Q13442 (HAP28_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PDAP1
Synonyms:	HASPP28

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	181 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Enhances PDGFA-stimulated cell growth in fibroblasts, but inhibits the mitogenic effect of PDGFB By similarity.
Sequence similarities	Belongs to the PDAP1 family.

Ontologies

Keywords
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Traceable author statement Ref.1. Source: ProtInc signal transduction Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 181	181	28 kDa heat- and acid-stable phosphoprotein		PRO_0000083897
Amino acid modifications
	Modified residue	19	1	Phosphoserine Ref.9 Ref.13
	Modified residue	57	1	Phosphoserine Ref.7 Ref.9 Ref.10 Ref.13
	Modified residue	60	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15
	Modified residue	63	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15
	Modified residue	70	1	Phosphotyrosine By similarity
	Modified residue	132	1	N6-acetyllysine Ref.12
	Modified residue	176	1	Phosphoserine Ref.9 Ref.11 Ref.13
Experimental info
	Sequence conflict	1	1	M → MI in AAB07135. Ref.5
	Sequence conflict	13	1	R → W in AAB07135. Ref.5
	Sequence conflict	25	1	A → T in AAB07135. Ref.5
	Sequence conflict	29	1	A → S in AAB07135. Ref.5
	Sequence conflict	67	1	E → D in AAB07135. Ref.5
	Sequence conflict	80	1	L → F in AAB07135. Ref.5
	Sequence conflict	126	1	K → R in AAB07135. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q13442 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F97914C7920ABAB3	FASTA	181	20,630
	10 20 30 40 50 60 MPKGGRKGGH KGRARQYTSP EEIDAQLQAE KQKAREEEEQ KEGGDGAAGD PKKEKKSLDS 70 80 90 100 110 120 DESEDEEDDY QQKRKGVEGL IDIENPNRVA QTTKKVTQLD LDGPKELSRR EREEIEKQKA 130 140 150 160 170 180 KERYMKMHLA GKTEQAKADL ARLAIIRKQR EEAARKKEEE RKAKDDATLS GKRMQSLSLN K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. 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-57 AND SER-63, MASS SPECTROMETRY. Tissue: Prostate cancer.
[8]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, MASS SPECTROMETRY. Tissue: Platelet.
[9]	"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-19; SER-57; SER-60; SER-63 AND SER-176, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[11]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00013297.
RefSeq	NP_055706.1. NM_014891.6.
UniGene	Hs.632296.
3D structure databases
ProteinModelPortal	Q13442.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13442. 5 interactions.
STRING	9606.ENSP00000222968.
PTM databases
PhosphoSite	Q13442.
Polymorphism databases
DMDM	2498464.
Proteomic databases
PaxDb	Q13442.
PeptideAtlas	Q13442.
PRIDE	Q13442.
Protocols and materials databases
DNASU	11333.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000350498; ENSP00000222968; ENSG00000106244.
GeneID	11333.
KEGG	hsa:11333.
UCSC	uc003uqe.3. human.
Organism-specific databases
CTD	11333.
GeneCards	GC07M098989.
HGNC	HGNC:14634. PDAP1.
HPA	CAB021103.
MIM	607075. gene.
neXtProt	NX_Q13442.
PharmGKB	PA33102.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG313368.
HOGENOM	HOG000241539.
HOVERGEN	HBG000319.
InParanoid	Q13442.
OMA	VNHKGRN.
OrthoDB	EOG480HZ9.
PhylomeDB	Q13442.
Gene expression databases
ArrayExpress	Q13442.
Bgee	Q13442.
CleanEx	HS_PDAP1.
Genevestigator	Q13442.
GermOnline	ENSG00000106244. Homo sapiens.
Family and domain databases
InterPro	IPR019380. Casein_kinase_sb_PP28. [Graphical view]
Pfam	PF10252. PP28. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PDAP1. human.
DrugBank	DB00102. Becaplermin.
GenomeRNAi	11333.
NextBio	43057.
PMAP-CutDB	Q13442.
SOURCE	Search...

Entry information

Entry name

HAP28_HUMAN

Accession

Primary (citable) accession number: Q13442
Secondary accession number(s): D6W5S5, Q92906

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 103 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.