MAP4_MOUSE
ID MAP4_MOUSE Reviewed; 1125 AA.
AC P27546; Q05BJ2; Q3UIS2; Q3UUH5; Q3UY36; Q7TPC6; Q7TPD4; Q80YQ5; Q8CFP5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Microtubule-associated protein 4;
DE Short=MAP-4;
GN Name=Map4; Synonyms=Mtap4;
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] (ISOFORM 1).
RX PubMed=1718985; DOI=10.1016/s0021-9258(18)54720-7;
RA West R.R., Tenbarge K.M., Olmsted J.B.;
RT "A model for microtubule-associated protein 4 structure. Domains defined by
RT comparisons of human, mouse, and bovine sequences.";
RL J. Biol. Chem. 266:21886-21896(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Heart, Hypothalamus, and Olfactory bulb;
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] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C3H/He, and C57BL/6J; TISSUE=Brain, Eye, and Osteoblast;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-617, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475; THR-503; SER-506;
RP SER-517 AND SER-1046, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-517, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-667, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; THR-260; SER-381;
RP THR-447; SER-475; THR-503; SER-506; THR-511; SER-512; SER-517; SER-598;
RP SER-617; THR-658; SER-667; SER-760; SER-901; SER-914 AND SER-1046, AND
RP IDENTIFICATION BY MASS 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).
RN [10]
RP INTERACTION WITH TRAF3IP1.
RX PubMed=26487268; DOI=10.1038/ncomms9666;
RA Bizet A.A., Becker-Heck A., Ryan R., Weber K., Filhol E., Krug P.,
RA Halbritter J., Delous M., Lasbennes M.C., Linghu B., Oakeley E.J.,
RA Zarhrate M., Nitschke P., Garfa-Traore M., Serluca F., Yang F.,
RA Bouwmeester T., Pinson L., Cassuto E., Dubot P., Elshakhs N.A., Sahel J.A.,
RA Salomon R., Drummond I.A., Gubler M.C., Antignac C., Chibout S.,
RA Szustakowski J.D., Hildebrandt F., Lorentzen E., Sailer A.W., Benmerah A.,
RA Saint-Mezard P., Saunier S.;
RT "Mutations in TRAF3IP1/IFT54 reveal a new role for IFT proteins in
RT microtubule stabilization.";
RL Nat. Commun. 6:8666-8666(2015).
CC -!- FUNCTION: Non-neuronal microtubule-associated protein. Promotes
CC microtubule assembly.
CC -!- SUBUNIT: Interacts with SEPTIN2; this interaction impedes tubulin-
CC binding. Interacts with TRAF3IP1 (PubMed:26487268). Interacts with
CC KNSTRN (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P27816,
CC ECO:0000269|PubMed:26487268}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P27816}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000250|UniProtKB:P27816}. Note=Recruitment to
CC microtubule is inhibited by microtubules polyglutamylation.
CC {ECO:0000250|UniProtKB:P27816}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P27546-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27546-2; Sequence=VSP_026097;
CC Name=3;
CC IsoId=P27546-3; Sequence=VSP_026095, VSP_026097;
CC Name=4;
CC IsoId=P27546-4; Sequence=VSP_026089, VSP_026090, VSP_026091,
CC VSP_026092, VSP_026093, VSP_026094,
CC VSP_026095, VSP_026096, VSP_026097;
CC -!- TISSUE SPECIFICITY: Testis, striated and cardiac muscle.
CC -!- PTM: Phosphorylated at serine residues in K-X-G-S motifs by
CC MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing
CC detachment from microtubules, and their disassembly (By similarity).
CC Phosphorylation on Ser-760 negatively regulates MAP4 activity to
CC promote microtubule assembly. Isoform 4 is phosphorylated on Ser-333
CC and Ser-334 (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH42645.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE27434.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M72414; AAA16372.1; -; mRNA.
DR EMBL; AK134996; BAE22377.1; -; mRNA.
