PIMRE_HUMAN
ID PIMRE_HUMAN Reviewed; 248 AA.
AC Q9BSJ6; Q96CT4; Q9NVV1; Q9NWB5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein PIMREG {ECO:0000305};
DE AltName: Full=CALM-interactor expressed in thymus and spleen {ECO:0000303|PubMed:19383357, ECO:0000303|PubMed:23419774};
DE AltName: Full=PICALM-interacting mitotic regulator {ECO:0000312|HGNC:HGNC:25483};
DE AltName: Full=Regulator of chromosome segregation protein 1 {ECO:0000303|PubMed:18757745};
GN Name=PIMREG {ECO:0000312|HGNC:HGNC:25483};
GN Synonyms=CATS {ECO:0000303|PubMed:19383357, ECO:0000303|PubMed:23419774},
GN FAM64A {ECO:0000312|HGNC:HGNC:25483}, RCS1 {ECO:0000303|PubMed:18757745};
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 MRNA] (ISOFORMS 1 AND 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Lung;
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 [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH PICALM, TISSUE SPECIFICITY, AND
RP IDENTIFICATION OF ISOFORMS 1 AND 2.
RX PubMed=16491119; DOI=10.1038/sj.onc.1209438;
RA Archangelo L.F., Glaesner J., Krause A., Bohlander S.K.;
RT "The novel CALM interactor CATS influences the subcellular localization of
RT the leukemogenic fusion protein CALM/AF10.";
RL Oncogene 25:4099-4109(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=19383357; DOI=10.1016/j.molonc.2008.08.001;
RA Archangelo L.F., Greif P.A., Hoelzel M., Harasim T., Kremmer E.,
RA Przemeck G.K., Eick D., Deshpande A.J., Buske C., de Angelis M.H.,
RA Saad S.T., Bohlander S.K.;
RT "The CALM and CALM/AF10 interactor CATS is a marker for proliferation.";
RL Mol. Oncol. 2:356-367(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-199 AND SER-201, 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 [8]
RP FUNCTION IN MITOSIS PROGRESSION, INTERACTION WITH NURD COMPLEX,
RP DEVELOPMENTAL STAGE, D-BOX MOTIF, MUTAGENESIS OF 14-ARG--LEU-17 AND
RP 53-ARG--LEU-56, AND UBIQUITINATION.
RX PubMed=18757745; DOI=10.1073/pnas.0709227105;
RA Zhao W.M., Coppinger J.A., Seki A., Cheng X.L., Yates J.R. III, Fang G.;
RT "RCS1, a substrate of APC/C, controls the metaphase to anaphase
RT transition.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13415-13420(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-129 AND SER-131, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-131, AND MUTAGENESIS OF
RP SER-129 AND SER-131.
RX PubMed=23419774; DOI=10.1016/j.bbamcr.2013.02.004;
RA Archangelo L.F., Greif P.A., Maucuer A., Manceau V., Koneru N.,
RA Bigarella C.L., Niemann F., Dos Santos M.T., Kobarg J., Bohlander S.K.,
RA Saad S.T.;
RT "The CATS (FAM64A) protein is a substrate of the kinase interacting
RT stathmin (KIS).";
RL Biochim. Biophys. Acta 1833:1269-1279(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: During mitosis, may play a role in the control of metaphase-
CC to-anaphase transition. {ECO:0000269|PubMed:18757745}.
CC -!- SUBUNIT: Isoform 1 and isoform 2 interact with PICALM; this interaction
CC may target PICALM to the nucleus (PubMed:16491119). During mitosis,
CC associates with HDAC2 and MTA2 subunits of the chromatin-remodeling
CC NuRD complex; this association is strongest at prometaphase and
CC decreases as the cell progresses through metaphase and anaphase
CC (PubMed:18757745). {ECO:0000269|PubMed:16491119,
CC ECO:0000269|PubMed:18757745}.
