STAR8_HUMAN
ID STAR8_HUMAN Reviewed; 1023 AA.
AC Q92502; A8K6T2; D3DVT9; Q5JST0; Q68DG7;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=StAR-related lipid transfer protein 8;
DE AltName: Full=Deleted in liver cancer 3 protein;
DE Short=DLC-3;
DE AltName: Full=START domain-containing protein 8;
DE Short=StARD8;
DE AltName: Full=START-GAP3;
GN Name=STARD8; Synonyms=DLC3, KIAA0189;
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=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 MRNA] (ISOFORM 2).
RC TISSUE=Endometrial tumor;
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 [4]
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 [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-608.
RX PubMed=17976533; DOI=10.1016/j.bbrc.2007.10.052;
RA Kawai K., Kiyota M., Seike J., Deki Y., Yagisawa H.;
RT "START-GAP3/DLC3 is a GAP for RhoA and Cdc42 and is localized in focal
RT adhesions regulating cell morphology.";
RL Biochem. Biophys. Res. Commun. 364:783-789(2007).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=17297465; DOI=10.1038/sj.onc.1210244;
RA Durkin M.E., Ullmannova V., Guan M., Popescu N.C.;
RT "Deleted in liver cancer 3 (DLC-3), a novel Rho GTPase-activating protein,
RT is downregulated in cancer and inhibits tumor cell growth.";
RL Oncogene 26:4580-4589(2007).
RN [9]
RP INTERACTION WITH TNS1.
RX PubMed=17517630; DOI=10.1073/pnas.0703033104;
RA Qian X., Li G., Asmussen H.K., Asnaghi L., Vass W.C., Braverman R.,
RA Yamada K.M., Popescu N.C., Papageorge A.G., Lowy D.R.;
RT "Oncogenic inhibition by a deleted in liver cancer gene requires
RT cooperation between tensin binding and Rho-specific GTPase-activating
RT protein activities.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9012-9017(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-235, AND
RP IDENTIFICATION BY 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 [11]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-188 AND LYS-242.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Accelerates GTPase activity of RHOA and CDC42, but not RAC1.
CC Stimulates the hydrolysis of phosphatidylinositol 4,5-bisphosphate by
CC PLCD1. {ECO:0000269|PubMed:17976533}.
CC -!- SUBUNIT: Binds both the SH2 and PTB domains of TNS1.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:17976533}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=DLC3beta;
CC IsoId=Q92502-1; Sequence=Displayed;
CC Name=2; Synonyms=DLC3alpha;
CC IsoId=Q92502-2; Sequence=VSP_032984;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in kidney,
CC lung and placenta. {ECO:0000269|PubMed:17297465}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11506.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D80011; BAA11506.2; ALT_INIT; mRNA.
DR EMBL; AK291747; BAF84436.1; -; mRNA.
DR EMBL; CR749411; CAH18253.1; -; mRNA.
DR EMBL; AL360076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05374.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05375.1; -; Genomic_DNA.
DR EMBL; BC035587; AAH35587.1; -; mRNA.
DR CCDS; CCDS14390.1; -. [Q92502-1]
DR CCDS; CCDS48134.1; -. [Q92502-2]
DR PIR; B59430; B59430.
DR RefSeq; NP_001135975.1; NM_001142503.2. [Q92502-2]
DR RefSeq; NP_001135976.1; NM_001142504.2. [Q92502-1]
DR RefSeq; NP_055540.2; NM_014725.4. [Q92502-1]
DR RefSeq; XP_011529371.1; XM_011531069.2. [Q92502-1]
DR AlphaFoldDB; Q92502; -.
DR SMR; Q92502; -.
DR BioGRID; 115102; 20.
DR DIP; DIP-60949N; -.
DR IntAct; Q92502; 5.
DR MINT; Q92502; -.
DR STRING; 9606.ENSP00000363727; -.
DR iPTMnet; Q92502; -.
DR PhosphoSitePlus; Q92502; -.
DR BioMuta; STARD8; -.
DR DMDM; 90110072; -.
DR EPD; Q92502; -.
DR jPOST; Q92502; -.
DR MassIVE; Q92502; -.
DR MaxQB; Q92502; -.
DR PaxDb; Q92502; -.
DR PeptideAtlas; Q92502; -.
DR PRIDE; Q92502; -.
DR ProteomicsDB; 75270; -. [Q92502-1]
DR ProteomicsDB; 75271; -. [Q92502-2]
DR Antibodypedia; 27311; 130 antibodies from 21 providers.
DR DNASU; 9754; -.
DR Ensembl; ENST00000252336.10; ENSP00000252336.6; ENSG00000130052.14. [Q92502-1]
DR Ensembl; ENST00000374597.3; ENSP00000363725.3; ENSG00000130052.14. [Q92502-1]
DR Ensembl; ENST00000374599.8; ENSP00000363727.3; ENSG00000130052.14. [Q92502-2]
DR GeneID; 9754; -.
DR KEGG; hsa:9754; -.
DR MANE-Select; ENST00000374599.8; ENSP00000363727.3; NM_001142503.3; NP_001135975.1. [Q92502-2]
DR UCSC; uc004dxa.4; human. [Q92502-1]
DR CTD; 9754; -.
DR DisGeNET; 9754; -.