DR EMBL; AK138416; BAE23650.1; -; mRNA.
DR EMBL; AK146790; BAE27434.1; ALT_INIT; mRNA.
DR EMBL; BC042645; AAH42645.1; ALT_INIT; mRNA.
DR EMBL; BC044654; AAH44654.1; -; mRNA.
DR EMBL; BC050893; AAH50893.1; -; mRNA.
DR EMBL; BC055332; AAH55332.1; -; mRNA.
DR EMBL; BC055364; AAH55364.1; -; mRNA.
DR CCDS; CCDS57704.1; -. [P27546-1]
DR CCDS; CCDS81083.1; -. [P27546-4]
DR PIR; B41206; B41206.
DR RefSeq; NP_001192259.1; NM_001205330.1. [P27546-1]
DR RefSeq; NP_001192261.1; NM_001205332.1. [P27546-3]
DR RefSeq; NP_001298092.1; NM_001311163.1.
DR RefSeq; NP_001298093.1; NM_001311164.1.
DR RefSeq; NP_032659.2; NM_008633.4.
DR RefSeq; XP_017168653.1; XM_017313164.1.
DR AlphaFoldDB; P27546; -.
DR BioGRID; 201586; 21.
DR IntAct; P27546; 14.
DR MINT; P27546; -.
DR STRING; 10090.ENSMUSP00000035055; -.
DR iPTMnet; P27546; -.
DR PhosphoSitePlus; P27546; -.
DR SwissPalm; P27546; -.
DR EPD; P27546; -.
DR jPOST; P27546; -.
DR MaxQB; P27546; -.
DR PaxDb; P27546; -.
DR PeptideAtlas; P27546; -.
DR PRIDE; P27546; -.
DR ProteomicsDB; 295779; -. [P27546-1]
DR ProteomicsDB; 295780; -. [P27546-2]
DR ProteomicsDB; 295781; -. [P27546-3]
DR ProteomicsDB; 295782; -. [P27546-4]
DR Antibodypedia; 29982; 385 antibodies from 29 providers.
DR DNASU; 17758; -.
DR Ensembl; ENSMUST00000035055; ENSMUSP00000035055; ENSMUSG00000032479. [P27546-1]
DR Ensembl; ENSMUST00000165876; ENSMUSP00000132662; ENSMUSG00000032479. [P27546-2]
DR GeneID; 17758; -.
DR KEGG; mmu:17758; -.
DR UCSC; uc009rsz.3; mouse. [P27546-2]
DR UCSC; uc009rta.3; mouse. [P27546-1]
DR UCSC; uc009rtb.3; mouse. [P27546-3]
DR CTD; 4134; -.
DR MGI; MGI:97178; Map4.
DR VEuPathDB; HostDB:ENSMUSG00000032479; -.
DR eggNOG; KOG2418; Eukaryota.
DR GeneTree; ENSGT00940000164123; -.
DR HOGENOM; CLU_043626_0_0_1; -.
DR InParanoid; P27546; -.
DR OMA; EMALGEN; -.
DR PhylomeDB; P27546; -.
DR BioGRID-ORCS; 17758; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Map4; mouse.
DR PRO; PR:P27546; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P27546; protein.
DR Bgee; ENSMUSG00000032479; Expressed in retinal neural layer and 268 other tissues.
DR ExpressionAtlas; P27546; baseline and differential.
DR Genevisible; P27546; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0051301; P:cell division; ISO:MGI.
DR GO; GO:0051294; P:establishment of spindle orientation; IDA:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:ARUK-UCL.
DR GO; GO:0051012; P:microtubule sliding; IDA:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; IDA:MGI.
DR GO; GO:1902856; P:negative regulation of non-motile cilium assembly; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR InterPro; IPR027323; MAP4.
DR InterPro; IPR001084; MAP_tubulin-bd_rpt.
DR PANTHER; PTHR11501:SF16; PTHR11501:SF16; 1.
DR Pfam; PF00418; Tubulin-binding; 4.
