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O60256 (KPRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoribosyl pyrophosphate synthase-associated protein 2

Short name=PRPP synthase-associated protein 2
Alternative name(s):
41 kDa phosphoribosypyrophosphate synthetase-associated protein
Short name=PAP41
Gene names
Name:PRPSAP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis.

Subunit structure

Binds to PRPS1 and PRPS2.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60256-1)

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: O60256-2)

The sequence of this isoform differs from the canonical sequence as follows:
     41-80: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O60256-3)

The sequence of this isoform differs from the canonical sequence as follows:
     269-317: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Phosphoribosyl pyrophosphate synthase-associated protein 2
PRO_0000141082

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9
Modified residue2271Phosphoserine Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13

Natural variations

Alternative sequence41 – 8040Missing in isoform 2.
VSP_044731
Alternative sequence269 – 31749Missing in isoform 3.
VSP_046462

Experimental info

Sequence conflict1211K → R in BAG64840. Ref.2

Secondary structure

...................................................... 369
Helix Strand Turn

Details...

Sequences

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

Last modified August 1, 1998. Version 1.
Checksum: 12A0E46BD4AC55BF

FASTA36940,926
        10         20         30         40         50         60 
MFCVTPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ VYQEPNRETR 

        70         80         90        100        110        120 
VQIQESVRGK DVFIIQTVSK DVNTTIMELL IMVYACKTSC AKSIIGVIPY FPYSKQCKMR 

       130        140        150        160        170        180 
KRGSIVSKLL ASMMCKAGLT HLITMDLHQK EIQGFFNIPV DNLRASPFLL QYIQEEIPDY 

       190        200        210        220        230        240 
RNAVIVAKSP ASAKRAQSFA ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS 

       250        260        270        280        290        300 
LEIPMLIPKE KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG 

       310        320        330        340        350        360 
LLSSDAPRRI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD ISMILSEAIR RIHNGESMSY 


LFRNIGLDD 

« Hide

Isoform 2 [UniParc].

Checksum: 8920D91D0C8535EF
Show »

FASTA32936,297
Isoform 3 [UniParc].

Checksum: 4844D7A06BBE45FC
Show »

FASTA32035,548

References

« Hide 'large scale' references
[1]"Molecular cloning of a human cDNA for the 41-kDa phosphoribosylpyrophosphate synthetase-associated protein."
Katashima R., Iwahana H., Fujimura M., Yamaoka T., Ishizuka T., Tatibana M., Itakura M.
Biochim. Biophys. Acta 1396:245-250(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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 2).
Tissue: Trachea.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 3).
Tissue: Brain and Uterus.
[6]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 18-36; 49-57; 61-97; 103-115; 137-181; 205-232; 250-288; 293-330; 338-350 AND 352-363, PHOSPHORYLATION AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[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-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Human phosphoribosylpyrophosphate synthetase-associated protein 41 (Pap41)."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 13-369.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB007851 mRNA. Translation: BAA25435.1.
AK303911 mRNA. Translation: BAG64840.1.
CR457082 mRNA. Translation: CAG33363.1.
AC090286 Genomic DNA. No translation available.
AC107982 Genomic DNA. No translation available.
BC106050 mRNA. Translation: AAI06051.1.
BC101670 mRNA. Translation: AAI01671.1.
BC101672 mRNA. Translation: AAI01673.1.
BC143475 mRNA. Translation: AAI43476.1.
RefSeqNP_001230865.1. NM_001243936.1.
NP_001230869.1. NM_001243940.1.
NP_001230870.1. NM_001243941.1.
NP_001230871.1. NM_001243942.1.
NP_002758.1. NM_002767.3.
XP_005256781.1. XM_005256724.1.
XP_005256782.1. XM_005256725.1.
XP_005256783.1. XM_005256726.1.
UniGeneHs.632236.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JI4X-ray2.55A13-369[»]
ProteinModelPortalO60256.
SMRO60256. Positions 19-368.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111619. 10 interactions.
IntActO60256. 1 interaction.
MINTMINT-5003869.
STRING9606.ENSP00000268835.

Chemistry

BindingDBO60256.
ChEMBLCHEMBL2646.

PTM databases

PhosphoSiteO60256.

Proteomic databases

PaxDbO60256.
PeptideAtlasO60256.
PRIDEO60256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268835; ENSP00000268835; ENSG00000141127. [O60256-1]
ENST00000419071; ENSP00000392536; ENSG00000141127. [O60256-2]
ENST00000542013; ENSP00000439129; ENSG00000141127. [O60256-3]
GeneID5636.
KEGGhsa:5636.
UCSCuc002guo.2. human. [O60256-1]
uc010vyk.2. human.

Organism-specific databases

CTD5636.
GeneCardsGC17P018702.
HGNCHGNC:9467. PRPSAP2.
HPAHPA021881.
MIM603762. gene.
neXtProtNX_O60256.
PharmGKBPA33822.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0462.
HOGENOMHOG000210451.
HOVERGENHBG001520.
InParanoidO60256.
OMAKLLAKMM.
PhylomeDBO60256.
TreeFamTF106367.

Gene expression databases

ArrayExpressO60256.
BgeeO60256.
CleanExHS_PRPSAP2.
GenevestigatorO60256.

Family and domain databases

InterProIPR005946. Rib-P_diPkinase.
[Graphical view]
PfamPF14572. Pribosyl_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR01251. ribP_PPkin. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPRPSAP2. human.
EvolutionaryTraceO60256.
GeneWikiPRPSAP2.
GenomeRNAi5636.
NextBio21902.
PROO60256.
SOURCESearch...

Entry information

Entry nameKPRB_HUMAN
AccessionPrimary (citable) accession number: O60256
Secondary accession number(s): B4E1M8 expand/collapse secondary AC list , B7ZKZ1, E7EMY2, Q6IAS2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 108 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM