonsyndromic intellectual disability.";
RL Nat. Genet. 42:486-488(2010).
CC -!- FUNCTION: Is a guanine nucleotide exchange factor for the ARF GTP-
CC binding proteins. {ECO:0000269|PubMed:26793055}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5JU85-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JU85-3; Sequence=VSP_041372, VSP_041373, VSP_041374;
CC Name=3;
CC IsoId=Q5JU85-4; Sequence=VSP_059605, VSP_059606;
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney and small intestine.
CC Weakly expressed in placenta, pancreas, ovary, prostate and liver.
CC {ECO:0000269|PubMed:9628581}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked 1 (XLID1)
CC [MIM:309530]: A disorder characterized by significantly below average
CC general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC Intellectual deficiency is the only primary symptom of non-syndromic X-
CC linked forms, while syndromic forms present with associated physical,
CC neurological and/or psychiatric manifestations.
CC {ECO:0000269|PubMed:20473311, ECO:0000269|PubMed:26793055}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the BRAG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25448.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA25448.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAI42091.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB011094; BAA25448.1; ALT_SEQ; mRNA.
DR EMBL; AK095232; BAG53009.1; -; mRNA.
DR EMBL; AC245102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161779; CAI42091.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL139396; CAI42091.1; JOINED; Genomic_DNA.
DR EMBL; FJ154891; ACR15956.1; -; mRNA.
DR CCDS; CCDS35298.1; -. [Q5JU85-3]
DR CCDS; CCDS48130.1; -. [Q5JU85-2]
DR CCDS; CCDS87748.1; -. [Q5JU85-4]
DR PIR; T00080; T00080.
DR RefSeq; NP_001104595.1; NM_001111125.2. [Q5JU85-2]
DR RefSeq; NP_001230126.1; NM_001243197.1. [Q5JU85-4]
DR RefSeq; NP_055890.1; NM_015075.1. [Q5JU85-3]
DR RefSeq; XP_016884848.1; XM_017029359.1.
DR PDB; 6FAE; X-ray; 2.35 A; A=729-1099.
DR PDBsum; 6FAE; -.
DR AlphaFoldDB; Q5JU85; -.
DR SMR; Q5JU85; -.
DR BioGRID; 116724; 43.
DR DIP; DIP-59490N; -.
DR IntAct; Q5JU85; 9.
DR MINT; Q5JU85; -.
DR STRING; 9606.ENSP00000379712; -.
DR iPTMnet; Q5JU85; -.
DR PhosphoSitePlus; Q5JU85; -.
DR BioMuta; IQSEC2; -.
DR DMDM; 74742276; -.
DR EPD; Q5JU85; -.
DR jPOST; Q5JU85; -.
DR MassIVE; Q5JU85; -.
DR MaxQB; Q5JU85; -.
DR PaxDb; Q5JU85; -.
DR PeptideAtlas; Q5JU85; -.
DR PRIDE; Q5JU85; -.
DR ProteomicsDB; 63261; -. [Q5JU85-2]
DR ProteomicsDB; 63262; -. [Q5JU85-3]
DR Antibodypedia; 583; 68 antibodies from 21 providers.
DR DNASU; 23096; -.
DR Ensembl; ENST00000375365.2; ENSP00000364514.2; ENSG00000124313.18. [Q5JU85-3]
DR Ensembl; ENST00000639161.2; ENSP00000491796.1; ENSG00000124313.18. [Q5JU85-4]
DR Ensembl; ENST00000642864.1; ENSP00000495726.1; ENSG00000124313.18. [Q5JU85-2]
DR Ensembl; ENST00000674510.1; ENSP00000502054.1; ENSG00000124313.18. [Q5JU85-2]
DR GeneID; 23096; -.
DR KEGG; hsa:23096; -.
DR MANE-Select; ENST00000642864.1; ENSP00000495726.1; NM_001111125.3; NP_001104595.1.
DR UCSC; uc004dsc.4; human. [Q5JU85-2]
DR CTD; 23096; -.
DR DisGeNET; 23096; -.
DR GeneCards; IQSEC2; -.
DR HGNC; HGNC:29059; IQSEC2.
DR HPA; ENSG00000124313; Tissue enhanced (skeletal).
DR MalaCards; IQSEC2; -.
DR MIM; 300522; gene.
DR MIM; 309530; phenotype.
DR neXtProt; NX_Q5JU85; -.
DR OpenTargets; ENSG00000124313; -.
DR Orphanet; 217377; Microduplication Xp11.22p11.23 syndrome.
DR Orphanet; 397933; Severe intellectual disability-progressive postnatal microcephaly-midline stereotypic hand movements syndrome.
DR Orphanet; 819; Smith-Magenis syndrome.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA134870898; -.
