KDM2B_HUMAN
ID KDM2B_HUMAN Reviewed; 1336 AA.
AC Q8NHM5; A8MRS1; Q1RLM7; Q8NCI2; Q96HC7; Q96SL0; Q96T03; Q9NS96; Q9UF75;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Lysine-specific demethylase 2B;
DE EC=1.14.11.27 {ECO:0000269|PubMed:16362057, ECO:0000269|PubMed:26237645};
DE AltName: Full=CXXC-type zinc finger protein 2;
DE AltName: Full=F-box and leucine-rich repeat protein 10;
DE AltName: Full=F-box protein FBL10;
DE AltName: Full=F-box/LRR-repeat protein 10;
DE AltName: Full=JmjC domain-containing histone demethylation protein 1B;
DE AltName: Full=Jumonji domain-containing EMSY-interactor methyltransferase motif protein;
DE Short=Protein JEMMA;
DE AltName: Full=Protein-containing CXXC domain 2;
DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1B;
GN Name=KDM2B;
GN Synonyms=CXXC2, FBL10, FBXL10, JHDM1B, NDY1 {ECO:0000303|PubMed:27568929},
GN PCCX2;
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] (ISOFORM 1).
RA Hughes-Davies L.;
RT "JEMMA (Jumonji domain, EMSY-interactor, methyltransferase motif) is a
RT novel protein which interacts with EMSY.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 504-1336 (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 710-1336 (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1336 (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 480-1336 (ISOFORM 2).
RC TISSUE=Fibroblast;
RA Fujino T., Hasegawa M., Shibata S., Kishimoto T., Imai S., Takano T.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16362057; DOI=10.1038/nature04433;
RA Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H.,
RA Tempst P., Zhang Y.;
RT "Histone demethylation by a family of JmjC domain-containing proteins.";
RL Nature 439:811-816(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN JMJC.
RX PubMed=17994099; DOI=10.1038/nature06255;
RA Frescas D., Guardavaccaro D., Bassermann F., Koyama-Nasu R., Pagano M.;
RT "JHDM1B/FBXL10 is a nucleolar protein that represses transcription of
RT ribosomal RNA genes.";
RL Nature 450:309-313(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-493; SER-975 AND SER-979, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; SER-477; THR-493 AND
RP SER-497, AND IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-474; SER-951;
RP SER-975; SER-979; SER-1018 AND SER-1031, AND IDENTIFICATION BY MASS
RP 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-890, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-890, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=26237645; DOI=10.1038/ncb3209;
RA Jiang Y., Qian X., Shen J., Wang Y., Li X., Liu R., Xia Y., Chen Q.,
RA Peng G., Lin S.Y., Lu Z.;
RT "Local generation of fumarate promotes DNA repair through inhibition of
RT histone H3 demethylation.";
RL Nat. Cell Biol. 17:1158-1168(2015).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-890, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-857 AND LYS-890, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21] {ECO:0007744|PDB:5JH5}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1059-1336, AND SUBUNIT.
RX PubMed=27568929; DOI=10.1016/j.str.2016.07.011;
RA Wong S.J., Gearhart M.D., Taylor A.B., Nanyes D.R., Ha D.J., Robinson A.K.,
RA Artigas J.A., Lee O.J., Demeler B., Hart P.J., Bardwell V.J., Kim C.A.;
RT "KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires
RT Cooperation between PCGF1 and BCORL1.";
RL Structure 24:1795-1801(2016).
RN [22] {ECO:0007744|PDB:6BVA}
RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 1060-1104 IN COMPLEX WITH SKP1
RP AND UBB, INTERACTION OF SKP1-KDM2B COMPLEX WITH UBB, AND MUTAGENESIS OF
RP VAL-1064; VAL-1069 AND ALA-1072.
RX PubMed=30033217; DOI=10.1016/j.str.2018.06.004;
RA Gorelik M., Manczyk N., Pavlenco A., Kurinov I., Sidhu S.S., Sicheri F.;
RT "A Structure-Based Strategy for Engineering Selective Ubiquitin Variant
RT Inhibitors of Skp1-Cul1-F-Box Ubiquitin Ligases.";
RL Structure 26:1226-1236.E3(2018).
RN [23] {ECO:0007744|PDB:4O64}
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 607-723, DOMAIN CXXC-TYPE
RP ZINC-FINGER, AND ZINC-BINDING.
RX PubMed=29276034; DOI=10.1016/j.str.2017.11.022;
RA Xu C., Liu K., Lei M., Yang A., Li Y., Hughes T.R., Min J.;
RT "DNA Sequence Recognition of Human CXXC Domains and Their Structural
RT Determinants.";
RL Structure 26:85-95.e3(2018).
CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of
CC histone H3, thereby playing a central role in histone code
CC (PubMed:16362057, PubMed:17994099, PubMed:26237645). Preferentially
CC demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36'
CC residue while it has weak or no activity for mono- and tri-methylated
CC H3 'Lys-36' (PubMed:16362057, PubMed:17994099, PubMed:26237645).
CC Preferentially binds the transcribed region of ribosomal RNA and
CC represses the transcription of ribosomal RNA genes which inhibits cell
CC growth and proliferation (PubMed:16362057, PubMed:17994099). May also
CC serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex (Probable).
CC {ECO:0000269|PubMed:16362057, ECO:0000269|PubMed:17994099,
CC ECO:0000269|PubMed:26237645, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC Evidence={ECO:0000269|PubMed:16362057, ECO:0000269|PubMed:26237645};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9Y2K7};
CC -!- ACTIVITY REGULATION: Histone demethylase activity is inhibited by
CC fumarate. {ECO:0000269|PubMed:26237645}.
CC -!- SUBUNIT: Interacts with SKP1, forming heterodimers (PubMed:27568929).
CC The heterodimeric KDM2B-SKP1 complex interacts with the PCGF1-BCORL1
CC heterodimeric complex to form a homotetrameric polycomb repression
CC complex 1 (PRC1.1) (PubMed:27568929). Directly interacts with CUL1. The
CC SKP1-KDM2B complex interacts with UBB (PubMed:30033217).
CC {ECO:0000269|PubMed:27568929, ECO:0000269|PubMed:30033217,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q8NHM5; Q6W2J9: BCOR; NbExp=5; IntAct=EBI-3955564, EBI-950027;
CC Q8NHM5; P63208: SKP1; NbExp=3; IntAct=EBI-3955564, EBI-307486;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17994099}.
CC Nucleus {ECO:0000269|PubMed:26237645}. Chromosome
CC {ECO:0000269|PubMed:26237645}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8NHM5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NHM5-2; Sequence=VSP_011340, VSP_011341;
CC Name=3;
CC IsoId=Q8NHM5-3; Sequence=VSP_017475, VSP_017476;
CC Name=4;
CC IsoId=Q8NHM5-4; Sequence=VSP_043146, VSP_043147, VSP_043148;
CC Name=5;
CC IsoId=Q8NHM5-5; Sequence=VSP_057394, VSP_057395, VSP_057396;
CC -!- DOMAIN: The LRR repeats are required for the interaction with the
CC PCGF1-BCORL1 heterodimeric complex. {ECO:0000269|PubMed:27568929}.
CC -!- DOMAIN: The JmjC domain mediates demethylation activity
CC (PubMed:17994099). It is also required for repression of ribosomal RNA
CC genes (PubMed:17994099). {ECO:0000269|PubMed:17994099}.
CC -!- DOMAIN: The CXXC zinc finger mediates binding to DNA containing
CC unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides.
CC {ECO:0000269|PubMed:29276034}.
CC -!- DOMAIN: The F-box domain mediates interaction with UBB.
CC {ECO:0000269|PubMed:30033217}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08735.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB55112.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB55301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC11159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ459424; CAD30700.1; -; mRNA.
DR EMBL; AK027440; BAB55112.1; ALT_INIT; mRNA.
DR EMBL; AK027692; BAB55301.1; ALT_INIT; mRNA.
DR EMBL; AK074718; BAC11159.1; ALT_INIT; mRNA.
DR EMBL; AK127328; BAG54483.1; -; mRNA.
DR EMBL; AC048337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC145422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC877509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008735; AAH08735.2; ALT_INIT; mRNA.
DR EMBL; BC115379; AAI15380.1; -; mRNA.
DR EMBL; AL133572; CAB63721.2; -; mRNA.
DR EMBL; AB031230; BAA97672.1; -; mRNA.
DR CCDS; CCDS41849.1; -. [Q8NHM5-4]
DR CCDS; CCDS41850.1; -. [Q8NHM5-1]
DR PIR; T43477; T43477.
DR RefSeq; NP_001005366.1; NM_001005366.1. [Q8NHM5-4]
DR RefSeq; NP_115979.3; NM_032590.4. [Q8NHM5-1]
DR PDB; 4O64; X-ray; 2.13 A; A/B/C=607-723.
DR PDB; 5JH5; X-ray; 2.55 A; A=1059-1336.
