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O60256

- KPRB_HUMAN

UniProt

O60256 - KPRB_HUMAN

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Protein

Phosphoribosyl pyrophosphate synthase-associated protein 2

Gene

PRPSAP2

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

Functioni

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

GO - Molecular functioni

  1. enzyme inhibitor activity Source: ProtInc
  2. magnesium ion binding Source: InterPro
  3. ribose phosphate diphosphokinase activity Source: InterPro

GO - Biological processi

  1. bone development Source: Ensembl
  2. negative regulation of catalytic activity Source: GOC
  3. nucleobase-containing compound metabolic process Source: ProtInc
  4. nucleotide biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Nucleotide biosynthesis

Names & Taxonomyi

Protein namesi
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 namesi
Name:PRPSAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:9467. PRPSAP2.

Subcellular locationi

GO - Cellular componenti

  1. ribose phosphate diphosphokinase complex Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33822.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Phosphoribosyl pyrophosphate synthase-associated protein 2PRO_0000141082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei227 – 2271Phosphoserine6 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO60256.
PaxDbiO60256.
PeptideAtlasiO60256.
PRIDEiO60256.

PTM databases

PhosphoSiteiO60256.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO60256.
CleanExiHS_PRPSAP2.
ExpressionAtlasiO60256. baseline and differential.
GenevestigatoriO60256.

Organism-specific databases

HPAiHPA021881.

Interactioni

Subunit structurei

Binds to PRPS1 and PRPS2.

Protein-protein interaction databases

BioGridi111619. 14 interactions.
IntActiO60256. 3 interactions.
MINTiMINT-5003869.
STRINGi9606.ENSP00000268835.

Structurei

Secondary structure

1
369
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 244Combined sources
Helixi29 – 324Combined sources
Helixi33 – 4210Combined sources
Beta strandi49 – 535Combined sources
Beta strandi59 – 635Combined sources
Beta strandi71 – 755Combined sources
Helixi82 – 9817Combined sources
Beta strandi102 – 1076Combined sources
Helixi126 – 13611Combined sources
Beta strandi141 – 1466Combined sources
Helixi150 – 1556Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi160 – 1634Combined sources
Helixi166 – 17611Combined sources
Helixi180 – 1823Combined sources
Beta strandi183 – 1897Combined sources
Helixi190 – 1923Combined sources
Helixi193 – 20210Combined sources
Beta strandi206 – 2105Combined sources
Beta strandi256 – 2583Combined sources
Beta strandi263 – 27210Combined sources
Helixi276 – 28712Combined sources
Beta strandi292 – 3009Combined sources
Helixi306 – 3127Combined sources
Beta strandi317 – 3248Combined sources
Helixi327 – 3315Combined sources
Beta strandi336 – 3394Combined sources
Helixi342 – 35413Combined sources
Beta strandi362 – 3643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JI4X-ray2.55A13-369[»]
ProteinModelPortaliO60256.
SMRiO60256. Positions 19-368.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60256.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0462.
GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiO60256.
OMAiKLLAKMM.
PhylomeDBiO60256.
TreeFamiTF106367.

Family and domain databases

Gene3Di3.40.50.2020. 3 hits.
InterProiIPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 2 hits.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60256-1) [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
MFCVTPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ
60 70 80 90 100
VYQEPNRETR VQIQESVRGK DVFIIQTVSK DVNTTIMELL IMVYACKTSC
110 120 130 140 150
AKSIIGVIPY FPYSKQCKMR KRGSIVSKLL ASMMCKAGLT HLITMDLHQK
160 170 180 190 200
EIQGFFNIPV DNLRASPFLL QYIQEEIPDY RNAVIVAKSP ASAKRAQSFA
210 220 230 240 250
ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS LEIPMLIPKE
260 270 280 290 300
KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG
310 320 330 340 350
LLSSDAPRRI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD ISMILSEAIR
360
RIHNGESMSY LFRNIGLDD
Length:369
Mass (Da):40,926
Last modified:August 1, 1998 - v1
Checksum:i12A0E46BD4AC55BF
GO
Isoform 2 (identifier: O60256-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     41-80: Missing.

Note: No experimental confirmation available.

Show »
Length:329
Mass (Da):36,297
Checksum:i8920D91D0C8535EF
GO
Isoform 3 (identifier: O60256-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     269-317: Missing.

Note: No experimental confirmation available.

Show »
Length:320
Mass (Da):35,548
Checksum:i4844D7A06BBE45FC
GO
Isoform 4 (identifier: O60256-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.

Note: No experimental confirmation available.

