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Protein

Protein PRRC2B

Gene

PRRC2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PRRC2B
Alternative name(s):
HLA-B-associated transcript 2-like 1
Proline-rich coiled-coil protein 2B
Gene namesi
Name:PRRC2B
Synonyms:BAT2L, BAT2L1, KIAA0515
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:28121. PRRC2B.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165585468.

Polymorphism and mutation databases

BioMutaiPRRC2B.
DMDMi308153415.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22292229Protein PRRC2BPRO_0000274481Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei166 – 1661PhosphoserineCombined sources
Modified residuei168 – 1681PhosphoserineCombined sources
Modified residuei222 – 2221PhosphoserineBy similarity
Modified residuei226 – 2261PhosphoserineCombined sources
Modified residuei228 – 2281PhosphothreonineCombined sources
Modified residuei388 – 3881PhosphoserineCombined sources
Modified residuei416 – 4161PhosphoserineCombined sources
Modified residuei480 – 4801PhosphoserineCombined sources
Modified residuei556 – 5561PhosphoserineCombined sources
Modified residuei613 – 6131PhosphoserineCombined sources
Modified residuei736 – 7361PhosphothreonineCombined sources
Modified residuei740 – 7401PhosphoserineCombined sources
Modified residuei745 – 7451PhosphoserineCombined sources
Modified residuei765 – 7651PhosphoserineCombined sources
Cross-linki963 – 963Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1132 – 11321PhosphoserineCombined sources
Modified residuei1231 – 12311PhosphoserineCombined sources
Modified residuei1470 – 14701PhosphoserineCombined sources
Modified residuei1507 – 15071PhosphoserineCombined sources
Cross-linki1510 – 1510Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1754 – 17541PhosphoserineCombined sources
Modified residuei1843 – 18431PhosphoserineCombined sources
Isoform 1 (identifier: Q5JSZ5-5)
Modified residuei776 – 7761PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ5JSZ5.
MaxQBiQ5JSZ5.
PaxDbiQ5JSZ5.
PeptideAtlasiQ5JSZ5.
PRIDEiQ5JSZ5.

PTM databases

iPTMnetiQ5JSZ5.

Miscellaneous databases

PMAP-CutDBQ5JSZ5.

Expressioni

Gene expression databases

BgeeiQ5JSZ5.
CleanExiHS_BAT2L.
ExpressionAtlasiQ5JSZ5. baseline and differential.
GenevisibleiQ5JSZ5. HS.

Organism-specific databases

HPAiHPA021022.
HPA064301.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
EHMT2Q96KQ72EBI-744891,EBI-744366
Hoxa1P090223EBI-744891,EBI-3957603From a different organism.

Protein-protein interaction databases

BioGridi124226. 41 interactions.
IntActiQ5JSZ5. 23 interactions.
MINTiMINT-2877452.
STRINGi9606.ENSP00000349856.

Structurei

3D structure databases

ProteinModelPortaliQ5JSZ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili495 – 55359Sequence analysisAdd
BLAST
Coiled coili1563 – 158725Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi391 – 3955Poly-Glu
Compositional biasi616 – 64732Gln-richAdd
BLAST
Compositional biasi1953 – 19564Poly-Ala

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4817. Eukaryota.
ENOG4110ERT. LUCA.
GeneTreeiENSGT00530000063496.
HOVERGENiHBG095505.
InParanoidiQ5JSZ5.
OMAiIPGNHIP.
OrthoDBiEOG7DZ8J2.
PhylomeDBiQ5JSZ5.
TreeFamiTF328738.

