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Protein PIMREG (CALM-interactor expressed in thymus and spleen) (PICALM-interacting mitotic regulator) (Regulator of chromosome segregation protein 1)

 PIMRE_HUMAN             Reviewed;         248 AA.
Q9BSJ6; Q96CT4; Q9NVV1; Q9NWB5;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-FEB-2018, entry version 114.
RecName: Full=Protein PIMREG {ECO:0000305};
AltName: Full=CALM-interactor expressed in thymus and spleen {ECO:0000303|PubMed:19383357, ECO:0000303|PubMed:23419774};
AltName: Full=PICALM-interacting mitotic regulator {ECO:0000312|HGNC:HGNC:25483};
AltName: Full=Regulator of chromosome segregation protein 1 {ECO:0000303|PubMed:18757745};
Name=PIMREG {ECO:0000312|HGNC:HGNC:25483};
Synonyms=CATS {ECO:0000303|PubMed:19383357,
ECO:0000303|PubMed:23419774}, FAM64A {ECO:0000312|HGNC:HGNC:25483},
RCS1 {ECO:0000303|PubMed:18757745};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, INTERACTION WITH PICALM, TISSUE SPECIFICITY, AND
IDENTIFICATION OF ISOFORMS 1 AND 2.
PubMed=16491119; DOI=10.1038/sj.onc.1209438;
Archangelo L.F., Glaesner J., Krause A., Bohlander S.K.;
"The novel CALM interactor CATS influences the subcellular
localization of the leukemogenic fusion protein CALM/AF10.";
Oncogene 25:4099-4109(2006).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[6]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=19383357; DOI=10.1016/j.molonc.2008.08.001;
Archangelo L.F., Greif P.A., Hoelzel M., Harasim T., Kremmer E.,
Przemeck G.K., Eick D., Deshpande A.J., Buske C., de Angelis M.H.,
Saad S.T., Bohlander S.K.;
"The CALM and CALM/AF10 interactor CATS is a marker for
proliferation.";
Mol. Oncol. 2:356-367(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-199 AND SER-201,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
FUNCTION IN MITOSIS PROGRESSION, INTERACTION WITH NURD COMPLEX,
DEVELOPMENTAL STAGE, D-BOX MOTIF, MUTAGENESIS OF 14-ARG--LEU-17 AND
53-ARG--LEU-56, AND UBIQUITINATION.
PubMed=18757745; DOI=10.1073/pnas.0709227105;
Zhao W.M., Coppinger J.A., Seki A., Cheng X.L., Yates J.R. III,
Fang G.;
"RCS1, a substrate of APC/C, controls the metaphase to anaphase
transition.";
Proc. Natl. Acad. Sci. U.S.A. 105:13415-13420(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-129 AND SER-131,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[11]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-131, AND MUTAGENESIS OF
SER-129 AND SER-131.
PubMed=23419774; DOI=10.1016/j.bbamcr.2013.02.004;
Archangelo L.F., Greif P.A., Maucuer A., Manceau V., Koneru N.,
Bigarella C.L., Niemann F., Dos Santos M.T., Kobarg J.,
Bohlander S.K., Saad S.T.;
"The CATS (FAM64A) protein is a substrate of the kinase interacting
stathmin (KIS).";
Biochim. Biophys. Acta 1833:1269-1279(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-16, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: During mitosis, may play a role in the control of
metaphase-to-anaphase transition. {ECO:0000269|PubMed:18757745}.
-!- SUBUNIT: Isoform 1 and isoform 2 interact with PICALM; this
interaction may target PICALM to the nucleus (PubMed:16491119).
During mitosis, associates with HDAC2 and MTA2 subunits of the
chromatin-remodeling NuRD complex; this association is strongest
at prometaphase and decreases as the cell progresses through
metaphase and anaphase (PubMed:18757745).
{ECO:0000269|PubMed:16491119, ECO:0000269|PubMed:18757745}.