Show »
Length:283
Mass (Da):31,322
Checksum:i25A38F2CDBFC3429
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211K → R in BAG64840. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8686Missing in isoform 4. 1 PublicationVSP_054765Add
BLAST
Alternative sequencei41 – 8040Missing in isoform 2. 1 PublicationVSP_044731Add
BLAST
Alternative sequencei269 – 31749Missing in isoform 3. 1 PublicationVSP_046462Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007851 mRNA. Translation: BAA25435.1.
AK303911 mRNA. Translation: BAG64840.1.
AK304544 mRNA. Translation: BAG65341.1.
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.
CCDSiCCDS11200.1. [O60256-1]
CCDS58525.1. [O60256-3]
CCDS58526.1. [O60256-2]
CCDS58527.1. [O60256-4]
RefSeqiNP_001230865.1. NM_001243936.1. [O60256-2]
NP_001230869.1. NM_001243940.1. [O60256-3]
NP_001230870.1. NM_001243941.1. [O60256-4]
NP_001230871.1. NM_001243942.1. [O60256-4]
NP_002758.1. NM_002767.3. [O60256-1]
XP_005256781.1. XM_005256724.1. [O60256-1]
XP_005256782.1. XM_005256725.1. [O60256-1]
XP_005256783.1. XM_005256726.1. [O60256-1]
XP_005256784.1. XM_005256727.2. [O60256-4]
XP_005256786.1. XM_005256729.2. [O60256-4]
UniGeneiHs.632236.

Genome annotation databases

EnsembliENST00000268835; ENSP00000268835; ENSG00000141127. [O60256-1]
ENST00000419071; ENSP00000392536; ENSG00000141127. [O60256-2]
ENST00000536323; ENSP00000443967; ENSG00000141127. [O60256-4]
ENST00000542013; ENSP00000439129; ENSG00000141127. [O60256-3]
ENST00000610773; ENSP00000481322; ENSG00000141127. [O60256-4]
GeneIDi5636.
KEGGihsa:5636.
UCSCiuc002guo.2. human. [O60256-1]
uc010vyk.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007851 mRNA. Translation: BAA25435.1 .
AK303911 mRNA. Translation: BAG64840.1 .
AK304544 mRNA. Translation: BAG65341.1 .
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 .
CCDSi CCDS11200.1. [O60256-1 ]
CCDS58525.1. [O60256-3 ]
CCDS58526.1. [O60256-2 ]
CCDS58527.1. [O60256-4 ]
RefSeqi NP_001230865.1. NM_001243936.1. [O60256-2 ]
NP_001230869.1. NM_001243940.1. [O60256-3 ]
NP_001230870.1. NM_001243941.1. [O60256-4 ]
NP_001230871.1. NM_001243942.1. [O60256-4 ]
NP_002758.1. NM_002767.3. [O60256-1 ]
XP_005256781.1. XM_005256724.1. [O60256-1 ]
XP_005256782.1. XM_005256725.1. [O60256-1 ]
XP_005256783.1. XM_005256726.1. [O60256-1 ]
XP_005256784.1. XM_005256727.2. [O60256-4 ]
XP_005256786.1. XM_005256729.2. [O60256-4 ]
UniGenei Hs.632236.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JI4 X-ray 2.55 A 13-369 [» ]
ProteinModelPortali O60256.
SMRi O60256. Positions 19-368.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111619. 14 interactions.
IntActi O60256. 3 interactions.
MINTi MINT-5003869.
STRINGi 9606.ENSP00000268835.

Chemistry

BindingDBi O60256.
ChEMBLi CHEMBL2646.

PTM databases

PhosphoSitei O60256.

Proteomic databases

MaxQBi O60256.
PaxDbi O60256.
PeptideAtlasi O60256.
PRIDEi O60256.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268835 ; ENSP00000268835 ; ENSG00000141127 . [O60256-1 ]
ENST00000419071 ; ENSP00000392536 ; ENSG00000141127 . [O60256-2 ]
ENST00000536323 ; ENSP00000443967 ; ENSG00000141127 . [O60256-4 ]
ENST00000542013 ; ENSP00000439129 ; ENSG00000141127 . [O60256-3 ]
ENST00000610773 ; ENSP00000481322 ; ENSG00000141127 . [O60256-4 ]
GeneIDi 5636.
KEGGi hsa:5636.
UCSCi uc002guo.2. human. [O60256-1 ]
uc010vyk.2. human.

Organism-specific databases

CTDi 5636.
GeneCardsi GC17P018702.
HGNCi HGNC:9467. PRPSAP2.
HPAi HPA021881.
MIMi 603762. gene.
neXtProti NX_O60256.
PharmGKBi PA33822.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0462.
GeneTreei ENSGT00550000074583.
HOGENOMi HOG000210451.
HOVERGENi HBG001520.
InParanoidi O60256.
OMAi KLLAKMM.
PhylomeDBi O60256.
TreeFami TF106367.

Miscellaneous databases

ChiTaRSi PRPSAP2. human.
EvolutionaryTracei O60256.
GeneWikii PRPSAP2.
GenomeRNAii 5636.
NextBioi 21902.
PROi O60256.
SOURCEi Search...

Gene expression databases

Bgeei O60256.
CleanExi HS_PRPSAP2.
ExpressionAtlasi O60256. baseline and differential.
Genevestigatori O60256.

Family and domain databases

Gene3Di 3.40.50.2020. 3 hits.
InterProi IPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view ]
Pfami PF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53271. SSF53271. 2 hits.
TIGRFAMsi TIGR01251. ribP_PPkin. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORMS 2 AND 4).
    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, 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. 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. 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.

Entry informationi

Entry nameiKPRB_HUMAN
AccessioniPrimary (citable) accession number: O60256
Secondary accession number(s): B4E1M8
, B4E329, B7ZKZ1, E7EMY2, Q6IAS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: August 1, 1998
Last modified: November 26, 2014
This is version 115 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3