PHIP_MOUSE
ID PHIP_MOUSE Reviewed; 1821 AA.
AC Q8VDD9; Q3TS96; Q80VI6; Q9EPY1; Q9ESL6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=PH-interacting protein;
DE Short=PHIP;
DE AltName: Full=IRS-1 PH domain-binding protein;
DE AltName: Full=Neuronal differentiation-related protein;
DE Short=NDRP;
DE AltName: Full=WD repeat-containing protein 11;
GN Name=Phip; Synonyms=Ndrp, Phip1, Wdr11;
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] OF 1-1779.
RA Antonarakis S.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-999, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=11098134; DOI=10.1093/oxfordjournals.jbchem.a022843;
RA Kato H., Chen S., Kiyama H., Ikeda K., Kimura N., Nakashima K., Taga T.;
RT "Identification of a novel WD repeat-containing gene predominantly
RT expressed in developing and regenerating neurons.";
RL J. Biochem. 128:923-932(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-893.
RC STRAIN=Czech II; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 745-1458.
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 924-1821, FUNCTION, INTERACTION WITH IRS1 AND
RP IRS2, AND TISSUE SPECIFICITY.
RX PubMed=11018022; DOI=10.1074/jbc.c000611200;
RA Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.;
RT "Cloning and characterization of PHIP, a novel insulin receptor substrate-1
RT pleckstrin homology domain interacting protein.";
RL J. Biol. Chem. 275:40492-40497(2000).
RN [6]
RP PROTEIN SEQUENCE OF 1589-1596, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP FUNCTION.
RX PubMed=12242307; DOI=10.1128/mcb.22.20.7325-7336.2002;
RA Farhang-Fallah J., Randhawa V.K., Nimnual A., Klip A., Bar-Sagi D.,
RA Rozakis-Adcock M.;
RT "The pleckstrin homology (PH) domain-interacting protein couples the
RT insulin receptor substrate 1 PH domain to insulin signaling pathways
RT leading to mitogenesis and GLUT4 translocation.";
RL Mol. Cell. Biol. 22:7325-7336(2002).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17636024; DOI=10.1128/mcb.02409-06;
RA Podcheko A., Northcott P., Bikopoulos G., Lee A., Bommareddi S.R.,
RA Kushner J.A., Farhang-Fallah J., Rozakis-Adcock M.;
RT "Identification of a WD40 repeat-containing isoform of PHIP as a novel
RT regulator of beta-cell growth and survival.";
RL Mol. Cell. Biol. 27:6484-6496(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281 AND SER-1283, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281 AND SER-1283, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281; SER-1283; SER-1315 AND
RP SER-1783, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1533, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Probable regulator of the insulin and insulin-like growth
CC factor signaling pathways. Stimulates cell proliferation through
CC regulation of cyclin transcription and has an anti-apoptotic activity
CC through AKT1 phosphorylation and activation. Plays a role in the
CC regulation of cell morphology and cytoskeletal organization.
CC {ECO:0000269|PubMed:11018022, ECO:0000269|PubMed:12242307,
CC ECO:0000269|PubMed:17636024}.
CC -!- SUBUNIT: Interacts (via bromo domain) with acetylated lysine residues
CC on histone H1.4, histone H3 and H4 (in vitro) (By similarity).
CC Interacts with IRS1 and IRS2. {ECO:0000250,
CC ECO:0000269|PubMed:11018022}.
CC -!- INTERACTION:
CC Q8VDD9; P35570: Irs1; Xeno; NbExp=2; IntAct=EBI-1369766, EBI-520230;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17636024}.
CC -!- TISSUE SPECIFICITY: Widely expressed with most abundant expression
CC detected in pancreatic islets, brain and skeletal muscle. Predominantly
CC expressed in developing and regenerating neurons. Expressed in adult
CC brain (granular layer of the olfactorium bulb, hippocampus, dentate
CC gyrus and cerebellum internal granular layer). Expressed in the CA3
CC region of adult hippocampus, adult and fetal retina, perinatal dorsal
CC root ganglion and embryonal olfactory epithelia (at protein level).
CC {ECO:0000269|PubMed:11018022, ECO:0000269|PubMed:11098134,
CC ECO:0000269|PubMed:17636024}.
CC -!- DEVELOPMENTAL STAGE: Expressed at highest levels at 17.5 dpc in the
CC neural layer of the retina and olfactory epithelia.
