UNKL_HUMAN
ID UNKL_HUMAN Reviewed; 680 AA.
AC Q9H9P5; B0QYN6; B1GXI8; Q96EV1; Q96RZ1; Q9BWL5; Q9H5K0; Q9UJJ8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Putative E3 ubiquitin-protein ligase UNKL;
DE EC=2.3.2.-;
DE AltName: Full=RING finger protein unkempt-like;
DE AltName: Full=Zinc finger CCCH domain-containing protein 5-like;
GN Name=UNKL; Synonyms=C16orf28, ZC3H5L, ZC3HDC5L;
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 4), FUNCTION, INTERACTION WITH RAC1 AND
RP SMARCD2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-639 AND CYS-670.
RX PubMed=20148946; DOI=10.1111/j.1742-4658.2010.07575.x;
RA Lores P., Visvikis O., Luna R., Lemichez E., Gacon G.;
RT "The SWI/SNF protein BAF60b is ubiquitinated through a signalling process
RT involving Rac GTPase and the RING finger protein Unkempt.";
RL FEBS J. 277:1453-1464(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [GENOMIC DNA] (ISOFORMS 2 AND 6).
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
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] (ISOFORMS 3 AND 5).
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 [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).
CC -!- FUNCTION: May participate in a protein complex showing an E3 ligase
CC activity regulated by RAC1. Ubiquitination is directed towards itself
CC and possibly other substrates, such as SMARCD2/BAF60b. Intrinsic E3
CC ligase activity has not been proven. {ECO:0000269|PubMed:20148946}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Isoform 4 (C-terminal) interacts with the GTP-bound form of
CC RAC1. Isoform 4 (C-terminal) interacts with SMARCD2/BAF60b.
CC {ECO:0000269|PubMed:20148946}.
CC -!- INTERACTION:
CC Q9H9P5; P63000: RAC1; NbExp=2; IntAct=EBI-7797561, EBI-413628;
CC Q9H9P5; Q92925: SMARCD2; NbExp=2; IntAct=EBI-7797561, EBI-358441;
CC Q9H9P5-5; Q86V38: ATN1; NbExp=3; IntAct=EBI-12817837, EBI-11954292;
CC Q9H9P5-5; P0C7T5: ATXN1L; NbExp=3; IntAct=EBI-12817837, EBI-8624731;
CC Q9H9P5-5; O95817: BAG3; NbExp=3; IntAct=EBI-12817837, EBI-747185;
CC Q9H9P5-5; O95429: BAG4; NbExp=3; IntAct=EBI-12817837, EBI-2949658;
CC Q9H9P5-5; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-12817837, EBI-12011224;
CC Q9H9P5-5; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-12817837, EBI-11530605;
CC Q9H9P5-5; Q02930-3: CREB5; NbExp=3; IntAct=EBI-12817837, EBI-10192698;
CC Q9H9P5-5; P02489: CRYAA; NbExp=3; IntAct=EBI-12817837, EBI-6875961;
CC Q9H9P5-5; P53672: CRYBA2; NbExp=3; IntAct=EBI-12817837, EBI-750444;
CC Q9H9P5-5; P23142-4: FBLN1; NbExp=3; IntAct=EBI-12817837, EBI-11956479;
CC Q9H9P5-5; O43559: FRS3; NbExp=3; IntAct=EBI-12817837, EBI-725515;
CC Q9H9P5-5; O14908-2: GIPC1; NbExp=3; IntAct=EBI-12817837, EBI-25913156;
CC Q9H9P5-5; P52597: HNRNPF; NbExp=3; IntAct=EBI-12817837, EBI-352986;
CC Q9H9P5-5; P49639: HOXA1; NbExp=3; IntAct=EBI-12817837, EBI-740785;
CC Q9H9P5-5; Q7L273: KCTD9; NbExp=3; IntAct=EBI-12817837, EBI-4397613;
CC Q9H9P5-5; Q92876: KLK6; NbExp=3; IntAct=EBI-12817837, EBI-2432309;
CC Q9H9P5-5; P25800: LMO1; NbExp=4; IntAct=EBI-12817837, EBI-8639312;
