ZN318_MOUSE
ID ZN318_MOUSE Reviewed; 2237 AA.
AC Q99PP2; B0V2M3; B9EK88; Q3TZL5; Q8BMX9; Q9JJ01;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Zinc finger protein 318;
DE AltName: Full=Testicular zinc finger protein;
GN Name=Znf318; Synonyms=Tzf, Zfp318;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 175-2237 (ISOFORM 2), FUNCTION (ISOFORM 2),
RP AND TISSUE SPECIFICITY (ISOFORM 2).
RC STRAIN=ddY; TISSUE=Testis;
RX PubMed=10873617; DOI=10.1006/bbrc.2000.2953;
RA Inoue A., Ishiji A., Kasagi S., Ishizuka M., Hirose S., Baba T.,
RA Hagiwara H.;
RT "The transcript for a novel protein with a zinc finger motif is expressed
RT at specific stages of mouse spermatogenesis.";
RL Biochem. Biophys. Res. Commun. 273:398-403(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 175-2237 (ISOFORM 1), FUNCTION (ISOFORMS 1
RP AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY
RP (ISOFORMS 1 AND 2).
RC STRAIN=ddY;
RX PubMed=12589823; DOI=10.1016/s0006-291x(03)00085-8;
RA Ishizuka M., Ohshima H., Tamura N., Nakada T., Inoue A., Hirose S.,
RA Hagiwara H.;
RT "Molecular cloning and characteristics of a novel zinc finger protein and
RT its splice variant whose transcripts are expressed during
RT spermatogenesis.";
RL Biochem. Biophys. Res. Commun. 301:1079-1085(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-2237 (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 566-1230 AND 2172-2237 (ISOFORM
RP 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP FUNCTION (ISOFORM 2), AND INTERACTION WITH AR (ISOFORM 2).
RX PubMed=15882980; DOI=10.1016/j.bbrc.2005.04.024;
RA Ishizuka M., Kawate H., Takayanagi R., Ohshima H., Tao R.-H., Hagiwara H.;
RT "A zinc finger protein TZF is a novel corepressor of androgen receptor.";
RL Biochem. Biophys. Res. Commun. 331:1025-1031(2005).
RN [7]
RP FUNCTION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2),
RP INTERACTION WITH AR (ISOFORM 1), AND SUBUNIT.
RX PubMed=16446156; DOI=10.1016/j.bbrc.2005.12.213;
RA Tao R.H., Kawate H., Ohnaka K., Ishizuka M., Hagiwara H., Takayanagi R.;
RT "Opposite effects of alternative TZF spliced variants on androgen
RT receptor.";
RL Biochem. Biophys. Res. Commun. 341:515-521(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-167; SER-205;
RP TYR-237; SER-239; SER-246 AND SER-2206, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: [Isoform 2]: Acts as a transcriptional corepressor for AR-
CC mediated transactivation function. May act as a transcriptional
CC regulator during spermatogenesis and in particular, during meiotic
CC division. {ECO:0000269|PubMed:10873617, ECO:0000269|PubMed:12589823,
CC ECO:0000269|PubMed:15882980}.
CC -!- FUNCTION: [Isoform 1]: Acts as a transcriptional coactivator for AR-
CC mediated transactivation function. May act as a transcriptional
CC regulator during spermatogenesis and in particular, during meiotic
CC division. {ECO:0000269|PubMed:12589823, ECO:0000269|PubMed:16446156}.
CC -!- SUBUNIT: Homodimer. Heterodimer of isoform 1 and isoform 2. Isoform 1
CC and isoform 2 interact with AR. {ECO:0000269|PubMed:15882980,
CC ECO:0000269|PubMed:16446156}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:12589823, ECO:0000269|PubMed:16446156}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:12589823, ECO:0000269|PubMed:16446156}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=TZF-L;
CC IsoId=Q99PP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99PP2-2; Sequence=VSP_016594, VSP_016595;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in
CC testis, moderately expressed in adrenal gland and uterus and faintly
CC expressed in brain, kidney and liver. Isoform 1 is expressed more in
CC adrenal gland, uterus and liver than isoform 2 is. Expression during
CC testicular development of isoform 1 and isoform 2 is restricted to
CC spermatocytes at the pachytene stage of meiotic prophase and to round
CC and elongated spermatids. {ECO:0000269|PubMed:10873617,
CC ECO:0000269|PubMed:12589823}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF61636.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF61636.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAI50731.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI50731.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAK00650.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK00650.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC151275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF159455; AAF61636.1; ALT_SEQ; mRNA.
DR EMBL; AF227194; AAK00650.1; ALT_SEQ; mRNA.
DR EMBL; BC150730; AAI50731.1; ALT_SEQ; mRNA.
DR EMBL; AK011661; BAC25342.1; -; mRNA.
DR EMBL; AK157779; BAE34193.1; -; mRNA.
