ID MAFB_HUMAN Reviewed; 323 AA. AC Q9Y5Q3; B3KNE1; Q9H1F1; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2002, sequence version 2. DT 24-JAN-2024, entry version 184. DE RecName: Full=Transcription factor MafB; DE Short=Maf-B; DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog B; GN Name=MAFB; Synonyms=KRML; 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 [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Bone marrow; RX PubMed=10444328; DOI=10.1006/geno.1999.5884; RA Wang P.W., Eisenbart J.D., Cordes S.P., Barsh G.S., Stoffel M., RA Le Beau M.M.; RT "Human KRML (MAFB): cDNA cloning, genomic structure, and evaluation as a RT candidate tumor suppressor gene in myeloid leukemias."; RL Genomics 59:275-281(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 INTERACTION WITH LRP1. RX PubMed=15135046; DOI=10.1016/j.febslet.2004.03.069; RA Petersen H.H., Hilpert J., Jacobsen C., Lauwers A., Roebroek A.J.M., RA Willnow T.E.; RT "Low-density lipoprotein receptor-related protein interacts with MafB, a RT regulator of hindbrain development."; RL FEBS Lett. 565:23-27(2004). RN [7] RP PHOSPHORYLATION. RX PubMed=15963504; DOI=10.1016/j.febslet.2005.04.086; RA Sii-Felice K., Pouponnot C., Gillet S., Lecoin L., Girault J.-A., RA Eychene A., Felder-Schmittbuhl M.-P.; RT "MafA transcription factor is phosphorylated by p38 MAP kinase."; RL FEBS Lett. 579:3547-3554(2005). RN [8] RP PHOSPHORYLATION. RX PubMed=18042454; DOI=10.1016/j.molcel.2007.11.009; RA Rocques N., Abou Zeid N., Sii-Felice K., Lecoin L., RA Felder-Schmittbuhl M.-P., Eychene A., Pouponnot C.; RT "GSK-3-mediated phosphorylation enhances Maf-transforming activity."; RL Mol. Cell 28:584-597(2007). RN [9] RP REVIEW, AND FUNCTION. RX PubMed=19143053; DOI=10.1038/nrc2460; RA Eychene A., Rocques N., Pouponnot C.; RT "A new MAFia in cancer."; RL Nat. Rev. Cancer 8:683-693(2008). RN [10] RP INVOLVEMENT IN MCTO, AND VARIANTS MCTO LEU-54; LEU-59; PRO-62; ARG-63; RP CYS-66; LEU-69; ALA-70; LEU-70; SER-71 AND LEU-71. RX PubMed=22387013; DOI=10.1016/j.ajhg.2012.01.003; RA Zankl A., Duncan E.L., Leo P.J., Clark G.R., Glazov E.A., Addor M.C., RA Herlin T., Kim C.A., Leheup B.P., McGill J., McTaggart S., Mittas S., RA Mitchell A.L., Mortier G.R., Robertson S.P., Schroeder M., Terhal P., RA Brown M.A.; RT "Multicentric carpotarsal osteolysis is caused by mutations clustering in RT the amino-terminal transcriptional activation domain of MAFB."; RL Am. J. Hum. Genet. 90:494-501(2012). RN [11] RP INVOLVEMENT IN DURS3, AND FUNCTION. RX PubMed=27181683; DOI=10.1016/j.ajhg.2016.03.023; RA Park J.G., Tischfield M.A., Nugent A.A., Cheng L., Di Gioia S.A., RA Chan W.M., Maconachie G., Bosley T.M., Summers C.G., Hunter D.G., RA Robson C.D., Gottlob I., Engle E.C.; RT "Loss of MAFB function in humans and mice causes Duane syndrome, aberrant RT extraocular muscle innervation, and inner-ear defects."; RL Am. J. Hum. Genet. 98:1220-1227(2016). CC -!