CUL4B_MOUSE
ID CUL4B_MOUSE Reviewed; 970 AA.
AC A2A432; Q3TU30; Q8BSL3; Q8CHD6; Q91YZ7; Q99KS9; Q9CZM5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cullin-4B {ECO:0000305};
DE Short=CUL-4B {ECO:0000303|PubMed:16052071};
GN Name=Cul4b {ECO:0000303|PubMed:16052071, ECO:0000312|MGI:MGI:1919834};
GN Synonyms=Kiaa0695 {ECO:0000303|PubMed:12465718};
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] {ECO:0000312|EMBL:AAP84984.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=129/Sv {ECO:0000312|EMBL:AAP84984.1};
RC TISSUE=Embryonic carcinoma {ECO:0000312|EMBL:AAP84984.1};
RX PubMed=16052071; DOI=10.1007/bf02703670;
RA Tripathi R., Sastry K.S., Kota S.K., Srinivas U.K.;
RT "Cloning and characterization of mouse cullin4B/E3 ubiquitin ligase.";
RL J. Biosci. 30:329-337(2005).
RN [2] {ECO:0000312|EMBL:BAC27992.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC27992.1};
RC TISSUE=Embryonic head {ECO:0000312|EMBL:BAE36141.1},
RC Head {ECO:0000312|EMBL:BAE36141.1}, and
RC Wolffian duct {ECO:0000312|EMBL:BAC27992.1};
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] {ECO:0000312|EMBL:CAM17145.1}
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 [4] {ECO:0000312|EMBL:EDL29019.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAH04026.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH04026.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH10347.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH04026.1};
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] {ECO:0000312|EMBL:BAC41443.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-970 (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC41443.3};
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15; SER-17; THR-106; SER-110
RP AND THR-202, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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: Core component of multiple cullin-RING-based E3 ubiquitin-
CC protein ligase complexes which mediate the ubiquitination and
CC subsequent proteasomal degradation of target proteins. The functional
CC specificity of the E3 ubiquitin-protein ligase complex depends on the
CC variable substrate recognition subunit. CUL4B may act within the
CC complex as a scaffold protein, contributing to catalysis through
CC positioning of the substrate and the ubiquitin-conjugating enzyme.
CC Plays a role as part of the E3 ubiquitin-protein ligase complex in
CC polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in
CC response to radiation-induced DNA damage. Targeted to UV damaged
CC chromatin by DDB2 and may be important for DNA repair and DNA
CC replication. A number of DCX complexes (containing either TRPC4AP or
CC DCAF12 as substrate-recognition component) are part of the DesCEND
CC (destruction via C-end degrons) pathway, which recognizes a C-degron
CC located at the extreme C terminus of target proteins, leading to their
CC ubiquitination and degradation. The DCX(AMBRA1) complex is a master
CC regulator of the transition from G1 to S cell phase by mediating
CC ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3). The
CC DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3
CC ubiquitin-protein ligase complexes by mediating ubiquitination and
CC degradation of Elongin-C (ELOC) component of CRL5 complexes. Required
CC for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently,
CC normal G1 cell cycle progression. Regulates the mammalian target-of-
CC rapamycin (mTOR) pathway involved in control of cell growth, size and
CC metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is
CC dependent upon 26S proteasome function and requires interaction between
CC CUL4B and MLST8. With CUL4A, contributes to ribosome biogenesis.
CC {ECO:0000250|UniProtKB:Q13620}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q13620}.
CC -!- SUBUNIT: Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin-
CC protein ligase complexes that seem to be formed of DDB1, CUL4A or
CC CUL4B, RBX1 and a variable substrate recognition component which seems
CC to belong to a protein family described as DCAF (Ddb1- and Cul4-
CC associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins.