Family and domain databases

InterProiIPR009738. BAT2_N.
IPR033184. PRRC2.
[Graphical view]
PANTHERiPTHR14038. PTHR14038. 1 hit.
PfamiPF07001. BAT2_N. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 5 (identifier: Q5JSZ5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSDRLGQITK GKDGKSKYST LSLFDKYKGK SVDAIRSSVI PRHGLQSLGK
60 70 80 90 100
VAAARRMPPP ANLPSLKSEN KGNDPNIVIV PKDGTGWANK QDQQDPKSSS
110 120 130 140 150
ATASQPPESL PQPGLQKSVS NLQKPTQSIS QENTNSVPGG PKSWAQLNGK
160 170 180 190 200
PVGHEGGLRG SSRLLSFSPE EFPTLKAAGG QDKAGKEKGV LDLSYGPGPS
210 220 230 240 250
LRPQNVTSWR EGGGRHIISA TSLSTSPTEL GSRNSSTGDG APSSACTSDS
260 270 280 290 300
KDPSLRPAQP VRKGASQFMG NVYHPPTYHD MLPAFMCSPK SSENQGTVER
310 320 330 340 350
GSFPLPQLRL EPRVPFRQFQ MNDQDGKENR LGLSRPLRPL RQLVERAPRP
360 370 380 390 400
TIINAENLKG LDDLDADADD GWAGLHEEVD YSEKLKFSDD EEEEEVVKDG
410 420 430 440 450
RPKWNSWDPR RQRQLSMSSA DSADAKRTRE EGKDWAEAVG ASRVVRKAPD
460 470 480 490 500
PQPPPRKLHG WAPGPDYQKS SMGSMFRQQS IEDKEDKPPP RQKFIQSEMS
510 520 530 540 550
EAVERARKRR EEEERRAREE RLAACAAKLK QLDQKCKQAR KAGEARKQAE
560 570 580 590 600
KEVPWSPSAE KASPQENGPA VHKGSPEFPA QETPTTFPEE APTVSPAVAQ
610 620 630 640 650
SNSSEEEARE AGSPAQEFKY QKSLPPRFQR QQQQQQQEQL YKMQHWQPVY
660 670 680 690 700
PPPSHPQRTF YPHHPQMLGF DPRWMMMPSY MDPRITPTRT PVDFYPSALH
710 720 730 740 750
PSGLMKPMMP QESLNGTGCR SEDQNCVPPL QERKVTPIDS PPVWSPEGYM
760 770 780 790 800
ALQSKGYPLP HPKSSDTLAM DMRVRNESSF SASLGRAGGV SAQRDLFEER
810 820 830 840 850
GEEYLSAFDK KAQADFDSCI SSQRIGQELL FPPQENVQDA GAPGGHTQNL
860 870 880 890 900
RCSPLEPDFV PDEKKPECGS WDVSHQPETA DTAHGVERET PREGTAFNIS
910 920 930 940 950
SWDKNGSPNK QPSSEPEWTP EPRSSSSQHP EQTGRTRRSG PIKKPVLKAL
960 970 980 990 1000
KVEDKEKELE KIKQELGEES TRLAKEKEQS PTAEKDEDEE NDASLANSST
1010 1020 1030 1040 1050
TTLEDKGPGH ATFGREATKF EEEEKPDKAW EARPPRESSD VPPMKRNNWI
1060 1070 1080 1090 1100
FIDEEQAFGV RGQARGRGRG FREFTFRGRP AGGNGSGLCG GGVLGARSIY
1110 1120 1130 1140 1150
CSSQRSGRGR GLREFARPED CPRAKPRRRV ASETHSEGSE YEELPKRRRQ
1160 1170 1180 1190 1200
RGSENGNEGS LLEREESTLK KGDCRDSWRS NKGCSEDHSG LDAKSRGPRA
1210 1220 1230 1240 1250
FGRALPPRLS NCGYGRRTFV SKESPHWQSK SPGSSWQEYG PSDTCGSRRP
1260 1270 1280 1290 1300
TDRDYVPDSY RHPDAFGGRG FEDSRAEDKR SFFQDEHVAD SENAENRPFR
1310 1320 1330 1340 1350
RRRPPRQDKP PRFRRLRQER ESLGLWGPEE EPHLLAGQWP GRPKLCSGDK
1360 1370 1380 1390 1400
SGTVGRRSPE LSYQNSSDHA NEEWETASES SDFSERRERR EGPGSEPDSQ
1410 1420 1430 1440 1450
VDGGLSGASL GEKKELAKRS FSSQRPVVDR QSRKLEPGGF GEKPVRPGGG
1460 1470 1480 1490 1500
DTSPRYESQQ NGTPLKVKRS PDEALPGGLS GCSSGSGHSP YALERAAHAS
1510 1520 1530 1540 1550
ADLPEASSKK AEKEAKLAAP RAGEQGEAMK QFDLNYGSAI IENCGSSPGE
1560 1570 1580 1590 1600
ESEVGSMVGE GFIEVLTKKQ RRLLEEERRK KEQAVQVPVK GRGLSSRIPP
1610 1620 1630 1640 1650
RFAKKQNNLC LEQGDVTVPG SSLGTEIWES SSQALPVQAP ANDSWRKAVT
1660 1670 1680 1690 1700
AFSSTETGSA EQGFKSSQGD SGVDLSAESR ESSATSSQRS SPYGTLKPEE
1710 1720 1730 1740 1750
MSGPGLAEPK ADSHKEQAPK PSEQKDSEQG SGQSKEHRPG PIGNERSLKN
1760 1770 1780 1790 1800
RKGSEGAERL QGAVVPPVNG VEIHVDSVLP VPPIEFGVSP KDSDFSLPPG
1810 1820 1830 1840 1850
SASGPTGSPV VKLQDALASN AGLTQSIPIL RRDHHIQRAI GLSPMSFPTA
1860 1870 1880 1890 1900
DLTLKMESAR KAWENSPSLP EQSSPGGAGS GIQPPSSVGA SSGVNYSSFG
1910 1920 1930 1940 1950
GVSMPPMPVA SVAPSASMPG SHLPPLYLDG HVFASQPRLV PQTIPQQQSY
1960 1970 1980 1990 2000
QQAAAAQQIP ISLHTSLQAQ AQLGLRGGLP VSQSQEIFSS LQPFRSQVYM
2010 2020 2030 2040 2050
HPSLSPPSTM ILSGGTALKP PYSAFPGMQP LEMVKPQSGS PYQPMSGNQA
2060 2070 2080 2090 2100
LVYEGQLSQA AGLGASQMLD SQLPQLTMPL PRYGSGQQPL ILPQSIQLPP
2110 2120 2130 2140 2150
GQSLSVGAPR RIPPPGSQPP VLNTSREPSQ MEMKGFHFAD SKQNVPSGGP
2160 2170 2180 2190 2200
VPSPQTYRPS SASPSGKPSG SAVNMGSVQG HYVQQAKQRV DEKPSLGAVK
2210 2220
LQEAPSAASQ MKRTGAIKPR AVKVEESKA
Length:2,229
Mass (Da):242,967
Last modified:October 5, 2010 - v2
Checksum:i0F5F13DAC0217A6D
GO
Isoform 2 (identifier: Q5JSZ5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1903: Missing.

