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Protein

28 kDa heat- and acid-stable phosphoprotein

Gene

PDAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Enhances PDGFA-stimulated cell growth in fibroblasts, but inhibits the mitogenic effect of PDGFB.By similarity

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: ProtInc
  • signal transduction Source: ProtInc
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
Synonyms:HASPP28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:14634. PDAP1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33102.

Polymorphism and mutation databases

BioMutaiPDAP1.
DMDMi2498464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18118128 kDa heat- and acid-stable phosphoproteinPRO_0000083897Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13442.
MaxQBiQ13442.
PaxDbiQ13442.
PeptideAtlasiQ13442.
PRIDEiQ13442.
TopDownProteomicsiQ13442.

PTM databases

iPTMnetiQ13442.
PhosphoSiteiQ13442.

Miscellaneous databases

PMAP-CutDBQ13442.

Expressioni

Gene expression databases

BgeeiQ13442.
CleanExiHS_PDAP1.
ExpressionAtlasiQ13442. baseline and differential.
GenevisibleiQ13442. HS.

Organism-specific databases

HPAiCAB021103.
HPA050294.
HPA060836.

Interactioni

Protein-protein interaction databases

BioGridi116461. 15 interactions.
IntActiQ13442. 8 interactions.
MINTiMINT-5002803.
STRINGi9606.ENSP00000222968.

Structurei

3D structure databases

ProteinModelPortaliQ13442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PDAP1 family.Curated

Phylogenomic databases

eggNOGiKOG3375. Eukaryota.
ENOG4111T3A. LUCA.
GeneTreeiENSGT00390000018509.
HOGENOMiHOG000241539.
HOVERGENiHBG000319.
InParanoidiQ13442.
OMAiCTGRKGG.
OrthoDBiEOG7WX0C5.
PhylomeDBiQ13442.
TreeFamiTF324338.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q13442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKGGRKGGH KGRARQYTSP EEIDAQLQAE KQKAREEEEQ KEGGDGAAGD
60 70 80 90 100
PKKEKKSLDS DESEDEEDDY QQKRKGVEGL IDIENPNRVA QTTKKVTQLD
110 120 130 140 150
LDGPKELSRR EREEIEKQKA KERYMKMHLA GKTEQAKADL ARLAIIRKQR
160 170 180
EEAARKKEEE RKAKDDATLS GKRMQSLSLN K
Length:181
Mass (Da):20,630
Last modified:November 1, 1996 - v1
Checksum:iF97914C7920ABAB3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → MI in AAB07135 (Ref. 5) Curated
Sequence conflicti13 – 131R → W in AAB07135 (Ref. 5) Curated
Sequence conflicti25 – 251A → T in AAB07135 (Ref. 5) Curated
Sequence conflicti29 – 291A → S in AAB07135 (Ref. 5) Curated
Sequence conflicti67 – 671E → D in AAB07135 (Ref. 5) Curated
Sequence conflicti80 – 801L → F in AAB07135 (Ref. 5) Curated
Sequence conflicti126 – 1261K → R in AAB07135 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41745 mRNA. Translation: AAC50462.1.
AC004922 Genomic DNA. Translation: AAF03506.1.
CH471091 Genomic DNA. Translation: EAW76675.1.
CH471091 Genomic DNA. Translation: EAW76676.1.
BC000684 mRNA. Translation: AAH00684.1.
BC007873 mRNA. Translation: AAH07873.1.
U65960 Genomic DNA. Translation: AAB07135.1.
CCDSiCCDS5662.1.
RefSeqiNP_055706.1. NM_014891.6.
UniGeneiHs.632296.

Genome annotation databases

EnsembliENST00000350498; ENSP00000222968; ENSG00000106244.
GeneIDi11333.
KEGGihsa:11333.
UCSCiuc003uqe.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41745 mRNA. Translation: AAC50462.1.
AC004922 Genomic DNA. Translation: AAF03506.1.
CH471091 Genomic DNA. Translation: EAW76675.1.
CH471091 Genomic DNA. Translation: EAW76676.1.
BC000684 mRNA. Translation: AAH00684.1.
BC007873 mRNA. Translation: AAH07873.1.
U65960 Genomic DNA. Translation: AAB07135.1.
CCDSiCCDS5662.1.
RefSeqiNP_055706.1. NM_014891.6.
UniGeneiHs.632296.

3D structure databases

ProteinModelPortaliQ13442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116461. 15 interactions.
IntActiQ13442. 8 interactions.
MINTiMINT-5002803.
STRINGi9606.ENSP00000222968.

PTM databases

iPTMnetiQ13442.
PhosphoSiteiQ13442.

Polymorphism and mutation databases

BioMutaiPDAP1.
DMDMi2498464.

Proteomic databases

EPDiQ13442.
MaxQBiQ13442.
PaxDbiQ13442.
PeptideAtlasiQ13442.
PRIDEiQ13442.
TopDownProteomicsiQ13442.

Protocols and materials databases

DNASUi11333.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000350498; ENSP00000222968; ENSG00000106244.
GeneIDi11333.
KEGGihsa:11333.
UCSCiuc003uqe.5. human.

Organism-specific databases

CTDi11333.
GeneCardsiPDAP1.
HGNCiHGNC:14634. PDAP1.
HPAiCAB021103.
HPA050294.
HPA060836.
MIMi607075. gene.
neXtProtiNX_Q13442.
PharmGKBiPA33102.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3375. Eukaryota.
ENOG4111T3A. LUCA.
GeneTreeiENSGT00390000018509.
HOGENOMiHOG000241539.
HOVERGENiHBG000319.
InParanoidiQ13442.
OMAiCTGRKGG.
OrthoDBiEOG7WX0C5.
PhylomeDBiQ13442.
TreeFamiTF324338.

Miscellaneous databases

ChiTaRSiPDAP1. human.
GeneWikiiPDAP1.
GenomeRNAii11333.
PMAP-CutDBQ13442.
PROiQ13442.
SOURCEiSearch...

Gene expression databases

BgeeiQ13442.
CleanExiHS_PDAP1.
ExpressionAtlasiQ13442. baseline and differential.
GenevisibleiQ13442. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a novel platelet-derived growth factor-associated protein."
    Fischer W.H., Schubert D.
    J. Neurochem. 66:2213-2216(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Neuroretina.
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Kidney and Uterus.
  5. "5' flanking sequence of HASPP28."
    Huang F.L.
    Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-171.
  6. "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-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-57; SER-60; SER-63 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(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.
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-63 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-19; SER-57; SER-60; SER-63 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-60 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [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.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHAP28_HUMAN
AccessioniPrimary (citable) accession number: Q13442
Secondary accession number(s): D6W5S5, Q92906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 130 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. 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.