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Protein PRRC2C (BAT2 domain-containing protein 1) (HBV X-transactivated gene 2 protein) (HBV XAg-transactivated protein 2) (HLA-B-associated transcript 2-like 2) (Proline-rich and coiled-coil-containing protein 2C)

 PRC2C_HUMAN             Reviewed;        2896 AA.
Q9Y520; Q05DM8; Q49A39; Q6PD54; Q9H2N2; Q9HA05; Q9NSM8; Q9NXL3;
Q9UF29; Q9UPQ6;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
20-JUN-2018, entry version 116.
RecName: Full=Protein PRRC2C;
AltName: Full=BAT2 domain-containing protein 1;
AltName: Full=HBV X-transactivated gene 2 protein;
AltName: Full=HBV XAg-transactivated protein 2;
AltName: Full=HLA-B-associated transcript 2-like 2;
AltName: Full=Proline-rich and coiled-coil-containing protein 2C;
Name=PRRC2C; Synonyms=BAT2D1, BAT2L2, KIAA1096, XTP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Liu Y., Cheng J., Lu Y., Wang G., Mu J., Li K., Zhang L.;
"Cloning and identification of human gene 2 transactivated by
hepatitis B virus X antigen.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Rhodes S., Huckle E.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-577 (ISOFORM 7).
Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-571 (ISOFORM 7), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-561 (ISOFORM 2).
TISSUE=Brain, Placenta, and Skin;
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).
[6]
PROTEIN SEQUENCE OF 17-27; 106-119; 375-387; 451-461; 639-665;
795-804; 834-859; 1317-1324; 1516-1526; 1996-2007; 2101-2110;
2130-2148; 2629-2637 AND 2662-2679, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
Submitted (JUL-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 931-2896 (ISOFORM 5), AND
VARIANT CYS-1624.
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[8]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1454-2896 (ISOFORM 6), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2393-2896 (ISOFORM 4).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2029-2862 (ISOFORM 4).
TISSUE=Colon mucosa, and Mammary gland;
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).
[11]
TISSUE SPECIFICITY.
PubMed=12443540; DOI=10.1089/104454902760599681;
Huang W.C., Taylor S., Nguyen T.B., Tomaszewski J.E., Libertino J.A.,
Malkowicz S.B., McGarvey T.W.;
"KIAA1096, a gene on chromosome 1q, is amplified and overexpressed in
bladder cancer.";
DNA Cell Biol. 21:707-715(2002).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500; SER-779; SER-878;
SER-2105 AND THR-2673, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2105; THR-2682 AND
SER-2686, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2143 AND THR-2673, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2105, AND 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-191; SER-779;
SER-878; SER-2013; SER-2143 AND THR-2673, 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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-878, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-392, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779; SER-801; THR-1965;
SER-2013; SER-2105 AND THR-2673, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1246; SER-1248;
SER-1263; THR-1265; THR-1267; SER-2013; SER-2105 AND SER-2694, 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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-395; SER-500;
SER-779; SER-785; SER-867; SER-878; SER-920; SER-1242; SER-1246;
SER-1248; SER-1249; SER-1263; THR-1265; THR-1267; SER-1544; THR-1965;
SER-2105; SER-2143; SER-2260 AND THR-2673, 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND THR-1267, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-242; ARG-255; ARG-266;
ARG-279 AND ARG-281, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1133, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1133, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[27]
VARIANT [LARGE SCALE ANALYSIS] THR-906, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1;
IsoId=Q9Y520-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y520-2; Sequence=VSP_035244;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9Y520-3; Sequence=VSP_035247, VSP_035248;
Name=4;
IsoId=Q9Y520-4; Sequence=VSP_035249;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9Y520-5; Sequence=VSP_035245;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q9Y520-6; Sequence=VSP_035246, VSP_035249;
Note=No experimental confirmation available.;
Name=7;
IsoId=Q9Y520-7; Sequence=VSP_035250;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Overexpressed in bladder cancer.
