ECM29_HUMAN
ID ECM29_HUMAN Reviewed; 1845 AA.
AC Q5VYK3; O15074; Q8WU82;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Proteasome adapter and scaffold protein ECM29 {ECO:0000305};
DE AltName: Full=Ecm29 proteasome adapter and scaffold {ECO:0000312|HGNC:HGNC:29020};
DE AltName: Full=Proteasome-associated protein ECM29 homolog;
GN Name=ECPAS {ECO:0000312|HGNC:HGNC:29020}; Synonyms=ECM29, KIAA0368;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-194.
RG The MGC Project Team;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 182-1845.
RC TISSUE=Hippocampus;
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 MRNA] OF 405-1845.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1301-1845.
RC TISSUE=B-cell;
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, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15496406; DOI=10.1074/jbc.m410444200;
RA Gorbea C., Goellner G.M., Teter K., Holmes R.K., Rechsteiner M.;
RT "Characterization of mammalian Ecm29, a 26 S proteasome-associated protein
RT that localizes to the nucleus and membrane vesicles.";
RL J. Biol. Chem. 279:54849-54861(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS11; VPS26A; VPS36;
RP RAB11FIP4; RABEP1; DCTN1; DCTN2; KIF5B; MYH7; MYH10; MYO10 AND ARF6.
RX PubMed=20682791; DOI=10.1074/jbc.m110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E.,
RA Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-830, AND IDENTIFICATION BY
RP 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-836, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1039, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
CC -!- FUNCTION: Adapter/scaffolding protein that binds to the 26S proteasome,
CC motor proteins and other compartment specific proteins. May couple the
CC proteasome to different compartments including endosome, endoplasmic
CC reticulum and centrosome. May play a role in ERAD and other enhanced
CC proteolysis (PubMed:15496406). Promotes proteasome dissociation under
CC oxidative stress (By similarity). {ECO:0000250|UniProtKB:Q6PDI5,
CC ECO:0000269|PubMed:15496406, ECO:0000269|PubMed:20682791}.
CC -!- SUBUNIT: Non-stoichiometric component of the proteasome; associates
CC with the 26S proteasome. Interacts (via N-terminus) with VPS11, VPS26A,
CC VPS36, RAB11FIP4 and RABEP1. Interacts (via C-terminus) with DCTN1,
CC DCTN2, KIF5B, MYH7, MYH10, MYO10 and ARF6.
CC {ECO:0000269|PubMed:15496406, ECO:0000269|PubMed:20682791}.
CC -!- INTERACTION:
CC Q5VYK3; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-521451, EBI-741181;
CC Q5VYK3; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-521451, EBI-11522760;
CC Q5VYK3; Q8WZ55: BSND; NbExp=3; IntAct=EBI-521451, EBI-7996695;
CC Q5VYK3; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-521451, EBI-2548702;
CC Q5VYK3; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-521451, EBI-11522780;
CC Q5VYK3; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-521451, EBI-1054315;
CC Q5VYK3; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-521451, EBI-12831978;
CC Q5VYK3; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-521451, EBI-18053395;
CC Q5VYK3; Q969L2: MAL2; NbExp=5; IntAct=EBI-521451, EBI-944295;
CC Q5VYK3; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-521451, EBI-1044859;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:15496406}. Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000269|PubMed:15496406}. Endosome
CC {ECO:0000269|PubMed:15496406}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:15496406}. Nucleus
CC {ECO:0000269|PubMed:15496406}. Endosome, multivesicular body
CC {ECO:0000269|PubMed:20682791}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:20682791}.
CC -!- SIMILARITY: Belongs to the ECM29 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21127.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL354661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL159168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AI916718; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK127247; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB002366; BAA20823.1; -; mRNA.
DR EMBL; BC021127; AAH21127.1; ALT_INIT; mRNA.
DR RefSeq; XP_005251907.1; XM_005251850.3.
DR AlphaFoldDB; Q5VYK3; -.
DR BioGRID; 116966; 293.
DR IntAct; Q5VYK3; 73.
DR MINT; Q5VYK3; -.
DR STRING; 9606.ENSP00000259335; -.
DR ChEMBL; CHEMBL4295853; -.
DR GlyGen; Q5VYK3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VYK3; -.
DR MetOSite; Q5VYK3; -.
DR PhosphoSitePlus; Q5VYK3; -.
DR SwissPalm; Q5VYK3; -.
