RB12B_HUMAN
ID RB12B_HUMAN Reviewed; 1001 AA.
AC Q8IXT5; A8MYB5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=RNA-binding protein 12B;
DE AltName: Full=RNA-binding motif protein 12B;
GN Name=RBM12B;
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=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-276; SER-278 AND SER-280, AND
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-319, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250; SER-254; SER-278 AND
RP SER-638, AND 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278; SER-280; SER-638 AND
RP THR-640, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-101; SER-278;
RP SER-280; SER-292; SER-294; SER-377; SER-575 AND SER-591, AND IDENTIFICATION
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-575; SER-710 AND
RP SER-718, AND 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-151, 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-151, 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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-151, 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-151; LYS-335; LYS-514;
RP LYS-541 AND LYS-895, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- INTERACTION:
CC Q8IXT5; O00555: CACNA1A; NbExp=2; IntAct=EBI-3044077, EBI-766279;
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DR EMBL; AC010834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS43755.1; -.
DR RefSeq; NP_976324.2; NM_203390.2.
DR RefSeq; XP_005250972.1; XM_005250915.4.
DR RefSeq; XP_011515329.1; XM_011517027.2.
DR RefSeq; XP_011515330.1; XM_011517028.2.
DR RefSeq; XP_011515331.1; XM_011517029.2.
DR RefSeq; XP_016868895.1; XM_017013406.1.
DR RefSeq; XP_016868896.1; XM_017013407.1.
DR RefSeq; XP_016868897.1; XM_017013408.1.
DR AlphaFoldDB; Q8IXT5; -.
DR BioGRID; 133227; 75.
DR IntAct; Q8IXT5; 20.
DR STRING; 9606.ENSP00000382239; -.
DR GlyGen; Q8IXT5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IXT5; -.
DR PhosphoSitePlus; Q8IXT5; -.
DR BioMuta; RBM12B; -.
DR DMDM; 215273872; -.
DR EPD; Q8IXT5; -.
DR jPOST; Q8IXT5; -.
DR MassIVE; Q8IXT5; -.
DR MaxQB; Q8IXT5; -.
DR PaxDb; Q8IXT5; -.
DR PeptideAtlas; Q8IXT5; -.
DR PRIDE; Q8IXT5; -.
DR ProteomicsDB; 71064; -.
DR Antibodypedia; 6688; 53 antibodies from 18 providers.
DR DNASU; 389677; -.
DR Ensembl; ENST00000399300.7; ENSP00000382239.2; ENSG00000183808.12.
DR Ensembl; ENST00000517700.6; ENSP00000427729.2; ENSG00000183808.12.
DR Ensembl; ENST00000518597.2; ENSP00000428269.2; ENSG00000183808.12.
DR Ensembl; ENST00000519109.6; ENSP00000430474.2; ENSG00000183808.12.
DR Ensembl; ENST00000520560.6; ENSP00000429807.2; ENSG00000183808.12.
DR GeneID; 389677; -.
DR KEGG; hsa:389677; -.
DR MANE-Select; ENST00000520560.6; ENSP00000429807.2; NM_001377960.1; NP_001364889.1.
DR UCSC; uc003yfz.5; human.
DR CTD; 389677; -.
DR DisGeNET; 389677; -.
DR GeneCards; RBM12B; -.
DR HGNC; HGNC:32310; RBM12B.
DR HPA; ENSG00000183808; Low tissue specificity.
DR neXtProt; NX_Q8IXT5; -.
DR OpenTargets; ENSG00000183808; -.
DR PharmGKB; PA142671098; -.
DR VEuPathDB; HostDB:ENSG00000183808; -.
DR eggNOG; KOG4307; Eukaryota.
DR GeneTree; ENSGT00940000158322; -.
DR InParanoid; Q8IXT5; -.
DR OMA; DRDDHSH; -.
DR OrthoDB; 249376at2759; -.
DR PhylomeDB; Q8IXT5; -.
DR TreeFam; TF331899; -.
DR PathwayCommons; Q8IXT5; -.
DR SignaLink; Q8IXT5; -.