Show »
Length:326
Mass (Da):34,382
Checksum:i8173024F1E23876D
GO
Isoform 3 (identifier: Q5JSZ5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1903: Missing.
     2075-2075: Q → QQ

Show »
Length:327
Mass (Da):34,510
Checksum:iB4A913AB7ADD9BFE
GO
Isoform 4 (identifier: Q5JSZ5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1903: Missing.
     2159-2229: PSSASPSGKP...RAVKVEESKA → QNNEWMRNPAWEP

Show »
Length:268
Mass (Da):28,737
Checksum:iFF58D2A53BC14113
GO
Isoform 1 (identifier: Q5JSZ5-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     775-1468: Missing.

Show »
Length:1,535
Mass (Da):165,527
Checksum:iE0BACA25A0E75CF2
GO

Sequence cautioni

The sequence CAH18678.1 differs from that shown. Reason: Erroneous termination at position 637. Translated as Gln.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti936 – 9361T → S in CAH18678 (PubMed:17974005).Curated
Sequence conflicti981 – 9811P → L in CAH18678 (PubMed:17974005).Curated
Sequence conflicti1044 – 10441M → T in CAH18678 (PubMed:17974005).Curated
Sequence conflicti1276 – 12761A → V in CAH18678 (PubMed:17974005).Curated
Sequence conflicti1933 – 19331F → L in AAU10087 (Ref. 2) Curated
Sequence conflicti1985 – 19851Q → R in AAU10087 (Ref. 2) Curated
Sequence conflicti2069 – 20691L → S in AAU10087 (Ref. 2) Curated
Sequence conflicti2135 – 21351G → S in AAU10087 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti417 – 4171M → V.
Corresponds to variant rs34553878 [ dbSNP | Ensembl ].
VAR_057735
Natural varianti1630 – 16301S → T.
Corresponds to variant rs10736851 [ dbSNP | Ensembl ].
VAR_030289
Natural varianti1675 – 16751L → P.
Corresponds to variant rs10751478 [ dbSNP | Ensembl ].
VAR_030290

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 19031903Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_022760Add
BLAST
Alternative sequencei775 – 1468694Missing in isoform 1. CuratedVSP_039905Add
BLAST
Alternative sequencei2075 – 20751Q → QQ in isoform 3. 1 PublicationVSP_022761
Alternative sequencei2159 – 222971PSSAS…EESKA → QNNEWMRNPAWEP in isoform 4. 1 PublicationVSP_022762Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026162 mRNA. Translation: BAB15380.1.
AY700780 mRNA. Translation: AAU10087.1.
AL358781 Genomic DNA. Translation: CAI40214.1.
AL358781 Genomic DNA. Translation: CAI40218.1.
BC012289 mRNA. Translation: AAH12289.1.
CR749818 mRNA. Translation: CAH18678.1. Sequence problems.
AB011087 mRNA. Translation: BAA25441.1.
CCDSiCCDS48044.1. [Q5JSZ5-1]
PIRiT00083.
RefSeqiNP_037450.2. NM_013318.3. [Q5JSZ5-1]
UniGeneiHs.743955.