{ECO:0000269|PubMed:12443540}.
-!- SEQUENCE CAUTION:
Sequence=AAH06090.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH45713.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH58930.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA90997.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AF488829; AAO49478.1; -; mRNA.
EMBL; AL096857; CAB51071.1; -; mRNA.
EMBL; AL021579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z98750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF253978; AAG44627.1; -; mRNA.
EMBL; BC006090; AAH06090.1; ALT_SEQ; mRNA.
EMBL; BC045713; AAH45713.1; ALT_SEQ; mRNA.
EMBL; BC058930; AAH58930.1; ALT_SEQ; mRNA.
EMBL; AB029019; BAA83048.2; -; mRNA.
EMBL; AL133635; CAB63759.1; -; mRNA.
EMBL; AL162004; CAB82345.1; -; mRNA.
EMBL; AK000190; BAA90997.1; ALT_SEQ; mRNA.
EMBL; AK022492; BAB14056.1; -; mRNA.
CCDS; CCDS1296.2; -. [Q9Y520-4]
PIR; T43454; T43454.
PIR; T47182; T47182.
RefSeq; NP_055987.2; NM_015172.3. [Q9Y520-4]
RefSeq; XP_005245074.1; XM_005245017.2. [Q9Y520-7]
RefSeq; XP_006711301.1; XM_006711238.3. [Q9Y520-1]
UniGene; Hs.494614; -.
ProteinModelPortal; Q9Y520; -.
BioGrid; 116822; 41.
DIP; DIP-47285N; -.
IntAct; Q9Y520; 30.
MINT; Q9Y520; -.
STRING; 9606.ENSP00000343629; -.
iPTMnet; Q9Y520; -.
PhosphoSitePlus; Q9Y520; -.
BioMuta; PRRC2C; -.
DMDM; 341942262; -.
EPD; Q9Y520; -.
PaxDb; Q9Y520; -.
PeptideAtlas; Q9Y520; -.
PRIDE; Q9Y520; -.
ProteomicsDB; 86273; -.
ProteomicsDB; 86274; -. [Q9Y520-2]
ProteomicsDB; 86275; -. [Q9Y520-3]
ProteomicsDB; 86276; -. [Q9Y520-4]
ProteomicsDB; 86277; -. [Q9Y520-5]
ProteomicsDB; 86278; -. [Q9Y520-6]
ProteomicsDB; 86279; -. [Q9Y520-7]
Ensembl; ENST00000338920; ENSP00000343629; ENSG00000117523. [Q9Y520-4]
Ensembl; ENST00000426496; ENSP00000410219; ENSG00000117523. [Q9Y520-4]
GeneID; 23215; -.
KEGG; hsa:23215; -.
UCSC; uc010pmg.3; human. [Q9Y520-1]
CTD; 23215; -.
DisGeNET; 23215; -.
EuPathDB; HostDB:ENSG00000117523.15; -.
GeneCards; PRRC2C; -.
H-InvDB; HIX0001329; -.
H-InvDB; HIX0159969; -.
HGNC; HGNC:24903; PRRC2C.
HPA; HPA025766; -.
HPA; HPA028659; -.
MIM; 617373; gene.
neXtProt; NX_Q9Y520; -.
OpenTargets; ENSG00000117523; -.
PharmGKB; PA165750415; -.
eggNOG; KOG4817; Eukaryota.
eggNOG; ENOG4111VEG; LUCA.
GeneTree; ENSGT00530000063496; -.
HOVERGEN; HBG107491; -.
InParanoid; Q9Y520; -.
TreeFam; TF328738; -.
ChiTaRS; PRRC2C; human.
GenomeRNAi; 23215; -.
PRO; PR:Q9Y520; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117523; -.
CleanEx; HS_BAT2D1; -.
ExpressionAtlas; Q9Y520; baseline and differential.
Genevisible; Q9Y520; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
InterPro; IPR009738; BAT2_N.