DR PROSITE; PS00229; TAU_MAP_1; 4.
DR PROSITE; PS51491; TAU_MAP_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Microtubule; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT CHAIN 2..1125
FT /note="Microtubule-associated protein 4"
FT /id="PRO_0000072752"
FT REPEAT 896..926
FT /note="Tau/MAP 1"
FT REPEAT 965..995
FT /note="Tau/MAP 2"
FT REPEAT 996..1026
FT /note="Tau/MAP 3"
FT REPEAT 1027..1058
FT /note="Tau/MAP 4"
FT REGION 49..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 349
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 494
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 503
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 511
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M7W5"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 658
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 915
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT CROSSLNK 811
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT VAR_SEQ 1..26
FT /note="MADLSLVDALTEPPPEIEGEIKRDFM -> MSLPEKQPAALT (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026089"
FT VAR_SEQ 30..259
FT /note="EAEPYDDIVGETVEKTEFIPLLDGDEKTGNSESKKKPCLDTSQVEGIPSSKP
FT TLLANGDHGMEGNNTAGSPTDFLEERVDYPDYQSSQNWPEDASFCFQPQQVLDTDQAEP
FT FNEHRDDGLADLLFVSSGPTNASAFTERDNPSEDSYGMLPCDSFASTAVVSQEWSVGAP
FT NSPCSESCVSPEVTIETLQPATELSKAAEVESVKEQLPAKALETMAEQTTDVVHSPSTD
FT T -> AAEDEQLSKGNPPECGMDSRKEIGQDGFEWQRTEGKLNEIGLNVSMDGQLKDRL
FT VKNSSFLEQNKLGFFEGKLDKELSIEKPNKAYQETSGHLESGYVISGTCQPSEGNLVHQ
FT KAAEFHPGLTEGKDKAATVQGKVAGKSGLEIKSQPDLNFPGAADTLTQHGEEQETSAWN
FT ANFYSVTQSPQAA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026090"
FT VAR_SEQ 263..419
FT /note="PDTEAALAKDIEEITKPDVILANVTQPSTESDMFLAQDMELLTGTEAAHANN
FT IILPTEPDESSTKDVAPPMEEEIVPGNDTTSPKETETTLPIKMDLAPPEDVLLTKETEL
FT APAKGMVSLSEIEEALAKNDESSAEIPVAQETVVSETEVVLATEVV -> KEKNGLVSS
FT CSVTGVMSDNSGQLNNKSPLLVAITHPDPTSEHLPTTSPPITMVEFTQENLNAGQDKEL
FT EKLRSSEEGPMLDQVPQQKKAIRRALSECYHLSVPPAVNLVDKYPELPAREE (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026091"
FT VAR_SEQ 424..531
FT /note="PITTLTKDVTLPLEAERPLVTDMTPSLETEMTLGKETAPPTETNLGMAKDMS
FT PLPESEVTLGKDVVILPETKVAEFNNVTPLSEEEVTSVKDMSPSAETEAPLAKNAD ->
FT LLPPTSSPMPSPMPRKLGVPAMRRSMTVAEDQSASCRLSAGELASLSASQVPTALTFEE
FT PVAKEREEQIHFSNDSNSSGKKELGIAGLY (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026092"
FT VAR_SEQ 535..625
FT /note="GTELIVDNSMAPASDLALPLETKVATVPIKDKGTVQTEEKPREDSQLASMQH
FT KGQSTVPPCTASPEPVKAAEQMSTLPIDAPSPLENLEQK -> KLEQIPEGSHKGKGQK
FT NTGETRVDSCPFICLGGEKQLMALAGKKEIEVTATQSIPSLLLE (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026093"
FT VAR_SEQ 629..637
FT /note="GSQPSEPCS -> RD (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026094"