-!- INTERACTION:
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-2568609, EBI-741181;
Q6RW13-2:AGTRAP; NbExp=3; IntAct=EBI-2568609, EBI-11522760;
Q7L4P6:BEND5; NbExp=3; IntAct=EBI-2568609, EBI-724373;
O95273:CCNDBP1; NbExp=6; IntAct=EBI-2568609, EBI-748961;
Q8NHQ1:CEP70; NbExp=6; IntAct=EBI-2568609, EBI-739624;
Q96DZ9-2:CMTM5; NbExp=3; IntAct=EBI-2568609, EBI-11522780;
Q8NF50:DOCK8; NbExp=3; IntAct=EBI-2568609, EBI-2548605;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-2568609, EBI-618309;
Q96ED9-2:HOOK2; NbExp=3; IntAct=EBI-2568609, EBI-10961706;
Q6A162:KRT40; NbExp=6; IntAct=EBI-2568609, EBI-10171697;
Q969L2:MAL2; NbExp=3; IntAct=EBI-2568609, EBI-944295;
P04156:PRNP; NbExp=5; IntAct=EBI-2568609, EBI-977302;
Q6NUQ1:RINT1; NbExp=3; IntAct=EBI-2568609, EBI-726876;
Q8IUQ4-2:SIAH1; NbExp=3; IntAct=EBI-2568609, EBI-11522811;
Q96R06:SPAG5; NbExp=3; IntAct=EBI-2568609, EBI-413317;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-2568609, EBI-2212028;
Q12800:TFCP2; NbExp=3; IntAct=EBI-2568609, EBI-717422;
P14373:TRIM27; NbExp=9; IntAct=EBI-2568609, EBI-719493;
Q8N1B4:VPS52; NbExp=3; IntAct=EBI-2568609, EBI-2799833;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16491119,
ECO:0000269|PubMed:19383357}. Nucleus, nucleolus
{ECO:0000269|PubMed:19383357}. Note=Partially localizes to the
nucleolus. {ECO:0000269|PubMed:19383357}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BSJ6-1; Sequence=Displayed;
Name=2;
IsoId=Q9BSJ6-2; Sequence=VSP_023997;
-!- TISSUE SPECIFICITY: Expressed in thymus (at protein level).
Detected in spleen, colon, ovary and small intestines.
{ECO:0000269|PubMed:16491119, ECO:0000269|PubMed:19383357}.
-!- DEVELOPMENTAL STAGE: Regulated in a cell-cycle dependent manner,
with lowest levels in quiescent cells or at G1 phase. Progressive
up-regulation starting at S phase and peaking at G2 and G2/M
phases, followed by a drastic drop as cells exit mitosis (at
protein level). {ECO:0000269|PubMed:18757745}.
-!- DOMAIN: The N-terminal destruction box 2 (D-box 2) is required for
APC/C ubiquitination and proteasomal degradation.
{ECO:0000269|PubMed:18757745}.
-!- PTM: Ubiquitinated by the anaphase-promoting complex/cyclosome
(APC/C) complex in the presence of FZR1, leading to its
degradation by the proteasome during mitotic exit. However,
degradation is not essential for normal mitotic progression within
a single cell cycle. {ECO:0000269|PubMed:18757745}.
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EMBL; AK001018; BAA91468.1; -; mRNA.
EMBL; AK001353; BAA91644.1; -; mRNA.
EMBL; AC055872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005004; AAH05004.1; -; mRNA.
EMBL; BC013966; AAH13966.1; -; mRNA.
CCDS; CCDS32541.1; -. [Q9BSJ6-2]
CCDS; CCDS56016.1; -. [Q9BSJ6-1]
RefSeq; NP_001182157.1; NM_001195228.1. [Q9BSJ6-1]
RefSeq; NP_061886.2; NM_019013.2. [Q9BSJ6-2]
UniGene; Hs.592116; -.
