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Protein

28 kDa heat- and acid-stable phosphoprotein

Gene

Pdap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
28 kDa heat- and acid-stable phosphoprotein
Alternative name(s):
PDGF-associated protein
Short name:
PAP
PDGFA-associated protein 1
Short name:
PAP1
Gene namesi
Name:Pdap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2448536. Pdap1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18118128 kDa heat- and acid-stable phosphoproteinPRO_0000083898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphothreonineBy similarity
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei57 – 571PhosphoserineCombined sources
Modified residuei60 – 601PhosphoserineCombined sources
Modified residuei63 – 631PhosphoserineCombined sources
Modified residuei70 – 701PhosphotyrosineCombined sources
Modified residuei132 – 1321N6-acetyllysineBy similarity
Modified residuei164 – 1641N6-acetyllysineCombined sources
Modified residuei176 – 1761PhosphoserineBy similarity
Modified residuei178 – 1781PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by several kinases in vitro. In vivo, can be phosphorylated by CK2.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ3UHX2.
MaxQBiQ3UHX2.
PaxDbiQ3UHX2.
PRIDEiQ3UHX2.
TopDownProteomicsiQ3UHX2.

PTM databases

iPTMnetiQ3UHX2.
PhosphoSiteiQ3UHX2.

Expressioni

Gene expression databases

BgeeiQ3UHX2.
CleanExiMM_PDAP1.
ExpressionAtlasiQ3UHX2. baseline and differential.
GenevisibleiQ3UHX2. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi231191. 1 interaction.
STRINGi10090.ENSMUSP00000031627.

Structurei

3D structure databases

ProteinModelPortaliQ3UHX2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PDAP1 family.Curated

Phylogenomic databases

eggNOGiKOG3375. Eukaryota.
ENOG4111T3A. LUCA.
GeneTreeiENSGT00390000018509.
HOGENOMiHOG000241539.
HOVERGENiHBG000319.
InParanoidiQ3UHX2.
OMAiCTGRKGG.
OrthoDBiEOG7WX0C5.
PhylomeDBiQ3UHX2.
TreeFamiTF324338.

Family and domain databases

InterProiIPR019380. Casein_kinase_sb_PP28.
[Graphical view]
PfamiPF10252. PP28. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3UHX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKGGRKGGH KGRVRQYTSP EEIDAQLQAE KQKANEEDEQ EEGGDGASGD
60 70 80 90 100
PKKEKKSLDS DESEDEDDDY QQKRKGVEGL IDIENPNRVA QTTKKVTQLD
110 120 130 140 150
LDGPKELSRR EREEIEKQKA KERYMKMHLA GKTEQAKADL ARLAIIRKQR
160 170 180
EEAARKKEEE RKAKDDATLS GKRMQSLSLN K
Length:181
Mass (Da):20,605
Last modified:October 11, 2005 - v1
Checksum:iC9A74B7C41174F87
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147170 mRNA. Translation: BAE27734.1.
BC007162 mRNA. Translation: AAH07162.1.
BC106168 mRNA. Translation: AAI06169.1.
CCDSiCCDS39384.1.
RefSeqiNP_001028485.1. NM_001033313.3.
UniGeneiMm.188851.

Genome annotation databases

EnsembliENSMUST00000031627; ENSMUSP00000031627; ENSMUSG00000029623.
GeneIDi231887.
KEGGimmu:231887.
UCSCiuc009ame.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147170 mRNA. Translation: BAE27734.1.
BC007162 mRNA. Translation: AAH07162.1.
BC106168 mRNA. Translation: AAI06169.1.
CCDSiCCDS39384.1.
RefSeqiNP_001028485.1. NM_001033313.3.
UniGeneiMm.188851.

3D structure databases

ProteinModelPortaliQ3UHX2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231191. 1 interaction.
STRINGi10090.ENSMUSP00000031627.

PTM databases

iPTMnetiQ3UHX2.
PhosphoSiteiQ3UHX2.

Proteomic databases

EPDiQ3UHX2.
MaxQBiQ3UHX2.
PaxDbiQ3UHX2.
PRIDEiQ3UHX2.
TopDownProteomicsiQ3UHX2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031627; ENSMUSP00000031627; ENSMUSG00000029623.
GeneIDi231887.
KEGGimmu:231887.
UCSCiuc009ame.1. mouse.

Organism-specific databases

CTDi11333.
MGIiMGI:2448536. Pdap1.

Phylogenomic databases

eggNOGiKOG3375. Eukaryota.
ENOG4111T3A. LUCA.
GeneTreeiENSGT00390000018509.
HOGENOMiHOG000241539.
HOVERGENiHBG000319.
InParanoidiQ3UHX2.
OMAiCTGRKGG.
OrthoDBiEOG7WX0C5.
PhylomeDBiQ3UHX2.
TreeFamiTF324338.

Miscellaneous databases

ChiTaRSiPdap1. mouse.
PROiQ3UHX2.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UHX2.
CleanExiMM_PDAP1.
ExpressionAtlasiQ3UHX2. baseline and differential.
GenevisibleiQ3UHX2. MM.

Family and domain databases

InterProiIPR019380. Casein_kinase_sb_PP28.
[Graphical view]
PfamiPF10252. PP28. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Heart.
  2. "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] OF 2-181.
    Strain: FVB/N.
    Tissue: Colon and Mammary tumor.
  3. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
    Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
    J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-63 AND TYR-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHAP28_MOUSE
AccessioniPrimary (citable) accession number: Q3UHX2
Secondary accession number(s): A0JLS1, Q3KQJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 11, 2005
Last modified: July 6, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.