ING4_MOUSE
ID ING4_MOUSE Reviewed; 249 AA.
AC Q8C0D7; Q8C1S7; Q8K3Q5; Q8K3Q6; Q8K3Q7; Q9D7F9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Inhibitor of growth protein 4;
DE AltName: Full=p29ING4;
GN Name=Ing4;
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 [MRNA] (ISOFORMS 3; 4 AND 5), ALTERNATIVE SPLICING
RP (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BCL2A1, AND
RP TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Mammary gland;
RX PubMed=11888890;
RA Ha S., Lee S., Chung M., Choi Y.;
RT "Mouse ING1 homologue, a protein interacting with A1, enhances cell death
RT and is inhibited by A1 in mammary epithelial cells.";
RL Cancer Res. 62:1275-1278(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, Pancreas, Testis, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127; LYS-129; LYS-146; LYS-148
RP AND LYS-156, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP STRUCTURE BY NMR OF 168-245.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PHD domain in ING1-like protein BAC25079.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Component of HBO1 complexes, which specifically mediate
CC acetylation of histone H3 at 'Lys-14' (H3K14ac), and have reduced
CC activity toward histone H4. Through chromatin acetylation it may
CC function in DNA replication. May inhibit tumor progression by
CC modulating the transcriptional output of signaling pathways which
CC regulate cell proliferation. Can suppress brain tumor angiogenesis
CC through transcriptional repression of RELA/NFKB3 target genes when
CC complexed with RELA. May also specifically suppress loss of contact
CC inhibition elicited by activated oncogenes such as MYC. Represses
CC hypoxia inducible factor's (HIF) activity by interacting with HIF
CC prolyl hydroxylase 2 (EGLN1) (By similarity). Can enhance apoptosis
CC induced by serum starvation in mammary epithelial cell line HC11
CC (PubMed:11888890). {ECO:0000250|UniProtKB:Q9UNL4,
CC ECO:0000269|PubMed:11888890}.
CC -!- SUBUNIT: Homodimer. Component of the HBO1 complex composed of
CC KAT7/HBO1, MEAF6, ING4 or ING5, and one scaffold subunit: complexes
CC containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1
CC specificity towards H3K14ac, while complexes containing JADE scaffold
CC (JADE1, JADE2 and JADE3) mediate acetylation of histone H4. Interacts
CC with H3K4me3 and to a lesser extent with H3K4me2, the interaction
CC augments KAT7/HBO1 acetylation activity on H3 tails. Interacts with
CC EP300, RELA and TP53; these interactions may be indirect. Interacts
CC with EGLN1. {ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- SUBUNIT: [Isoform 3]: Interacts with BCL2A1.
CC {ECO:0000269|PubMed:11888890}.
CC -!- SUBUNIT: [Isoform 4]: Interacts with BCL2A1.
CC {ECO:0000269|PubMed:11888890}.
CC -!- SUBUNIT: [Isoform 5]: Interacts with BCL2A1.
CC {ECO:0000269|PubMed:11888890}.
CC -!- INTERACTION:
CC Q8C0D7; P22605: Rarb; NbExp=3; IntAct=EBI-645598, EBI-2903247;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11888890}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8C0D7-1; Sequence=Displayed;
CC Name=2; Synonyms=mINGh-M {ECO:0000303|PubMed:11888890};
CC IsoId=Q8C0D7-2; Sequence=VSP_012521, VSP_012522;
CC Name=3; Synonyms=mINGh-L2 {ECO:0000303|PubMed:11888890};
CC IsoId=Q8C0D7-3; Sequence=VSP_012521, VSP_012522, VSP_012526,
CC VSP_012527;
CC Name=4; Synonyms=mINGh-L {ECO:0000303|PubMed:11888890};
CC IsoId=Q8C0D7-4; Sequence=VSP_012521, VSP_012522, VSP_012523;
CC Name=5; Synonyms=mINGh-S {ECO:0000303|PubMed:11888890};
CC IsoId=Q8C0D7-5; Sequence=VSP_012520, VSP_012524, VSP_012525;
CC -!- TISSUE SPECIFICITY: Isoform 2, isoform 3, isoform 4 and isoform 5 are
CC expressed in the mammary gland, ovary, spleen and muscle.
CC {ECO:0000269|PubMed:11888890}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in the mammary gland, ovary,
CC spleen and muscle. {ECO:0000269|PubMed:11888890}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in the mammary gland, ovary,
CC spleen and muscle. {ECO:0000269|PubMed:11888890}.
CC -!- TISSUE SPECIFICITY: [Isoform 4]: Expressed in the mammary gland, ovary,
CC spleen and muscle. {ECO:0000269|PubMed:11888890}.
CC -!- TISSUE SPECIFICITY: [Isoform 5]: Expressed in the mammary gland, ovary,
CC spleen and muscle. {ECO:0000269|PubMed:11888890}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- DOMAIN: The N-terminal coiled-coil domain mediates homodimerization.
CC {ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- PTM: Citrullination by PADI4 within the nuclear localization signal
CC disrupts the interaction with p53 and increases susceptibility to
CC degradation. {ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25009.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY035880; AAK63168.1; -; mRNA.
DR EMBL; AY035881; AAK63169.1; -; mRNA.
DR EMBL; AY036107; AAK64509.1; -; mRNA.
DR EMBL; AK002821; BAC25009.1; ALT_FRAME; mRNA.
DR EMBL; AK009267; BAB26183.1; -; mRNA.
DR EMBL; AK031633; BAC27489.1; -; mRNA.