DR PDB; 6BVA; X-ray; 2.66 A; E/F=1060-1104.
DR PDBsum; 4O64; -.
DR PDBsum; 5JH5; -.
DR PDBsum; 6BVA; -.
DR AlphaFoldDB; Q8NHM5; -.
DR SMR; Q8NHM5; -.
DR BioGRID; 124197; 140.
DR CORUM; Q8NHM5; -.
DR IntAct; Q8NHM5; 86.
DR MINT; Q8NHM5; -.
DR STRING; 9606.ENSP00000366271; -.
DR BindingDB; Q8NHM5; -.
DR ChEMBL; CHEMBL3779760; -.
DR iPTMnet; Q8NHM5; -.
DR PhosphoSitePlus; Q8NHM5; -.
DR BioMuta; KDM2B; -.
DR DMDM; 51316032; -.
DR EPD; Q8NHM5; -.
DR jPOST; Q8NHM5; -.
DR MassIVE; Q8NHM5; -.
DR MaxQB; Q8NHM5; -.
DR PaxDb; Q8NHM5; -.
DR PeptideAtlas; Q8NHM5; -.
DR PRIDE; Q8NHM5; -.
DR ProteomicsDB; 61239; -.
DR ProteomicsDB; 73723; -. [Q8NHM5-1]
DR ProteomicsDB; 73724; -. [Q8NHM5-2]
DR ProteomicsDB; 73725; -. [Q8NHM5-3]
DR ProteomicsDB; 73726; -. [Q8NHM5-4]
DR Antibodypedia; 31579; 321 antibodies from 30 providers.
DR DNASU; 84678; -.
DR Ensembl; ENST00000377069.8; ENSP00000366269.3; ENSG00000089094.20. [Q8NHM5-4]
DR Ensembl; ENST00000377071.9; ENSP00000366271.3; ENSG00000089094.20. [Q8NHM5-1]
DR Ensembl; ENST00000611216.4; ENSP00000480847.1; ENSG00000089094.20. [Q8NHM5-5]
DR GeneID; 84678; -.
DR KEGG; hsa:84678; -.
DR MANE-Select; ENST00000377071.9; ENSP00000366271.3; NM_032590.5; NP_115979.3.
DR UCSC; uc058uhm.1; human. [Q8NHM5-1]
DR UCSC; uc058uhn.1; human.
DR CTD; 84678; -.
DR DisGeNET; 84678; -.
DR GeneCards; KDM2B; -.
DR HGNC; HGNC:13610; KDM2B.
DR HPA; ENSG00000089094; Low tissue specificity.
DR MIM; 609078; gene.
DR neXtProt; NX_Q8NHM5; -.
DR OpenTargets; ENSG00000089094; -.
DR PharmGKB; PA164721242; -.
DR VEuPathDB; HostDB:ENSG00000089094; -.
DR eggNOG; KOG1633; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000154717; -.
DR HOGENOM; CLU_003540_0_1_1; -.
DR InParanoid; Q8NHM5; -.
DR OMA; LWKRMNC; -.
DR OrthoDB; 324938at2759; -.
DR PhylomeDB; Q8NHM5; -.
DR TreeFam; TF106480; -.
DR BioCyc; MetaCyc:HS01631-MON; -.
DR PathwayCommons; Q8NHM5; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR SignaLink; Q8NHM5; -.
DR SIGNOR; Q8NHM5; -.
DR BioGRID-ORCS; 84678; 26 hits in 1134 CRISPR screens.
DR ChiTaRS; KDM2B; human.
DR GenomeRNAi; 84678; -.
DR Pharos; Q8NHM5; Tchem.
DR PRO; PR:Q8NHM5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8NHM5; protein.
DR Bgee; ENSG00000089094; Expressed in oviduct epithelium and 183 other tissues.
DR ExpressionAtlas; Q8NHM5; baseline and differential.
DR Genevisible; Q8NHM5; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045322; F:unmethylated CpG binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; ISS:BHF-UCL.
DR GO; GO:0030900; P:forebrain development; ISS:BHF-UCL.
DR GO; GO:0021592; P:fourth ventricle development; ISS:BHF-UCL.
DR GO; GO:0030902; P:hindbrain development; ISS:BHF-UCL.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR GO; GO:0070544; P:histone H3-K36 demethylation; IDA:UniProtKB.
DR GO; GO:0021993; P:initiation of neural tube closure; ISS:BHF-UCL.
DR GO; GO:0021670; P:lateral ventricle development; ISS:BHF-UCL.
DR GO; GO:0030901; P:midbrain development; ISS:BHF-UCL.