InterPro; IPR033184; PRRC2.
PANTHER; PTHR14038; PTHR14038; 1.
Pfam; PF07001; BAT2_N; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Direct protein sequencing; Isopeptide bond; Methylation;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 2896 Protein PRRC2C.
/FTId=PRO_0000349239.
COILED 1020 1046 {ECO:0000255}.
COILED 1682 1717 {ECO:0000255}.
COMPBIAS 407 410 Poly-Pro.
COMPBIAS 467 650 Glu-rich.
COMPBIAS 666 703 Gln-rich.
COMPBIAS 697 769 Pro-rich.
COMPBIAS 1059 1082 Pro-rich.
COMPBIAS 1341 1443 Arg-rich.
COMPBIAS 1760 1934 Ala-rich.
COMPBIAS 2345 2634 Gln-rich.
MOD_RES 27 27 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 191 191 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 242 242 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q3TLH4}.
MOD_RES 242 242 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 255 255 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 266 266 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 279 279 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 281 281 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 392 392 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 500 500 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 779 779 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 801 801 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 867 867 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 878 878 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 929 929 Phosphoserine.
{ECO:0000250|UniProtKB:Q3TLH4}.
MOD_RES 1242 1242 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1246 1246 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1248 1248 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1249 1249 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1263 1263 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1265 1265 Phosphothreonine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1267 1267 Phosphothreonine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1544 1544 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1965 1965 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1983 1983 Phosphoserine.
{ECO:0000250|UniProtKB:Q3TLH4}.
MOD_RES 2013 2013 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 2105 2105 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2143 2143 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2260 2260 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2673 2673 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2682 2682 Phosphothreonine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 2686 2686 Phosphoserine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 2694 2694 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 2814 2814 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q3TLH4}.
MOD_RES 2823 2823 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q3TLH4}.
MOD_RES 2823 2823 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q3TLH4}.
CROSSLNK 1133 1133 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 243 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035244.
VAR_SEQ 37 37 T -> TVA (in isoform 7).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_035250.
VAR_SEQ 1759 1805 Missing (in isoform 5).
{ECO:0000303|PubMed:10470851}.
/FTId=VSP_035245.
VAR_SEQ 2185 2249 Missing (in isoform 6).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_035246.
VAR_SEQ 2687 2700 PFRATSTSPNSQSS -> SGLLLQVRTASPAK (in
isoform 3). {ECO:0000303|Ref.1,
ECO:0000303|Ref.2}.
/FTId=VSP_035247.
VAR_SEQ 2701 2896 Missing (in isoform 3).
{ECO:0000303|Ref.1, ECO:0000303|Ref.2}.
/FTId=VSP_035248.
VAR_SEQ 2732 2810 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_035249.
VARIANT 235 235 A -> T (in dbSNP:rs10913157).
/FTId=VAR_046290.
VARIANT 343 343 N -> K (in dbSNP:rs36013361).
/FTId=VAR_046291.
VARIANT 468 468 E -> G (in dbSNP:rs704839).
/FTId=VAR_046292.
VARIANT 906 906 A -> T (in dbSNP:rs760644).
{ECO:0000244|PubMed:21269460}.
/FTId=VAR_046293.
VARIANT 959 959 P -> S (in dbSNP:rs34269512).
/FTId=VAR_046294.
VARIANT 1624 1624 S -> C (in dbSNP:rs235468).
{ECO:0000269|PubMed:10470851}.
/FTId=VAR_046295.
VARIANT 1771 1771 P -> S (in dbSNP:rs1687056).
/FTId=VAR_046296.
VARIANT 1868 1868 L -> R (in dbSNP:rs3820169).
/FTId=VAR_046297.
VARIANT 1885 1885 A -> T (in dbSNP:rs12025905).
/FTId=VAR_046298.
VARIANT 1924 1924 P -> R (in dbSNP:rs183523).
/FTId=VAR_046299.