DR VEuPathDB; HostDB:ENSG00000124313; -.
DR eggNOG; KOG0931; Eukaryota.
DR GeneTree; ENSGT00940000159667; -.
DR HOGENOM; CLU_004328_0_0_1; -.
DR InParanoid; Q5JU85; -.
DR OMA; RERGQMS; -.
DR OrthoDB; 837077at2759; -.
DR PhylomeDB; Q5JU85; -.
DR TreeFam; TF323811; -.
DR PathwayCommons; Q5JU85; -.
DR SignaLink; Q5JU85; -.
DR SIGNOR; Q5JU85; -.
DR BioGRID-ORCS; 23096; 14 hits in 711 CRISPR screens.
DR ChiTaRS; IQSEC2; human.
DR GeneWiki; IQSEC2; -.
DR GenomeRNAi; 23096; -.
DR Pharos; Q5JU85; Tbio.
DR PRO; PR:Q5JU85; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q5JU85; protein.
DR Bgee; ENSG00000124313; Expressed in right hemisphere of cerebellum and 163 other tissues.
DR ExpressionAtlas; Q5JU85; baseline and differential.
DR Genevisible; Q5JU85; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR CDD; cd13318; PH_IQSEC; 1.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR033742; IQSEC_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF16453; IQ_SEC7_PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Disease variant; Intellectual disability; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1488
FT /note="IQ motif and SEC7 domain-containing protein 2"
FT /id="PRO_0000245608"
FT DOMAIN 347..376
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 746..939
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 50..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..74
FT /evidence="ECO:0000255"
FT COMPBIAS 50..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..560
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1251
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1380
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1474
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 1173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT MOD_RES 1345
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU25"
FT VAR_SEQ 1..245
FT /note="MEAGSGPPGGPGSESPNRAVEYLLELNNIIESQQQLLETQRRRIEELEGQLD
FT QLTQENRDLREESQLHRGELHRDPHGARDSPGRESQYQNLRETQFHHRELRESQFHQAA
FT RDVGYPNREGAYQNREAVYRDKERDASYPLQDTTGYTARERDVAQCHLHHENPALGRER
FT GGREAGPAHPGREKEAGYSAAVGVGPRPPRERGQLSRGASRSSSPGAGGGHSTSTSTSP
FT ATTLQRKSDGENSRTV -> MEPPGRSSRSTASHTLHQYCCPTQVLDSMKLTPSGRLAE
FT S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_041372"
FT VAR_SEQ 1..73
FT /note="MEAGSGPPGGPGSESPNRAVEYLLELNNIIESQQQLLETQRRRIEELEGQLD
FT QLTQENRDLREESQLHRGELH -> MEPPGRSSRSTASHTLHQYCCPTQVLDSMKLTPS
FT GRLAESREEEEEEETEEEEEEDAHQFCCPASECSSPSSR (in isoform 3)"
FT /id="VSP_059605"
FT VAR_SEQ 74..1488
FT /note="Missing (in isoform 3)"
FT /id="VSP_059606"
FT VAR_SEQ 1152..1154
FT /note="KRG -> VCY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_041373"
FT VAR_SEQ 1155..1488
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_041374"
FT VARIANT 359
FT /note="R -> C (in XLID1; dbSNP:rs267607188)"
FT /evidence="ECO:0000269|PubMed:20473311"
FT /id="VAR_063742"
FT VARIANT 758
FT /note="R -> Q (in XLID1; dbSNP:rs267607189)"
FT /evidence="ECO:0000269|PubMed:20473311"
FT /id="VAR_063743"
FT VARIANT 789
FT /note="A -> V (in XLID1; decreased guanine nucleotide
FT exchange factor activity; dbSNP:rs875989799)"
FT /evidence="ECO:0000269|PubMed:26793055"
FT /id="VAR_078260"
FT VARIANT 801
FT /note="Q -> P (in XLID1; dbSNP:rs267607187)"
FT /evidence="ECO:0000269|PubMed:20473311"
FT /id="VAR_063744"
FT VARIANT 863
FT /note="R -> W (in XLID1; dbSNP:rs267607186)"