CC Q9H9P5-5; Q8IV28: NID2; NbExp=3; IntAct=EBI-12817837, EBI-10261509;
CC Q9H9P5-5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12817837, EBI-741158;
CC Q9H9P5-5; O15160: POLR1C; NbExp=3; IntAct=EBI-12817837, EBI-1055079;
CC Q9H9P5-5; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-12817837, EBI-710402;
CC Q9H9P5-5; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-12817837, EBI-12000762;
CC Q9H9P5-5; Q9ULW5: RAB26; NbExp=3; IntAct=EBI-12817837, EBI-958239;
CC Q9H9P5-5; Q96PF1: TGM7; NbExp=3; IntAct=EBI-12817837, EBI-12029034;
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Nucleus. Note=Isoform 4
CC is primarily localized in the cytoplasm but has the ability to shuttle
CC between the nucleus and the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=4;
CC IsoId=Q9H9P5-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9H9P5-1; Sequence=VSP_039433, VSP_039443;
CC Name=2;
CC IsoId=Q9H9P5-2; Sequence=VSP_039433;
CC Name=3;
CC IsoId=Q9H9P5-3; Sequence=VSP_039432, VSP_039441, VSP_039443;
CC Name=5;
CC IsoId=Q9H9P5-5; Sequence=VSP_039436, VSP_039437;
CC Name=6;
CC IsoId=Q9H9P5-6; Sequence=VSP_039434, VSP_039435, VSP_039438,
CC VSP_039439, VSP_039440, VSP_039442;
CC -!- DOMAIN: Although this protein contains a RING domain, intrinsic E3
CC ligase activity has not been proven. {ECO:0000269|PubMed:20148946}.
CC -!- PTM: Isoform 4 is ubiquitinated in the C-terminal. Ubiquitination is
CC enhanced by activated RAC1. The presence of the RING finger domain is
CC not essential for ubiquitination to occur.
CC -!- MISCELLANEOUS: [Isoform 4]: Splice site between exons 6 and 7 is non-
CC canonical.
CC -!- SIMILARITY: Belongs to the unkempt family. {ECO:0000305}.
CC -!- CAUTION: Was termed Unkempt. {ECO:0000305|PubMed:20148946}.
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DR EMBL; AM944365; CAQ16184.1; -; mRNA.
DR EMBL; AK022685; BAB14178.1; -; mRNA.
DR EMBL; AK027013; BAB15626.1; -; mRNA.
DR EMBL; AE006467; AAK61278.1; -; Genomic_DNA.
DR EMBL; AE006467; AAK61279.1; -; Genomic_DNA.
DR EMBL; AL031709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL032819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85659.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85660.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85662.1; -; Genomic_DNA.
DR EMBL; BC000150; AAH00150.1; -; mRNA.
DR EMBL; BC011924; AAH11924.1; -; mRNA.
DR CCDS; CCDS32359.1; -. [Q9H9P5-5]
DR CCDS; CCDS53980.1; -. [Q9H9P5-2]
DR CCDS; CCDS61787.1; -. [Q9H9P5-3]
DR PIR; T45063; T45063.
DR RefSeq; NP_001032202.1; NM_001037125.3. [Q9H9P5-5]
DR RefSeq; NP_001180317.2; NM_001193388.3.
DR RefSeq; NP_001180318.1; NM_001193389.1. [Q9H9P5-2]
DR RefSeq; NP_001263343.1; NM_001276414.1. [Q9H9P5-3]
DR RefSeq; XP_016879057.1; XM_017023568.1.
DR RefSeq; XP_016879058.1; XM_017023569.1. [Q9H9P5-1]
DR AlphaFoldDB; Q9H9P5; -.
DR SMR; Q9H9P5; -.
DR BioGRID; 122243; 67.
DR IntAct; Q9H9P5; 34.
DR MINT; Q9H9P5; -.
DR STRING; 9606.ENSP00000301712; -.
DR iPTMnet; Q9H9P5; -.
DR PhosphoSitePlus; Q9H9P5; -.