VARIANT 2717 2717 T -> A (in dbSNP:rs2421847).
/FTId=VAR_059584.
CONFLICT 454 456 EIS -> GIY (in Ref. 5; AAH45713).
{ECO:0000305}.
CONFLICT 561 561 Q -> P (in Ref. 5; AAH45713).
{ECO:0000305}.
CONFLICT 1940 1940 V -> A (in Ref. 9; CAB82345).
{ECO:0000305}.
CONFLICT 2443 2443 A -> V (in Ref. 10; BAB14056).
{ECO:0000305}.
CONFLICT 2539 2539 I -> V (in Ref. 10; BAA90997).
{ECO:0000305}.
SEQUENCE 2896 AA; 316911 MW; F0E037C36F04CDF9 CRC64;
MSEKSGQSTK AKDGKKYATL SLFNTYKGKS LETQKTTARH GLQSLGKVGI SRRMPPPANL
PSLKAENKGN DPNVNIVPKD GTGWASKQEQ HEEEKTPEVP PAQPKPGVAA PPEVAPAPKS
WASNKQGGQG DGIQVNSQFQ QEFPSLQAAG DQEKKEKETN DDNYGPGPSL RPPNVACWRD
GGKAAGSPSS SDQDEKLPGQ DESTAGTSEQ NDILKVVEKR IACGPPQAKL NGQQAALASQ
YRAMMPPYMF QQYPRMTYPP LHGPMRFPPS LSETNKGLRG RGPPPSWASE PERPSILSAS
ELKELDKFDN LDAEADEGWA GAQMEVDYTE QLNFSDDDEQ GSNSPKENNS EDQGSKASEN
NENKKETDEV SNTKSSSQIP AQPSVAKVPY GKGPSFNQER GTSSHLPPPP KLLAQQHPPP
DRQAVPGRPG PFPSKQQVAD EDEIWKQRRR QQSEISAAVE RARKRREEEE RRMEEQRKAA
CAEKLKRLDE KLGILEKQPS PEEIRERERE KEREREKELE KEQEQEREKE REKDRERQQE
KEKELEKEQE KQREMEKERK QEKEKELERQ KEKEKELQKM KEQEKECELE KEREKLEEKI
EPREPNLEPM VEKQESENSC NKEEEPVFTR QDSNRSEKEA TPVVHETEPE SGSQPRPAVL
SGYFKQFQKS LPPRFQRQQE QMKQQQWQQQ QQQGVLPQTV PSQPSSSTVP PPPHRPLYQP
MQPHPQHLAS MGFDPRWLMM QSYMDPRMMS GRPAMDIPPI HPGMIPPKPL MRRDQMEGSP
NSSESFEHIA RSARDHAISL SEPRMLWGSD PYPHAEPQQA TTPKATEEPE DVRSEAALDQ
EQITAAYSVE HNQLEAHPKA DFIRESSEAQ VQKFLSRSVE DVRPHHTDAN NQSACFEAPD
QKTLSAPQEE RISAVESQPS RKRSVSHGSN HTQKPDEQRS EPSAGIPKVT SRCIDSKEPI
ERPEEKPKKE GFIRSSEGPK PEKVYKSKSE TRWGPRPSSN RREEVNDRPV RRSGPIKKPV
LRDMKEEREQ RKEKEGEKAE KVTEKVVVKP EKTEKKDLPP PPPPPQPPAP IQPQSVPPPI
QPEAEKFPST ETATLAQKPS QDTEKPLEPV STVQVEPAVK TVNQQTMAAP VVKEEKQPEK
VISKDLVIER PRPDSRPAVK KESTLPPRTY WKEARERDWF PDQGYRGRGR GEYYSRGRSY
RGSYGGRGRG GRGHTRDYPQ YRDNKPRAEH IPSGPLRQRE ESETRSESSD FEVVPKRRRQ
