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P48634 (PRC2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein PRRC2A
Alternative name(s):
HLA-B-associated transcript 2
Large proline-rich protein BAT2
Proline-rich and coiled-coil-containing protein 2A
Protein G2
Gene names
Name:PRRC2A
Synonyms:BAT2, G2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2157 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the regulation of pre-mRNA splicing. Ref.10

Subcellular location

Cytoplasm. Nucleus Ref.11.

Tissue specificity

Limited to cell-lines of leukemic origin.

Developmental stage

Broadly expressed during the 11th week of gestation, with highest levels in the central nervous system, spinal ganglia, osteoblasts and osteocytes (at protein level). Ref.11

Sequence caution

The sequence AAA35585.1 differs from that shown. Reason: Frameshift at positions 38 and 58.

The sequence AAA35586.1 differs from that shown. Reason: Frameshift at positions 38 and 58.

The sequence BAE06116.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA78744.1 differs from that shown. Reason: Frameshift at positions 38 and 58.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48634-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P48634-2)

The sequence of this isoform differs from the canonical sequence as follows:
     413-424: Missing.
     1050-1148: RSREFRSYRE...PPPPGAPPSP → QANSAVTESF...PTTRSPTLHR
     1155-1177: ARGGRVFTPRGVPSRRGRGGGRP → CPGVGESSLPEGAISPGPRRREA
     1852-1864: AMDSQLHPNSGGF → SHGLSITSKQWRL
Isoform 3 (identifier: P48634-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1050-1148: RSREFRSYRE...PPPPGAPPSP → QANSAVTESF...PTTRSPTLHR
     1155-1177: ARGGRVFTPRGVPSRRGRGGGRP → CPGVGESSLPEGAISPGPRRREA
     1852-1864: AMDSQLHPNSGGF → SHGLSITSKQWRL
Isoform 4 (identifier: P48634-4)

The sequence of this isoform differs from the canonical sequence as follows:
     834-1457: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21572157Protein PRRC2A
PRO_0000064829

Regions

Repeat41 – 95551-1
Repeat98 – 154571-2
Repeat281 – 337571-3
Repeat337 – 430942-1
Repeat488 – 561742-2
Repeat1757 – 1812561-4
Repeat1916 – 1965503-1
Repeat1982 – 2031503-2
Repeat2057 – 2106503-3
Region41 – 181217724 X 57 AA type A repeats
Region337 – 5612252 X type B repeats
Region1916 – 21061913 X 50 AA type C repeats
Compositional bias466 – 4716Poly-Arg
Compositional bias472 – 4754Poly-Glu
Compositional bias658 – 66912Poly-Gln
Compositional bias696 – 7005Poly-Pro
Compositional bias826 – 8338Poly-Pro
Compositional bias913 – 9164Poly-Pro
Compositional bias955 – 9584Poly-Pro
Compositional bias1139 – 11424Poly-Pro
Compositional bias1239 – 12446Poly-Arg
Compositional bias1355 – 13606Poly-Gly
Compositional bias1413 – 14219Poly-Gly
Compositional bias1451 – 14577Poly-Pro

Amino acid modifications

Modified residue271N6-acetyllysine Ref.18
Modified residue351N6-acetyllysine By similarity
Modified residue1661Phosphoserine By similarity
Modified residue3421Phosphoserine Ref.12 Ref.21
Modified residue3501Phosphoserine Ref.12 Ref.21
Modified residue3801Phosphoserine Ref.15 Ref.17 Ref.19 Ref.21
Modified residue3831Phosphoserine Ref.15
Modified residue4561Phosphoserine Ref.15 Ref.17
Modified residue6101Phosphothreonine Ref.15 Ref.17
Modified residue7591Phosphoserine Ref.15
Modified residue7611Phosphoserine Ref.15 Ref.17
Modified residue7641Phosphoserine Ref.15
Modified residue8081Phosphoserine Ref.19
Modified residue9971Phosphothreonine By similarity
Modified residue10041Phosphoserine By similarity
Modified residue10851Phosphoserine Ref.15
Modified residue10891Phosphoserine Ref.15 Ref.17
Modified residue10921Phosphoserine Ref.15
Modified residue10941Phosphotyrosine Ref.15
Modified residue11101Phosphoserine Ref.21
Modified residue11471Phosphoserine Ref.15
Modified residue11961N6-acetyllysine Ref.18
Modified residue12191Phosphoserine Ref.14 Ref.19 Ref.21
Modified residue13061Phosphoserine Ref.15
Modified residue13531Phosphothreonine Ref.19
Modified residue21131Phosphoserine Ref.19

