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Q92733 (PRCC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proline-rich protein PRCC
Alternative name(s):
Papillary renal cell carcinoma translocation-associated gene protein
Gene names
Name:PRCC
Synonyms:TPRC
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May regulate cell cycle progression through interaction with MAD2L2. Ref.7

Subunit structure

Interacts with MAD2L2; the interaction is direct. Ref.7

Subcellular location

Nucleus Ref.7.

Tissue specificity

Ubiquitous in fetal and adult tissues.

Involvement in disease

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

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentNucleus
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle checkpoint

Inferred from direct assay Ref.7. Source: UniProtKB

   Cellular componentnucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular functionprotein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Proline-rich protein PRCC
PRO_0000058568

Regions

Region1 – 100100Mediates interaction with MAD2L2
Compositional bias18 – 258Poly-Glu
Compositional bias52 – 554Poly-Pro
Compositional bias79 – 846Poly-Pro
Compositional bias91 – 944Poly-Pro
Compositional bias235 – 2395Poly-Thr

Amino acid modifications

Modified residue81Phosphoserine Ref.8
Modified residue91Phosphoserine Ref.8
Modified residue121Phosphoserine Ref.8
Modified residue1571Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12
Modified residue1591Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12
Modified residue2181Phosphoserine Ref.8
Modified residue2391Phosphothreonine Ref.11
Modified residue2411Phosphoserine Ref.11
Modified residue2431Phosphoserine Ref.11
Modified residue2671Phosphoserine Ref.10 Ref.11

Natural variations

Natural variant1361P → S. Ref.3
Corresponds to variant rs11264542 [ dbSNP | Ensembl ].
VAR_024341

Sequences

Sequence LengthMass (Da)Tools
Q92733 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: F99CFD9D42725D57

FASTA49152,418
        10         20         30         40         50         60 
MSLVAYASSD ESEPDEAEPE PEEEEAVAPT SGPALGGLFA SLPAPKGPAL LPPPPQMLAP 

        70         80         90        100        110        120 
AFPPPLLLPP PTGDPRLQPP PPLPFGLGGF PPPPGVSPAE AAGVGEGLGL GLPSPRGPGL 

       130        140        150        160        170        180 
NLPPPIGGAG PPLGLPKPKK RKEPVKIAAP ELHKGDSDSE EDEPTKKKTI LQGSSEGTGL 

       190        200        210        220        230        240 
SALLPQPKNL TVKETNRLLL PHAFSRKPSD GSPDTKPSRL ASKTKTSSLA PVVGTTTTTP 

       250        260        270        280        290        300 
SPSAIKAAAK SAALQVTKQI TQEEDDSDEE VAPENFFSLP EKAEPPGVEP YPYPIPTVPE 

       310        320        330        340        350        360 
ELPPGTEPEP AFQDDAANAP LEFKMAAGSS GAPWMPKPGD DYSYNQFSTY GDANAAGAYY 

       370        380        390        400        410        420 
QDYYSGGYYP AQDPALVPPQ EIAPDASFID DEAFKRLQGK RNRGREEINF VEIKGDDQLS 

       430        440        450        460        470        480 
GAQQWMTKSL TEEKTMKSFS KKKGEQPTGQ QRRKHQITYL IHQAKERELE LKNTWSENKL 

       490 
SRRQTQAKYG F 

« Hide

References

« Hide 'large scale' references
[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: 8872474] [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: 8986805] [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. 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: 14702039] [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. expand/collapse author list , 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: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [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: 11717438] [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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-9; SER-12; SER-157; SER-159 AND SER-218, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-159, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[10]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159 AND SER-267, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-239; SER-241; SER-243 AND SER-267, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[12]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-159, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[13]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00294618.
RefSeqNP_005964.3. NM_005973.4.
UniGeneHs.516948.

3D structure databases

ProteinModelPortalQ92733.
ModBaseSearch...

Protein-protein interaction databases

IntActQ92733. 1 interaction.
MINTMINT-4536336.
STRINGQ92733.

PTM databases

PhosphoSiteQ92733.

Polymorphism databases

DMDM2498802.

Proteomic databases

PRIDEQ92733.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000271526; ENSP00000271526; ENSG00000143294.
GeneID5546.
KEGGhsa:5546.
UCSCuc001fqa.1. human.

Organism-specific databases

CTD5546.
GeneCardsGC01P156720.
H-InvDBHIX0001176.
HGNCHGNC:9343. PRCC.
HPACAB017151.
HPA019463.
HPA019481.
MIM179755. gene.
neXtProtNX_Q92733.
Orphanet47044. Familial papillary renal cell carcinoma.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14677.
HOGENOMHBG714870.
HOVERGENHBG002845.
InParanoidQ92733.
OMAAPKTKPS.
OrthoDBEOG4MSCZR.
PhylomeDBQ92733.

Gene expression databases

ArrayExpressQ92733.
BgeeQ92733.
CleanExHS_PRCC.
GenevestigatorQ92733.
GermOnlineENSG00000143294. Homo sapiens.

Family and domain databases

InterProIPR018800. PRCC_C.
[Graphical view]
KOK13105.
PfamPF10253. PRCC_Cterm. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio21488.
SOURCESearch...

Entry information

Entry namePRCC_HUMAN
AccessionPrimary (citable) accession number: Q92733
Secondary accession number(s): A8K1F7 expand/collapse secondary AC list , O00665, O00724, Q5SZ06
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 100 of the entry and version 1 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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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