P56211 (ARP19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-regulated phosphoprotein 19
Short name=ARPP-19

Gene names

Name:

ARPP19

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	112 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression. Ref.19
Subunit structure	Interacts (when phosphorylated at Ser-62) with PPP2R2D By similarity. Interacts with SNCA. Ref.12
Subcellular location	Cytoplasm By similarity.
Induction	Expression may be regulated by miR-451. Ref.18
Post-translational modification	Phosphorylation at Ser-62 by GWL during mitosis is essential for interaction with PPP2R2D (PR55-delta) and subsequent inactivation of PP2A By similarity. Phosphorylated by PKA. Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
Sequence similarities	Belongs to the endosulfine family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Protein phosphatase inhibitor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Inferred from mutant phenotype Ref.19. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from mutant phenotype Ref.19. Source: UniProtKB positive regulation of gluconeogenesis Inferred from direct assay Ref.1. Source: UniProtKB positive regulation of glucose import Non-traceable author statement Ref.1. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	potassium channel regulator activity Inferred from direct assay Ref.1. Source: UniProtKB protein phosphatase 2A binding Inferred from sequence or structural similarity. Source: UniProtKB protein phosphatase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW protein phosphatase type 2A regulator activity Inferred from sequence or structural similarity. Source: UniProtKB receptor binding Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform ARPP-19 (identifier: P56211-1)

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 ARPP-16 (identifier: P56211-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 112	111	cAMP-regulated phosphoprotein 19		PRO_0000008041
Amino acid modifications
	Modified residue	2	1	N-acetylserine; in isoform ARPP-19 By similarity
	Modified residue	17	1	N-acetylmethionine; in isoform ARPP-16 By similarity
	Modified residue	62	1	Phosphoserine; by GWL Probable
	Modified residue	104	1	Phosphoserine; by PKA By similarity
	Modified residue	109	1	N6-acetyllysine Ref.17
Natural variations
	Alternative sequence	1 – 16	16	Missing in isoform ARPP-16.		VSP_018555