DR CCDS; CCDS28826.2; -. [Q99PP2-2]
DR CCDS; CCDS28827.2; -. [Q99PP2-1]
DR PIR; JC7316; JC7316.
DR RefSeq; NP_067321.2; NM_021346.2. [Q99PP2-2]
DR RefSeq; NP_997554.2; NM_207671.4. [Q99PP2-1]
DR AlphaFoldDB; Q99PP2; -.
DR SMR; Q99PP2; -.
DR BioGRID; 208360; 4.
DR IntAct; Q99PP2; 2.
DR MINT; Q99PP2; -.
DR STRING; 10090.ENSMUSP00000109109; -.
DR iPTMnet; Q99PP2; -.
DR PhosphoSitePlus; Q99PP2; -.
DR jPOST; Q99PP2; -.
DR MaxQB; Q99PP2; -.
DR PaxDb; Q99PP2; -.
DR PeptideAtlas; Q99PP2; -.
DR PRIDE; Q99PP2; -.
DR ProteomicsDB; 302079; -. [Q99PP2-1]
DR ProteomicsDB; 302080; -. [Q99PP2-2]
DR Antibodypedia; 16456; 94 antibodies from 21 providers.
DR Ensembl; ENSMUST00000113481; ENSMUSP00000109109; ENSMUSG00000015597. [Q99PP2-1]
DR Ensembl; ENSMUST00000138127; ENSMUSP00000116544; ENSMUSG00000015597. [Q99PP2-2]
DR GeneID; 57908; -.
DR KEGG; mmu:57908; -.
DR CTD; 57908; -.
DR MGI; MGI:1889348; Zfp318.
DR VEuPathDB; HostDB:ENSMUSG00000015597; -.
DR eggNOG; ENOG502R1ZF; Eukaryota.
DR GeneTree; ENSGT00390000000614; -.
DR InParanoid; Q99PP2; -.
DR OMA; CQSRPYE; -.
DR OrthoDB; 44718at2759; -.
DR TreeFam; TF350583; -.
DR BioGRID-ORCS; 57908; 8 hits in 71 CRISPR screens.
DR ChiTaRS; Zfp318; mouse.
DR PRO; PR:Q99PP2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99PP2; protein.
DR Bgee; ENSMUSG00000015597; Expressed in embryonic post-anal tail and 245 other tissues.
DR ExpressionAtlas; Q99PP2; baseline and differential.
DR Genevisible; B0V2M3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR SMART; SM00451; ZnF_U1; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Isopeptide bond; Meiosis;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..2237
FT /note="Zinc finger protein 318"
FT /id="PRO_0000191808"
FT ZN_FING 1085..1119
FT /note="Matrin-type 1"
FT ZN_FING 1158..1180
FT /note="Matrin-type 2"
FT REGION 1..1114
FT /note="Interaction with AR"
FT /evidence="ECO:0000269|PubMed:16446156"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1790..1867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2039..2064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2178..2237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 348..376
FT /evidence="ECO:0000255"
FT COILED 904..1003
FT /evidence="ECO:0000255"
FT COILED 1798..1827
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1829..1846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1853..1867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2039..2061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2178..2201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 237
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 865
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 1445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 1878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 1908
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 1988
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 2044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 2054
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 2140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 2143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 2194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT MOD_RES 2206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 577
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT CROSSLNK 596