CC {ECO:0000269|PubMed:11098134}.
CC -!- INDUCTION: In motor neurons after injury.
CC {ECO:0000269|PubMed:11098134}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG45146.1; Type=Miscellaneous discrepancy; Note=Intron retention. This sequence is incomplete at the 5' end and extensively differs from that shown.; Evidence={ECO:0000305};
CC Sequence=AAH49950.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB16299.1; Type=Miscellaneous discrepancy; Note=Intron retention. This sequence is incomplete at the 3' end and extensively differs from that shown.; Evidence={ECO:0000305};
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DR EMBL; AJ303103; CAC83119.1; -; mRNA.
DR EMBL; AB049460; BAB16299.1; ALT_SEQ; mRNA.
DR EMBL; BC049950; AAH49950.1; ALT_TERM; mRNA.
DR EMBL; AK162189; BAE36779.1; -; mRNA.
DR EMBL; AF310251; AAG45146.1; ALT_SEQ; mRNA.
DR CCDS; CCDS40706.1; -.
DR AlphaFoldDB; Q8VDD9; -.
DR SMR; Q8VDD9; -.
DR IntAct; Q8VDD9; 6.
DR MINT; Q8VDD9; -.
DR STRING; 10090.ENSMUSP00000034787; -.
DR iPTMnet; Q8VDD9; -.
DR PhosphoSitePlus; Q8VDD9; -.
DR EPD; Q8VDD9; -.
DR jPOST; Q8VDD9; -.
DR MaxQB; Q8VDD9; -.
DR PaxDb; Q8VDD9; -.
DR PRIDE; Q8VDD9; -.
DR ProteomicsDB; 301813; -.
DR UCSC; uc009qvw.1; mouse.
DR MGI; MGI:1932404; Phip.
DR eggNOG; KOG0644; Eukaryota.
DR InParanoid; Q8VDD9; -.
DR PhylomeDB; Q8VDD9; -.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR ChiTaRS; Phip; mouse.
DR PRO; PR:Q8VDD9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VDD9; protein.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005158; F:insulin receptor binding; IEA:InterPro.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1904692; P:positive regulation of type B pancreatic cell proliferation; IGI:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IMP:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IGI:MGI.
DR Gene3D; 1.20.920.10; -; 2.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR028738; PHIP.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR16266:SF4; PTHR16266:SF4; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF47370; SSF47370; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Bromodomain; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
KW WD repeat.
FT CHAIN 1..1821
FT /note="PH-interacting protein"
FT /id="PRO_0000297758"
FT REPEAT 181..222
FT /note="WD 1"
FT REPEAT 224..262
FT /note="WD 2"
FT REPEAT 265..310
FT /note="WD 3"
FT REPEAT 319..360
FT /note="WD 4"
FT REPEAT 363..402
FT /note="WD 5"
FT REPEAT 422..461
FT /note="WD 6"
FT REPEAT 464..504
FT /note="WD 7"
FT REPEAT 512..551
FT /note="WD 8"
FT DOMAIN 1176..1246
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1333..1403
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 653..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..1129
FT /note="Mediates interaction with IRS1"
FT /evidence="ECO:0000269|PubMed:11018022"
FT REGION 1282..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1623..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 1315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1359
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 1405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 1479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 1497
