RBGP1_HUMAN
ID RBGP1_HUMAN Reviewed; 1069 AA.
AC Q9Y3P9; B9A6L2; Q05CW2; Q6ZMY1; Q9HA28; Q9P0E2; Q9UG67;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Rab GTPase-activating protein 1;
DE AltName: Full=GAP and centrosome-associated protein;
DE AltName: Full=Rab6 GTPase-activating protein GAPCenA;
GN Name=RABGAP1; ORFNames=HSPC094;
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] {ECO:0000305, ECO:0000312|EMBL:CAB40267.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RAB6A
RP AND TUBULIN GAMMA, AND SUBCELLULAR LOCATION.
RC TISSUE=Placenta {ECO:0000312|EMBL:CAB40267.2};
RX PubMed=10202141; DOI=10.1093/emboj/18.7.1772;
RA Cuif M.-H., Possmayer F., Zander H., Bordes N., Jollivet F.,
RA Couedel-Courteille A., Janoueix-Lerosey I., Langsley G., Bornens M.,
RA Goud B.;
RT "Characterization of GAPCenA, a GTPase activating protein for Rab6, part of
RT which associates with the centrosome.";
RL EMBO J. 18:1772-1782(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAF28917.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Umbilical cord blood;
RA Zhang Q.H., Ye M., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L., Fan H.Y.,
RA Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAD18594.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Mammary gland, and Testis {ECO:0000312|EMBL:BAD18594.1};
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAF28917.1}
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 [7] {ECO:0000305, ECO:0000312|EMBL:AAH54492.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta {ECO:0000312|EMBL:AAH20609.1}, and
RC Uterus {ECO:0000312|EMBL:AAH54492.1};
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 824-1069 (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 [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=16395330; DOI=10.1038/sj.emboj.7600929;
RA Miserey-Lenkei S., Couedel-Courteille A., Del Nery E., Bardin S., Piel M.,
RA Racine V., Sibarita J.-B., Perez F., Bornens M., Goud B.;
RT "A role for the Rab6A' GTPase in the inactivation of the Mad2-spindle
RT checkpoint.";
RL EMBO J. 25:278-289(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-996, AND IDENTIFICATION BY
RP 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=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND THR-996, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: May act as a GTPase-activating protein of RAB6A. May play a
CC role in microtubule nucleation by centrosome. May participate in a
CC RAB6A-mediated pathway involved in the metaphase-anaphase transition.
CC {ECO:0000269|PubMed:10202141, ECO:0000269|PubMed:16395330}.
CC -!- SUBUNIT: Interacts with RAB6A and tubulin gamma.
CC {ECO:0000269|PubMed:10202141}.
CC -!- INTERACTION:
CC Q9Y3P9; Q9H0R8: GABARAPL1; NbExp=2; IntAct=EBI-1057545, EBI-746969;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10202141}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:10202141}. Note=Predominantly cytosolic but also
CC associated with the centrosome. {ECO:0000269|PubMed:10202141}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:10202141};
CC IsoId=Q9Y3P9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14702039};
CC IsoId=Q9Y3P9-2; Sequence=VSP_052510, VSP_052513, VSP_052514;
CC Name=3;
CC IsoId=Q9Y3P9-3; Sequence=VSP_052515;
CC Name=4 {ECO:0000269|PubMed:14702039};
CC IsoId=Q9Y3P9-4; Sequence=VSP_052511, VSP_052512;
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28917.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH20609.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH54492.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AK022408; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=CAB40267.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ011679; CAB40267.2; ALT_INIT; mRNA.
DR EMBL; AB449897; BAH16640.1; -; mRNA.
DR EMBL; AF161357; AAF28917.1; ALT_FRAME; mRNA.
DR EMBL; AK022408; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK131449; BAD18594.1; -; mRNA.
DR EMBL; AC007066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87555.1; -; Genomic_DNA.
DR EMBL; BC020609; AAH20609.1; ALT_SEQ; mRNA.
DR EMBL; BC054492; AAH54492.1; ALT_INIT; mRNA.
DR EMBL; AL050195; CAB43313.1; -; mRNA.
DR CCDS; CCDS6848.2; -. [Q9Y3P9-1]
DR PIR; T13163; T13163.
