Full text data of PRRC2A
PRRC2A
(BAT2, G2)
[Confidence: low (only semi-automatic identification from reviews)]
Protein PRRC2A (HLA-B-associated transcript 2; Large proline-rich protein BAT2; Proline-rich and coiled-coil-containing protein 2A; Protein G2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein PRRC2A (HLA-B-associated transcript 2; Large proline-rich protein BAT2; Proline-rich and coiled-coil-containing protein 2A; Protein G2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P48634
ID PRC2A_HUMAN Reviewed; 2157 AA.
AC P48634; B0UX77; B0UZE9; B0UZL3; O95875; Q05BK4; Q4LE37; Q5SQ29;
read moreAC Q5SQ30; Q5ST84; Q5STX6; Q5STX7; Q68DW9; Q6P9P7; Q6PIN1; Q8MGQ9;
AC Q96QC6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Protein PRRC2A;
DE AltName: Full=HLA-B-associated transcript 2;
DE AltName: Full=Large proline-rich protein BAT2;
DE AltName: Full=Proline-rich and coiled-coil-containing protein 2A;
DE AltName: Full=Protein G2;
GN Name=PRRC2A; Synonyms=BAT2, G2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND VARIANTS
RP ARG-57; GLU-742; PRO-1503 AND VAL-1895.
RC TISSUE=T-cell;
RX PubMed=2156268; DOI=10.1073/pnas.87.6.2374;
RA Banerji J., Sands J., Strominger J.L., Spies T.;
RT "A gene pair from the human major histocompatibility complex encodes
RT large proline-rich proteins with multiple repeated motifs and a single
RT ubiquitin-like domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2374-2378(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS
RP LEU-106; LYS-544; PRO-1503 AND VAL-1895.
RC TISSUE=Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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], AND VARIANTS LYS-544;
RP ALA-1285; PRO-1503; HIS-1740; VAL-1895 AND LEU-2130.
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-544;
RP PRO-1503 AND VAL-1895.
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LEU-106;
RP LYS-544; PRO-1503; HIS-1740; VAL-1895 AND SER-2006.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-544;
RP PRO-1503; HIS-1740 AND VAL-1895.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP CYS-477; LYS-544; PRO-1503 AND VAL-1895.
RC TISSUE=Lymph, Placenta, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1874 (ISOFORM 3), AND VARIANTS
RP LYS-544; LYS-694; ALA-1415; PRO-1503 AND ALA-1744.
RX PubMed=8499947; DOI=10.1038/ng0293-137;
RA Iris F.J.M., Bougueleret L., Prieur S., Caterina D., Primas G.,
RA Perrot V., Jurka J., Rodriguez-Tome P., Claverie J.-M., Dausset J.,
RA Cohen D.;
RT "Dense Alu clustering and a potential new member of the NF kappa B
RT family within a 90 kilobase HLA class III segment.";
RL Nat. Genet. 3:137-145(1993).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 871-2157 (ISOFORM 1), AND
RP VARIANTS PRO-1503 AND VAL-1895.
RC TISSUE=Uterine endothelium;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP FUNCTION.
RX PubMed=14667819; DOI=10.1016/S0888-7543(03)00235-0;
RA Lehner B., Semple J.I., Brown S.E., Counsell D., Campbell R.D.,
RA Sanderson C.M.;
RT "Analysis of a high-throughput yeast two-hybrid system and its use to
RT predict the function of intracellular proteins encoded within the
RT human MHC class III region.";
RL Genomics 83:153-167(2004).
RN [11]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15752841; DOI=10.1016/j.vaccine.2004.08.003;
RA Schneiders A., Thiel S., Winkler J., Moeller P., Koch N.;
RT "Antibodies generated by a novel DNA vaccination identify the MHC
RT class III encoded BAT2 polypeptide.";
RL Vaccine 23:2540-2550(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342; SER-350 AND
RP SER-1089, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1219, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-383; SER-456;
RP THR-610; SER-759; SER-761; SER-764; SER-1085; SER-1089; SER-1092;
RP TYR-1094; SER-1147 AND SER-1306, AND MASS SPECTROMETRY.
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 [16]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-456; THR-610;
RP SER-761 AND SER-1089, AND MASS SPECTROMETRY.
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-1196, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-808; SER-1219;
RP THR-1353 AND SER-2113, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342; SER-350; SER-380;
RP SER-1089; SER-1110 AND SER-1219, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-1087 AND HIS-1152.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May play a role in the regulation of pre-mRNA splicing.
CC -!- INTERACTION:
CC P54253:ATXN1; NbExp=4; IntAct=EBI-347545, EBI-930964;
CC P05412:JUN; NbExp=2; IntAct=EBI-347545, EBI-852823;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P48634-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48634-2; Sequence=VSP_015099, VSP_015100, VSP_015101,
CC VSP_015102;
CC Name=3;
CC IsoId=P48634-3; Sequence=VSP_015100, VSP_015101, VSP_015102;
CC Note=Ref.8 (CAA78744) sequence is in conflict in position:
CC 1082:M->L;
CC Name=4;
CC IsoId=P48634-4; Sequence=VSP_030865;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Limited to cell-lines of leukemic origin.
CC -!- DEVELOPMENTAL STAGE: Broadly expressed during the 11th week of
CC gestation, with highest levels in the central nervous system,
CC spinal ganglia, osteoblasts and osteocytes (at protein level).
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35585.1; Type=Frameshift; Positions=38, 58;
CC Sequence=AAA35586.1; Type=Frameshift; Positions=38, 58;
CC Sequence=BAE06116.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=CAA78744.1; Type=Frameshift; Positions=38, 58;
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DR EMBL; M33509; AAA35585.1; ALT_FRAME; mRNA.
DR EMBL; M33518; AAA35586.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M33512; AAA35586.1; JOINED; Genomic_DNA.
DR EMBL; AB210034; BAE06116.1; ALT_INIT; mRNA.
DR EMBL; AF129756; AAD18086.1; -; Genomic_DNA.
DR EMBL; CR354443; CAQ06970.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63391.1; -; Genomic_DNA.
DR EMBL; AL662847; CAI17698.2; -; Genomic_DNA.
DR EMBL; AL662801; CAI18313.1; -; Genomic_DNA.