FT /evidence="ECO:0000269|PubMed:20473311"
FT /id="VAR_063745"
FT CONFLICT 689
FT /note="E -> K (in Ref. 2; BAG53009)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="E -> G (in Ref. 2; BAG53009)"
FT /evidence="ECO:0000305"
FT HELIX 750..766
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 768..777
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 785..794
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 800..807
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 813..824
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 833..843
FT /evidence="ECO:0007829|PDB:6FAE"
FT STRAND 847..849
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 850..867
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 869..873
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 879..896
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 902..904
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 908..914
FT /evidence="ECO:0007829|PDB:6FAE"
FT TURN 915..918
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 926..938
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 948..957
FT /evidence="ECO:0007829|PDB:6FAE"
FT STRAND 958..961
FT /evidence="ECO:0007829|PDB:6FAE"
FT STRAND 972..980
FT /evidence="ECO:0007829|PDB:6FAE"
FT TURN 990..993
FT /evidence="ECO:0007829|PDB:6FAE"
FT STRAND 994..1000
FT /evidence="ECO:0007829|PDB:6FAE"
FT STRAND 1003..1009
FT /evidence="ECO:0007829|PDB:6FAE"
FT STRAND 1019..1026
FT /evidence="ECO:0007829|PDB:6FAE"
FT STRAND 1030..1035
FT /evidence="ECO:0007829|PDB:6FAE"
FT STRAND 1041..1048
FT /evidence="ECO:0007829|PDB:6FAE"
FT STRAND 1057..1062
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 1066..1092
FT /evidence="ECO:0007829|PDB:6FAE"
SQ SEQUENCE 1488 AA; 162784 MW; 52F8B7BE28A175F3 CRC64;
MEAGSGPPGG PGSESPNRAV EYLLELNNII ESQQQLLETQ RRRIEELEGQ LDQLTQENRD
LREESQLHRG ELHRDPHGAR DSPGRESQYQ NLRETQFHHR ELRESQFHQA ARDVGYPNRE
GAYQNREAVY RDKERDASYP LQDTTGYTAR ERDVAQCHLH HENPALGRER GGREAGPAHP
GREKEAGYSA AVGVGPRPPR ERGQLSRGAS RSSSPGAGGG HSTSTSTSPA TTLQRKSDGE
NSRTVSVEGD APGSDLSTAV DSPGSQPPYR LSQLPPSSSH MGGPPAGVGL PWAQRARLQP
ASVALRKQEE EEIKRSKALS DSYELSTDLQ DKKVEMLERK YGGSFLSRRA ARTIQTAFRQ
YRMNKNFERL RSSASESRMS RRIILSNMRM QFSFEEYEKA QNPAYFEGKP ASLDEGAMAG
ARSHRLERGL PYGGSCGGGI DGGGSSVTTS GEFSNDITEL EDSFSKQVKS LAESIDEALN
CHPSGPMSEE PGSAQLEKRE SKEQQEDSSA TSFSDLPLYL DDTVPQQSPE RLPSTEPPPQ
GRPEFWAPAP LPPVPPPVPS GTREDGSREE GTRRGPGCLE CRDFRLRAAH LPLLTIEPPS
DSSVDLSDRS DRGSVHRQLV YEADGCSPHG TLKHKGPPGR APIPHRHYPA PEGPAPAPPG
PLPPAPNSGT GPSGVAGGRR LGKCEAAGEN SDGGDNESLE SSSNSNETIN CSSGSSSRDS
LREPPATGLC KQTYQRETRH SWDSPAFNND VVQRRHYRIG LNLFNKKPEK GIQYLIERGF
LSDTPVGVAH FILERKGLSR QMIGEFLGNR QKQFNRDVLD CVVDEMDFSS MDLDDALRKF
QSHIRVQGEA QKVERLIEAF SQRYCVCNPA LVRQFRNPDT IFILAFAIIL LNTDMYSPSV
KAERKMKLDD FIKNLRGVDN GEDIPRDLLV GIYQRIQGRE LRTNDDHVSQ VQAVERMIVG
KKPVLSLPHR RLVCCCQLYE VPDPNRPQRL GLHQREVFLF NDLLVVTKIF QKKKILVTYS
FRQSFPLVEM HMQLFQNSYY QFGIKLLSAV PGGERKVLII FNAPSLQDRL RFTSDLRESI
AEVQEMEKYR VESELEKQKG MMRPNASQPG GAKDSVNGTM ARSSLEDTYG AGDGLKRGAL
SSSLRDLSDA GKRGRRNSVG SLDSTIEGSV ISSPRPHQRM PPPPPPPPPE EYKSQRPVSN
SSSFLGSLFG SKRGKGPFQM PPPPTGQASA SSSSASSTHH HHHHHHHGHS HGGLGVLPDG
QSKLQALHAQ YCQGPGPAPP PYLPPQQPSL PPPPQQPPPL PQLGSIPPPP ASAPPVGPHR
HFHAHGPVPG PQHYTLGRPG RAPRRGAGGH PQFAPHGRHP LHQPTSPLPL YSPAPQHPPA
HKQGPKHFIF SHHPQMMPAA GAAGGPGSRP PGGSYSHPHH PQSPLSPHSP IPPHPSYPPL
PPPSPHTPHS PLPPTSPHGP LHASGPPGTA NPPSANPKAK PSRISTVV
