O60256 (KPRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Coding sequence diversity	Alternative splicing
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	nucleobase-containing compound metabolic process Traceable author statement Ref.1. Source: ProtInc nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	ribose phosphate diphosphokinase complex Inferred from electronic annotation. Source: Compara
Molecular_function	enzyme inhibitor activity Traceable author statement Ref.1. Source: ProtInc magnesium ion binding Inferred from electronic annotation. Source: InterPro ribose phosphate diphosphokinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 369

369

Phosphoribosyl pyrophosphate synthase-associated protein 2

PRO_0000141082

Amino acid modifications

Modified residue

227

1

Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12

Natural variations

Alternative sequence

41 – 80

40

Missing in isoform 2.

VSP_044731

Alternative sequence

269 – 317

49

Missing in isoform 3.

VSP_046462

Experimental info

Sequence conflict

121

1

K → R in BAG64840. Ref.2

Secondary structure

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369

Helix Strand Turn

Details...

Beta strand

21 – 24

4

Helix

29 – 32

4

Helix

33 – 42

10

Beta strand

49 – 53

5

Beta strand

59 – 63

5

Beta strand

71 – 75

5

Helix

82 – 98

17

Beta strand

102 – 107

6

Helix

126 – 136

11

Beta strand

141 – 146

6

Helix

150 – 155

6

Beta strand

156 – 158

3

Beta strand

160 – 163

4

Helix

166 – 176

11

Helix

180 – 182

3

Beta strand

183 – 189

7

Helix

190 – 192

3

Helix

193 – 202

10

Beta strand

206 – 210

5

Beta strand

256 – 258

3

Beta strand

263 – 272

10

Helix

276 – 287

12

Beta strand

292 – 300

9

Helix

306 – 312

7

Beta strand

317 – 324

8

Helix

327 – 331

5

Beta strand

336 – 339

4

Helix

342 – 354

13

Beta strand

362 – 364

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 12A0E46BD4AC55BF	FASTA	369	40,926
	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
	Isoform 2 [UniParc]. Checksum: 8920D91D0C8535EF	FASTA	329	36,297
	10 20 30 40 50 60 MFCVTPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE DVNTTIMELL IMVYACKTSC 70 80 90 100 110 120 AKSIIGVIPY FPYSKQCKMR KRGSIVSKLL ASMMCKAGLT HLITMDLHQK EIQGFFNIPV 130 140 150 160 170 180 DNLRASPFLL QYIQEEIPDY RNAVIVAKSP ASAKRAQSFA ERLRLGIAVI HGEAQDAESD 190 200 210 220 230 240 LVDGRHSPPM VRSVAAIHPS LEIPMLIPKE KPPITVVGDV GGRIAIIVDD IIDDVDSFLA 250 260 270 280 290 300 AAETLKERGA YKIFVMATHG LLSSDAPRRI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD 310 320 ISMILSEAIR RIHNGESMSY LFRNIGLDD
	Isoform 3 [UniParc]. Checksum: 4844D7A06BBE45FC	FASTA	320	35,548
	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 GGRIAIIVVV VTNTIPHEVQ KLQCPKIKTV DISMILSEAI 310 320 RRIHNGESMS YLFRNIGLDD

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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, MASS SPECTROMETRY.
[13]	"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.

IPI

IPI00003168.
IPI00796213.
IPI00942171.

RefSeq

NP_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.

UniGene

Hs.632236.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JI4	X-ray	2.55	A	13-369	[»]

ProteinModelPortal

O60256.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60256. 1 interaction.

STRING

9606.ENSP00000268835.

PTM databases

PhosphoSite

O60256.

Proteomic databases

PaxDb

O60256.

PeptideAtlas

O60256.

PRIDE

O60256.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000268835; ENSP00000268835; ENSG00000141127.
ENST00000419071; ENSP00000392536; ENSG00000141127.
ENST00000542013; ENSP00000439129; ENSG00000141127.
ENST00000576388; ENSP00000461715; ENSG00000141127.

GeneID

5636.

KEGG

hsa:5636.

UCSC

uc002guo.2. human.

Organism-specific databases

CTD

5636.

GeneCards

GC17P018702.

HGNC

HGNC:9467. PRPSAP2.

HPA

HPA021881.

MIM

603762. gene.

neXtProt

NX_O60256.

PharmGKB

PA33822.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0462.

HOGENOM

HOG000210451.

HOVERGEN

HBG001520.

InParanoid

O60256.

OMA

TRIFERQ.

PhylomeDB

O60256.

Gene expression databases

ArrayExpress

O60256.

Bgee

O60256.

CleanEx

HS_PRPSAP2.

Genevestigator

O60256.

GermOnline

ENSG00000141127. Homo sapiens.

Family and domain databases

InterPro

IPR005946. Rib-P_diPkinase.
[Graphical view]

TIGRFAMs

TIGR01251. ribP_PPkin. 1 hit.

ProtoNet

Search...

Other

BindingDB

O60256.

ChEMBL

CHEMBL2646.

ChiTaRS

PRPSAP2. human.

EvolutionaryTrace

O60256.

GenomeRNAi

5636.

NextBio

21902.

SOURCE

Search...

Entry information

Entry name

KPRB_HUMAN

Accession

Primary (citable) accession number: O60256
Secondary accession number(s): B4E1M8 , B7ZKZ1, E7EMY2, Q6IAS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2002
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.