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Protein

Proline-rich protein PRCC

Gene

PRCC

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

Functioni

May regulate cell cycle progression through interaction with MAD2L2.1 Publication

GO - Biological processi

  • mitotic cell cycle checkpoint Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Proline-rich protein PRCC
Alternative name(s):
Papillary renal cell carcinoma translocation-associated gene protein
Gene namesi
Name:PRCC
Synonyms:TPRC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9343. PRCC.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving PRCC is found in patients with papillary renal cell carcinoma. Translocation t(X;1)(p11.2;q21.2) with TFE3.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

MalaCardsiPRCC.
Orphaneti319308. Translocation renal cell carcinoma.
PharmGKBiPA33704.

Polymorphism and mutation databases

BioMutaiPRCC.
DMDMi2498802.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Proline-rich protein PRCCPRO_0000058568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971PhosphoserineCombined sources
Modified residuei114 – 1141PhosphoserineCombined sources
Modified residuei157 – 1571PhosphoserineCombined sources
Modified residuei159 – 1591PhosphoserineCombined sources
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei218 – 2181PhosphoserineCombined sources
Modified residuei239 – 2391PhosphothreonineCombined sources
Modified residuei241 – 2411PhosphoserineCombined sources
Modified residuei267 – 2671PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ92733.
MaxQBiQ92733.
PaxDbiQ92733.
PRIDEiQ92733.

PTM databases

iPTMnetiQ92733.
PhosphoSiteiQ92733.

Expressioni

Tissue specificityi

Ubiquitous in fetal and adult tissues.

Gene expression databases

BgeeiQ92733.
CleanExiHS_PRCC.
ExpressionAtlasiQ92733. baseline and differential.
GenevisibleiQ92733. HS.

Organism-specific databases

HPAiCAB017151.
HPA019463.
HPA019481.

Interactioni

Subunit structurei

Interacts with MAD2L2; the interaction is direct.1 Publication

Protein-protein interaction databases

BioGridi111537. 35 interactions.
IntActiQ92733. 22 interactions.
MINTiMINT-4536336.
STRINGi9606.ENSP00000271526.

Structurei

3D structure databases

ProteinModelPortaliQ92733.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 100100Mediates interaction with MAD2L2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 258Poly-Glu
Compositional biasi52 – 554Poly-Pro
Compositional biasi79 – 846Poly-Pro
Compositional biasi91 – 944Poly-Pro
Compositional biasi235 – 2395Poly-Thr

Phylogenomic databases

eggNOGiKOG3903. Eukaryota.
ENOG4111HM1. LUCA.
GeneTreeiENSGT00390000009042.
HOGENOMiHOG000247067.
HOVERGENiHBG002845.
InParanoidiQ92733.
KOiK13105.
OMAiMNLPPPQ.
OrthoDBiEOG73FQN5.
PhylomeDBiQ92733.
TreeFamiTF318780.

Family and domain databases

InterProiIPR018800. PRCC.
[Graphical view]
PfamiPF10253. PRCC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92733-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLVAYASSD ESEPDEAEPE PEEEEAVAPT SGPALGGLFA SLPAPKGPAL
60 70 80 90 100
LPPPPQMLAP AFPPPLLLPP PTGDPRLQPP PPLPFGLGGF PPPPGVSPAE
110 120 130 140 150
AAGVGEGLGL GLPSPRGPGL NLPPPIGGAG PPLGLPKPKK RKEPVKIAAP
160 170 180 190 200
ELHKGDSDSE EDEPTKKKTI LQGSSEGTGL SALLPQPKNL TVKETNRLLL
210 220 230 240 250
PHAFSRKPSD GSPDTKPSRL ASKTKTSSLA PVVGTTTTTP SPSAIKAAAK
260 270 280 290 300
SAALQVTKQI TQEEDDSDEE VAPENFFSLP EKAEPPGVEP YPYPIPTVPE
310 320 330 340 350
ELPPGTEPEP AFQDDAANAP LEFKMAAGSS GAPWMPKPGD DYSYNQFSTY
360 370 380 390 400
GDANAAGAYY QDYYSGGYYP AQDPALVPPQ EIAPDASFID DEAFKRLQGK
410 420 430 440 450
RNRGREEINF VEIKGDDQLS GAQQWMTKSL TEEKTMKSFS KKKGEQPTGQ
460 470 480 490
QRRKHQITYL IHQAKERELE LKNTWSENKL SRRQTQAKYG F
Length:491
Mass (Da):52,418
Last modified:February 1, 1997 - v1
Checksum:iF99CFD9D42725D57
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti136 – 1361P → S.1 Publication
Corresponds to variant rs11264542 [ dbSNP | Ensembl ].
VAR_024341

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97124 mRNA. Translation: CAA65791.1.
X99720 Genomic DNA. Translation: CAA68060.1.
AK289872 mRNA. Translation: BAF82561.1.
AL590666 Genomic DNA. Translation: CAI16350.1.
CH471121 Genomic DNA. Translation: EAW52909.1.
BC004913 mRNA. Translation: AAH04913.1.
CCDSiCCDS1157.1.
RefSeqiNP_005964.3. NM_005973.4.
UniGeneiHs.516948.