DR EMBL; AL805934; CAI18500.1; -; Genomic_DNA.
DR EMBL; BX511262; CAI95572.1; -; Genomic_DNA.
DR EMBL; CR753892; CAQ06959.1; -; Genomic_DNA.
DR EMBL; CR759761; CAQ10847.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03452.1; -; Genomic_DNA.
DR EMBL; BC030127; AAH30127.1; -; mRNA.
DR EMBL; BC032134; AAH32134.1; -; mRNA.
DR EMBL; BC042295; AAH42295.1; -; mRNA.
DR EMBL; BC060668; AAH60668.1; -; mRNA.
DR EMBL; Z15025; CAA78744.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CR749245; CAH18101.1; -; mRNA.
DR PIR; B35098; B35098.
DR PIR; S37671; S37671.
DR RefSeq; NP_004629.3; NM_004638.3.
DR RefSeq; NP_542417.2; NM_080686.2.
DR UniGene; Hs.123239; -.
DR UniGene; Hs.436093; -.
DR ProteinModelPortal; P48634; -.
DR IntAct; P48634; 32.
DR MINT; MINT-1032109; -.
DR STRING; 9606.ENSP00000404619; -.
DR DMDM; 296439424; -.
DR PaxDb; P48634; -.
DR PRIDE; P48634; -.
DR Ensembl; ENST00000376007; ENSP00000365175; ENSG00000204469.
DR Ensembl; ENST00000376033; ENSP00000365201; ENSG00000204469.
DR Ensembl; ENST00000383455; ENSP00000372947; ENSG00000206427.
DR Ensembl; ENST00000383464; ENSP00000372956; ENSG00000206427.
DR Ensembl; ENST00000414956; ENSP00000404619; ENSG00000226618.
DR Ensembl; ENST00000416335; ENSP00000415182; ENSG00000231370.
DR Ensembl; ENST00000422962; ENSP00000415363; ENSG00000231825.
DR Ensembl; ENST00000428775; ENSP00000387910; ENSG00000225164.
DR Ensembl; ENST00000430737; ENSP00000413977; ENSG00000231825.
DR Ensembl; ENST00000432252; ENSP00000408226; ENSG00000225748.
DR Ensembl; ENST00000435971; ENSP00000409444; ENSG00000225164.
DR Ensembl; ENST00000439762; ENSP00000400540; ENSG00000231370.
DR Ensembl; ENST00000454306; ENSP00000387477; ENSG00000225748.
DR Ensembl; ENST00000458561; ENSP00000396812; ENSG00000226618.
DR GeneID; 7916; -.
DR KEGG; hsa:7916; -.
DR UCSC; uc003nvb.4; human.
DR CTD; 7916; -.
DR GeneCards; GC06P031719; -.
DR GeneCards; GC06Pj31575; -.
DR GeneCards; GC06Pk31570; -.
DR GeneCards; GC06Pl31627; -.
DR GeneCards; GC06Pm31664; -.
DR GeneCards; GC06Pn31578; -.
DR GeneCards; GC06Po31578; -.
DR HGNC; HGNC:13918; PRRC2A.
DR HPA; CAB026383; -.
DR MIM; 142580; gene.
DR neXtProt; NX_P48634; -.
DR PharmGKB; PA25263; -.
DR eggNOG; NOG271062; -.
DR HOVERGEN; HBG004820; -.
DR InParanoid; P48634; -.
DR OMA; REKCHER; -.
DR OrthoDB; EOG7DZ8J2; -.
DR PhylomeDB; P48634; -.
DR ChiTaRS; PRRC2A; human.
DR GeneWiki; BAT2; -.
DR GenomeRNAi; 7916; -.
DR NextBio; 30387; -.
DR PRO; PR:P48634; -.
DR Bgee; P48634; -.
DR Genevestigator; P48634; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR009738; BAT2_N.
DR Pfam; PF07001; BAT2_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 2157 Protein PRRC2A.
FT /FTId=PRO_0000064829.
FT REPEAT 41 95 1-1.
FT REPEAT 98 154 1-2.
FT REPEAT 281 337 1-3.
FT REPEAT 337 430 2-1.
FT REPEAT 488 561 2-2.
FT REPEAT 1757 1812 1-4.
FT REPEAT 1916 1965 3-1.
FT REPEAT 1982 2031 3-2.
FT REPEAT 2057 2106 3-3.
FT REGION 41 1812 4 X 57 AA type A repeats.
FT REGION 337 561 2 X type B repeats.
FT REGION 1916 2106 3 X 50 AA type C repeats.
FT COMPBIAS 466 471 Poly-Arg.
FT COMPBIAS 472 475 Poly-Glu.
FT COMPBIAS 658 669 Poly-Gln.
FT COMPBIAS 696 700 Poly-Pro.
FT COMPBIAS 826 833 Poly-Pro.
FT COMPBIAS 913 916 Poly-Pro.
FT COMPBIAS 955 958 Poly-Pro.
FT COMPBIAS 1139 1142 Poly-Pro.
FT COMPBIAS 1239 1244 Poly-Arg.
FT COMPBIAS 1355 1360 Poly-Gly.
FT COMPBIAS 1413 1421 Poly-Gly.
FT COMPBIAS 1451 1457 Poly-Pro.
FT MOD_RES 27 27 N6-acetyllysine.
FT MOD_RES 166 166 Phosphoserine (By similarity).
FT MOD_RES 342 342 Phosphoserine.
FT MOD_RES 350 350 Phosphoserine.
FT MOD_RES 380 380 Phosphoserine.
FT MOD_RES 383 383 Phosphoserine.
FT MOD_RES 456 456 Phosphoserine.
FT MOD_RES 610 610 Phosphothreonine.
FT MOD_RES 759 759 Phosphoserine.
FT MOD_RES 761 761 Phosphoserine.
FT MOD_RES 764 764 Phosphoserine.
FT MOD_RES 808 808 Phosphoserine.
FT MOD_RES 997 997 Phosphothreonine (By similarity).
FT MOD_RES 1004 1004 Phosphoserine (By similarity).
FT MOD_RES 1085 1085 Phosphoserine.
FT MOD_RES 1089 1089 Phosphoserine.
FT MOD_RES 1092 1092 Phosphoserine.
FT MOD_RES 1094 1094 Phosphotyrosine.
