TTF2_HUMAN
ID TTF2_HUMAN Reviewed; 1162 AA.
AC Q9UNY4; A8K4Q2; O75921; Q5T2K7; Q5VVU8; Q8N6I8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Transcription termination factor 2;
DE EC=3.6.4.-;
DE AltName: Full=Lodestar homolog;
DE AltName: Full=RNA polymerase II termination factor;
DE AltName: Full=Transcription release factor 2;
DE Short=F2;
DE Short=HuF2;
GN Name=TTF2;
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 1), AND FUNCTION.
RX PubMed=9748214; DOI=10.1074/jbc.273.40.25541;
RA Liu M., Xie Z., Price D.H.;
RT "A human RNA polymerase II transcription termination factor is a SWI2/SNF2
RT family member.";
RL J. Biol. Chem. 273:25541-25544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDC5L,
RP IDENTIFICATION AS PART OF THE SPLICEOSOME, AND VARIANT HIS-1155.
RX PubMed=12927788; DOI=10.1016/s0006-291x(03)01486-4;
RA Leonard D., Ajuh P., Lamond A.I., Legerski R.J.;
RT "hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA
RT splicing.";
RL Biochem. Biophys. Res. Commun. 308:793-801(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-167.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 FUNCTION.
RX PubMed=10455150; DOI=10.1074/jbc.274.35.24779;
RA Hara R., Selby C.P., Liu M., Price D.H., Sancar A.;
RT "Human transcription release factor 2 dissociates RNA polymerases I and II
RT stalled at a cyclobutane thymine dimer.";
RL J. Biol. Chem. 274:24779-24786(1999).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15125840; DOI=10.1016/s1097-2765(04)00234-5;
RA Jiang Y., Liu M., Spencer C.A., Price D.H.;
RT "Involvement of transcription termination factor 2 in mitotic repression of
RT transcription elongation.";
RL Mol. Cell 14:375-385(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-883, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-908, AND
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 [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-883, AND IDENTIFICATION BY
RP 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).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-143, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: DsDNA-dependent ATPase which acts as a transcription
CC termination factor by coupling ATP hydrolysis with removal of RNA
CC polymerase II from the DNA template. May contribute to mitotic
CC transcription repression. May also be involved in pre-mRNA splicing.
CC {ECO:0000269|PubMed:10455150, ECO:0000269|PubMed:12927788,
CC ECO:0000269|PubMed:15125840, ECO:0000269|PubMed:9748214}.
CC -!- SUBUNIT: Interacts with CDC5L. Part of the spliceosome.
CC {ECO:0000269|PubMed:12927788}.
CC -!- INTERACTION:
CC Q9UNY4; Q99459: CDC5L; NbExp=5; IntAct=EBI-2322921, EBI-374880;
CC Q9UNY4-2; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-11980463, EBI-948296;
CC Q9UNY4-2; Q99081-3: TCF12; NbExp=3; IntAct=EBI-11980463, EBI-11952764;
CC Q9UNY4-2; P15884-3: TCF4; NbExp=3; IntAct=EBI-11980463, EBI-13636688;
CC Q9UNY4-2; Q15025: TNIP1; NbExp=3; IntAct=EBI-11980463, EBI-357849;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15125840}. Nucleus
CC {ECO:0000269|PubMed:15125840}. Note=Cytoplasmic during interphase.
CC Relocates to the nucleus as cells enter mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNY4-2; Sequence=VSP_015370, VSP_015371;
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AF073771; AAC64044.1; -; mRNA.
DR EMBL; AF080255; AAD49435.1; -; mRNA.
DR EMBL; AK291017; BAF83706.1; -; mRNA.
DR EMBL; AL391476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030058; AAH30058.1; -; mRNA.
DR CCDS; CCDS892.1; -. [Q9UNY4-1]
DR RefSeq; NP_003585.3; NM_003594.3. [Q9UNY4-1]
DR RefSeq; XP_016858044.1; XM_017002555.1. [Q9UNY4-1]
DR AlphaFoldDB; Q9UNY4; -.