CC -!- INTERACTION:
CC Q9BSJ6; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-2568609, EBI-741181;
CC Q9BSJ6; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-2568609, EBI-11522760;
CC Q9BSJ6; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-2568609, EBI-742909;
CC Q9BSJ6; Q7L4P6: BEND5; NbExp=3; IntAct=EBI-2568609, EBI-724373;
CC Q9BSJ6; O95273: CCNDBP1; NbExp=6; IntAct=EBI-2568609, EBI-748961;
CC Q9BSJ6; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-2568609, EBI-739624;
CC Q9BSJ6; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-2568609, EBI-11522780;
CC Q9BSJ6; P67870: CSNK2B; NbExp=3; IntAct=EBI-2568609, EBI-348169;
CC Q9BSJ6; Q8NF50: DOCK8; NbExp=3; IntAct=EBI-2568609, EBI-2548605;
CC Q9BSJ6; P50402: EMD; NbExp=3; IntAct=EBI-2568609, EBI-489887;
CC Q9BSJ6; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2568609, EBI-618309;
CC Q9BSJ6; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-2568609, EBI-10961706;
CC Q9BSJ6; Q6A162: KRT40; NbExp=6; IntAct=EBI-2568609, EBI-10171697;
CC Q9BSJ6; Q969L2: MAL2; NbExp=3; IntAct=EBI-2568609, EBI-944295;
CC Q9BSJ6; P04156: PRNP; NbExp=5; IntAct=EBI-2568609, EBI-977302;
CC Q9BSJ6; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-2568609, EBI-726876;
CC Q9BSJ6; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-2568609, EBI-11522811;
CC Q9BSJ6; Q96R06: SPAG5; NbExp=3; IntAct=EBI-2568609, EBI-413317;
CC Q9BSJ6; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-2568609, EBI-2212028;
CC Q9BSJ6; Q12800: TFCP2; NbExp=3; IntAct=EBI-2568609, EBI-717422;
CC Q9BSJ6; P14373: TRIM27; NbExp=9; IntAct=EBI-2568609, EBI-719493;
CC Q9BSJ6; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-2568609, EBI-2799833;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16491119,
CC ECO:0000269|PubMed:19383357}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:19383357}. Note=Partially localizes to the
CC nucleolus. {ECO:0000269|PubMed:19383357}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BSJ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BSJ6-2; Sequence=VSP_023997;
CC -!- TISSUE SPECIFICITY: Expressed in thymus (at protein level). Detected in
CC spleen, colon, ovary and small intestines.
CC {ECO:0000269|PubMed:16491119, ECO:0000269|PubMed:19383357}.
CC -!- DEVELOPMENTAL STAGE: Regulated in a cell-cycle dependent manner, with
CC lowest levels in quiescent cells or at G1 phase. Progressive up-
CC regulation starting at S phase and peaking at G2 and G2/M phases,
CC followed by a drastic drop as cells exit mitosis (at protein level).
CC {ECO:0000269|PubMed:18757745}.
CC -!- DOMAIN: The N-terminal destruction box 2 (D-box 2) is required for
CC APC/C ubiquitination and proteasomal degradation.
CC {ECO:0000269|PubMed:18757745}.
CC -!- PTM: Ubiquitinated by the anaphase-promoting complex/cyclosome (APC/C)
CC complex in the presence of FZR1, leading to its degradation by the
CC proteasome during mitotic exit. However, degradation is not essential
CC for normal mitotic progression within a single cell cycle.
CC {ECO:0000269|PubMed:18757745}.
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DR EMBL; AK001018; BAA91468.1; -; mRNA.
DR EMBL; AK001353; BAA91644.1; -; mRNA.
DR EMBL; AC055872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005004; AAH05004.1; -; mRNA.
DR EMBL; BC013966; AAH13966.1; -; mRNA.
DR CCDS; CCDS32541.1; -. [Q9BSJ6-2]
DR CCDS; CCDS56016.1; -. [Q9BSJ6-1]
DR RefSeq; NP_001182157.1; NM_001195228.1. [Q9BSJ6-1]
DR RefSeq; NP_061886.2; NM_019013.2. [Q9BSJ6-2]
DR AlphaFoldDB; Q9BSJ6; -.
DR BioGRID; 119983; 40.
DR DIP; DIP-56370N; -.
DR IntAct; Q9BSJ6; 29.
DR MINT; Q9BSJ6; -.
DR STRING; 9606.ENSP00000250056; -.
DR GlyGen; Q9BSJ6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BSJ6; -.
DR PhosphoSitePlus; Q9BSJ6; -.
DR BioMuta; PIMREG; -.
DR DMDM; 74733018; -.
DR EPD; Q9BSJ6; -.
DR jPOST; Q9BSJ6; -.
DR MassIVE; Q9BSJ6; -.
DR MaxQB; Q9BSJ6; -.
DR PaxDb; Q9BSJ6; -.
DR PeptideAtlas; Q9BSJ6; -.
DR PRIDE; Q9BSJ6; -.
DR ProteomicsDB; 78904; -. [Q9BSJ6-1]
DR ProteomicsDB; 78905; -. [Q9BSJ6-2]
DR Antibodypedia; 42756; 76 antibodies from 15 providers.