FT MOD_RES 1110 1110 Phosphoserine.
FT MOD_RES 1147 1147 Phosphoserine.
FT MOD_RES 1196 1196 N6-acetyllysine.
FT MOD_RES 1219 1219 Phosphoserine.
FT MOD_RES 1306 1306 Phosphoserine.
FT MOD_RES 1353 1353 Phosphothreonine.
FT MOD_RES 2113 2113 Phosphoserine.
FT VAR_SEQ 413 424 Missing (in isoform 2).
FT /FTId=VSP_015099.
FT VAR_SEQ 834 1457 Missing (in isoform 4).
FT /FTId=VSP_030865.
FT VAR_SEQ 1050 1148 RSREFRSYREFRGDDGRGGGTGGPNHPPAPRGRTASETRSE
FT GSEYEEIPKRRRQRGSETGSETHESDLAPSDKEAPTPKEGT
FT LTQVPLAPPPPGAPPSP -> QANSAVTESFEEMMGVEVGQ
FT GDQTTLLLPEAAMPARHGARVQSMRKSPSGAGSGAQKQAAR
FT PMRVIWLLQTRRLPHPRREHSPRSSRSPTTRSPTLHR (in
FT isoform 2 and isoform 3).
FT /FTId=VSP_015100.
FT VAR_SEQ 1155 1177 ARGGRVFTPRGVPSRRGRGGGRP -> CPGVGESSLPEGAI
FT SPGPRRREA (in isoform 2 and isoform 3).
FT /FTId=VSP_015101.
FT VAR_SEQ 1852 1864 AMDSQLHPNSGGF -> SHGLSITSKQWRL (in
FT isoform 2 and isoform 3).
FT /FTId=VSP_015102.
FT VARIANT 57 57 P -> R (in dbSNP:rs1062968).
FT /FTId=VAR_023215.
FT VARIANT 82 82 D -> V (in dbSNP:rs6921213).
FT /FTId=VAR_045992.
FT VARIANT 106 106 P -> L (in dbSNP:rs2280801).
FT /FTId=VAR_023216.
FT VARIANT 477 477 R -> C (in dbSNP:rs17857493).
FT /FTId=VAR_045993.
FT VARIANT 544 544 T -> K (in dbSNP:rs1046080).
FT /FTId=VAR_023217.
FT VARIANT 694 694 Q -> K (in dbSNP:rs2844469).
FT /FTId=VAR_023218.
FT VARIANT 742 742 D -> E (in dbSNP:rs1046081).
FT /FTId=VAR_023219.
FT VARIANT 804 804 R -> C (in dbSNP:rs11538262).
FT /FTId=VAR_045994.
FT VARIANT 1087 1087 T -> I (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035796.
FT VARIANT 1152 1152 R -> H (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035797.
FT VARIANT 1285 1285 G -> A (in dbSNP:rs2736158).
FT /FTId=VAR_023220.
FT VARIANT 1407 1407 S -> N (in dbSNP:rs35464047).
FT /FTId=VAR_045995.
FT VARIANT 1415 1415 G -> A (in dbSNP:rs2857703).
FT /FTId=VAR_023221.
FT VARIANT 1503 1503 L -> P (in dbSNP:rs2272593).
FT /FTId=VAR_023222.
FT VARIANT 1544 1544 G -> D (in dbSNP:rs34175432).
FT /FTId=VAR_045996.
FT VARIANT 1563 1563 R -> Q (in dbSNP:rs11538263).
FT /FTId=VAR_045997.
FT VARIANT 1740 1740 R -> H (in dbSNP:rs1046089).
FT /FTId=VAR_023223.
FT VARIANT 1744 1744 G -> A (in dbSNP:rs2844491).
FT /FTId=VAR_023224.
FT VARIANT 1774 1774 V -> M (in dbSNP:rs11538264).
FT /FTId=VAR_045998.
FT VARIANT 1775 1775 V -> M (in dbSNP:rs11538264).
FT /FTId=VAR_023225.
FT VARIANT 1895 1895 L -> V (in dbSNP:rs3132453).
FT /FTId=VAR_023226.
FT VARIANT 2006 2006 P -> S (in dbSNP:rs10885).
FT /FTId=VAR_023227.
FT VARIANT 2075 2075 R -> W (in dbSNP:rs34137317).
FT /FTId=VAR_056742.
FT VARIANT 2130 2130 P -> L (in dbSNP:rs1046756).
FT /FTId=VAR_023228.
FT CONFLICT 57 57 P -> A (in Ref. 8; CAA78744).
FT CONFLICT 107 123 ESQPLPASQTPASNQPK -> NRTTAGFTDACLQPAE (in
FT Ref. 8; CAA78744).
FT CONFLICT 762 762 G -> L (in Ref. 1; AAA35585/AAA35586).
FT CONFLICT 762 762 G -> R (in Ref. 8; CAA78744).
FT CONFLICT 764 764 S -> L (in Ref. 1; AAA35585/AAA35586 and
FT 8; CAA78744).
FT CONFLICT 846 846 A -> T (in Ref. 8; CAA78744).
FT CONFLICT 902 911 PARGVGSGGQ -> LPASRSGA (in Ref. 1;
FT AAA35585/AAA35586 and 8; CAA78744).
FT CONFLICT 934 934 R -> G (in Ref. 7; AAH42295).
FT CONFLICT 1049 1049 A -> G (in Ref. 1; AAA35585/AAA35586).
FT CONFLICT 1300 1300 R -> P (in Ref. 1; AAA35585/AAA35586).
FT CONFLICT 1461 1461 Missing (in Ref. 8; CAA78744).
FT CONFLICT 1626 1626 S -> T (in Ref. 1; AAA35585/AAA35586).