CC Component of the DCX(DTL) complex with the putative substrate
CC recognition component DTL. Component of the DCX(DDB2) complex with the
CC putative substrate recognition component DDB2. Component of DCX
CC complexes part of the DesCEND (destruction via C-end degrons) pathway,
CC which contain either TRPC4AP or DCAF12 as substrate-recognition
CC component. Component of the DCX(AMBRA1) complex with the substrate
CC recognition component AMBRA1. Part of a complex with RBX1 and
CC TIP120A/CAND1. Interacts with RBX1, GRWD1, MLST8, SMU1, TLE2, TLE3,
CC DCAF1, DDA1, DCAF6, DCAF17, DDB2, DCAF8, TIP120A/CAND1 and TMEM113.
CC Interacts with cyclin E (CCNE1 or CCNE2) and with importins alpha-1
CC (KPNA2), alpha-3 (KPNA4), alpha-5 (KPNA1) and beta-1 (KPNB1). May
CC interact with WDR26, WDR51B, SNRNP40, WDR61, WDR76 and WDR5. Interacts
CC (unneddylated form) with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and
CC DCUN1D5; these interactions promote the cullin neddylation.
CC {ECO:0000250|UniProtKB:Q13620}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13620}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16052071,
CC ECO:0000269|PubMed:16141072, ECO:0000269|PubMed:19468303};
CC IsoId=A2A432-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12465718};
CC IsoId=A2A432-2; Sequence=VSP_039242;
CC -!- PTM: Neddylated. Deneddylated via its interaction with the COP9
CC signalosome (CSN) complex (By similarity).
CC {ECO:0000250|UniProtKB:Q13620}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04026.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH10347.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC41443.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY330868; AAP84984.1; -; mRNA.
DR EMBL; AK012410; BAB28222.2; -; mRNA.
DR EMBL; AK032701; BAC27992.1; -; mRNA.
DR EMBL; AK160998; BAE36141.1; -; mRNA.
DR EMBL; AL513356; CAM17145.1; -; Genomic_DNA.
DR EMBL; CH466570; EDL29019.1; -; Genomic_DNA.
DR EMBL; BC004026; AAH04026.1; ALT_INIT; mRNA.
DR EMBL; BC010347; AAH10347.1; ALT_INIT; mRNA.
DR EMBL; AB093259; BAC41443.3; ALT_INIT; Transcribed_RNA.
DR CCDS; CCDS40948.1; -. [A2A432-1]
DR RefSeq; NP_001103612.1; NM_001110142.1. [A2A432-1]
DR RefSeq; NP_082564.3; NM_028288.5. [A2A432-1]
DR AlphaFoldDB; A2A432; -.
DR SMR; A2A432; -.
DR BioGRID; 215452; 63.
DR ComplexPortal; CPX-651; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant.
DR IntAct; A2A432; 2.
DR STRING; 10090.ENSMUSP00000059276; -.
DR iPTMnet; A2A432; -.
DR PhosphoSitePlus; A2A432; -.
DR EPD; A2A432; -.
DR jPOST; A2A432; -.
DR MaxQB; A2A432; -.
DR PaxDb; A2A432; -.
DR PeptideAtlas; A2A432; -.
DR PRIDE; A2A432; -.
DR ProteomicsDB; 285230; -. [A2A432-1]
DR ProteomicsDB; 285231; -. [A2A432-2]
DR Antibodypedia; 531; 441 antibodies from 35 providers.
DR DNASU; 72584; -.
DR Ensembl; ENSMUST00000050083; ENSMUSP00000059276; ENSMUSG00000031095. [A2A432-1]
DR Ensembl; ENSMUST00000115118; ENSMUSP00000110771; ENSMUSG00000031095. [A2A432-1]
DR GeneID; 72584; -.
DR KEGG; mmu:72584; -.
DR UCSC; uc009taa.2; mouse. [A2A432-1]
DR CTD; 8450; -.
DR MGI; MGI:1919834; Cul4b.
DR VEuPathDB; HostDB:ENSMUSG00000031095; -.
DR eggNOG; KOG2167; Eukaryota.
DR GeneTree; ENSGT00940000155339; -.
DR InParanoid; A2A432; -.
DR OMA; WPTYPVM; -.
DR PhylomeDB; A2A432; -.