FT VAR_SEQ 927..964
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026095"
FT VAR_SEQ 965..995
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026096"
FT VAR_SEQ 1124..1125
FT /note="SI -> N (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026097"
FT CONFLICT 225
FT /note="K -> E (in Ref. 3; AAH55364)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="V -> A (in Ref. 3; AAH55364)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..395
FT /note="ES -> VR (in Ref. 1; AAA16372)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="T -> I (in Ref. 3; AAH55332)"
FT /evidence="ECO:0000305"
FT CONFLICT 955
FT /note="A -> V (in Ref. 3; AAH55364)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="G -> V (in Ref. 1; AAA16372)"
FT /evidence="ECO:0000305"
FT CONFLICT 993
FT /note="G -> C (in Ref. 1; AAA16372)"
FT /evidence="ECO:0000305"
FT CONFLICT 1053
FT /note="L -> F (in Ref. 1; AAA16372)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="K -> KV (in Ref. 3; AAH44654/AAH55364)"
FT /evidence="ECO:0000305"
FT CONFLICT 1089
FT /note="A -> R (in Ref. 1; AAA16372)"
FT /evidence="ECO:0000305"
FT MOD_RES P27546-4:333
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES P27546-4:334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT P27546-4:435
FT /note="K -> E (in Ref. 2; BAE23650/BAE22377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1125 AA; 117429 MW; E948B7F1F5B903E9 CRC64;
MADLSLVDAL TEPPPEIEGE IKRDFMAALE AEPYDDIVGE TVEKTEFIPL LDGDEKTGNS
ESKKKPCLDT SQVEGIPSSK PTLLANGDHG MEGNNTAGSP TDFLEERVDY PDYQSSQNWP
EDASFCFQPQ QVLDTDQAEP FNEHRDDGLA DLLFVSSGPT NASAFTERDN PSEDSYGMLP
CDSFASTAVV SQEWSVGAPN SPCSESCVSP EVTIETLQPA TELSKAAEVE SVKEQLPAKA
LETMAEQTTD VVHSPSTDTT PGPDTEAALA KDIEEITKPD VILANVTQPS TESDMFLAQD
MELLTGTEAA HANNIILPTE PDESSTKDVA PPMEEEIVPG NDTTSPKETE TTLPIKMDLA
PPEDVLLTKE TELAPAKGMV SLSEIEEALA KNDESSAEIP VAQETVVSET EVVLATEVVL
PSDPITTLTK DVTLPLEAER PLVTDMTPSL ETEMTLGKET APPTETNLGM AKDMSPLPES
EVTLGKDVVI LPETKVAEFN NVTPLSEEEV TSVKDMSPSA ETEAPLAKNA DLHSGTELIV
DNSMAPASDL ALPLETKVAT VPIKDKGTVQ TEEKPREDSQ LASMQHKGQS TVPPCTASPE
PVKAAEQMST LPIDAPSPLE NLEQKETPGS QPSEPCSGVS RQEEAKAAVG VTGNDITTPP
NKEPPPSPEK KAKPLATTQP AKTSTSKAKT QPTSLPKQPA PTTSGGLNKK PMSLASGSVP
AAPHKRPAAA TATARPSTLP ARDVKPKPIT EAKVAEKRTS PSKPSSAPAL KPGPKTTPTV
SKATSPSTLV STGPSSRSPA TTLPKRPTSI KTEGKPADVK RMTAKSASAD LSRSKTTSAS
SVKRNTTPTG AAPPAGMTST RVKPMSAPSR SSGALSVDKK PTSTKPSSSA PRVSRLATTV
SAPDLKSVRS KVGSTENIKH QPGGGRAKVE KKTEAATTAG KPEPNAVTKA AGSIASAQKP
PAGKVQIVSK KVSYSHIQSK CGSKDNIKHV PGGGNVQIQN KKVDISKVSS KCGSKANIKH
KPGGGDVKIE SQKLNFKEKA QAKVGSLDNV GHLPAGGAVK TEGGGSEALP CPGPPAGEEP
VIPEAAPDAG APTSASGLSG HTTLSGGGDQ REPQTLDSQI QETSI