SQ SEQUENCE 2157 AA; 228863 MW; 7353342E72F0D393 CRC64;
MSDRSGPTAK GKDGKKYSSL NLFDTYKGKS LEIQKPAVAP RHGLQSLGKV AIARRMPPPA
NLPSLKAENK GNDPNVSLVP KDGTGWASKQ EQSDPKSSDA STAQPPESQP LPASQTPASN
QPKRPPAAPE NTPLVPSGVK SWAQASVTHG AHGDGGRASS LLSRFSREEF PTLQAAGDQD
KAAKERESAE QSSGPGPSLR PQNSTTWRDG GGRGPDELEG PDSKLHHGHD PRGGLQPSGP
PQFPPYRGMM PPFMYPPYLP FPPPYGPQGP YRYPTPDGPS RFPRVAGPRG SGPPMRLVEP
VGRPSILKED NLKEFDQLDQ ENDDGWAGAH EEVDYTEKLK FSDEEDGRDS DEEGAEGHRD
SQSASGEERP PEADGKKGNS PNSEPPTPKT AWAETSRPPE TEPGPPAPKP PLPPPHRGPA
GNWGPPGDYP DRGGPPCKPP APEDEDEAWR QRRKQSSSEI SLAVERARRR REEEERRMQE
ERRAACAEKL KRLDEKFGAP DKRLKAEPAA PPAAPSTPAP PPAVPKELPA PPAPPPASAP
TPETEPEEPA QAPPAQSTPT PGVAAAPTLV SGGGSTSSTS SGSFEASPVE PQLPSKEGPE
PPEEVPPPTT PPVPKVEPKG DGIGPTRQPP SQGLGYPKYQ KSLPPRFQRQ QQEQLLKQQQ
QHQWQQHQQG SAPPTPVPPS PPQPVTLGAV PAPQAPPPPP KALYPGALGR PPPMPPMNFD
PRWMMIPPYV DPRLLQGRPP LDFYPPGVHP SGLVPRERSD SGGSSSEPFD RHAPAMLRER
GTPPVDPKLA WVGDVFTATP AEPRPLTSPL RQAADEDDKG MRSETPPVPP PPPYLASYPG
FPENGAPGPP ISRFPLEEPG PRPLPWPPGS DEVAKIQTPP PKKEPPKEET AQLTGPEAGR
KPARGVGSGG QGPPPPRRES RTETRWGPRP GSSRRGIPPE EPGAPPRRAG PIKKPPPPTK
VEELPPKPLE QGDETPKPPK PDPLKITKGK LGGPKETPPN GNLSPAPRLR RDYSYERVGP
TSCRGRGRGE YFARGRGFRG TYGGRGRGAR SREFRSYREF RGDDGRGGGT GGPNHPPAPR
GRTASETRSE GSEYEEIPKR RRQRGSETGS ETHESDLAPS DKEAPTPKEG TLTQVPLAPP
PPGAPPSPAP ARFTARGGRV FTPRGVPSRR GRGGGRPPPQ VCPGWSPPAK SLAPKKPPTG
PLPPSKEPLK EKLIPGPLSP VARGGSNGGS NVGMEDGERP RRRRHGRAQQ QDKPPRFRRL
KQERENAARG SEGKPSLTLP ASAPGPEEAL TTVTVAPAPR RAAAKSPDLS NQNSDQANEE
WETASESSDF TSERRGDKEA PPPVLLTPKA VGTPGGGGGG AVPGISAMSR GDLSQRAKDL
SKRSFSSQRP GMERQNRRPG PGGKAGSSGS SSGGGGGGPG GRTGPGRGDK RSWPSPKNRS
RPPEERPPGL PLPPPPPSSS AVFRLDQVIH SNPAGIQQAL AQLSSRQGSV TAPGGHPRHK
PGLPQAPQGP SPRPPTRYEP QRVNSGLSSD PHFEEPGPMV RGVGGTPRDS AGVSPFPPKR
RERPPRKPEL LQEESLPPPH SSGFLGSKPE GPGPQAESRD TGTEALTPHI WNRLHTATSR
KSYRPSSMEP WMEPLSPFED VAGTEMSQSD SGVDLSGDSQ VSSGPCSQRS SPDGGLKGAA
EGPPKRPGGS SPLNAVPCEG PPGSEPPRRP PPAPHDGDRK ELPREQPLPP GPIGTERSQR
TDRGTEPGPI RPSHRPGPPV QFGTSDKDSD LRLVVGDSLK AEKELTASVT EAIPVSRDWE
LLPSAAASAE PQSKNLDSGH CVPEPSSSGQ RLYPEVFYGS AGPSSSQISG GAMDSQLHPN
SGGFRPGTPS LHPYRSQPLY LPPGPAPPSA LLSGLALKGQ FLDFSTMQAT ELGKLPAGGV
LYPPPSFLYS PAFCPSPLPD TSLLQVRQDL PSPSDFYSTP LQPGGQSGFL PSGAPAQQML
LPMVDSQLPV VNFGSLPPAP PPAPPPLSLL PVGPALQPPS LAVRPPPAPA TRVLPSPARP
FPASLGRAEL HPVELKPFQD YQKLSSNLGG PGSSRTPPTG RSFSGLNSRL KATPSTYSGV
FRTQRVDLYQ QASPPDALRW IPKPWERTGP PPREGPSRRA EEPGSRGDKE PGLPPPR
//
ID PRC2A_HUMAN Reviewed; 2157 AA.
AC P48634; B0UX77; B0UZE9; B0UZL3; O95875; Q05BK4; Q4LE37; Q5SQ29;
read moreAC Q5SQ30; Q5ST84; Q5STX6; Q5STX7; Q68DW9; Q6P9P7; Q6PIN1; Q8MGQ9;
AC Q96QC6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Protein PRRC2A;
DE AltName: Full=HLA-B-associated transcript 2;
DE AltName: Full=Large proline-rich protein BAT2;
DE AltName: Full=Proline-rich and coiled-coil-containing protein 2A;
DE AltName: Full=Protein G2;
GN Name=PRRC2A; Synonyms=BAT2, G2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND VARIANTS
RP ARG-57; GLU-742; PRO-1503 AND VAL-1895.
RC TISSUE=T-cell;
RX PubMed=2156268; DOI=10.1073/pnas.87.6.2374;
RA Banerji J., Sands J., Strominger J.L., Spies T.;
RT "A gene pair from the human major histocompatibility complex encodes
RT large proline-rich proteins with multiple repeated motifs and a single
RT ubiquitin-like domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2374-2378(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS
RP LEU-106; LYS-544; PRO-1503 AND VAL-1895.
RC TISSUE=Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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], AND VARIANTS LYS-544;
RP ALA-1285; PRO-1503; HIS-1740; VAL-1895 AND LEU-2130.