RGSETDTDSE IHESASDKDS LSKGKLPKRE ERPENKKPVK PHSSFKPDNH VRIDNRLLEK
PYVRDDDKAK PGFLPKGEPT RRGRGGTFRR GGRDPGGRPS RPSTLRRPAY RDNQWNPRQS
EVPKPEDGEP PRRHEQFIPI AADKRPPKFE RKFDPARERP RRQRPTRPPR QDKPPRFRRL
REREAASKSN EVVAVPTNGT VNNVAQEPVN TLGDISGNKT PDLSNQNSSD QANEEWETAS
ESSDFNERRE RDEKKNADLN AQTVVKVGEN VLPPKREIAK RSFSSQRPVD RQNRRGNNGP
PKSGRNFSGP RNERRSGPPS KSGKRGPFDD QPAGTTGVDL INGSSAHHQE GVPNGTGQKN
SKDSTGKKRE DPKPGPKKPK EKVDALSQFD LNNYASVVII DDHPEVTVIE DPQSNLNDDG
FTEVVSKKQQ KRLQDEERRK KEEQVIQVWN KKNANEKGRS QTSKLPPRFA KKQATGIQQA
QSSASVPPLA SAPLPPSTSA SVPASTSAPL PATLTPVPAS TSAPVPASTL APVLASTSAP
VPASPLAPVS ASASVSASVP ASTSAAAITS SSAPASAPAP TPILASVSTP ASVTILASAS
IPILASALAS TSAPTPAPAA SSPAAPVITA PTIPASAPTA SVPLAPASAS APAPAPTPVS
APNPAPPAPA QTQAQTHKPV QNPLQTTSQS SKQPPPSIRL PSAQTPNGTD YVASGKSIQT
PQSHGTLTAE LWDNKVAPPA VLNDISKKLG PISPPQPPSV SAWNKPLTSF GSAPSSEGAK
NGQESGLEIG TDTIQFGAPA SNGNENEVVP VLSEKSADKI PEPKEQRQKQ PRAGPIKAQK
LPDLSPVENK EHKPGPIGKE RSLKNRKVKD AQQVEPEGQE KPSPATVRST DPVTTKETKA
VSEMSTEIGT MISVSSAEYG TNAKESVTDY TTPSSSLPNT VATNNTKMED TLVNNVPLPN
TLPLPKRETI QQSSSLTSVP PTTFSLTFKM ESARKAWENS PNVREKGSPV TSTAPPIATG
VSSSASGPST ANYNSFSSAS MPQIPVASVT PTASLSGAGT YTTSSLSTKS TTTSDPPNIC
KVKPQQLQTS SLPSASHFSQ LSCMPSLIAQ QQQNPQVYVS QSAAAQIPAF YMDTSHLFNT
QHARLAPPSL AQQQGFQPGL SQPTSVQQIP IPIYAPLQGQ HQAQLSLGAG PAVSQAQELF
SSSLQPYRSQ PAFMQSSLSQ PSVVLSGTAI HNFPTVQHQE LAKAQSGLAF QQTSNTQPIP
ILYEHQLGQA SGLGGSQLID THLLQARANL TQASNLYSGQ VQQPGQTNFY NTAQSPSALQ
QVTVPLPASQ LSLPNFGSTG QPLIALPQTL QPPLQHTTPQ AQAQSLSRPA QVSQPFRGLI
PAGTQHSMIA TTGKMSEMEL KAFGSGIDIK PGTPPIAGRS TTPTSSPFRA TSTSPNSQSS
KMNSIVYQKQ FQSAPATVRM TQPFPTQFAP QILSQPNLVP PLVRAPHTNT FPAPVQRPPM
ALASQMPPPL TTGLMSHARL PHVARGPCGS LSGVRGNQAQ AALKAEQDMK AKQRAEVLQS
TQRFFSEQQQ SKQIGGGKAQ KVDSDSSKPP ETLTDPPGVC QEKVEEKPPP APSIATKPVR
TGPIKPQAIK TEETKS


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