DR SMR; Q9UNY4; -.
DR BioGRID; 114036; 174.
DR IntAct; Q9UNY4; 62.
DR MINT; Q9UNY4; -.
DR STRING; 9606.ENSP00000358478; -.
DR iPTMnet; Q9UNY4; -.
DR MetOSite; Q9UNY4; -.
DR PhosphoSitePlus; Q9UNY4; -.
DR BioMuta; TTF2; -.
DR DMDM; 73920148; -.
DR EPD; Q9UNY4; -.
DR jPOST; Q9UNY4; -.
DR MassIVE; Q9UNY4; -.
DR MaxQB; Q9UNY4; -.
DR PaxDb; Q9UNY4; -.
DR PeptideAtlas; Q9UNY4; -.
DR PRIDE; Q9UNY4; -.
DR ProteomicsDB; 85342; -. [Q9UNY4-1]
DR ProteomicsDB; 85343; -. [Q9UNY4-2]
DR Antibodypedia; 1775; 190 antibodies from 26 providers.
DR DNASU; 8458; -.
DR Ensembl; ENST00000369466.9; ENSP00000358478.3; ENSG00000116830.12. [Q9UNY4-1]
DR GeneID; 8458; -.
DR KEGG; hsa:8458; -.
DR MANE-Select; ENST00000369466.9; ENSP00000358478.3; NM_003594.4; NP_003585.3.
DR UCSC; uc001egy.4; human. [Q9UNY4-1]
DR CTD; 8458; -.
DR DisGeNET; 8458; -.
DR GeneCards; TTF2; -.
DR HGNC; HGNC:12398; TTF2.
DR HPA; ENSG00000116830; Low tissue specificity.
DR MIM; 604718; gene.
DR neXtProt; NX_Q9UNY4; -.
DR OpenTargets; ENSG00000116830; -.
DR PharmGKB; PA37063; -.
DR VEuPathDB; HostDB:ENSG00000116830; -.
DR eggNOG; KOG4439; Eukaryota.
DR GeneTree; ENSGT00940000162718; -.
DR HOGENOM; CLU_000315_2_2_1; -.
DR InParanoid; Q9UNY4; -.
DR OMA; PEHGTFC; -.
DR OrthoDB; 132523at2759; -.
DR PhylomeDB; Q9UNY4; -.
DR TreeFam; TF316297; -.
DR PathwayCommons; Q9UNY4; -.
DR SignaLink; Q9UNY4; -.
DR SIGNOR; Q9UNY4; -.
DR BioGRID-ORCS; 8458; 411 hits in 1092 CRISPR screens.
DR ChiTaRS; TTF2; human.
DR GeneWiki; TTF2; -.
DR GenomeRNAi; 8458; -.
DR Pharos; Q9UNY4; Tbio.
DR PRO; PR:Q9UNY4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UNY4; protein.
DR Bgee; ENSG00000116830; Expressed in sural nerve and 145 other tissues.
DR ExpressionAtlas; Q9UNY4; baseline and differential.