Genome annotation databases

EnsembliENST00000271526; ENSP00000271526; ENSG00000143294.
GeneIDi5546.
KEGGihsa:5546.
UCSCiuc001fqa.4. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97124 mRNA. Translation: CAA65791.1.
X99720 Genomic DNA. Translation: CAA68060.1.
AK289872 mRNA. Translation: BAF82561.1.
AL590666 Genomic DNA. Translation: CAI16350.1.
CH471121 Genomic DNA. Translation: EAW52909.1.
BC004913 mRNA. Translation: AAH04913.1.
CCDSiCCDS1157.1.
RefSeqiNP_005964.3. NM_005973.4.
UniGeneiHs.516948.

3D structure databases

ProteinModelPortaliQ92733.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111537. 35 interactions.
IntActiQ92733. 22 interactions.
MINTiMINT-4536336.
STRINGi9606.ENSP00000271526.

PTM databases

iPTMnetiQ92733.
PhosphoSiteiQ92733.

Polymorphism and mutation databases

BioMutaiPRCC.
DMDMi2498802.

Proteomic databases

EPDiQ92733.
MaxQBiQ92733.
PaxDbiQ92733.
PRIDEiQ92733.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000271526; ENSP00000271526; ENSG00000143294.
GeneIDi5546.
KEGGihsa:5546.
UCSCiuc001fqa.4. human.

Organism-specific databases

CTDi5546.
GeneCardsiPRCC.
HGNCiHGNC:9343. PRCC.
HPAiCAB017151.
HPA019463.
HPA019481.
MalaCardsiPRCC.
MIMi179755. gene.
neXtProtiNX_Q92733.
Orphaneti319308. Translocation renal cell carcinoma.
PharmGKBiPA33704.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3903. Eukaryota.
ENOG4111HM1. LUCA.
GeneTreeiENSGT00390000009042.
HOGENOMiHOG000247067.
HOVERGENiHBG002845.
InParanoidiQ92733.
KOiK13105.
OMAiMNLPPPQ.
OrthoDBiEOG73FQN5.
PhylomeDBiQ92733.
TreeFamiTF318780.

Miscellaneous databases

ChiTaRSiPRCC. human.
GeneWikiiPRCC_(gene).
GenomeRNAii5546.
NextBioi21488.
PROiQ92733.
SOURCEiSearch...

Gene expression databases

BgeeiQ92733.
CleanExiHS_PRCC.
ExpressionAtlasiQ92733. baseline and differential.
GenevisibleiQ92733. HS.

Family and domain databases

InterProiIPR018800. PRCC.
[Graphical view]
PfamiPF10253. PRCC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The t(X;1)(p11.2;q21.2) translocation in papillary renal cell carcinoma fuses a novel gene PRCC to the TFE3 transcription factor gene."
    Sidhar S.K., Clark J., Gill S., Hamoudi R., Crew A.J., Gwilliam R., Ross M., Linehan W.M., Birdsall S., Shipley J., Cooper C.S.
    Hum. Mol. Genet. 5:1333-1338(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH TFE3.
    Tissue: Monocyte.
  2. "Fusion of the transcription factor TFE3 gene to a novel gene, PRCC, in t(X;1)(p11;q21)-positive papillary renal cell carcinomas."
    Weterman M.A.J., Wilbrink M., Geurts van Kessel A.
    Proc. Natl. Acad. Sci. U.S.A. 93:15294-15298(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHROMOSOMAL TRANSLOCATION WITH TFE3.
  3. "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], VARIANT SER-136.
    Tissue: Caudate nucleus.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Lung.
  7. "Impairment of MAD2B-PRCC interaction in mitotic checkpoint defective t(X;1)-positive renal cell carcinomas."
    Weterman M.A., van Groningen J.J., Tertoolen L., van Kessel A.G.
    Proc. Natl. Acad. Sci. U.S.A. 98:13808-13813(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION.
  8. "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-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159 AND SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-97; SER-114; SER-157; SER-159; SER-212; THR-239 AND SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-157 AND SER-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-157 AND SER-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPRCC_HUMAN
AccessioniPrimary (citable) accession number: Q92733
Secondary accession number(s): A8K1F7
, O00665, O00724, Q5SZ06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 11, 2016
This is version 142 of the entry and version 1 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 1
    Human chromosome 1: 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
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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.