Sequences

	Sequence		Length	Mass (Da)
	Isoform ARPP-19 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F19652B545C839AB	FASTA	112	12,323
	10 20 30 40 50 60 MSAEVPEAAS AEEQKEMEDK VTSPEKAEEA KLKARYPHLG QKPGGSDFLR KRLQKGQKYF 70 80 90 100 110 DSGDYNMAKA KMKNKQLPTA APDKTEVTGD HIPTPQDLPQ RKPSLVASKL AG
	Isoform ARPP-16 [UniParc]. Checksum: E29FF03CFF5DB609	FASTA	96	10,635
	10 20 30 40 50 60 MEDKVTSPEK AEEAKLKARY PHLGQKPGGS DFLRKRLQKG QKYFDSGDYN MAKAKMKNKQ 70 80 90 LPTAAPDKTE VTGDHIPTPQ DLPQRKPSLV ASKLAG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human alpha-endosulfine, a possible regulator of sulfonylurea-sensitive K(ATP) channel: molecular cloning, expression and biological properties." Heron L., Virsolvy A., Peyrollier K., Gribble F.M., Le Cam A., Ashcroft F.M., Bataille D. Proc. Natl. Acad. Sci. U.S.A. 95:8387-8391(1998) [PubMed: 9653196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ARPP-19). Tissue: Brain.
[2]	"Identification of okadaic-acid-induced genes by mRNA differential display in glioma cells." Chin L.S., Singh S.K., Wang Q., Murray S.F. J. Biomed. Sci. 7:152-159(2000) [PubMed: 10754390] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ARPP-19). Tissue: Brain.
[3]	"Expression of mRNAs encoding ARPP-16/19, ARPP-21, and DARPP-32 in human brain tissue." Brene S., Lindefors N., Ehrlich M., Taubes T., Horiuchi A., Kopp J., Hall H., Sedvall G., Greengard P., Persson H. J. Neurosci. 14:985-998(1994) [PubMed: 8120638] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ARPP-16). Tissue: Brain.
[4]	"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 ARPP-19).
[5]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ARPP-19). Tissue: Amygdala.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ARPP-19). Tissue: Spinal cord.
[7]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed: 16572171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ARPP-19). Tissue: Placenta.
[10]	"Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line." Shu H., Chen S., Bi Q., Mumby M., Brekken D.L. Mol. Cell. Proteomics 3:279-286(2004) [PubMed: 14729942] [Abstract] Cited for: PHOSPHORYLATION AT SER-62, MASS SPECTROMETRY.
[11]	"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: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, MASS SPECTROMETRY. Tissue: Prostate cancer.
[12]	"Conformation-specific binding of alpha-synuclein to novel protein partners detected by phage display and NMR spectroscopy." Woods W.S., Boettcher J.M., Zhou D.H., Kloepper K.D., Hartman K.L., Ladror D.T., Qi Z., Rienstra C.M., George J.M. J. Biol. Chem. 282:34555-34567(2007) [PubMed: 17893145] [Abstract] Cited for: INTERACTION WITH SNCA.
[13]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, MASS SPECTROMETRY. Tissue: Platelet.
[15]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109, MASS SPECTROMETRY.
[18]	"miR-451 enhances erythroid differentiation in K562 cells." Bruchova-Votavova H., Yoon D., Prchal J.T. Leuk. Lymphoma 51:686-693(2010) [PubMed: 20218812] [Abstract] Cited for: INDUCTION.
[19]	"The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A." Gharbi-Ayachi A., Labbe J.C., Burgess A., Vigneron S., Strub J.M., Brioudes E., Van-Dorsselaer A., Castro A., Lorca T. Science 330:1673-1677(2010) [PubMed: 21164014] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ223091 mRNA. Translation: CAA11115.1. AF084555 mRNA. Translation: AAD52044.1. CR457132 mRNA. Translation: CAG33413.1. AL833077 mRNA. Translation: CAD89929.1. AK311751 mRNA. Translation: BAG34694.1. AC025917 Genomic DNA. No translation available. CH471082 Genomic DNA. Translation: EAW77454.1. BC003418 mRNA. Translation: AAH03418.1. BC100015 mRNA. Translation: AAI00016.1.
IPI	IPI00328526. IPI00745466.
RefSeq	NP_006619.1. NM_006628.4.
UniGene	Hs.713393.
3D structure databases
ProteinModelPortal	P56211.
ModBase	Search...
Protein-protein interaction databases
STRING	P56211.
PTM databases
PhosphoSite	P56211.
Polymorphism databases
DMDM	3023326.
Proteomic databases
PRIDE	P56211.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000249822; ENSP00000249822; ENSG00000128989.
GeneID	10776.
KEGG	hsa:10776.
UCSC	uc002acd.1. human.
Organism-specific databases
CTD	10776.
GeneCards	GC15M052839.
H-InvDB	HIX0012254.
HGNC	HGNC:16967. ARPP19.
MIM	605487. gene.
neXtProt	NX_P56211.
PharmGKB	PA165478498.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20498.
GeneTree	ENSGT00390000010139.
HOGENOM	HBG564616.
HOVERGEN	HBG000297.
InParanoid	P56211.
OMA	QEMEDKV.
OrthoDB	EOG4KH2WG.
PhylomeDB	P56211.
Gene expression databases
ArrayExpress	P56211.
Bgee	P56211.
Genevestigator	P56211.
GermOnline	ENSG00000128989. Homo sapiens.
Family and domain databases
InterPro	IPR006760. Endosulphine. [Graphical view]
Pfam	PF04667. Endosulfine. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	40918.
SOURCE	Search...

Entry information

Entry name

ARP19_HUMAN

Accession

Primary (citable) accession number: P56211
Secondary accession number(s): B2R497 , Q6IAM2, Q86TA6, Q9UD70

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 101 of the entry and version 2 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.