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT CROSSLNK 607
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VUA4"
FT VAR_SEQ 1115..1154
FT /note="TLDPYNRPWASKTQSEAKQDTVKRTDKITVPAKGSEFLIP -> GQFQKSSH
FT FQTEGLKQMFLLQECRDRNHRDYGNNVRPCGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10873617"
FT /id="VSP_016594"
FT VAR_SEQ 1155..2237
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10873617"
FT /id="VSP_016595"
FT CONFLICT 223
FT /note="V -> D (in Ref. 2; AAF61636 and 3; AAK00650)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="S -> F (in Ref. 4; AAI50731)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="K -> R (in Ref. 2; AAF61636 and 3; AAK00650)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="F -> N (in Ref. 2; AAF61636 and 3; AAK00650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2237 AA; 246324 MW; 97B600577866BA14 CRC64;
MYRSGSRSSV SSHRSKDGSA SGPPPGRPVG ASSGPTRRPS SPPPPSCSSL RLPARRHRSP
SGHRGRWASP SPPRGRRGSP SPPRGRRASP SPTRGRRASP SPPRGRRGSP SPPRARRGSP
SPPRSRRHYP PGLGGFRGSI RGESRADFAR DGRGDHPGGG GGSRRRSPGL CSDSSLEESL
RITVGNDHFC VSTPERRRLS DRLGSPVDGL QDMDRDDLTD DSVFTRSSQC SRGLERYISR
EEGPLSPFLG QLDEDYRTRE TFLHRPEFSP QSSCHDELLR GTERNRDKLK SSSYSIRSEE
RSREAKRPRY DDTEKVHSSG GDHSSFTSGT RNYRQRRSSP SPRFLDPEFR ELDLARRKRE
EEEEQSRSLS QELVGVGDDQ IGCSIPGLAG VLTTSEPGYS LQRPEEVPMM PKKSILKKRI
EADMKPSLQL ESFSSGASSG EDHPLYSEHS PLPLSGAIAA FTSEIENKGT TVEADLKEPQ
SNLYQWGPLR EIPKDNSEKF DSFLGFKEKL DLKAEGLEQQ TDFLLPHERA SQDGSGFSRI
LSMLADPTIT QEKRRRSFPD IEDEEKFLYG DEEEDIKSES PLKSLEDPES AGTRQKANSL
PSTPAVKLES LEESNPEYAK IHNLLKTIGL DIGVAEIGKL AARTQERLHG KKPSSRPSAD
RRLSADRHLS GDRHFSADRC SSVEHSFTAD WRSSDPHRPE SRETHHSNTQ SPEVSHPHPA
SPVDPYLRTK NSPPFLKSDH PVCHVSGPEV VGSGFQSSVA VRCMLPSAPS TPIRLPHSAA
LSQFHIPGAS QFAAARIPPN YQGSVIPSAS FDAYRHYMAY AASRWPMYPA SQPPSHPLSD
PHRLLPVTKQ AARSRPNLRV IPTVTPAKPK QEIPVLGSIS VKRIPVRVSI PSLIKYNPKK
ISDEKNRASQ KQKVIEEREK LKTEQEARQK KMFYLTTELE RLHKQQGEML RKKRREKDGH
KDPLLMEVSR LQDSIMKDIA ELHKETEEAE KKQSELDKVA QILGIDIFDK SLKSSNDSKE
STEKPEKEKS KSPEKELSPS NSSSSNKESK MNEKSCIKSP SSTESLQPTV KQSDQPVAAY
EYYDAGSHWC KDCNTTCGTM FDFFTHMHNK KHTQTLDPYN RPWASKTQSE AKQDTVKRTD
KITVPAKGSE FLIPVTGFYC QLCEEFLGDP ISGEQHVKGH QHNENYKKYV EENPLYEERR
NLDRQAGLAV VLETERRRQN ELKRKLNEKP KEEKIEKKAR IVREVKEDDK APGELEEQLS
EDGSAPEKGE VKGNASLRPQ VKEEVKKEPS VASIAASFGK FSWKKPEKEE EKGSVVTPGA
PKEDTVETSK DRDDGKAEVG KAKPIKIKLS GKTVIAHTSP WTPVVTTSTQ TKIRPNLPIP
STVLRKSGSA TVSKPAPLNT FLSIKSSGTS TKPLPVVKES SSDLLLPPDI ISKAFGGEEV
VLKGSPEEKV ELAEKNEPSQ VPEQMLALLP PPPPPPPPPP PPPPPPPPQA VPQLSAPSPA
QANVVLTPVK SNSVISQTFS LGFQGPNILN PGLPVAFMAS EQPTVIPSDE TAPGVSESDW
DQTLISMLVR PPPPLSSVFS EQAKKLEKRN SCLATANAKD LYDIFYSSGG KGAHETKLSS
STLANGESSS LPRTESSDFS STCTLNSSMS SEDLPQCSAL VTATEISNLE NPISKGMEST
GKWSVVDQID PKSRDSTYSF LQPLTRLYQN KPYEIVSPKT DTLVMWTSGS SQNDTHKDRP
PEGKIRFDLG EPGPPGTDST SHLSDTHCQT NGPQKLIEIN LIDNQNKNQE VYQSEGCRES
EMKRKTELKG KVATEEEEEE EEEGANSIED SNSNHGNRNT WEGEIGQPKL STVDKKGEQS
SKLMTGHENT SKVVIELSPS LPSKRTKIDL FPSLLQNPKS MPELLLLSPA GSGLCLKRQE
IWERPEKPGL EDVELQGTRP ELTVTIESKV LENFDTTHLE VEGFASLRNL GDMHANFHNS
QTEQTRRSPT ALSEKMSEEI SVSSVMCNPS SSSDIEPVPS FSGFPLESPK TLVLNFETEG
AHSSSNSRNG RITSNSLETG HPVENVGHDL GGERTHQALD LLAGGMLSED VKETSPLQKD
LLRMESTTVS PSGLGPSPCL PDLVDFVTRT PGVPKQKPCS PLSEPDAFLK CSSLEMGSPP
PEILSVSVSE VAVPQVSEDN DSALNLVKTP PSGSPSRDQV VGGNVSPREM PEQEAAVDVI
PDHTRSNVYN SQDYLNG