DR TreeFam; TF101153; -.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 72584; 9 hits in 112 CRISPR screens.
DR ChiTaRS; Cul4b; mouse.
DR PRO; PR:A2A432; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2A432; protein.
DR Bgee; ENSMUSG00000031095; Expressed in secondary oocyte and 237 other tissues.
DR ExpressionAtlas; A2A432; baseline and differential.
DR Genevisible; A2A432; MM.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IC:ComplexPortal.
DR GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0048708; P:astrocyte differentiation; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0034644; P:cellular response to UV; IC:ComplexPortal.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070914; P:UV-damage excision repair; ISO:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR033044; CUL4B.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 1.
DR PANTHER; PTHR11932:SF66; PTHR11932:SF66; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; DNA damage; DNA repair; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..970
FT /note="Cullin-4B"
FT /id="PRO_0000394426"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 112..115
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q13620"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13619"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13620"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13620"
FT CROSSLNK 247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q13619"
FT CROSSLNK 916
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13620"
FT VAR_SEQ 693..721
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12465718"
FT /id="VSP_039242"
FT CONFLICT 56
FT /note="P -> A (in Ref. 2; BAB28222)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="Q -> E (in Ref. 6; BAC41443)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="K -> E (in Ref. 2; BAB28222)"
FT /evidence="ECO:0000305"
FT CONFLICT 933
FT /note="Q -> R (in Ref. 1; AAP84984 and 2; BAC27992)"
FT /evidence="ECO:0000305"
FT CONFLICT 966
FT /note="Y -> S (in Ref. 6; BAC41443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 970 AA; 110699 MW; 87D518B268A21849 CRC64;
MSRSTRSKER RENDTDSEDN SSETSNQERR RCRQGPPRPP YPPLLPPVFP PPTPPPQVRR
TRGLQDLGAM KSVCPGTSGF SSPNPSAASA AAQEVRSATD GNTSTTPPTS AKKRKLNSSS
SSSNSSNERE DFDSTSSSST PPQPRDSASP STSSFCLGVP VATSSHVPIQ KKLRFEDTLE
FVGIDTKMAE ESSSSSSSSS PTAATSQQQQ QQQLKTKSIL ISSVASVHHA NGLAKSSTAV
SSFANSKPGS AKKLVIKNFK DKPKLPENYT DETWQKLKEA VEAIQNSTSI KYNLEELYQA
VENLCSHKIS ANLYKQLRQI CEDHIKAQIH QFREDSLDSV LFLKKIDRCW QNHCRQMIMI
RSIFLFLDRT YVLQNSMLPS IWDMGLELFR AHIISDQKVQ TKTIDGILLL IERERNGEAI
DRSLLRSLLS MLSDLQIYQD SFEQQFLQET NRLYAAEGQK LMQEREVPEY LHHVNKRLEE
EADRLITYLD QTTQKSLIAS VEKQLLGEHL TAILQKGLNS LLDENRIQDL SLLYQLFSRV
RGGVQVLLQQ WIEYIKAFGS TIVINPEKDK TMVQELLDFK DKVDHIIDTC FLKNEKFINA
MKEAFETFIN KRPNKPAELI AKYVDSKLRA GNKEATDEEL EKMLDKIMII FRFIYGKDVF
EAFYKKDLAK RLLVGKSASV DAEKSMLSKL KHECGAAFTS KLEGMFKDME LSKDIMIQFK
QYMQNQNVPG NIELTVNILT MGYWPTYVPM EVHLPPEMVK LQEIFKTFYL GKHSGRKLQW
QSTLGHCVLK AEFKEGKKEL QVSLFQTMVL LMFNEGEEFS LEEIKHATGI EDGELRRTLQ
SLACGKARVL AKNPKGKDIE DGDKFICNDD FKHKLFRIKI NQIQMKETVE EQASTTERVF
QDRQYQIDAA IVRIMKMRKT LSHNLLVSEV YNQLKFPVKP ADLKKRIESL IDRDYMERDK
ENPNQYNYIA