DR EMBL; AK050522; BAC34304.1; -; mRNA.
DR EMBL; BC009127; AAH09127.1; -; mRNA.
DR CCDS; CCDS39632.1; -. [Q8C0D7-2]
DR CCDS; CCDS90121.1; -. [Q8C0D7-1]
DR RefSeq; NP_579923.1; NM_133345.2. [Q8C0D7-2]
DR PDB; 1WEN; NMR; -; A=188-245.
DR PDB; 1WEU; NMR; -; A=168-245.
DR PDBsum; 1WEN; -.
DR PDBsum; 1WEU; -.
DR AlphaFoldDB; Q8C0D7; -.
DR BMRB; Q8C0D7; -.
DR SMR; Q8C0D7; -.
DR BioGRID; 205719; 1.
DR ComplexPortal; CPX-794; HBO1-4.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-795; HBO1-4.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-796; HBO1-4.3 histone acetyltransferase complex.
DR IntAct; Q8C0D7; 5.
DR MINT; Q8C0D7; -.
DR STRING; 10090.ENSMUSP00000121519; -.
DR iPTMnet; Q8C0D7; -.
DR PhosphoSitePlus; Q8C0D7; -.
DR EPD; Q8C0D7; -.
DR MaxQB; Q8C0D7; -.
DR PaxDb; Q8C0D7; -.
DR PeptideAtlas; Q8C0D7; -.
DR PRIDE; Q8C0D7; -.
DR ProteomicsDB; 267245; -. [Q8C0D7-1]
DR ProteomicsDB; 267246; -. [Q8C0D7-2]
DR ProteomicsDB; 267247; -. [Q8C0D7-3]
DR ProteomicsDB; 267248; -. [Q8C0D7-4]
DR ProteomicsDB; 267249; -. [Q8C0D7-5]
DR Antibodypedia; 22581; 267 antibodies from 32 providers.
DR DNASU; 28019; -.
DR Ensembl; ENSMUST00000032480; ENSMUSP00000032480; ENSMUSG00000030330. [Q8C0D7-2]
DR Ensembl; ENSMUST00000112417; ENSMUSP00000108036; ENSMUSG00000030330. [Q8C0D7-5]
DR Ensembl; ENSMUST00000140131; ENSMUSP00000121519; ENSMUSG00000030330. [Q8C0D7-1]
DR GeneID; 28019; -.
DR KEGG; mmu:28019; -.
DR UCSC; uc009dtd.1; mouse. [Q8C0D7-2]
DR UCSC; uc009dtf.1; mouse. [Q8C0D7-1]
DR CTD; 51147; -.
DR MGI; MGI:107307; Ing4.
DR VEuPathDB; HostDB:ENSMUSG00000030330; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000159033; -.
DR HOGENOM; CLU_031900_5_1_1; -.
DR InParanoid; Q8C0D7; -.
DR OMA; SHGQMIM; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q8C0D7; -.
DR TreeFam; TF352014; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 28019; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Ing4; mouse.
DR EvolutionaryTrace; Q8C0D7; -.
DR PRO; PR:Q8C0D7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8C0D7; protein.
DR Bgee; ENSMUSG00000030330; Expressed in cortical plate and 130 other tissues.
DR Genevisible; Q8C0D7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0016570; P:histone modification; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045926; P:negative regulation of growth; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:1902164; P:positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISO:MGI.
DR GO; GO:0006473; P:protein acetylation; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR028638; ING4/ING5.
DR InterPro; IPR028651; ING_fam.
DR InterPro; IPR024610; ING_N_histone-binding.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10333; PTHR10333; 1.
DR PANTHER; PTHR10333:SF41; PTHR10333:SF41; 1.
DR Pfam; PF12998; ING; 1.
DR SMART; SM01408; ING; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell cycle;
KW Chromatin regulator; Citrullination; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Tumor suppressor; Zinc; Zinc-finger.
FT CHAIN 1..249
FT /note="Inhibitor of growth protein 4"
FT /id="PRO_0000212669"
FT ZN_FING 196..245
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 115..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..118
FT /evidence="ECO:0000255"
FT MOTIF 127..148
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 198
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 209
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 213
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 221
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNL4"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 129
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 133
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 156
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 166
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT VAR_SEQ 127..130
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11888890"
FT /id="VSP_012520"
FT VAR_SEQ 131
FT /note="K -> S (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11888890,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_012521"
FT VAR_SEQ 132
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11888890,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_012522"
FT VAR_SEQ 168..249
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11888890"
FT /id="VSP_012523"
FT VAR_SEQ 170..172
FT /note="EYG -> MER (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11888890"
FT /id="VSP_012524"
FT VAR_SEQ 173..249
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11888890"
FT /id="VSP_012525"
FT VAR_SEQ 217..228
FT /note="CSIEWFHFACVG -> VRTVSSGLGEEL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11888890"
FT /id="VSP_012526"
FT VAR_SEQ 229..249
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11888890"
FT /id="VSP_012527"
FT CONFLICT 105
FT /note="A -> S (in Ref. 2; BAC27489)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="G -> S (in Ref. 2; BAC27489)"
FT /evidence="ECO:0000305"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1WEN"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:1WEN"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1WEN"
SQ SEQUENCE 249 AA; 28528 MW; 6C5C5582A249E412 CRC64;
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE
KLALLRQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD
YDSSSSKGKK KGRTQKEKKA ARARSKGKNS DEEAPKAAQK KLKLVRTSPE YGMPSVTFGS
VHPSDVLDMP VDPNEPTYCL CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP
RCSQERKKK