Genome annotation databases

EnsembliENST00000357304; ENSP00000349856; ENSG00000130723. [Q5JSZ5-1]
ENST00000405995; ENSP00000384606; ENSG00000130723. [Q5JSZ5-5]
ENST00000458550; ENSP00000398853; ENSG00000130723. [Q5JSZ5-4]
GeneIDi84726.
KEGGihsa:84726.
UCSCiuc004cam.2. human. [Q5JSZ5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026162 mRNA. Translation: BAB15380.1.
AY700780 mRNA. Translation: AAU10087.1.
AL358781 Genomic DNA. Translation: CAI40214.1.
AL358781 Genomic DNA. Translation: CAI40218.1.
BC012289 mRNA. Translation: AAH12289.1.
CR749818 mRNA. Translation: CAH18678.1. Sequence problems.
AB011087 mRNA. Translation: BAA25441.1.
CCDSiCCDS48044.1. [Q5JSZ5-1]
PIRiT00083.
RefSeqiNP_037450.2. NM_013318.3. [Q5JSZ5-1]
UniGeneiHs.743955.

3D structure databases

ProteinModelPortaliQ5JSZ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124226. 41 interactions.
IntActiQ5JSZ5. 23 interactions.
MINTiMINT-2877452.
STRINGi9606.ENSP00000349856.

PTM databases

iPTMnetiQ5JSZ5.

Polymorphism and mutation databases

BioMutaiPRRC2B.
DMDMi308153415.

Proteomic databases

EPDiQ5JSZ5.
MaxQBiQ5JSZ5.
PaxDbiQ5JSZ5.
PeptideAtlasiQ5JSZ5.
PRIDEiQ5JSZ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357304; ENSP00000349856; ENSG00000130723. [Q5JSZ5-1]
ENST00000405995; ENSP00000384606; ENSG00000130723. [Q5JSZ5-5]
ENST00000458550; ENSP00000398853; ENSG00000130723. [Q5JSZ5-4]
GeneIDi84726.
KEGGihsa:84726.
UCSCiuc004cam.2. human. [Q5JSZ5-1]

Organism-specific databases

CTDi84726.
GeneCardsiPRRC2B.
H-InvDBHIX0201341.
HGNCiHGNC:28121. PRRC2B.
HPAiHPA021022.
HPA064301.
neXtProtiNX_Q5JSZ5.
PharmGKBiPA165585468.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4817. Eukaryota.
ENOG4110ERT. LUCA.
GeneTreeiENSGT00530000063496.
HOVERGENiHBG095505.
InParanoidiQ5JSZ5.
OMAiIPGNHIP.
OrthoDBiEOG7DZ8J2.
PhylomeDBiQ5JSZ5.
TreeFamiTF328738.

Miscellaneous databases

ChiTaRSiPRRC2B. human.
GeneWikiiKIAA0515.
GenomeRNAii84726.
PMAP-CutDBQ5JSZ5.
PROiQ5JSZ5.

Gene expression databases

BgeeiQ5JSZ5.
CleanExiHS_BAT2L.
ExpressionAtlasiQ5JSZ5. baseline and differential.
GenevisibleiQ5JSZ5. HS.

Family and domain databases

InterProiIPR009738. BAT2_N.
IPR033184. PRRC2.
[Graphical view]
PANTHERiPTHR14038. PTHR14038. 1 hit.
PfamiPF07001. BAT2_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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.
    , 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 3).
  2. Zhou G., Shen C., Li H., Ke R., Zhong G., Lin L., Yang S.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 2).
    Tissue: Eye.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-2229 (ISOFORM 5).
    Tissue: Colon carcinoma.
  6. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1560-2229.
    Tissue: Brain.
  7. "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-388 AND SER-1754, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
    Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
    J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1510.
    Tissue: Lung adenocarcinoma.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-168; SER-226; SER-416; THR-736; SER-740; SER-745; SER-1132; SER-1231; SER-1470 AND SER-1843, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "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].
  15. "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-166 AND SER-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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-166; SER-168; SER-388; SER-740; SER-745 AND SER-1507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-416, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; THR-228; SER-388; SER-416; SER-480; SER-556; SER-613; SER-740; SER-745 AND SER-765, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-963, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRC2B_HUMAN
AccessioniPrimary (citable) accession number: Q5JSZ5
Secondary accession number(s): O60270
, Q5JSZ7, Q66VZ2, Q68CR0, Q96EI9, Q9H683
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: October 5, 2010
Last modified: July 6, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.