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-544;
RP PRO-1503 AND VAL-1895.
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LEU-106;
RP LYS-544; PRO-1503; HIS-1740; VAL-1895 AND SER-2006.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-544;
RP PRO-1503; HIS-1740 AND VAL-1895.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP CYS-477; LYS-544; PRO-1503 AND VAL-1895.
RC TISSUE=Lymph, Placenta, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1874 (ISOFORM 3), AND VARIANTS
RP LYS-544; LYS-694; ALA-1415; PRO-1503 AND ALA-1744.
RX PubMed=8499947; DOI=10.1038/ng0293-137;
RA Iris F.J.M., Bougueleret L., Prieur S., Caterina D., Primas G.,
RA Perrot V., Jurka J., Rodriguez-Tome P., Claverie J.-M., Dausset J.,
RA Cohen D.;
RT "Dense Alu clustering and a potential new member of the NF kappa B
RT family within a 90 kilobase HLA class III segment.";
RL Nat. Genet. 3:137-145(1993).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 871-2157 (ISOFORM 1), AND
RP VARIANTS PRO-1503 AND VAL-1895.
RC TISSUE=Uterine endothelium;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP FUNCTION.
RX PubMed=14667819; DOI=10.1016/S0888-7543(03)00235-0;
RA Lehner B., Semple J.I., Brown S.E., Counsell D., Campbell R.D.,
RA Sanderson C.M.;
RT "Analysis of a high-throughput yeast two-hybrid system and its use to
RT predict the function of intracellular proteins encoded within the
RT human MHC class III region.";
RL Genomics 83:153-167(2004).
RN [11]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15752841; DOI=10.1016/j.vaccine.2004.08.003;
RA Schneiders A., Thiel S., Winkler J., Moeller P., Koch N.;
RT "Antibodies generated by a novel DNA vaccination identify the MHC
RT class III encoded BAT2 polypeptide.";
RL Vaccine 23:2540-2550(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342; SER-350 AND
RP SER-1089, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1219, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-383; SER-456;
RP THR-610; SER-759; SER-761; SER-764; SER-1085; SER-1089; SER-1092;
RP TYR-1094; SER-1147 AND SER-1306, AND MASS SPECTROMETRY.
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 [16]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-456; THR-610;
RP SER-761 AND SER-1089, AND MASS SPECTROMETRY.
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-1196, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-808; SER-1219;
RP THR-1353 AND SER-2113, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342; SER-350; SER-380;
RP SER-1089; SER-1110 AND SER-1219, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-1087 AND HIS-1152.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May play a role in the regulation of pre-mRNA splicing.
CC -!- INTERACTION:
CC P54253:ATXN1; NbExp=4; IntAct=EBI-347545, EBI-930964;
CC P05412:JUN; NbExp=2; IntAct=EBI-347545, EBI-852823;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P48634-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48634-2; Sequence=VSP_015099, VSP_015100, VSP_015101,
CC VSP_015102;
CC Name=3;
CC IsoId=P48634-3; Sequence=VSP_015100, VSP_015101, VSP_015102;
CC Note=Ref.8 (CAA78744) sequence is in conflict in position:
CC 1082:M->L;
CC Name=4;
CC IsoId=P48634-4; Sequence=VSP_030865;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Limited to cell-lines of leukemic origin.
CC -!- DEVELOPMENTAL STAGE: Broadly expressed during the 11th week of
CC gestation, with highest levels in the central nervous system,
CC spinal ganglia, osteoblasts and osteocytes (at protein level).
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35585.1; Type=Frameshift; Positions=38, 58;
CC Sequence=AAA35586.1; Type=Frameshift; Positions=38, 58;
CC Sequence=BAE06116.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=CAA78744.1; Type=Frameshift; Positions=38, 58;
CC -----------------------------------------------------------------------
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DR EMBL; M33509; AAA35585.1; ALT_FRAME; mRNA.
DR EMBL; M33518; AAA35586.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M33512; AAA35586.1; JOINED; Genomic_DNA.
DR EMBL; AB210034; BAE06116.1; ALT_INIT; mRNA.
DR EMBL; AF129756; AAD18086.1; -; Genomic_DNA.
DR EMBL; CR354443; CAQ06970.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63391.1; -; Genomic_DNA.
DR EMBL; AL662847; CAI17698.2; -; Genomic_DNA.
DR EMBL; AL662801; CAI18313.1; -; Genomic_DNA.
DR EMBL; AL805934; CAI18500.1; -; Genomic_DNA.
DR EMBL; BX511262; CAI95572.1; -; Genomic_DNA.
DR EMBL; CR753892; CAQ06959.1; -; Genomic_DNA.
DR EMBL; CR759761; CAQ10847.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03452.1; -; Genomic_DNA.
DR EMBL; BC030127; AAH30127.1; -; mRNA.
DR EMBL; BC032134; AAH32134.1; -; mRNA.
DR EMBL; BC042295; AAH42295.1; -; mRNA.
DR EMBL; BC060668; AAH60668.1; -; mRNA.
DR EMBL; Z15025; CAA78744.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CR749245; CAH18101.1; -; mRNA.
DR PIR; B35098; B35098.
DR PIR; S37671; S37671.
DR RefSeq; NP_004629.3; NM_004638.3.
DR RefSeq; NP_542417.2; NM_080686.2.
DR UniGene; Hs.123239; -.
DR UniGene; Hs.436093; -.
DR ProteinModelPortal; P48634; -.
DR IntAct; P48634; 32.
DR MINT; MINT-1032109; -.
DR STRING; 9606.ENSP00000404619; -.
DR DMDM; 296439424; -.
DR PaxDb; P48634; -.
DR PRIDE; P48634; -.
DR Ensembl; ENST00000376007; ENSP00000365175; ENSG00000204469.
DR Ensembl; ENST00000376033; ENSP00000365201; ENSG00000204469.
DR Ensembl; ENST00000383455; ENSP00000372947; ENSG00000206427.
DR Ensembl; ENST00000383464; ENSP00000372956; ENSG00000206427.
DR Ensembl; ENST00000414956; ENSP00000404619; ENSG00000226618.
DR Ensembl; ENST00000416335; ENSP00000415182; ENSG00000231370.
DR Ensembl; ENST00000422962; ENSP00000415363; ENSG00000231825.