DR BioMuta; KIAA0368; -.
DR DMDM; 61212960; -.
DR EPD; Q5VYK3; -.
DR jPOST; Q5VYK3; -.
DR MassIVE; Q5VYK3; -.
DR MaxQB; Q5VYK3; -.
DR PaxDb; Q5VYK3; -.
DR PeptideAtlas; Q5VYK3; -.
DR PRIDE; Q5VYK3; -.
DR ProteomicsDB; 65635; -.
DR Antibodypedia; 29523; 45 antibodies from 15 providers.
DR Ensembl; ENST00000338205.9; ENSP00000339889.5; ENSG00000136813.15.
DR UCSC; uc064vau.1; human.
DR GeneCards; ECPAS; -.
DR HGNC; HGNC:29020; ECPAS.
DR HPA; ENSG00000136813; Tissue enhanced (skeletal).
DR MIM; 616694; gene.
DR neXtProt; NX_Q5VYK3; -.
DR VEuPathDB; HostDB:ENSG00000136813; -.
DR eggNOG; KOG0915; Eukaryota.
DR HOGENOM; CLU_000880_2_0_1; -.
DR InParanoid; Q5VYK3; -.
DR OrthoDB; 167285at2759; -.
DR PhylomeDB; Q5VYK3; -.
DR PathwayCommons; Q5VYK3; -.
DR SignaLink; Q5VYK3; -.
DR BioGRID-ORCS; 23392; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; KIAA0368; human.
DR GeneWiki; KIAA0368; -.
DR GenomeRNAi; 23392; -.
DR Pharos; Q5VYK3; Tbio.
DR PRO; PR:Q5VYK3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5VYK3; protein.
DR Bgee; ENSG00000136813; Expressed in gastrocnemius and 211 other tissues.
DR ExpressionAtlas; Q5VYK3; baseline and differential.
DR Genevisible; Q5VYK3; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005771; C:multivesicular body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024372; Ecm29.
DR PANTHER; PTHR23346:SF19; PTHR23346:SF19; 1.
DR Pfam; PF13001; Ecm29; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Endoplasmic reticulum; Endosome; Isopeptide bond; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1845
FT /note="Proteasome adapter and scaffold protein ECM29"
FT /id="PRO_0000212559"
FT REPEAT 34..71
FT /note="HEAT 1"
FT REPEAT 113..150
FT /note="HEAT 2"
FT REPEAT 168..211
FT /note="HEAT 3"
FT REPEAT 332..368
FT /note="HEAT 4"
FT REPEAT 393..432
FT /note="HEAT 5"
FT REPEAT 435..472
FT /note="HEAT 6"
FT REPEAT 475..513
FT /note="HEAT 7"
FT REPEAT 689..726
FT /note="HEAT 8"
FT REPEAT 727..765
FT /note="HEAT 9"
FT REPEAT 789..826
FT /note="HEAT 10"
FT REPEAT 835..874
FT /note="HEAT 11"
FT REPEAT 876..913
FT /note="HEAT 12"
FT REPEAT 937..975
FT /note="HEAT 13"
FT REPEAT 981..1018
FT /note="HEAT 14"
FT REPEAT 1019..1056
FT /note="HEAT 15"
FT REPEAT 1118..1155
FT /note="HEAT 16"
FT REPEAT 1158..1195
FT /note="HEAT 17"
FT REPEAT 1200..1237
FT /note="HEAT 18"
FT REPEAT 1249..1287
FT /note="HEAT 19"
FT REPEAT 1291..1329
FT /note="HEAT 20"
FT REPEAT 1354..1392
FT /note="HEAT 21"
FT REPEAT 1396..1433
FT /note="HEAT 22"
FT REPEAT 1523..1560
FT /note="HEAT 23"
FT REPEAT 1564..1601
FT /note="HEAT 24"