DR BioGRID-ORCS; 389677; 22 hits in 1075 CRISPR screens.
DR ChiTaRS; RBM12B; human.
DR GenomeRNAi; 389677; -.
DR Pharos; Q8IXT5; Tdark.
DR PRO; PR:Q8IXT5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8IXT5; protein.
DR Bgee; ENSG00000183808; Expressed in calcaneal tendon and 192 other tissues.
DR ExpressionAtlas; Q8IXT5; baseline and differential.
DR Genevisible; Q8IXT5; HS.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR CDD; cd12746; RRM2_RBM12B; 1.
DR CDD; cd12513; RRM3_RBM12B; 1.
DR Gene3D; 3.30.70.330; -; 5.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034588; RBM12B_RRM2.
DR InterPro; IPR034858; RBM12B_RRM3.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 5.
DR SUPFAM; SSF54928; SSF54928; 4.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..1001
FT /note="RNA-binding protein 12B"
FT /id="PRO_0000273366"
FT DOMAIN 155..230
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 284..360
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 400..477
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 925..1001
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 119..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 640
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 151
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 CROSSLNK 335
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 514
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 895
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 250
FT /note="S -> F (in dbSNP:rs17853906)"
FT /id="VAR_047291"
FT VARIANT 605
FT /note="R -> C (in dbSNP:rs17857188)"
FT /id="VAR_047292"
FT VARIANT 864
FT /note="N -> H (in dbSNP:rs16916188)"
FT /id="VAR_052219"
SQ SEQUENCE 1001 AA; 118103 MW; A09C527B1A1EE845 CRC64;
MAVVIRLLGL PFIAGPVDIR HFFTGLTIPD GGVHIIGGEI GEAFIIFATD EDARRAISRS
GGFIKDSSVE LFLSSKAEMQ KTIEMKRTDR VGRGRPGSGT SGVDSLSNFI ESVKEEASNS
GYGSSINQDA GFHTNGTGHG NLRPRKTRPL KAENPYLFLR GLPYLVNEDD VRVFFSGLCV
DGVIFLKHHD GRNNGDAIVK FASCVDASGG LKCHRSFMGS RFIEVMQGSE QQWIEFGGNA
VKEGDVLRRS EEHSPPRGIN DRHFRKRSHS KSPRRTRSRS PLGFYVHLKN LSLSIDERDL
RNFFRGTDLT DEQIRFLYKD ENRTRYAFVM FKTLKDYNTA LSLHKTVLQY RPVHIDPISR
KQMLKFIARY EKKRSGSLER DRPGHVSQKY SQEGNSGQKL CIYIRNFPFD VTKVEVQKFF
ADFLLAEDDI YLLYDDKGVG LGEALVKFKS EEQAMKAERL NRRRFLGTEV LLRLISEAQI
QEFGVNFSVM SSEKMQARSQ SRERGDHSHL FDSKDPPIYS VGAFENFRHQ LEDLRQLDNF
KHPQRDFRQP DRHPPEDFRH SSEDFRFPPE DFRHSPEDFR RPREEDFRRP SEEDFRRPWE
EDFRRPPEDD FRHPREEDWR RPLEEDWRRP LEEDFRRSPT EDFRQLPEED FRQPPEEDLR
WLPEEDFRRP PEEDWRRPPE EDFRRPLQGE WRRPPEDDFR RPPEEDFRHS PEEDFRQSPQ
EHFRRPPQEH FRRPPPEHFR RPPPEHFRRP PPEHFRRPPP EHFRRPPPEH FRRPPPEHFR
RPPQEHFRRP PQEHFRRSRE EDFRHPPDED FRGPPDEDFR HPPDEDFRSP QEEDFRCPSD
EDFRQLPEED LREAPEEDPR LPDNFRPPGE DFRSPPDDFR SHRPFVNFGR PEGGKFDFGK
HNMGSFPEGR FMPDPKINCG SGRVTPIKIM NLPFKANVNE ILDFFHGYRI IPDSVSIQYN
EQGLPTGEAI VAMINYNEAM AAIKDLNDRP VGPRKVKLTL L