DR RefSeq; NP_036329.3; NM_012197.3. [Q9Y3P9-1]
DR RefSeq; XP_011516742.1; XM_011518440.2. [Q9Y3P9-1]
DR RefSeq; XP_011516743.1; XM_011518441.2. [Q9Y3P9-1]
DR RefSeq; XP_016870056.1; XM_017014567.1. [Q9Y3P9-1]
DR RefSeq; XP_016870057.1; XM_017014568.1. [Q9Y3P9-1]
DR RefSeq; XP_016870058.1; XM_017014569.1. [Q9Y3P9-1]
DR PDB; 4NC6; X-ray; 1.80 A; A=536-849.
DR PDBsum; 4NC6; -.
DR AlphaFoldDB; Q9Y3P9; -.
DR SMR; Q9Y3P9; -.
DR BioGRID; 117166; 72.
DR IntAct; Q9Y3P9; 34.
DR MINT; Q9Y3P9; -.
DR STRING; 9606.ENSP00000362751; -.
DR GlyGen; Q9Y3P9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3P9; -.
DR MetOSite; Q9Y3P9; -.
DR PhosphoSitePlus; Q9Y3P9; -.
DR BioMuta; RABGAP1; -.
DR DMDM; 156633605; -.
DR EPD; Q9Y3P9; -.
DR jPOST; Q9Y3P9; -.
DR MassIVE; Q9Y3P9; -.
DR MaxQB; Q9Y3P9; -.
DR PaxDb; Q9Y3P9; -.
DR PeptideAtlas; Q9Y3P9; -.
DR PRIDE; Q9Y3P9; -.
DR ProteomicsDB; 86054; -. [Q9Y3P9-1]
DR ProteomicsDB; 86055; -. [Q9Y3P9-2]
DR ProteomicsDB; 86056; -. [Q9Y3P9-3]
DR ProteomicsDB; 86057; -. [Q9Y3P9-4]
DR Antibodypedia; 30396; 264 antibodies from 27 providers.
DR DNASU; 23637; -.
DR Ensembl; ENST00000373647.9; ENSP00000362751.4; ENSG00000011454.18. [Q9Y3P9-1]
DR Ensembl; ENST00000456584.5; ENSP00000414386.1; ENSG00000011454.18. [Q9Y3P9-2]
DR GeneID; 23637; -.
DR KEGG; hsa:23637; -.
DR MANE-Select; ENST00000373647.9; ENSP00000362751.4; NM_012197.4; NP_036329.3.
DR UCSC; uc011lzh.3; human. [Q9Y3P9-1]
DR CTD; 23637; -.
DR DisGeNET; 23637; -.
DR GeneCards; RABGAP1; -.
DR HGNC; HGNC:17155; RABGAP1.
DR HPA; ENSG00000011454; Low tissue specificity.
DR MIM; 615882; gene.
DR neXtProt; NX_Q9Y3P9; -.
DR OpenTargets; ENSG00000011454; -.
DR PharmGKB; PA134977298; -.
DR VEuPathDB; HostDB:ENSG00000011454; -.
DR eggNOG; KOG1102; Eukaryota.
DR GeneTree; ENSGT00940000157216; -.
DR HOGENOM; CLU_007394_1_1_1; -.
DR InParanoid; Q9Y3P9; -.
DR OMA; KPSQGDC; -.
DR OrthoDB; 191811at2759; -.
DR PhylomeDB; Q9Y3P9; -.
DR TreeFam; TF317184; -.
DR PathwayCommons; Q9Y3P9; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SignaLink; Q9Y3P9; -.
DR BioGRID-ORCS; 23637; 15 hits in 1080 CRISPR screens.
DR ChiTaRS; RABGAP1; human.
DR GeneWiki; RABGAP1; -.
DR GenomeRNAi; 23637; -.
DR Pharos; Q9Y3P9; Tbio.
DR PRO; PR:Q9Y3P9; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y3P9; protein.
DR Bgee; ENSG00000011454; Expressed in secondary oocyte and 213 other tissues.
DR ExpressionAtlas; Q9Y3P9; baseline and differential.
DR Genevisible; Q9Y3P9; HS.
DR GO; GO:0005813; C:centrosome; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; TAS:ProtInc.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR033185; RabGAP1.