DR BioMuta; UNKL; -.
DR DMDM; 300669704; -.
DR EPD; Q9H9P5; -.
DR jPOST; Q9H9P5; -.
DR MassIVE; Q9H9P5; -.
DR MaxQB; Q9H9P5; -.
DR PaxDb; Q9H9P5; -.
DR PeptideAtlas; Q9H9P5; -.
DR PRIDE; Q9H9P5; -.
DR ProteomicsDB; 81339; -. [Q9H9P5-4]
DR ProteomicsDB; 81340; -. [Q9H9P5-1]
DR ProteomicsDB; 81341; -. [Q9H9P5-2]
DR ProteomicsDB; 81342; -. [Q9H9P5-3]
DR ProteomicsDB; 81343; -. [Q9H9P5-5]
DR ProteomicsDB; 81344; -. [Q9H9P5-6]
DR Antibodypedia; 34818; 113 antibodies from 19 providers.
DR DNASU; 64718; -.
DR Ensembl; ENST00000248104.11; ENSP00000248104.7; ENSG00000059145.19. [Q9H9P5-3]
DR Ensembl; ENST00000301712.5; ENSP00000301712.5; ENSG00000059145.19. [Q9H9P5-5]
DR Ensembl; ENST00000397464.5; ENSP00000380606.1; ENSG00000059145.19. [Q9H9P5-2]
DR Ensembl; ENST00000674376.1; ENSP00000501444.1; ENSG00000059145.19. [Q9H9P5-2]
DR GeneID; 64718; -.
DR KEGG; hsa:64718; -.
DR UCSC; uc002clo.3; human. [Q9H9P5-4]
DR CTD; 64718; -.
DR DisGeNET; 64718; -.
DR GeneCards; UNKL; -.
DR HGNC; HGNC:14184; UNKL.
DR HPA; ENSG00000059145; Low tissue specificity.
DR MIM; 617463; gene.
DR neXtProt; NX_Q9H9P5; -.
DR OpenTargets; ENSG00000059145; -.
DR PharmGKB; PA37855; -.
DR VEuPathDB; HostDB:ENSG00000059145; -.
DR eggNOG; KOG1595; Eukaryota.
DR GeneTree; ENSGT00940000158822; -.
DR HOGENOM; CLU_1363135_0_0_1; -.
DR InParanoid; Q9H9P5; -.
DR OrthoDB; 720138at2759; -.
DR PhylomeDB; Q9H9P5; -.
DR TreeFam; TF314982; -.
DR PathwayCommons; Q9H9P5; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9H9P5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 64718; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; UNKL; human.
DR GeneWiki; UNKL; -.
DR GenomeRNAi; 64718; -.
DR Pharos; Q9H9P5; Tdark.
DR PRO; PR:Q9H9P5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9H9P5; protein.
DR Bgee; ENSG00000059145; Expressed in secondary oocyte and 173 other tissues.
DR ExpressionAtlas; Q9H9P5; baseline and differential.
DR Genevisible; Q9H9P5; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045234; Unkempt-like.