DR Genevisible; Q9UNY4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0008023; C:transcription elongation factor complex; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:FlyBase.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006353; P:DNA-templated transcription, termination; TAS:ProtInc.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:ProtInc.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR010666; Znf_GRF.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF06839; zf-GRF; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; DNA-binding; Helicase;
KW Hydrolase; Isopeptide bond; Metal-binding; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Spliceosome; Transcription; Transcription regulation;
KW Transcription termination; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1162
FT /note="Transcription termination factor 2"
FT /id="PRO_0000074376"
FT DOMAIN 583..786
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 995..1157
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 5..39
FT /note="GRF-type"
FT REGION 97..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 737..740
FT /note="DEAH box"
FT COMPBIAS 142..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 596..603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 635..676
FT /note="DSCDFTSHGTLIICPASLIHHWKNEVEKRVNSNKLRVYLYHG -> GRQKCL
FT NSLPFPTSFEPPKRGTSSAKKGHLWSYLITLLENQY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015370"
FT VAR_SEQ 677..1162
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015371"
FT VARIANT 167
FT /note="K -> E (in dbSNP:rs998532)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_023393"
FT VARIANT 213
FT /note="K -> R (in dbSNP:rs7535524)"
FT /id="VAR_034431"
FT VARIANT 256
FT /note="E -> G (in dbSNP:rs34334470)"
FT /id="VAR_061234"
FT VARIANT 1134
FT /note="K -> R (in dbSNP:rs41276572)"
FT /id="VAR_061235"
FT VARIANT 1155
FT /note="D -> H (in dbSNP:rs34236116)"
FT /evidence="ECO:0000269|PubMed:12927788"
FT /id="VAR_061236"
FT CONFLICT 64
FT /note="L -> P (in Ref. 2; AAD49435)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="R -> G (in Ref. 2; AAD49435)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="H -> R (in Ref. 1; AAC64044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1162 AA; 129588 MW; 858BAA22B2D2D5C9 CRC64;
MEEVRCPEHG TFCFLKTGVR DGPNKGKSFY VCRADTCSFV RATDIPVSHC LLHEDFVVEL
QGLLLPQDKK EYRLFFRCIR SKAEGKRWCG SIPWQDPDSK EHSVSNKSQH ASETFHHSSN
WLRNPFKVLD KNQEPALWKQ LIKGEGEEKK ADKKQREKGD QLFDQKKEQK PEMMEKDLSS
GLVPKKKQSV VQEKKQEEGA EIQCEAETGG THKRDFSEIK SQQCQGNELT RPSASSQEKS
SGKSQDVQRE SEPLREKVTQ LLPQNVHSHN SISKPQKGGP LNKEYTNWEA KETKAKDGPS
IQATQKSLPQ GHFQERPETH SVPAPGGPAA QAAPAAPGLS LGEGREAATS SDDEEEDDVV
FVSSKPGSPL LFDSTLDLET KENLQFPDRS VQRKVSPASG VSKKVEPSDP VARRVYLTTQ
LKQKKSTLAS VNIQALPDKG QKLIKQIQEL EEVLSGLTLS PEQGTNEKSN SQVPQQSHFT
KTTTGPPHLV PPQPLPRRGT QPVGSLELKS ACQVTAGGSS QCYRGHTNQD HVHAVWKITS
EAIGQLHRSL ESCPGETVVA EDPAGLKVPL LLHQKQALAW LLWRESQKPQ GGILADDMGL
GKTLTMIALI LTQKNQEKKE EKEKSTALTW LSKDDSCDFT SHGTLIICPA SLIHHWKNEV
EKRVNSNKLR VYLYHGPNRD SRARVLSTYD IVITTYSLVA KEIPTNKQEA EIPGANLNVE
GTSTPLLRIA WARIILDEAH NVKNPRVQTS IAVCKLQACA RWAVTGTPIQ NNLLDMYSLL
KFLRCSPFDE FNLWRSQVDN GSKKGGERLS ILTKSLLLRR TKDQLDSTGR PLVILPQRKF
QLHHLKLSED EETVYNVFFA RSRSALQSYL KRHESRGNQS GRSPNNPFSR VALEFGSEEP
RHSEAADSPR SSTVHILSQL LRLRQCCCHL SLLKSALDPM ELKGEGLVLS LEEQLSALTL
SELRDSEPSS TVSLNGTFFK MELFEGMRES TKISSLLAEL EAIQRNSASQ KSVIVSQWTN
MLKVVALHLK KHGLTYATID GSVNPKQRMD LVEAFNHSRG PQVMLISLLA GGVGLNLTGG
NHLFLLDMHW NPSLEDQACD RIYRVGQQKD VVIHRFVCEG TVEEKILQLQ EKKKDLAKQV
LSGSGESVTK LTLADLRVLF GI