FT REPEAT 1611..1648
FT /note="HEAT 25"
FT REPEAT 1652..1689
FT /note="HEAT 26"
FT REPEAT 1785..1828
FT /note="HEAT 27"
FT REGION 193..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 836
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 1039
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VARIANT 472
FT /note="T -> S (in dbSNP:rs16916091)"
FT /id="VAR_055702"
FT CONFLICT 101
FT /note="I -> N (in Ref. 2; AI916718/AK127247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1845 AA; 204291 MW; 5809A9208F5B4441 CRC64;
MAAAAASASQ DELNQLERVF LRLGHAETDE QLQNIISKFL PPVLLKLSST QEGVRKKVME
LLVHLNKRIK SRPKIQLPVE TLLVQYQDPA AVSFVTNFTI IYVKMGYPRL PVEKQCELAP
TLLTAMEGKP QPQQDSLMHL LIPTLFHMKY PVESSKSASP FNLAEKPKTV QLLLDFMLDV
LLMPYGYVLN ESQSRQNSSS AQGSSSNSGG GSGIPQPPPG MSFYAAKRVI GDNPWTPEQL
EQCKLGIVKF IEAEQVPELE AVLHLVIASS DTRHSVATAA DLELKSKQSL IDWNNPAIIN
KMYKVYLGDI PLKTKEGAVL KPELKRDPVS TRVKLKIVPH LLRSRQAAET FPANIQVVYD
GLFGTNTNSK LRTLSLQFVH HICITCPEIK IKPLGPMLLN GLTKLINEYK EDPKLLSMAY
SAVGKLSSRM PHLFTKDIAL VQQLFEALCK EEPETRLAIQ EALSMMVGAY STLEGAQRTL
MEALVASYLI KPEVQVRQVA VKFASTVFPS DHIPSRYLLL LAAGDPREEV HGEAQRVLRC
LPGRNRKEST SEQMPSFPEM VYYIQEKASH RMKTPVKYMT GTTVLPFNPA AFGEIVLYLR
MCLAHSAGVV PTSQSLADMQ DHAPAIGRYI RTLMSSGQMA PSSSNKSGET NPVQIYIGLL
QQLLAGVGGL PVMYCLLEAV SVYPEKLATK FVDKTEWIKS LMNNSKEEMR ELAALFYSVV
VSTVSGNELK SMIEQLIKTT KDNHSPEIQH GSLLALGFTV GRYLAKKKMR MSEQQDLERN
ADTLPDQEEL IQSATETIGS FLDSTSPLLA IAACTALGEI GRNGPLPIPS EGSGFTKLHL
VESLLSRIPS SKETNKMKER AIQTLGYFPV GDGDFPHQKL LLQGLMDSVE AKQIELQFTI
GEAITSAAIG TSSVAARDAW QMTEEEYTPP AGAKVNDVVP WVLDVILNKH IISPNPHVRQ
AACIWLLSLV RKLSTHKEVK SHLKEIQSAF VSVLSENDEL SQDVASKGLG LVYELGNEQD
QQELVSTLVE TLMTGKRVKH EVSGETVVFQ GGALGKTPDG QGLSTYKELC SLASDLSQPD
LVYKFMNLAN HHAMWNSRKG AAFGFNVIAT RAGEQLAPFL PQLVPRLYRY QFDPNLGIRQ
AMTSIWNALV TDKSMVDKYL KEILQDLVKN LTSNMWRVRE SSCLALNDLL RGRPLDDIID
KLPEIWETLF RVQDDIKESV RKAAELALKT LSKVCVKMCD PAKGAAGQRT IAALLPCLLD
KGMMSTVTEV RALSINTLVK ISKSAGAMLK PHAPKLIPAL LESLSVLEPQ VLNYLSLRAT
EQEKAAMDSA RLSAAKSSPM METINMCLQY LDVSVLGELV PRLCELIRSG VGLGTKGGCA
SVIVSLTTQC PQDLTPYSGK LMSALLSGLT DRNSVIQKSC AFAMGHLVRT SRDSSTEKLL
QKLNGWYMEK EEPIYKTSCA LTIHAIGRYS PDVLKNHAKE VLPLAFLGMH EIADEEKSEK
EECNLWTEVW QENVPGSFGG IRLYLQELIT ITQKALQSQS WKMKAQGAIA MASIAKQTSS
LVPPYLGMIL TALLQGLAGR TWAGKEELLK AIACVVTACS AELEKSVPNQ PSTNEILQAV
LKECSKENVK YKIVAISCAA DILKATKEDR FQEFSNIVIP LIKKNSLESS GVRTTKNEEE
NEKEKELQLE YLLGAFESLG KAWPRNAETQ RCYRQELCKL MCERLKLSTW KVQLGVLQSM
NAFFQGLMLL EEEHADPEAL AEILLETCKS ITYSLENKTY SSVRTEALSV IELLLKKLEE
SKQWECLTSE CRVLLIESLA TMEPDSRPEL QEKAALLKKT LENLE