Natural variations

Alternative sequence413 – 42412Missing in isoform 2.
VSP_015099
Alternative sequence834 – 1457624Missing in isoform 4.
VSP_030865
Alternative sequence1050 – 114899RSREF…APPSP → QANSAVTESFEEMMGVEVGQ GDQTTLLLPEAAMPARHGAR VQSMRKSPSGAGSGAQKQAA RPMRVIWLLQTRRLPHPRRE HSPRSSRSPTTRSPTLHR in isoform 2 and isoform 3.
VSP_015100
Alternative sequence1155 – 117723ARGGR…GGGRP → CPGVGESSLPEGAISPGPRR REA in isoform 2 and isoform 3.
VSP_015101
Alternative sequence1852 – 186413AMDSQ…NSGGF → SHGLSITSKQWRL in isoform 2 and isoform 3.
VSP_015102
Natural variant571P → R. Ref.1
Corresponds to variant rs1062968 [ dbSNP | Ensembl ].
VAR_023215
Natural variant821D → V.
Corresponds to variant rs6921213 [ dbSNP | Ensembl ].
VAR_045992
Natural variant1061P → L. Ref.2 Ref.5
Corresponds to variant rs2280801 [ dbSNP | Ensembl ].
VAR_023216
Natural variant4771R → C. Ref.7
Corresponds to variant rs17857493 [ dbSNP | Ensembl ].
VAR_045993
Natural variant5441T → K. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Corresponds to variant rs1046080 [ dbSNP | Ensembl ].
VAR_023217
Natural variant6941Q → K. Ref.8
Corresponds to variant rs2844469 [ dbSNP | Ensembl ].
VAR_023218
Natural variant7421D → E. Ref.1
Corresponds to variant rs1046081 [ dbSNP | Ensembl ].
VAR_023219
Natural variant8041R → C.
Corresponds to variant rs11538262 [ dbSNP | Ensembl ].
VAR_045994
Natural variant10871T → I in a breast cancer sample; somatic mutation. Ref.22
VAR_035796
Natural variant11521R → H in a breast cancer sample; somatic mutation. Ref.22
VAR_035797
Natural variant12851G → A. Ref.3
Corresponds to variant rs2736158 [ dbSNP | Ensembl ].
VAR_023220
Natural variant14071S → N.
Corresponds to variant rs35464047 [ dbSNP | Ensembl ].
VAR_045995
Natural variant14151G → A. Ref.8
Corresponds to variant rs2857703 [ dbSNP | Ensembl ].
VAR_023221
Natural variant15031L → P. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Corresponds to variant rs2272593 [ dbSNP | Ensembl ].
VAR_023222
Natural variant15441G → D.
Corresponds to variant rs34175432 [ dbSNP | Ensembl ].
VAR_045996
Natural variant15631R → Q.
Corresponds to variant rs11538263 [ dbSNP | Ensembl ].
VAR_045997
Natural variant17401R → H. Ref.3 Ref.5 Ref.6
Corresponds to variant rs1046089 [ dbSNP | Ensembl ].
VAR_023223
Natural variant17441G → A. Ref.8
Corresponds to variant rs2844491 [ dbSNP | Ensembl ].
VAR_023224
Natural variant17741V → M.
Corresponds to variant rs11538264 [ dbSNP | Ensembl ].
VAR_045998
Natural variant17751V → M.
Corresponds to variant rs11538264 [ dbSNP | Ensembl ].
VAR_023225
Natural variant18951L → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.9
Corresponds to variant rs3132453 [ dbSNP | Ensembl ].
VAR_023226
Natural variant20061P → S. Ref.5
Corresponds to variant rs10885 [ dbSNP | Ensembl ].
VAR_023227
Natural variant20751R → W.
Corresponds to variant rs34137317 [ dbSNP | Ensembl ].
VAR_056742
Natural variant21301P → L. Ref.3
Corresponds to variant rs1046756 [ dbSNP | Ensembl ].
VAR_023228