- FUNCTION: Acts as a transcriptional activator or repressor CC (PubMed:27181683). Plays a pivotal role in regulating lineage-specific CC hematopoiesis by repressing ETS1-mediated transcription of erythroid- CC specific genes in myeloid cells. Required for monocytic, macrophage, CC osteoclast, podocyte and islet beta cell differentiation. Involved in CC renal tubule survival and F4/80 maturation. Activates the insulin and CC glucagon promoters. Together with PAX6, transactivates weakly the CC glucagon gene promoter through the G1 element. SUMO modification CC controls its transcriptional activity and ability to specify macrophage CC fate. Binds element G1 on the glucagon promoter (By similarity). CC Involved either as an oncogene or as a tumor suppressor, depending on CC the cell context. Required for the transcriptional activation of HOXB3 CC in the rhombomere r5 in the hindbrain (By similarity). CC {ECO:0000250|UniProtKB:P54841, ECO:0000269|PubMed:19143053, CC ECO:0000269|PubMed:27181683}. CC -!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip transcription CC factors. Binds DNA as a homodimer or a heterodimer. Forms homodimers CC and heterodimers with FOS, FOSB and FOSL2, but not with JUN proteins CC (JUN, JUNB and JUND). Interacts with PAX6; the interaction is direct. CC Interacts with ETS1 and LRP1 (By similarity). Interacts with the CC intracellular cytoplasmic domain of LRP1 (LRPICD); the interaction CC results in a moderate reduction of MAFB transcriptional potential. CC {ECO:0000250, ECO:0000269|PubMed:15135046}. CC -!- INTERACTION: CC Q9Y5Q3; O14867: BACH1; NbExp=3; IntAct=EBI-3649340, EBI-1263541; CC Q9Y5Q3; P01100: FOS; NbExp=2; IntAct=EBI-3649340, EBI-852851; CC Q9Y5Q3; Q14653: IRF3; NbExp=4; IntAct=EBI-3649340, EBI-2650369; CC Q9Y5Q3; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-3649340, EBI-10172511; CC Q9Y5Q3; O75444: MAF; NbExp=4; IntAct=EBI-3649340, EBI-2805091; CC Q9Y5Q3; Q9Y5Q3: MAFB; NbExp=3; IntAct=EBI-3649340, EBI-3649340; CC Q9Y5Q3; P0C746: HBZ; Xeno; NbExp=3; IntAct=EBI-3649340, EBI-10890294; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10444328}. CC -!- DOMAIN: The leucine-zipper domain is involved in the interaction with CC LRPICD. CC -!- PTM: Phosphorylated by GSK3 and MAPK13 on serine and threonine CC residues. {ECO:0000305|PubMed:15963504, ECO:0000305|PubMed:18042454}. CC -!- PTM: Sumoylated. Sumoylation on Lys-32 and Lys-297 stimulates its CC transcriptional repression activity and promotes macrophage CC differentiation from myeloid progenitors (By similarity). CC {ECO:0000250}. CC -!- DISEASE: Multicentric carpotarsal osteolysis syndrome (MCTO) CC [MIM:166300]: A rare skeletal disorder, usually presenting in early CC childhood with a clinical picture mimicking juvenile rheumatoid CC arthritis. Progressive destruction of the carpal and tarsal bone CC usually occurs and other bones may also be involved. Chronic renal CC failure is a frequent component of the syndrome. Intellectual CC disability and minor facial anomalies have been noted in some patients. CC {ECO:0000269|PubMed:22387013}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Duane retraction syndrome 3 with or without deafness (DURS3) CC [MIM:617041]: A form of Duane retraction syndrome, a congenital eye CC movement disorder characterized by a failure of cranial nerve VI (the CC abducens nerve) to develop normally, resulting in restriction or CC absence of abduction, adduction or both, narrowing of the palpebral CC fissure, and retraction of the globe on attempted adduction. CC Undiagnosed in children, it can lead to amblyopia, a permanent CC uncorrectable loss of vision. Some DURS3 patients manifest CC sensorineural hearing loss. {ECO:0000269|PubMed:27181683}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF134157; AAD30106.1; -; mRNA. DR EMBL; AK027324; BAG51303.1; -; mRNA. DR