DR Ensembl; ENST00000428775; ENSP00000387910; ENSG00000225164.
DR Ensembl; ENST00000430737; ENSP00000413977; ENSG00000231825.
DR Ensembl; ENST00000432252; ENSP00000408226; ENSG00000225748.
DR Ensembl; ENST00000435971; ENSP00000409444; ENSG00000225164.
DR Ensembl; ENST00000439762; ENSP00000400540; ENSG00000231370.
DR Ensembl; ENST00000454306; ENSP00000387477; ENSG00000225748.
DR Ensembl; ENST00000458561; ENSP00000396812; ENSG00000226618.
DR GeneID; 7916; -.
DR KEGG; hsa:7916; -.
DR UCSC; uc003nvb.4; human.
DR CTD; 7916; -.
DR GeneCards; GC06P031719; -.
DR GeneCards; GC06Pj31575; -.
DR GeneCards; GC06Pk31570; -.
DR GeneCards; GC06Pl31627; -.
DR GeneCards; GC06Pm31664; -.
DR GeneCards; GC06Pn31578; -.
DR GeneCards; GC06Po31578; -.
DR HGNC; HGNC:13918; PRRC2A.
DR HPA; CAB026383; -.
DR MIM; 142580; gene.
DR neXtProt; NX_P48634; -.
DR PharmGKB; PA25263; -.
DR eggNOG; NOG271062; -.
DR HOVERGEN; HBG004820; -.
DR InParanoid; P48634; -.
DR OMA; REKCHER; -.
DR OrthoDB; EOG7DZ8J2; -.
DR PhylomeDB; P48634; -.
DR ChiTaRS; PRRC2A; human.
DR GeneWiki; BAT2; -.
DR GenomeRNAi; 7916; -.
DR NextBio; 30387; -.
DR PRO; PR:P48634; -.
DR Bgee; P48634; -.
DR Genevestigator; P48634; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR009738; BAT2_N.
DR Pfam; PF07001; BAT2_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 2157 Protein PRRC2A.
FT /FTId=PRO_0000064829.
FT REPEAT 41 95 1-1.
FT REPEAT 98 154 1-2.
FT REPEAT 281 337 1-3.
FT REPEAT 337 430 2-1.
FT REPEAT 488 561 2-2.
FT REPEAT 1757 1812 1-4.
FT REPEAT 1916 1965 3-1.
FT REPEAT 1982 2031 3-2.
FT REPEAT 2057 2106 3-3.
FT REGION 41 1812 4 X 57 AA type A repeats.
FT REGION 337 561 2 X type B repeats.
FT REGION 1916 2106 3 X 50 AA type C repeats.
FT COMPBIAS 466 471 Poly-Arg.
FT COMPBIAS 472 475 Poly-Glu.
FT COMPBIAS 658 669 Poly-Gln.
FT COMPBIAS 696 700 Poly-Pro.
FT COMPBIAS 826 833 Poly-Pro.
FT COMPBIAS 913 916 Poly-Pro.
FT COMPBIAS 955 958 Poly-Pro.
FT COMPBIAS 1139 1142 Poly-Pro.
FT COMPBIAS 1239 1244 Poly-Arg.
FT COMPBIAS 1355 1360 Poly-Gly.
FT COMPBIAS 1413 1421 Poly-Gly.
FT COMPBIAS 1451 1457 Poly-Pro.
FT MOD_RES 27 27 N6-acetyllysine.
FT MOD_RES 166 166 Phosphoserine (By similarity).
FT MOD_RES 342 342 Phosphoserine.
FT MOD_RES 350 350 Phosphoserine.
FT MOD_RES 380 380 Phosphoserine.
FT MOD_RES 383 383 Phosphoserine.
FT MOD_RES 456 456 Phosphoserine.
FT MOD_RES 610 610 Phosphothreonine.
FT MOD_RES 759 759 Phosphoserine.
FT MOD_RES 761 761 Phosphoserine.
FT MOD_RES 764 764 Phosphoserine.
FT MOD_RES 808 808 Phosphoserine.
FT MOD_RES 997 997 Phosphothreonine (By similarity).
FT MOD_RES 1004 1004 Phosphoserine (By similarity).
FT MOD_RES 1085 1085 Phosphoserine.
FT MOD_RES 1089 1089 Phosphoserine.
FT MOD_RES 1092 1092 Phosphoserine.
FT MOD_RES 1094 1094 Phosphotyrosine.
FT MOD_RES 1110 1110 Phosphoserine.
FT MOD_RES 1147 1147 Phosphoserine.
FT MOD_RES 1196 1196 N6-acetyllysine.
FT MOD_RES 1219 1219 Phosphoserine.
FT MOD_RES 1306 1306 Phosphoserine.
FT MOD_RES 1353 1353 Phosphothreonine.
FT MOD_RES 2113 2113 Phosphoserine.
FT VAR_SEQ 413 424 Missing (in isoform 2).
FT /FTId=VSP_015099.
FT VAR_SEQ 834 1457 Missing (in isoform 4).
FT /FTId=VSP_030865.
FT VAR_SEQ 1050 1148 RSREFRSYREFRGDDGRGGGTGGPNHPPAPRGRTASETRSE
FT GSEYEEIPKRRRQRGSETGSETHESDLAPSDKEAPTPKEGT
FT LTQVPLAPPPPGAPPSP -> QANSAVTESFEEMMGVEVGQ
FT GDQTTLLLPEAAMPARHGARVQSMRKSPSGAGSGAQKQAAR
FT PMRVIWLLQTRRLPHPRREHSPRSSRSPTTRSPTLHR (in
FT isoform 2 and isoform 3).
FT /FTId=VSP_015100.
FT VAR_SEQ 1155 1177 ARGGRVFTPRGVPSRRGRGGGRP -> CPGVGESSLPEGAI
FT SPGPRRREA (in isoform 2 and isoform 3).
FT /FTId=VSP_015101.
FT VAR_SEQ 1852 1864 AMDSQLHPNSGGF -> SHGLSITSKQWRL (in
FT isoform 2 and isoform 3).
FT /FTId=VSP_015102.
FT VARIANT 57 57 P -> R (in dbSNP:rs1062968).
FT /FTId=VAR_023215.
FT VARIANT 82 82 D -> V (in dbSNP:rs6921213).
FT /FTId=VAR_045992.
FT VARIANT 106 106 P -> L (in dbSNP:rs2280801).
FT /FTId=VAR_023216.
FT VARIANT 477 477 R -> C (in dbSNP:rs17857493).
FT /FTId=VAR_045993.
FT VARIANT 544 544 T -> K (in dbSNP:rs1046080).
FT /FTId=VAR_023217.
FT VARIANT 694 694 Q -> K (in dbSNP:rs2844469).
FT /FTId=VAR_023218.
FT VARIANT 742 742 D -> E (in dbSNP:rs1046081).
FT /FTId=VAR_023219.
FT VARIANT 804 804 R -> C (in dbSNP:rs11538262).
FT /FTId=VAR_045994.
FT VARIANT 1087 1087 T -> I (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035796.
FT VARIANT 1152 1152 R -> H (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035797.
FT VARIANT 1285 1285 G -> A (in dbSNP:rs2736158).
FT /FTId=VAR_023220.
FT VARIANT 1407 1407 S -> N (in dbSNP:rs35464047).
FT /FTId=VAR_045995.
FT VARIANT 1415 1415 G -> A (in dbSNP:rs2857703).
FT /FTId=VAR_023221.
FT VARIANT 1503 1503 L -> P (in dbSNP:rs2272593).
FT /FTId=VAR_023222.
FT VARIANT 1544 1544 G -> D (in dbSNP:rs34175432).
FT /FTId=VAR_045996.
FT VARIANT 1563 1563 R -> Q (in dbSNP:rs11538263).
FT /FTId=VAR_045997.
FT VARIANT 1740 1740 R -> H (in dbSNP:rs1046089).
FT /FTId=VAR_023223.
FT VARIANT 1744 1744 G -> A (in dbSNP:rs2844491).
FT /FTId=VAR_023224.
FT VARIANT 1774 1774 V -> M (in dbSNP:rs11538264).
FT /FTId=VAR_045998.
FT VARIANT 1775 1775 V -> M (in dbSNP:rs11538264).
FT /FTId=VAR_023225.
FT VARIANT 1895 1895 L -> V (in dbSNP:rs3132453).
FT /FTId=VAR_023226.
FT VARIANT 2006 2006 P -> S (in dbSNP:rs10885).
FT /FTId=VAR_023227.
FT VARIANT 2075 2075 R -> W (in dbSNP:rs34137317).
FT /FTId=VAR_056742.
FT VARIANT 2130 2130 P -> L (in dbSNP:rs1046756).
FT /FTId=VAR_023228.
FT CONFLICT 57 57 P -> A (in Ref. 8; CAA78744).
FT CONFLICT 107 123 ESQPLPASQTPASNQPK -> NRTTAGFTDACLQPAE (in
FT Ref. 8; CAA78744).
FT CONFLICT 762 762 G -> L (in Ref. 1; AAA35585/AAA35586).
FT CONFLICT 762 762 G -> R (in Ref. 8; CAA78744).
FT CONFLICT 764 764 S -> L (in Ref. 1; AAA35585/AAA35586 and
FT 8; CAA78744).
FT CONFLICT 846 846 A -> T (in Ref. 8; CAA78744).
FT CONFLICT 902 911 PARGVGSGGQ -> LPASRSGA (in Ref. 1;
FT AAA35585/AAA35586 and 8; CAA78744).
FT CONFLICT 934 934 R -> G (in Ref. 7; AAH42295).
FT CONFLICT 1049 1049 A -> G (in Ref. 1; AAA35585/AAA35586).
FT CONFLICT 1300 1300 R -> P (in Ref. 1; AAA35585/AAA35586).
FT CONFLICT 1461 1461 Missing (in Ref. 8; CAA78744).
FT CONFLICT 1626 1626 S -> T (in Ref. 1; AAA35585/AAA35586).
SQ SEQUENCE 2157 AA; 228863 MW; 7353342E72F0D393 CRC64;
MSDRSGPTAK GKDGKKYSSL NLFDTYKGKS LEIQKPAVAP RHGLQSLGKV AIARRMPPPA
NLPSLKAENK GNDPNVSLVP KDGTGWASKQ EQSDPKSSDA STAQPPESQP LPASQTPASN
QPKRPPAAPE NTPLVPSGVK SWAQASVTHG AHGDGGRASS LLSRFSREEF PTLQAAGDQD
KAAKERESAE QSSGPGPSLR PQNSTTWRDG GGRGPDELEG PDSKLHHGHD PRGGLQPSGP
PQFPPYRGMM PPFMYPPYLP FPPPYGPQGP YRYPTPDGPS RFPRVAGPRG SGPPMRLVEP
VGRPSILKED NLKEFDQLDQ ENDDGWAGAH EEVDYTEKLK FSDEEDGRDS DEEGAEGHRD
SQSASGEERP PEADGKKGNS PNSEPPTPKT AWAETSRPPE TEPGPPAPKP PLPPPHRGPA
GNWGPPGDYP DRGGPPCKPP APEDEDEAWR QRRKQSSSEI SLAVERARRR REEEERRMQE
ERRAACAEKL KRLDEKFGAP DKRLKAEPAA PPAAPSTPAP PPAVPKELPA PPAPPPASAP
TPETEPEEPA QAPPAQSTPT PGVAAAPTLV SGGGSTSSTS SGSFEASPVE PQLPSKEGPE
PPEEVPPPTT PPVPKVEPKG DGIGPTRQPP SQGLGYPKYQ KSLPPRFQRQ QQEQLLKQQQ
QHQWQQHQQG SAPPTPVPPS PPQPVTLGAV PAPQAPPPPP KALYPGALGR PPPMPPMNFD
PRWMMIPPYV DPRLLQGRPP LDFYPPGVHP SGLVPRERSD SGGSSSEPFD RHAPAMLRER
GTPPVDPKLA WVGDVFTATP AEPRPLTSPL RQAADEDDKG MRSETPPVPP PPPYLASYPG
FPENGAPGPP ISRFPLEEPG PRPLPWPPGS DEVAKIQTPP PKKEPPKEET AQLTGPEAGR
KPARGVGSGG QGPPPPRRES RTETRWGPRP GSSRRGIPPE EPGAPPRRAG PIKKPPPPTK
VEELPPKPLE QGDETPKPPK PDPLKITKGK LGGPKETPPN GNLSPAPRLR RDYSYERVGP
TSCRGRGRGE YFARGRGFRG TYGGRGRGAR SREFRSYREF RGDDGRGGGT GGPNHPPAPR
GRTASETRSE GSEYEEIPKR RRQRGSETGS ETHESDLAPS DKEAPTPKEG TLTQVPLAPP
PPGAPPSPAP ARFTARGGRV FTPRGVPSRR GRGGGRPPPQ VCPGWSPPAK SLAPKKPPTG
PLPPSKEPLK EKLIPGPLSP VARGGSNGGS NVGMEDGERP RRRRHGRAQQ QDKPPRFRRL
KQERENAARG SEGKPSLTLP ASAPGPEEAL TTVTVAPAPR RAAAKSPDLS NQNSDQANEE
WETASESSDF TSERRGDKEA PPPVLLTPKA VGTPGGGGGG AVPGISAMSR GDLSQRAKDL
SKRSFSSQRP GMERQNRRPG PGGKAGSSGS SSGGGGGGPG GRTGPGRGDK RSWPSPKNRS
RPPEERPPGL PLPPPPPSSS AVFRLDQVIH SNPAGIQQAL AQLSSRQGSV TAPGGHPRHK
PGLPQAPQGP SPRPPTRYEP QRVNSGLSSD PHFEEPGPMV RGVGGTPRDS AGVSPFPPKR
RERPPRKPEL LQEESLPPPH SSGFLGSKPE GPGPQAESRD TGTEALTPHI WNRLHTATSR
KSYRPSSMEP WMEPLSPFED VAGTEMSQSD SGVDLSGDSQ VSSGPCSQRS SPDGGLKGAA
EGPPKRPGGS SPLNAVPCEG PPGSEPPRRP PPAPHDGDRK ELPREQPLPP GPIGTERSQR
TDRGTEPGPI RPSHRPGPPV QFGTSDKDSD LRLVVGDSLK AEKELTASVT EAIPVSRDWE
LLPSAAASAE PQSKNLDSGH CVPEPSSSGQ RLYPEVFYGS AGPSSSQISG GAMDSQLHPN
SGGFRPGTPS LHPYRSQPLY LPPGPAPPSA LLSGLALKGQ FLDFSTMQAT ELGKLPAGGV
LYPPPSFLYS PAFCPSPLPD TSLLQVRQDL PSPSDFYSTP LQPGGQSGFL PSGAPAQQML
LPMVDSQLPV VNFGSLPPAP PPAPPPLSLL PVGPALQPPS LAVRPPPAPA TRVLPSPARP
FPASLGRAEL HPVELKPFQD YQKLSSNLGG PGSSRTPPTG RSFSGLNSRL KATPSTYSGV
FRTQRVDLYQ QASPPDALRW IPKPWERTGP PPREGPSRRA EEPGSRGDKE PGLPPPR
//
MIM
142580
*RECORD*
*FIELD* NO
142580
*FIELD* TI
*142580 PROLINE-RICH COILED-COIL PROTEIN 2A; PRRC2A
;;HLA-B-ASSOCIATED TRANSCRIPT 2; BAT2;;
read moreD6S51E
*FIELD* TX
CLONING
Banerji et al. (1990) determined the complete cDNA sequences of BAT2 and
BAT3 (142590). BAT2 and BAT3 encode deduced proline-rich proteins of
2,142 and 1,132 residues with molecular masses of approximately 228 and
110 kD, respectively. The BAT2 sequence contains 4 RGD motifs, of which
3 are clustered within a 95-amino acid segment. BAT3 contains an
N-terminal ubiquitin-like domain.
MAPPING
Banerji et al. (1990) stated that the BAT2 and BAT3 genes map within the
class III region of the major histocompatibility complex on chromosome
6p21.3.
*FIELD* RF
1. Banerji, J.; Sands, J.; Strominger, J. L.; Spies, T.: A gene pair
from the human major histocompatibility complex encodes large proline-rich
proteins with multiple repeated motifs and a single ubiquitin-like
domain. Proc. Nat. Acad. Sci. 87: 2374-2378, 1990.
*FIELD* CD
Victor A. McKusick: 2/2/1989
*FIELD* ED
carol: 01/08/2014
alopez: 8/15/2011
carol: 7/18/2001
terry: 2/28/2000
carol: 2/22/1999
alopez: 9/5/1997
terry: 10/7/1994
supermim: 3/16/1992
supermim: 5/11/1990
supermim: 3/20/1990
carol: 3/9/1990
ddp: 10/27/1989
*RECORD*
*FIELD* NO
142580
*FIELD* TI
*142580 PROLINE-RICH COILED-COIL PROTEIN 2A; PRRC2A
;;HLA-B-ASSOCIATED TRANSCRIPT 2; BAT2;;
read moreD6S51E
*FIELD* TX
CLONING
Banerji et al. (1990) determined the complete cDNA sequences of BAT2 and
BAT3 (142590). BAT2 and BAT3 encode deduced proline-rich proteins of
2,142 and 1,132 residues with molecular masses of approximately 228 and
110 kD, respectively. The BAT2 sequence contains 4 RGD motifs, of which
3 are clustered within a 95-amino acid segment. BAT3 contains an
N-terminal ubiquitin-like domain.
MAPPING
Banerji et al. (1990) stated that the BAT2 and BAT3 genes map within the
class III region of the major histocompatibility complex on chromosome
6p21.3.
*FIELD* RF
1. Banerji, J.; Sands, J.; Strominger, J. L.; Spies, T.: A gene pair
from the human major histocompatibility complex encodes large proline-rich
proteins with multiple repeated motifs and a single ubiquitin-like
domain. Proc. Nat. Acad. Sci. 87: 2374-2378, 1990.
*FIELD* CD
Victor A. McKusick: 2/2/1989
*FIELD* ED
carol: 01/08/2014
alopez: 8/15/2011
carol: 7/18/2001
terry: 2/28/2000
carol: 2/22/1999
alopez: 9/5/1997
terry: 10/7/1994
supermim: 3/16/1992
supermim: 5/11/1990
supermim: 3/20/1990
carol: 3/9/1990
ddp: 10/27/1989