Experimental info

Sequence conflict571P → A in CAA78744. Ref.8
Sequence conflict107 – 12317ESQPL…SNQPK → NRTTAGFTDACLQPAE in CAA78744. Ref.8
Sequence conflict7621G → L in AAA35585. Ref.1
Sequence conflict7621G → L in AAA35586. Ref.1
Sequence conflict7621G → R in CAA78744. Ref.8
Sequence conflict7641S → L in AAA35585. Ref.1
Sequence conflict7641S → L in AAA35586. Ref.1
Sequence conflict7641S → L in CAA78744. Ref.8
Sequence conflict8461A → T in CAA78744. Ref.8
Sequence conflict902 – 91110PARGVGSGGQ → LPASRSGA in AAA35585. Ref.1
Sequence conflict902 – 91110PARGVGSGGQ → LPASRSGA in AAA35586. Ref.1
Sequence conflict902 – 91110PARGVGSGGQ → LPASRSGA in CAA78744. Ref.8
Sequence conflict9341R → G in AAH42295. Ref.7
Sequence conflict10491A → G in AAA35585. Ref.1
Sequence conflict10491A → G in AAA35586. Ref.1
Sequence conflict13001R → P in AAA35585. Ref.1
Sequence conflict13001R → P in AAA35586. Ref.1
Sequence conflict14611Missing in CAA78744. Ref.8
Sequence conflict16261S → T in AAA35585. Ref.1
Sequence conflict16261S → T in AAA35586. Ref.1
Isoform 3:
Sequence conflict10821M → L in CAA78744. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 7353342E72F0D393

FASTA2,157228,863
        10         20         30         40         50         60 
MSDRSGPTAK GKDGKKYSSL NLFDTYKGKS LEIQKPAVAP RHGLQSLGKV AIARRMPPPA 

        70         80         90        100        110        120 
NLPSLKAENK GNDPNVSLVP KDGTGWASKQ EQSDPKSSDA STAQPPESQP LPASQTPASN 

       130        140        150        160        170        180 
QPKRPPAAPE NTPLVPSGVK SWAQASVTHG AHGDGGRASS LLSRFSREEF PTLQAAGDQD 

       190        200        210        220        230        240 
KAAKERESAE QSSGPGPSLR PQNSTTWRDG GGRGPDELEG PDSKLHHGHD PRGGLQPSGP 

       250        260        270        280        290        300 
PQFPPYRGMM PPFMYPPYLP FPPPYGPQGP YRYPTPDGPS RFPRVAGPRG SGPPMRLVEP 

       310        320        330        340        350        360 
VGRPSILKED NLKEFDQLDQ ENDDGWAGAH EEVDYTEKLK FSDEEDGRDS DEEGAEGHRD 

       370        380        390        400        410        420 
SQSASGEERP PEADGKKGNS PNSEPPTPKT AWAETSRPPE TEPGPPAPKP PLPPPHRGPA 

       430        440        450        460        470        480 
GNWGPPGDYP DRGGPPCKPP APEDEDEAWR QRRKQSSSEI SLAVERARRR REEEERRMQE 

       490        500        510        520        530        540 
ERRAACAEKL KRLDEKFGAP DKRLKAEPAA PPAAPSTPAP PPAVPKELPA PPAPPPASAP 

       550        560        570        580        590        600 
TPETEPEEPA QAPPAQSTPT PGVAAAPTLV SGGGSTSSTS SGSFEASPVE PQLPSKEGPE 