EMBL; AL035665; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW76000.1; -; Genomic_DNA. DR EMBL; BC028098; AAH28098.1; -; mRNA. DR EMBL; BC036689; AAH36689.1; -; mRNA. DR CCDS; CCDS13311.1; -. DR RefSeq; NP_005452.2; NM_005461.4. DR AlphaFoldDB; Q9Y5Q3; -. DR SMR; Q9Y5Q3; -. DR BioGRID; 115261; 271. DR ComplexPortal; CPX-2479; bZIP transcription factor complex, BACH2-MAFB. DR ComplexPortal; CPX-2497; bZIP transcription factor complex, BACH1-MAFB. DR ComplexPortal; CPX-6567; bZIP transcription factor complex, ATF4-MAFB. DR ELM; Q9Y5Q3; -. DR IntAct; Q9Y5Q3; 18. DR MINT; Q9Y5Q3; -. DR STRING; 9606.ENSP00000362410; -. DR iPTMnet; Q9Y5Q3; -. DR PhosphoSitePlus; Q9Y5Q3; -. DR BioMuta; MAFB; -. DR DMDM; 21759268; -. DR EPD; Q9Y5Q3; -. DR MassIVE; Q9Y5Q3; -. DR PaxDb; 9606-ENSP00000362410; -. DR PeptideAtlas; Q9Y5Q3; -. DR ProteomicsDB; 86471; -. DR Pumba; Q9Y5Q3; -. DR Antibodypedia; 956; 366 antibodies from 33 providers. DR DNASU; 9935; -. DR Ensembl; ENST00000373313.3; ENSP00000362410.2; ENSG00000204103.4. DR GeneID; 9935; -. DR KEGG; hsa:9935; -. DR MANE-Select; ENST00000373313.3; ENSP00000362410.2; NM_005461.5; NP_005452.2. DR UCSC; uc002xji.4; human. DR AGR; HGNC:6408; -. DR CTD; 9935; -. DR DisGeNET; 9935; -. DR GeneCards; MAFB; -. DR GeneReviews; MAFB; -. DR HGNC; HGNC:6408; MAFB. DR HPA; ENSG00000204103; Tissue enhanced (parathyroid). DR MalaCards; MAFB; -. DR MIM; 166300; phenotype. DR MIM; 608968; gene. DR MIM; 617041; phenotype. DR neXtProt; NX_Q9Y5Q3; -. DR OpenTargets; ENSG00000204103; -. DR Orphanet; 233; Duane retraction syndrome. DR Orphanet; 529574; Duane retraction syndrome with congenital deafness. DR Orphanet; 2774; Multicentric carpo-tarsal osteolysis with or without nephropathy. DR PharmGKB; PA30535; -. DR VEuPathDB; HostDB:ENSG00000204103; -. DR eggNOG; KOG4196; Eukaryota. DR GeneTree; ENSGT00940000160486; -. DR HOGENOM; CLU_063062_0_0_1; -. DR InParanoid; Q9Y5Q3; -. DR OMA; PTEQKHH; -. DR OrthoDB; 5399309at2759; -. DR PhylomeDB; Q9Y5Q3; -. DR TreeFam; TF325689; -. DR PathwayCommons; Q9Y5Q3; -. DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis. DR SignaLink; Q9Y5Q3; -. DR SIGNOR; Q9Y5Q3; -. DR BioGRID-ORCS; 9935; 17 hits in 1176 CRISPR screens. DR ChiTaRS; MAFB; human. DR GeneWiki; MAFB_(gene); -. DR GenomeRNAi; 9935; -. DR Pharos; Q9Y5Q3; Tbio. DR PRO; PR:Q9Y5Q3; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9Y5Q3; Protein. DR Bgee; ENSG00000204103; Expressed in renal glomerulus and 199 other cell types or tissues. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB. DR GO; GO:0021599; P:abducens nerve formation; ISS:UniProtKB. DR GO; GO:0035284; P:brain segmentation; IEA:Ensembl. DR GO; GO:1903575; P:cornified envelope assembly; IEA:Ensembl. DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB. DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl. DR GO; GO:0140467; P:integrated stress response signaling; NAS:ComplexPortal. DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl. DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IDA:UniProtKB. DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0016485; P:protein processing; IEA:Ensembl. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IBA:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:Ensembl. DR GO; GO:0021571; P:rhombomere 5 development; IEA:Ensembl. DR GO; GO:0021572; P:rhombomere 6 development; IEA:Ensembl. DR GO; GO:0007379; P:segment specification; IEA:Ensembl. DR GO; GO:0007423; P:sensory organ development; TAS:ProtInc. DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl. DR GO; GO:0048538; P:thymus development; IEA:Ensembl. DR CDD; cd14718; bZIP_Maf_large; 1. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR004826; bZIP_Maf. DR InterPro; IPR046347; bZIP_sf. DR InterPro; IPR013592; Maf_TF_N. DR InterPro; IPR008917; TF_DNA-bd_sf. DR InterPro; IPR024874; Transcription_factor_Maf_fam. DR PANTHER; PTHR10129; TRANSCRIPTION FACTOR MAF; 1. DR PANTHER; PTHR10129:SF10; TRANSCRIPTION FACTOR MAFB; 1. DR Pfam; PF03131; bZIP_Maf; 1. DR Pfam; PF08383; Maf_N; 1. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR Genevisible; Q9Y5Q3; HS. PE 1: Evidence at protein level; KW Activator; Disease variant; DNA-binding; Isopeptide bond; Nucleus; KW Proto-oncogene; Reference proteome; Repressor; Transcription; KW Transcription regulation; Tumor suppressor; Ubl conjugation. FT CHAIN 1..323 FT /note="Transcription factor MafB" FT /id="PRO_0000076494" FT DOMAIN 238..301 FT /note="bZIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 34..78 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 116..210 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 238..263 FT /note="Basic motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 266..287 FT /note="Leucine-zipper" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT COMPBIAS 50..78 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 129..143 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CROSSLNK 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT CROSSLNK 297 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT VARIANT 54 FT /note="S -> L (in MCTO; dbSNP:rs730880014)" FT /evidence="ECO:0000269|PubMed:22387013" FT /id="VAR_067979" FT VARIANT 59 FT /note="P -> L (in MCTO)" FT /evidence="ECO:0000269|PubMed:22387013" FT /id="VAR_067980" FT VARIANT 62 FT /note="T -> P (in MCTO; dbSNP:rs387907004)" FT /evidence="ECO:0000269|PubMed:22387013" FT /id="VAR_067981" FT VARIANT 63 FT /note="P -> R (in MCTO)" FT /evidence="ECO:0000269|PubMed:22387013" FT /id="VAR_067982" FT VARIANT 66 FT /note="S -> C (in MCTO)" FT /evidence="ECO:0000269|PubMed:22387013" FT /id="VAR_067983" FT VARIANT 69 FT /note="S -> L (in MCTO; dbSNP:rs1555826433)" FT /evidence="ECO:0000269|PubMed:22387013" FT /id="VAR_067984" FT VARIANT 70 FT /note="S -> A (in MCTO; dbSNP:rs387907005)" FT /evidence="ECO:0000269|PubMed:22387013" FT /id="VAR_067985" FT VARIANT 70 FT /note="S -> L (in MCTO; dbSNP:rs387907006)" FT /evidence="ECO:0000269|PubMed:22387013" FT /id="VAR_067986" FT VARIANT 71 FT /note="P -> L (in MCTO; dbSNP:rs387907008)" FT /evidence="ECO:0000269|PubMed:22387013" FT /id="VAR_067987" FT VARIANT 71 FT /note="P -> S (in MCTO; dbSNP:rs387907007)" FT /evidence="ECO:0000269|PubMed:22387013" FT /id="VAR_067988" FT CONFLICT 52 FT /note="A -> V (in Ref. 1; AAD30106)" FT /evidence="ECO:0000305" FT CONFLICT 241 FT /note="Q -> H (in Ref. 1; AAD30106)" FT /evidence="ECO:0000305" SQ SEQUENCE 323 AA; 35792 MW; A0F3C09F8936CB16 CRC64; MAAELSMGPE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ PAGSVSSTPL STPCSSVPSS PSFSPTEQKT HLEDLYWMAS NYQQMNPEAL NLTPEDAVEA LIGSHPVPQP LQSFDSFRGA HHHHHHHHPH PHHAYPGAGV AHDELGPHAH PHHHHHHQAS PPPSSAASPA QQLPTSHPGP GPHATASATA AGGNGSVEDR FSDDQLVSMS VRELNRHLRG FTKDEVIRLK QKRRTLKNRG YAQSCRYKRV QQKHHLENEK TQLIQQVEQL KQEVSRLARE RDAYKVKCEK LANSGFREAG STSDSPSSPE FFL //