DR DNASU; 54478; -.
DR Ensembl; ENST00000250056.12; ENSP00000250056.8; ENSG00000129195.16. [Q9BSJ6-1]
DR Ensembl; ENST00000572447.6; ENSP00000459235.1; ENSG00000129195.16. [Q9BSJ6-2]
DR Ensembl; ENST00000576056.5; ENSP00000458534.1; ENSG00000129195.16. [Q9BSJ6-2]
DR GeneID; 54478; -.
DR KEGG; hsa:54478; -.
DR MANE-Select; ENST00000572447.6; ENSP00000459235.1; NM_019013.3; NP_061886.2. [Q9BSJ6-2]
DR UCSC; uc002gcu.3; human. [Q9BSJ6-1]
DR CTD; 54478; -.
DR DisGeNET; 54478; -.
DR GeneCards; PIMREG; -.
DR HGNC; HGNC:25483; PIMREG.
DR HPA; ENSG00000129195; Tissue enhanced (lymphoid).
DR MIM; 617611; gene.
DR neXtProt; NX_Q9BSJ6; -.
DR OpenTargets; ENSG00000129195; -.
DR PharmGKB; PA142671874; -.
DR VEuPathDB; HostDB:ENSG00000129195; -.
DR eggNOG; ENOG502S0SN; Eukaryota.
DR GeneTree; ENSGT00390000008128; -.
DR HOGENOM; CLU_1209428_0_0_1; -.
DR InParanoid; Q9BSJ6; -.
DR OMA; QMGPHAH; -.
DR PhylomeDB; Q9BSJ6; -.
DR TreeFam; TF336322; -.
DR PathwayCommons; Q9BSJ6; -.
DR SignaLink; Q9BSJ6; -.
DR SIGNOR; Q9BSJ6; -.
DR BioGRID-ORCS; 54478; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; FAM64A; human.
DR GenomeRNAi; 54478; -.
DR Pharos; Q9BSJ6; Tbio.
DR PRO; PR:Q9BSJ6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BSJ6; protein.
DR Bgee; ENSG00000129195; Expressed in ventricular zone and 108 other tissues.
DR ExpressionAtlas; Q9BSJ6; baseline and differential.
DR Genevisible; Q9BSJ6; HS.
DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR InterPro; IPR009932; RCS1.
DR PANTHER; PTHR35819; PTHR35819; 1.
DR Pfam; PF07326; RCS1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..248
FT /note="Protein PIMREG"
FT /id="PRO_0000281159"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..17
FT /note="D-box 1"
FT MOTIF 53..56
FT /note="D-box 2"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 16
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 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 131
FT /note="Phosphoserine; by UHMK1; in vitro"
FT /evidence="ECO:0000269|PubMed:23419774,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 229..248
FT /note="RKQALSDRQGFILKDVYASP -> SGDIVSLIHD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023997"
FT VARIANT 199
FT /note="S -> C (in dbSNP:rs16955870)"
FT /id="VAR_056873"
FT MUTAGEN 14..17
FT /note="RRSL->ARSA: Weak reduction in ubiquitination.
FT Complete loss of ubiquitination; when associated with 53-
FT A--A-56."
FT /evidence="ECO:0000269|PubMed:18757745"
FT MUTAGEN 53..56
FT /note="RLPL->ALPA: Great reduction in ubiquitination.
FT Complete loss of ubiquitination; when associated with 14-
FT A--A-17."
FT /evidence="ECO:0000269|PubMed:18757745"
FT MUTAGEN 129
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:23419774"
FT MUTAGEN 131
FT /note="S->A: Reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:23419774"
FT CONFLICT 58
FT /note="A -> T (in Ref. 1; BAA91468)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="M -> L (in Ref. 1; BAA91644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27480 MW; E981F1AF64375D5A CRC64;
MASRWQNMGT SVRRRSLQHQ EQLEDSKELQ PVVSHQETSV GALGSLCRQF QRRLPLRAVN
LNLRAGPSWK RLETPEPGQQ GLQAAARSAK SALGAVSQRI QESCQSGTKW LVETQVKARR
RKRGAQKGSG SPTHSLSQKS TRLSGAAPAH SAADPWEKEH HRLSVRMGSH AHPLRRSRRE
AAFRSPYSST EPLCSPSESD SDLEPVGAGI QHLQKLSQEL DEAIMAEERK QALSDRQGFI
LKDVYASP