       610        620        630        640        650        660 
PPEEVPPPTT PPVPKVEPKG DGIGPTRQPP SQGLGYPKYQ KSLPPRFQRQ QQEQLLKQQQ 

       670        680        690        700        710        720 
QHQWQQHQQG SAPPTPVPPS PPQPVTLGAV PAPQAPPPPP KALYPGALGR PPPMPPMNFD 

       730        740        750        760        770        780 
PRWMMIPPYV DPRLLQGRPP LDFYPPGVHP SGLVPRERSD SGGSSSEPFD RHAPAMLRER 

       790        800        810        820        830        840 
GTPPVDPKLA WVGDVFTATP AEPRPLTSPL RQAADEDDKG MRSETPPVPP PPPYLASYPG 

       850        860        870        880        890        900 
FPENGAPGPP ISRFPLEEPG PRPLPWPPGS DEVAKIQTPP PKKEPPKEET AQLTGPEAGR 

       910        920        930        940        950        960 
KPARGVGSGG QGPPPPRRES RTETRWGPRP GSSRRGIPPE EPGAPPRRAG PIKKPPPPTK 

       970        980        990       1000       1010       1020 
VEELPPKPLE QGDETPKPPK PDPLKITKGK LGGPKETPPN GNLSPAPRLR RDYSYERVGP 

      1030       1040       1050       1060       1070       1080 
TSCRGRGRGE YFARGRGFRG TYGGRGRGAR SREFRSYREF RGDDGRGGGT GGPNHPPAPR 

      1090       1100       1110       1120       1130       1140 
GRTASETRSE GSEYEEIPKR RRQRGSETGS ETHESDLAPS DKEAPTPKEG TLTQVPLAPP 

      1150       1160       1170       1180       1190       1200 
PPGAPPSPAP ARFTARGGRV FTPRGVPSRR GRGGGRPPPQ VCPGWSPPAK SLAPKKPPTG 

      1210       1220       1230       1240       1250       1260 
PLPPSKEPLK EKLIPGPLSP VARGGSNGGS NVGMEDGERP RRRRHGRAQQ QDKPPRFRRL 

      1270       1280       1290       1300       1310       1320 
KQERENAARG SEGKPSLTLP ASAPGPEEAL TTVTVAPAPR RAAAKSPDLS NQNSDQANEE 

      1330       1340       1350       1360       1370       1380 
WETASESSDF TSERRGDKEA PPPVLLTPKA VGTPGGGGGG AVPGISAMSR GDLSQRAKDL 

      1390       1400       1410       1420       1430       1440 
SKRSFSSQRP GMERQNRRPG PGGKAGSSGS SSGGGGGGPG GRTGPGRGDK RSWPSPKNRS 

      1450       1460       1470       1480       1490       1500 
RPPEERPPGL PLPPPPPSSS AVFRLDQVIH SNPAGIQQAL AQLSSRQGSV TAPGGHPRHK 

      1510       1520       1530       1540       1550       1560 
PGLPQAPQGP SPRPPTRYEP QRVNSGLSSD PHFEEPGPMV RGVGGTPRDS AGVSPFPPKR 

      1570       1580       1590       1600       1610       1620 
RERPPRKPEL LQEESLPPPH SSGFLGSKPE GPGPQAESRD TGTEALTPHI WNRLHTATSR 

      1630       1640       1650       1660       1670       1680 
KSYRPSSMEP WMEPLSPFED VAGTEMSQSD SGVDLSGDSQ VSSGPCSQRS SPDGGLKGAA 

      1690       1700       1710       1720       1730       1740 
EGPPKRPGGS SPLNAVPCEG PPGSEPPRRP PPAPHDGDRK ELPREQPLPP GPIGTERSQR 

      1750       1760       1770       1780       1790       1800 
TDRGTEPGPI RPSHRPGPPV QFGTSDKDSD LRLVVGDSLK AEKELTASVT EAIPVSRDWE 

      1810       1820       1830       1840       1850       1860 
LLPSAAASAE PQSKNLDSGH CVPEPSSSGQ RLYPEVFYGS AGPSSSQISG GAMDSQLHPN 