DR GeneCards; STARD8; -.
DR HGNC; HGNC:19161; STARD8.
DR HPA; ENSG00000130052; Low tissue specificity.
DR MIM; 300689; gene.
DR neXtProt; NX_Q92502; -.
DR OpenTargets; ENSG00000130052; -.
DR PharmGKB; PA38804; -.
DR VEuPathDB; HostDB:ENSG00000130052; -.
DR eggNOG; KOG2200; Eukaryota.
DR GeneTree; ENSGT00950000183061; -.
DR HOGENOM; CLU_004367_0_1_1; -.
DR InParanoid; Q92502; -.
DR OMA; EQCTISN; -.
DR OrthoDB; 218349at2759; -.
DR PhylomeDB; Q92502; -.
DR TreeFam; TF314044; -.
DR PathwayCommons; Q92502; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR SignaLink; Q92502; -.
DR SIGNOR; Q92502; -.
DR BioGRID-ORCS; 9754; 8 hits in 703 CRISPR screens.
DR ChiTaRS; STARD8; human.
DR GeneWiki; STARD8; -.
DR GenomeRNAi; 9754; -.
DR Pharos; Q92502; Tbio.
DR PRO; PR:Q92502; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q92502; protein.
DR Bgee; ENSG00000130052; Expressed in right lung and 152 other tissues.
DR ExpressionAtlas; Q92502; baseline and differential.
DR Genevisible; Q92502; HS.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; GTPase activation; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1023
FT /note="StAR-related lipid transfer protein 8"
FT /id="PRO_0000220676"
FT DOMAIN 573..777
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 809..1017
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 46..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 169
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K031"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K031"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K031"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K031"
FT VAR_SEQ 1
FT /note="M -> MPLLDVFWSCFRKVKCFPLLQVKKNAEAEAKRACEWLQATGFPQYVQ
FT LFEEGSFPLDIGSVKKNHGFLDEDSLGALCRRLM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_032984"
FT VARIANT 188
FT /note="G -> S (in a breast cancer sample; somatic mutation;
FT dbSNP:rs139380533)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036588"
FT VARIANT 242
FT /note="E -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036589"
FT VARIANT 327
FT /note="R -> Q (in dbSNP:rs55962426)"
FT /id="VAR_061816"
FT MUTAGEN 608
FT /note="R->E: No effect on cell morphology when
FT overexpressed."
FT /evidence="ECO:0000269|PubMed:17976533"
FT CONFLICT 466
FT /note="P -> S (in Ref. 1; BAA11506)"
FT /evidence="ECO:0000305"
FT CONFLICT Q92502-2:71
FT /note="D -> G (in Ref. 3; CAH18253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1023 AA; 112601 MW; F93804B352450DE2 CRC64;
MTLNNCASMK LEVHFQSKQN EDSEEEEQCT ISSHWAFQQE SKCWSPMGSS DLLAPPSPGL
PATSSCESVL TELSATSLPV ITVSLPPEPA DLPLPGRAPS SSDRPLLSPT QGQEGPQDKA
KKRHRNRSFL KHLESLRRKE KSGSQQAEPK HSPATSEKVS KASSFRSCRG FLSAGFYRAK
NWAATSAGGS GANTRKAWEA WPVASFRHPQ WTHRGDCLVH VPGDHKPGTF PRSLSIESLC
PEDGHRLADW QPGRRWGCEG RRGSCGSTGS HASTYDNLPE LYPAEPVMVG AEAEDEDDEE
SGGSYAHLDD ILQHVWGLQQ RVELWSRAMY PDLGPGDEEE EEATSSVEIA TVEVKCQAEA
LSQMEVPAHG ESPAWAQAEV QPAVLAPAQA PAEAEPVAQE EAEAPAPAPA PAPAQDSEQE
AHSGGEPTFA SSLSVEEGHS ISDTVASSSE LDSSGNSMNE AEAAGPLAGL QASMPRERRD
SGVGASLTRP CRKLRWHSFQ NSHRPSLNSE SLEINRQFAG QINLLHKGSL LRLTAFMEKY
TVPHKQGWVW SMPKFMRRNK TPDYRGQHVF GVPPLIHVQR TGQPLPQSIQ QAMRYLRSQC
LDQVGIFRKS GVKSRIQNLR QMNETSPDNV CYEGQSAYDV ADLLKQYFRD LPEPIFTSKL
TTTFLQIYQL LPKDQWLAAA QAATLLLPDE NREVLQTLLY FLSDIASAEE NQMTAGNLAV
CLAPSIFHLN VSKKDSPSPR IKSKRSLIGR PGPRDLSDNM AATQGLSHMI SDCKKLFQVP
QDMVLQLCSS YSAAELSPPG PALAELRQAQ AAGVSLSLYM EENIQDLLRD AAERFKGWMS
VPGPQHTELA CRKAPDGHPL RLWKASTEVA APPAVVLHRV LRERALWDED LLRAQVLEAL
MPGVELYHYV TDSMAPHPCR DFVVLRMWRS DLPRGGCLLV SQSLDPEQPV PESGVRALML
TSQYLMEPCG LGRSRLTHIC RADLRGRSPD WYNKVFGHLC AMEVAKIRDS FPTLQAAGPE
TKL