DR PANTHER; PTHR22957:SF439; PTHR22957:SF439; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Coiled coil; Cytoplasm;
KW Cytoskeleton; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1069
FT /note="Rab GTPase-activating protein 1"
FT /id="PRO_0000298779"
FT DOMAIN 142..298
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 566..752
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 798..1047
FT /evidence="ECO:0000255"
FT COMPBIAS 9..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 608
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 649
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AWA9"
FT MOD_RES 996
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052510"
FT VAR_SEQ 258..265
FT /note="RILYSFAT -> PQEKTLCK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052511"
FT VAR_SEQ 266..1069
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052512"
FT VAR_SEQ 480..1069
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_052515"
FT VAR_SEQ 637..667
FT /note="AYSVYDEEIGYCQGQSFLAAVLLLHMPEEQA -> VFHVKKKKDSILSGGST
FT LKLHKKQLQSVICI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052513"
FT VAR_SEQ 668..1069
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052514"
FT HELIX 540..549
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 559..564
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 572..580
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 586..595
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 603..611
FT /evidence="ECO:0007829|PDB:4NC6"
FT TURN 618..620
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 626..641
FT /evidence="ECO:0007829|PDB:4NC6"
FT TURN 643..645
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 651..659
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 664..675
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 680..684
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 686..688
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 689..705
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 707..715
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 720..722
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 725..730
FT /evidence="ECO:0007829|PDB:4NC6"
FT TURN 731..735
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 738..751
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 755..766
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 768..770
FT /evidence="ECO:0007829|PDB:4NC6"
FT TURN 771..773
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 776..784
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 786..790
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 794..806
FT /evidence="ECO:0007829|PDB:4NC6"
FT HELIX 811..828
FT /evidence="ECO:0007829|PDB:4NC6"
SQ SEQUENCE 1069 AA; 121737 MW; F3B09BD3CF993F3A CRC64;
MDDKASVGKI SVSSDSVSTL NSEDFVLVSR QGDETPSTNN GSDDEKTGLK IVGNGSEQQL
QKELADVLMD PPMDDQPGEK ELVKRSQLDG EGDGPLSNQL SASSTINPVP LVGLQKPEMS
LPVKPGQGDS EASSPFTPVA DEDSVVFSKL TYLGCASVNA PRSEVEALRM MSILRSQCQI
SLDVTLSVPN VSEGIVRLLD PQTNTEIANY PIYKILFCVR GHDGTPESDC FAFTESHYNA
ELFRIHVFRC EIQEAVSRIL YSFATAFRRS AKQTPLSATA APQTPDSDIF TFSVSLEIKE
DDGKGYFSAV PKDKDRQCFK LRQGIDKKIV IYVQQTTNKE LAIERCFGLL LSPGKDVRNS
DMHLLDLESM GKSSDGKSYV ITGSWNPKSP HFQVVNEETP KDKVLFMTTA VDLVITEVQE
PVRFLLETKV RVCSPNERLF WPFSKRSTTE NFFLKLKQIK QRERKNNTDT LYEVVCLESE
SERERRKTTA SPSVRLPQSG SQSSVIPSPP EDDEEEDNDE PLLSGSGDVS KECAEKILET
WGELLSKWHL NLNVRPKQLS SLVRNGVPEA LRGEVWQLLA GCHNNDHLVE KYRILITKES
PQDSAITRDI NRTFPAHDYF KDTGGDGQDS LYKICKAYSV YDEEIGYCQG QSFLAAVLLL
HMPEEQAFSV LVKIMFDYGL RELFKQNFED LHCKFYQLER LMQEYIPDLY NHFLDISLEA
HMYASQWFLT LFTAKFPLYM VFHIIDLLLC EGISVIFNVA LGLLKTSKDD LLLTDFEGAL
KFFRVQLPKR YRSEENAKKL MELACNMKIS QKKLKKYEKE YHTMREQQAQ QEDPIERFER
ENRRLQEANM RLEQENDDLA HELVTSKIAL RKDLDNAEEK ADALNKELLM TKQKLIDAEE
EKRRLEEESA QLKEMCRREL DKAESEIKKN SSIIGDYKQI CSQLSERLEK QQTANKVEIE
KIRQKVDDCE RCREFFNKEG RVKGISSTKE VLDEDTDEEK ETLKNQLREM ELELAQTKLQ
LVEAECKIQD LEHHLGLALN EVQAAKKTWF NRTLSSIKTA TGVQGKETC