DR GO; GO:0021555; P:midbrain-hindbrain boundary morphogenesis; ISS:BHF-UCL.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; ISS:BHF-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISS:BHF-UCL.
DR GO; GO:0021678; P:third ventricle development; ISS:BHF-UCL.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002857; Znf_CXXC.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF16866; PHD_4; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00367; LRR_CC; 6.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW Coiled coil; Dioxygenase; DNA-binding; Iron; Isopeptide bond;
KW Leucine-rich repeat; Metal-binding; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW rRNA-binding; Transcription; Transcription regulation; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1336
FT /note="Lysine-specific demethylase 2B"
FT /id="PRO_0000119853"
FT DOMAIN 178..346
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT DOMAIN 1059..1105
FT /note="F-box"
FT REPEAT 1093..1120
FT /note="LRR 1"
FT REPEAT 1133..1154
FT /note="LRR 2"
FT REPEAT 1156..1182
FT /note="LRR 3"
FT REPEAT 1222..1247
FT /note="LRR 4"
FT REPEAT 1248..1277
FT /note="LRR 5"
FT REPEAT 1278..1302
FT /note="LRR 6"
FT REPEAT 1303..1336
FT /note="LRR 7"
FT ZN_FING 606..652
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034"
FT ZN_FING 659..725
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146,
FT ECO:0000269|PubMed:29276034"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 943..971
FT /evidence="ECO:0000255"
FT COMPBIAS 410..428
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4O64"
FT BINDING 616
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4O64"
FT BINDING 619
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4O64"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4O64"
FT BINDING 627
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4O64"
FT BINDING 630
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4O64"
FT BINDING 646
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4O64"
FT BINDING 651
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:4O64"
FT BINDING 665
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:4O64"
FT BINDING 688
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:4O64"
FT BINDING 691
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:4O64"
FT BINDING 696
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:4O64"
FT BINDING 699
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:4O64"
FT BINDING 719
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:4O64"
FT BINDING 722
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:4O64"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 493
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1018
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 857
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 890
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057394"
FT VAR_SEQ 1..42
FT /note="MAGPQMGGSAEDHPPRKRHAAEKQKKKTVIYTKCFEFESATQ -> MEAEKD
FT SGRRL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043146"
FT VAR_SEQ 654..676
FT /note="PVLPHTAVCLVCGEAGKEDTVEE -> TAIRSLISACPSSNAVETSVILT
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057395"
FT VAR_SEQ 677..1336
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057396"
FT VAR_SEQ 730
FT /note="K -> KAYK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_011340"
FT VAR_SEQ 818..855
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043147"
FT VAR_SEQ 856..868
FT /note="LKPGKEDKLFRKK -> Q (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_017475"
FT VAR_SEQ 1204
FT /note="G -> GPG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_017476"
FT VAR_SEQ 1277..1336
FT /note="DCNKVTDQCLSFFKRCGNICHIDLRYCKQVTKEGCEQFIAEMSVSVQFGQVE
FT EKLLQKLS -> ASLLGRVFGLQFWGICEPQARKNAGWA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_011341"
FT VAR_SEQ 1320..1336
FT /note="VSVQFGQVEEKLLQKLS -> SFQGRSCSTTRLGDE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043148"
FT MUTAGEN 1064
FT /note="V->W: Increased interaction with UBB."
FT /evidence="ECO:0000269|PubMed:30033217"
FT MUTAGEN 1069
FT /note="V->A: Decreased ininteraction with UBB."
FT /evidence="ECO:0000269|PubMed:30033217"
FT MUTAGEN 1072
FT /note="A->Y: Increased interaction with UBB."