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 1525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 1533
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 1651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 1762
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT MOD_RES 1783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT CROSSLNK 1470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT CROSSLNK 1470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT CROSSLNK 1644
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT CROSSLNK 1670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
FT CONFLICT 672
FT /note="R -> G (in Ref. 3; AAH49950)"
FT /evidence="ECO:0000305"
FT CONFLICT 1065
FT /note="P -> R (in Ref. 4; BAE36779 and 5; AAG45146)"
FT /evidence="ECO:0000305"
FT CONFLICT 1155
FT /note="E -> D (in Ref. 5; AAG45146)"
FT /evidence="ECO:0000305"
FT CONFLICT 1392
FT /note="F -> S (in Ref. 4; BAE36779 and 5; AAG45146)"
FT /evidence="ECO:0000305"
FT CONFLICT 1776
FT /note="A -> T (in Ref. 5; AAG45146)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1821 AA; 206726 MW; 92E8DF0833F60FFA CRC64;
MSRERKGLSE LRSELYFLIA RFLEDGPCQQ AAQVLIREVA EKELLPRRTD WTGKEHPRTY
QNLVKYYRHL APDHLLQICH RLGPLLEQEI PQSVPGVQTL LGAGRQSLLR TNKSCKHVVW
KGSALAALHC GRPPESPVNY GSPPSIADTL FSRKLNGKYR LERLVPTAVY QHMKMHKRIL
GHLSSVYCVT FDRTGRRIFT GSDDCLVKIW ATDDGRLLAT LRGHAAEISD MAVNYENTMI
AAGSCDKMIR VWCLRTCAPL AVLQGHSASI TSLQFSPLCS GSKRYLSSTG ADGTICFWLW
DAGTLKINPR PTKFTERPRP GVQMICSSFS AGGMFLATGS TDHIIRVYFF GSGQPEKISE
LEFHTDKVDS IQFSNTSNRF VSGSRDGTAR IWQFKRREWK SILLDMATRP AGQNLQGIED
KITKMKVTMV AWDRHDNTVI TAVNNMTLKV WNSYTGQLIH VLMGHEDEVF VLEPHPFDPR
VLFSAGHDGN VIVWDLARGV KVRSYFNMIE GQGHGAVFDC KCSPDGQHFA CTDSHGHLLI
FGFGSSSKYD KIADQMFFHS DYRPLIRDAN NFVLDEQTQQ APHLMPPPFL VDVDGNPHPS
RYQRLVPGRE NCREEQLIPQ MGVTSSGLNQ VLSQQANQDI SPLDSMIQRL QQEQDLRRSG
EAGVSNASRV NRGSVSSTSE VHSPPNIGLR RSGQIEGVRQ MHSNAPRSEI ATERDLVAWS
RRVVVPELSA GVASRQEEWR TAKGEEEIKS YRSEEKRKHL TVAKENKILT VSKNHAHEHF
LDLGDSKKQQ ANQHNYRTRS ALEETPRPLE ELENGTSSSD EGEVLAVSGG TSEEEERAWH
SDGSSSDYSS DYSDWTADAG INLQPPKKVP KHKTKKPESS SDEEEESENQ KQKHIKKERK
KANEEKDGPT SPKKKKPKER KQKRLAVGEL TENGLTLEEW LPSAWITDTL PRRCPFVPQM
GDEVYYFRQG HEAYVEMARK NKIYSINPKK QPWHKMELRE QELMKIVGIK YEVGLPTLCC
LKLAFLDPDT GKLTGGSFTM KYHDMPDVID FLVLRQQFDD AKYRPWNIGD RFRSVIDDAW
WFGTIESQEP LQPEYPDSLF QCYNVCWDNG DTEKMSPWDM ELIPNNAVFP EELGTSVPLT
DVECRSLIYK PLDGEWGANP RDEECERIVG GINQLMTLDI ASAFVAPVDL QAYPMYCTVV
AYPTDLSTIK QRLENRFYRR FSSLMWEVRY IEHNTRTFNE PGSPIVKSAK FVTDLLLHFI
KDQTCYNIIP LYNSMKKKVL SDSEEEEKDA DVPGTSTRKR KDHQPRRRLR NRAQSYDIQA
WKKQCQELLN LIFQCEDSEP FRQPVDLLEY PDYRDIIDTP MDFATVRETL EAGNYESPME
LCKDVRLIFS NFKAYTPSKR SRIYSMSLRL SAFFEEHISS VLSDYKSALR FHKRNTISKK
RKKRNRSSSL SSSAASSPER KKRILKPQLK SEVSTSPFSI PTRSVLPRHN AAQMNGKPES
SSVVRTRSNR VAVDPVVTEQ PSTSSATKAF VSKTNTSAMP GKAMLENSVR HSKALSTLSS
PDPLTFSHAT KNNSAKENME KEKPVKRKMK SSVFSKASPL PKSAAVIEQG ECKNNVLIPG
TIQVNGHGGQ PSKLVKRGPG RKPKVEVNTS SGEVTHKKRG RKPKNLQCAK QENSEQNNMH
PIRADVLPSS TCNFLSETNA VKEDLLQKKS RGGRKPKRKM KTHNLDSELI VPTNVKVLRR
SNRKKTDDPI DEEEEFEELK GSEPHMRTRN QGRRTAFYNE DDSEEEQRQL LFEDTSLTFG
TSSRGRVRKL TEKAKANLIG W