ProteinModelPortal; Q9BSJ6; -.
BioGrid; 119983; 16.
DIP; DIP-56370N; -.
IntAct; Q9BSJ6; 24.
MINT; Q9BSJ6; -.
STRING; 9606.ENSP00000250056; -.
iPTMnet; Q9BSJ6; -.
PhosphoSitePlus; Q9BSJ6; -.
BioMuta; FAM64A; -.
DMDM; 74733018; -.
EPD; Q9BSJ6; -.
MaxQB; Q9BSJ6; -.
PaxDb; Q9BSJ6; -.
PeptideAtlas; Q9BSJ6; -.
PRIDE; Q9BSJ6; -.
Ensembl; ENST00000250056; ENSP00000250056; ENSG00000129195. [Q9BSJ6-1]
Ensembl; ENST00000572447; ENSP00000459235; ENSG00000129195. [Q9BSJ6-2]
Ensembl; ENST00000576056; ENSP00000458534; ENSG00000129195. [Q9BSJ6-2]
GeneID; 54478; -.
KEGG; hsa:54478; -.
UCSC; uc002gcu.3; human. [Q9BSJ6-1]
CTD; 54478; -.
DisGeNET; 54478; -.
EuPathDB; HostDB:ENSG00000129195.15; -.
GeneCards; PIMREG; -.
HGNC; HGNC:25483; PIMREG.
HPA; HPA043783; -.
HPA; HPA049934; -.
MIM; 617611; gene.
neXtProt; NX_Q9BSJ6; -.
OpenTargets; ENSG00000129195; -.
PharmGKB; PA142671874; -.
eggNOG; ENOG410IXNZ; Eukaryota.
eggNOG; ENOG4111M05; LUCA.
GeneTree; ENSGT00390000008128; -.
HOGENOM; HOG000293378; -.
HOVERGEN; HBG067744; -.
InParanoid; Q9BSJ6; -.
PhylomeDB; Q9BSJ6; -.
TreeFam; TF336322; -.
SIGNOR; Q9BSJ6; -.
GenomeRNAi; 54478; -.
PRO; PR:Q9BSJ6; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000129195; -.
CleanEx; HS_FAM64A; -.
ExpressionAtlas; Q9BSJ6; baseline and differential.
Genevisible; Q9BSJ6; HS.
GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
InterPro; IPR009932; RCS1.
PANTHER; PTHR35819; PTHR35819; 1.
Pfam; PF07326; DUF1466; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Complete proteome;
Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Ubl conjugation.
CHAIN 1 248 Protein PIMREG.
/FTId=PRO_0000281159.
MOTIF 14 17 D-box 1.
MOTIF 53 56 D-box 2.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 131 131 Phosphoserine; by UHMK1; in vitro.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:23419774}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 229 248 RKQALSDRQGFILKDVYASP -> SGDIVSLIHD (in
isoform 2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_023997.
VARIANT 199 199 S -> C (in dbSNP:rs16955870).
/FTId=VAR_056873.
MUTAGEN 14 17 RRSL->ARSA: Weak reduction in
ubiquitination. Complete loss of
ubiquitination; when associated with 53-
A--A-56. {ECO:0000269|PubMed:18757745}.
MUTAGEN 53 56 RLPL->ALPA: Great reduction in
ubiquitination. Complete loss of
ubiquitination; when associated with 14-
A--A-17. {ECO:0000269|PubMed:18757745}.
MUTAGEN 129 129 S->A: No effect on phosphorylation.
{ECO:0000269|PubMed:23419774}.
MUTAGEN 131 131 S->A: Reduced phosphorylation.
{ECO:0000269|PubMed:23419774}.
CONFLICT 58 58 A -> T (in Ref. 1; BAA91468).
{ECO:0000305}.
CONFLICT 167 167 M -> L (in Ref. 1; BAA91644).
{ECO:0000305}.
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


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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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