DR InterPro; IPR040594; Unkempt_Znf.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14493; PTHR14493; 2.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF18384; zf_CCCH_5; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 4.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..680
FT /note="Putative E3 ubiquitin-protein ligase UNKL"
FT /id="PRO_0000278667"
FT ZN_FING 75..104
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 115..145
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 243..277
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 283..310
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 639..674
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 563..619
FT /evidence="ECO:0000255"
FT COMPBIAS 375..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..501
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039432"
FT VAR_SEQ 1..498
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039433"
FT VAR_SEQ 96
FT /note="E -> ESLLGVLYPLWAPPPVPAPVGAPTVHPFLARWFSHVPWEPAGSADPR
FT ASSTPAGGTTWATGLLGDFDACGSQSRECVKGVWWTLLGFR (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_039434"
FT VAR_SEQ 199
FT /note="Q -> QALLPVALLRHRVAHFS (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_039435"
FT VAR_SEQ 245..277
FT /note="RSTPCPSVKHGDEWGEPSRCDGGDGCQYCHSRT -> SWQLGRRVLRLSPRA
FT NNPRVALPRVHTGPSSTA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039436"
FT VAR_SEQ 278..680
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039437"
FT VAR_SEQ 284
FT /note="E -> EGPVGSPVSGAFSVFSHAGLVADPSLWYPAEWSWHHVGHSRTINPEG
FT DKPSRLGPAPENIKRGNDFACDGRADAAGMAPHVCVFPIYK (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_039438"
FT VAR_SEQ 359
FT /note="Q -> QGVRAHGVYVFEQ (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_039439"
FT VAR_SEQ 419..554
FT /note="GSALDLHLSNVNIASLEKDLEEQDGHDLGAAGPRSLAGSAPVAIPGSLPRAP
FT SLHSPSSASTSPLGSLSQPLPGPVGSSAMTPPQQPPPLRSEPGTLGSAASSYSPLGLNG
FT VPGSIWDFVSGSFSPSPSPILSAGP -> ALEPTPSSPTSSAVQGVAGELGMGSGGQGC
FT WSHVVGALAAVPAWTHSGDLEWDPSTIRTRVNVGGGPAARPAMTLAREPQLLVVGGCPT
FT RNCSGPAASPQQLLDDAGQGGRGERDSSQRPLRPQTTHRQDTRPVPS (in isoform
FT 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_039440"
FT VAR_SEQ 502..525
FT /note="PQQPPPLRSEPGTLGSAASSYSPL -> MTCCSQVPPRRRPSLALSPRLDCN
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039441"
FT VAR_SEQ 555..680
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_039442"
FT VAR_SEQ 630
FT /note="V -> VKQLQEELEGLGVASTLPGLRGCGDIGTIPLPKLHSLQSQLRLDLEA
FT VDGV (in isoform 1 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039443"
FT MUTAGEN 639
FT /note="C->A: No effects on the interaction with RAC1 or
FT SMARCD2; when associated with A-670."
FT /evidence="ECO:0000269|PubMed:20148946"
FT MUTAGEN 670
FT /note="C->A: No effects on the interaction with RAC1 or
FT SMARCD2; when associated with A-639."
FT /evidence="ECO:0000269|PubMed:20148946"
FT CONFLICT 541
FT /note="S -> R (in Ref. 1; CAQ16184)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="I -> V (in Ref. 2; BAB14178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 680 AA; 73828 MW; FC3205EB1616075E CRC64;
MPSVSKAAAA ALSGSPPQTE KPTHYRYLKE FRTEQCPLFS QHKCAQHRPF TCFHWHFLNQ
RRRRPLRRRD GTFNYSPDVY CSKYNEATGV CPDGDECPYL HRTTGDTERK YHLRYYKTGT
CIHETDARGH CVKNGLHCAF AHGPLDLRPP VCDVRELQAQ EALQNGQLGG GEGVPDLQPG
VLASQAMIEK ILSEDPRWQD ANFVLGSYKT EQCPKPPRLC RQGYACPHYH NSRDRRRNPR
RFQYRSTPCP SVKHGDEWGE PSRCDGGDGC QYCHSRTEQQ FHPESTKCND MRQTGYCPRG
PFCAFAHVEK SLGMVNEWGC HDLHLTSPSS TGSGQPGNAK RRDSPAEGGP RGSEQDSKQN
HLAVFAAVHP PAPSVSSSVA SSLASSAGSG SSSPTALPAP PARALPLGPA SSTVEAVLGS
ALDLHLSNVN IASLEKDLEE QDGHDLGAAG PRSLAGSAPV AIPGSLPRAP SLHSPSSAST
SPLGSLSQPL PGPVGSSAMT PPQQPPPLRS EPGTLGSAAS SYSPLGLNGV PGSIWDFVSG
SFSPSPSPIL SAGPPSSSSA SPNGAELARV RRQLDEAKRK IRQWEESWQQ VKQVCDAWQR
EAQEAKERAR VADSDRQLAL QKKEEVEAQV IFQLRAKQCV ACRERAHGAV LRPCQHHILC
EPCAATAPEC PYCKGQPLQW