      1870       1880       1890       1900       1910       1920 
SGGFRPGTPS LHPYRSQPLY LPPGPAPPSA LLSGLALKGQ FLDFSTMQAT ELGKLPAGGV 

      1930       1940       1950       1960       1970       1980 
LYPPPSFLYS PAFCPSPLPD TSLLQVRQDL PSPSDFYSTP LQPGGQSGFL PSGAPAQQML 

      1990       2000       2010       2020       2030       2040 
LPMVDSQLPV VNFGSLPPAP PPAPPPLSLL PVGPALQPPS LAVRPPPAPA TRVLPSPARP 

      2050       2060       2070       2080       2090       2100 
FPASLGRAEL HPVELKPFQD YQKLSSNLGG PGSSRTPPTG RSFSGLNSRL KATPSTYSGV 

      2110       2120       2130       2140       2150 
FRTQRVDLYQ QASPPDALRW IPKPWERTGP PPREGPSRRA EEPGSRGDKE PGLPPPR 

« Hide

Isoform 2 [UniParc].

Checksum: 9DF7B60612E16D90
Show »

FASTA2,144227,840
Isoform 3 [UniParc].

Checksum: 13C2A71F42213DDC
Show »

FASTA2,156229,064
Isoform 4 [UniParc].

Checksum: 0F496D1F2EB629E7
Show »

FASTA1,533163,047

References

« Hide 'large scale' references
[1]"A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-like domain."
Banerji J., Sands J., Strominger J.L., Spies T.
Proc. Natl. Acad. Sci. U.S.A. 87:2374-2378(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), VARIANTS ARG-57; GLU-742; PRO-1503 AND VAL-1895.
Tissue: T-cell.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANTS LEU-106; LYS-544; PRO-1503 AND VAL-1895.
Tissue: Brain.
[3]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LYS-544; ALA-1285; PRO-1503; HIS-1740; VAL-1895 AND LEU-2130.
[4]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LYS-544; PRO-1503 AND VAL-1895.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LEU-106; LYS-544; PRO-1503; HIS-1740; VAL-1895 AND SER-2006.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LYS-544; PRO-1503; HIS-1740 AND VAL-1895.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS CYS-477; LYS-544; PRO-1503 AND VAL-1895.
Tissue: Lymph, Placenta and Uterus.
[8]"Dense Alu clustering and a potential new member of the NF kappa B family within a 90 kilobase HLA class III segment."
Iris F.J.M., Bougueleret L., Prieur S., Caterina D., Primas G., Perrot V., Jurka J., Rodriguez-Tome P., Claverie J.-M., Dausset J., Cohen D.
Nat. Genet. 3:137-145(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1874 (ISOFORM 3), VARIANTS LYS-544; LYS-694; ALA-1415; PRO-1503 AND ALA-1744.
[9]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 871-2157 (ISOFORM 1), VARIANTS PRO-1503 AND VAL-1895.
Tissue: Uterine endothelium.
[10]"Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region."
Lehner B., Semple J.I., Brown S.E., Counsell D., Campbell R.D., Sanderson C.M.
Genomics 83:153-167(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Antibodies generated by a novel DNA vaccination identify the MHC class III encoded BAT2 polypeptide."
Schneiders A., Thiel S., Winkler J., Moeller P., Koch N.
Vaccine 23:2540-2550(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342 AND SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-383; SER-456; THR-610; SER-759; SER-761; SER-764; SER-1085; SER-1089; SER-1092; TYR-1094; SER-1147 AND SER-1306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-456; THR-610; SER-761 AND SER-1089, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-1196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-808; SER-1219; THR-1353 AND SER-2113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342; SER-350; SER-380; SER-1110 AND SER-1219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-1087 AND HIS-1152.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33509 mRNA. Translation: AAA35585.1. Frameshift.
M33518, M33512 Genomic DNA. Translation: AAA35586.1. Frameshift.
AB210034 mRNA. Translation: BAE06116.1. Different initiation.
AF129756 Genomic DNA. Translation: AAD18086.1.
CR354443 Genomic DNA. Translation: CAQ06970.1.
BA000025 Genomic DNA. Translation: BAB63391.1.
AL662847 Genomic DNA. Translation: CAI17698.2.
AL662801 Genomic DNA. Translation: CAI18313.1.
AL805934 Genomic DNA. Translation: CAI18500.1.
BX511262 Genomic DNA. Translation: CAI95572.1.
CR753892 Genomic DNA. Translation: CAQ06959.1.
CR759761 Genomic DNA. Translation: CAQ10847.1.
CH471081 Genomic DNA. Translation: EAX03452.1.
BC030127 mRNA. Translation: AAH30127.1.
BC032134 mRNA. Translation: AAH32134.1.
BC042295 mRNA. Translation: AAH42295.1.
BC060668 mRNA. Translation: AAH60668.1.
Z15025 Genomic DNA. Translation: CAA78744.1. Frameshift.
CR749245 mRNA. Translation: CAH18101.1.
PIRB35098.
S37671.
RefSeqNP_004629.3. NM_004638.3.
NP_542417.2. NM_080686.2.
UniGeneHs.123239.
Hs.436093.