FT /evidence="ECO:0000269|PubMed:30033217"
FT CONFLICT 864
FT /note="L -> F (in Ref. 6; BAC11159)"
FT /evidence="ECO:0000305"
FT CONFLICT 1226
FT /note="T -> R (in Ref. 6; BAC11159)"
FT /evidence="ECO:0000305"
FT CONFLICT 1295
FT /note="I -> T (in Ref. 6; BAC11159)"
FT /evidence="ECO:0000305"
FT CONFLICT 1334
FT /note="K -> R (in Ref. 6; BAC11159)"
FT /evidence="ECO:0000305"
FT HELIX 617..620
FT /evidence="ECO:0007829|PDB:4O64"
FT HELIX 628..632
FT /evidence="ECO:0007829|PDB:4O64"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:4O64"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:4O64"
FT TURN 663..665
FT /evidence="ECO:0007829|PDB:4O64"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:4O64"
FT HELIX 677..682
FT /evidence="ECO:0007829|PDB:4O64"
FT STRAND 686..688
FT /evidence="ECO:0007829|PDB:4O64"
FT TURN 689..691
FT /evidence="ECO:0007829|PDB:4O64"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:4O64"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:4O64"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:4O64"
FT TURN 720..722
FT /evidence="ECO:0007829|PDB:4O64"
FT HELIX 1067..1074
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1079..1086
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1092..1095
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1099..1102
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 1103..1106
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1115..1124
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 1127..1130
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1138..1147
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 1153..1155
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1161..1164
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1165..1168
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 1169..1171
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 1176..1179
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1188..1195
FT /evidence="ECO:0007829|PDB:5JH5"
FT TURN 1211..1214
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 1217..1219
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1227..1236
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 1242..1244
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1253..1259
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1265..1269
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 1272..1274
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1284..1289
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 1297..1299
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 1308..1318
FT /evidence="ECO:0007829|PDB:5JH5"
FT TURN 1319..1321
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 1331..1334
FT /evidence="ECO:0007829|PDB:5JH5"
SQ SEQUENCE 1336 AA; 152615 MW; 3A1A17B8EA9EA953 CRC64;
MAGPQMGGSA EDHPPRKRHA AEKQKKKTVI YTKCFEFESA TQRPIDRQRY DENEDLSDVE
EIVSVRGFSL EEKLRSQLYQ GDFVHAMEGK DFNYEYVQRE ALRVPLIFRE KDGLGIKMPD
PDFTVRDVKL LVGSRRLVDV MDVNTQKGTE MSMSQFVRYY ETPEAQRDKL YNVISLEFSH
TKLEHLVKRP TVVDLVDWVD NMWPQHLKEK QTEATNAIAE MKYPKVKKYC LMSVKGCFTD
FHIDFGGTSV WYHVFRGGKI FWLIPPTLHN LALYEEWVLS GKQSDIFLGD RVERCQRIEL
KQGYTFFIPS GWIHAVYTPV DSLVFGGNIL HSFNVPMQLR IYEIEDRTRV QPKFRYPFYY
EMCWYVLERY VYCVTQRSHL TQEYQRESML IDAPRKPSID GFSSDSWLEM EEEACDQQPQ
EEEEKDEEGE GRDRAPKPPT DGSTSPTSTP SEDQEALGKK PKAPALRFLK RTLSNESEES
VKSTTLAVDY PKTPTGSPAT EVSAKWTHLT EFELKGLKAL VEKLESLPEN KKCVPEGIED
PQALLEGVKN VLKEHADDDP SLAITGVPVV TWPKKTPKNR AVGRPKGKLG PASAVKLAAN
RTTAGARRRR TRCRKCEACL RTECGECHFC KDMKKFGGPG RMKQSCIMRQ CIAPVLPHTA
VCLVCGEAGK EDTVEEEEGK FNLMLMECSI CNEIIHPGCL KIKESEGVVN DELPNCWECP
KCNHAGKTGK QKRGPGFKYA SNLPGSLLKE QKMNRDNKEG QEPAKRRSEC EEAPRRRSDE
HSKKVPPDGL LRRKSDDVHL RKKRKYEKPQ ELSGRKRASS LQTSPGSSSH LSPRPPLGSS
LSPWWRSSLT YFQQQLKPGK EDKLFRKKRR SWKNAEDRMA LANKPLRRFK QEPEDELPEA
PPKTRESDHS RSSSPTAGPS TEGAEGPEEK KKVKMRRKRR LPNKELSREL SKELNHEIQR
TENSLANENQ QPIKSEPESE GEEPKRPPGI CERPHRFSKG LNGTPRELRH QLGPSLRSPP
RVISRPPPSV SPPKCIQMER HVIRPPPISP PPDSLPLDDG AAHVMHREVW MAVFSYLSHQ
DLCVCMRVCR TWNRWCCDKR LWTRIDLNHC KSITPLMLSG IIRRQPVSLD LSWTNISKKQ
LSWLINRLPG LRDLVLSGCS WIAVSALCSS SCPLLRTLDV QWVEGLKDAQ MRDLLSPPTD
NRPGQMDNRS KLRNIVELRL AGLDITDASL RLIIRHMPLL SKLHLSYCNH VTDQSINLLT
AVGTTTRDSL TEINLSDCNK VTDQCLSFFK RCGNICHIDL RYCKQVTKEG CEQFIAEMSV
SVQFGQVEEK LLQKLS