3D structure databases

ProteinModelPortalP48634.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113646. 36 interactions.
IntActP48634. 32 interactions.
MINTMINT-1032109.
STRING9606.ENSP00000404619.

Polymorphism databases

DMDM296439424.

Proteomic databases

PaxDbP48634.
PRIDEP48634.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376007; ENSP00000365175; ENSG00000204469. [P48634-1]
ENST00000376033; ENSP00000365201; ENSG00000204469. [P48634-1]
ENST00000383455; ENSP00000372947; ENSG00000206427.
ENST00000383464; ENSP00000372956; ENSG00000206427.
ENST00000414956; ENSP00000404619; ENSG00000226618.
ENST00000416335; ENSP00000415182; ENSG00000231370.
ENST00000422962; ENSP00000415363; ENSG00000231825.
ENST00000428775; ENSP00000387910; ENSG00000225164.
ENST00000430737; ENSP00000413977; ENSG00000231825.
ENST00000432252; ENSP00000408226; ENSG00000225748.
ENST00000435971; ENSP00000409444; ENSG00000225164.
ENST00000439762; ENSP00000400540; ENSG00000231370.
ENST00000454306; ENSP00000387477; ENSG00000225748.
ENST00000458561; ENSP00000396812; ENSG00000226618.
GeneID7916.
KEGGhsa:7916.
UCSCuc003nvb.4. human. [P48634-1]

Organism-specific databases

CTD7916.
GeneCardsGC06P031719.
GC06Pj31575.
GC06Pk31570.
GC06Pl31627.
GC06Pm31664.
GC06Pn31578.
GC06Po31578.
HGNCHGNC:13918. PRRC2A.
HPACAB026383.
HPA046791.
MIM142580. gene.
neXtProtNX_P48634.
PharmGKBPA25263.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271062.
HOVERGENHBG004820.
InParanoidP48634.
OMAREKCHER.
OrthoDBEOG7DZ8J2.
PhylomeDBP48634.
TreeFamTF328738.

Gene expression databases

BgeeP48634.
GenevestigatorP48634.

Family and domain databases

InterProIPR009738. BAT2_N.
[Graphical view]
PfamPF07001. BAT2_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRRC2A. human.
GeneWikiBAT2.
GenomeRNAi7916.
NextBio30387.
PROP48634.
SOURCESearch...

Entry information

Entry namePRC2A_HUMAN
AccessionPrimary (citable) accession number: P48634
Secondary accession number(s): B0UX77 expand/collapse secondary AC list , B0UZE9, B0UZL3, O95875, Q05BK4, Q4LE37, Q5SQ29, Q5SQ30, Q5ST84, Q5STX6, Q5STX7, Q68DW9, Q6P9P7, Q6PIN1, Q8MGQ9, Q96QC6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM