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Protein

cAMP-regulated phosphoprotein 19

Gene

ARPP19

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

Functioni

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.1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB
  • negative regulation of catalytic activity Source: GOC
  • positive regulation of gluconeogenesis Source: UniProtKB
  • positive regulation of glucose import Source: UniProtKB
  • regulation of protein phosphatase type 2A activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-2465910. MASTL Facilitates Mitotic Progression.
SIGNORiP56211.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-regulated phosphoprotein 19
Short name:
ARPP-19
Gene namesi
Name:ARPP19
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:16967. ARPP19.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165478498.

Polymorphism and mutation databases

BioMutaiARPP19.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 112111cAMP-regulated phosphoprotein 19PRO_0000008041Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei62 – 621Phosphoserine; by GWLCurated
Modified residuei104 – 1041Phosphoserine; by PKABy similarity
Modified residuei109 – 1091N6-acetyllysineCombined sources
Isoform ARPP-16 (identifier: P56211-2)
Modified residuei1 – 11N-acetylmethionineBy similarity

Post-translational modificationi

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.By similarity
Isoform ARPP-16 contains a N-acetylmethionine at position 1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP56211.
MaxQBiP56211.
PaxDbiP56211.
PRIDEiP56211.

PTM databases

iPTMnetiP56211.
PhosphoSiteiP56211.

Expressioni

Inductioni

Expression may be regulated by miR-451.1 Publication

Gene expression databases

BgeeiP56211.
ExpressionAtlasiP56211. baseline and differential.
GenevisibleiP56211. HS.

Organism-specific databases

HPAiHPA056851.

Interactioni

Subunit structurei

Interacts (when phosphorylated at Ser-62) with PPP2R2D (By similarity). Interacts with SNCA.By similarity1 Publication

GO - Molecular functioni

  • protein phosphatase 2A binding Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115994. 8 interactions.
IntActiP56211. 1 interaction.
STRINGi9606.ENSP00000249822.

Structurei

3D structure databases

ProteinModelPortaliP56211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the endosulfine family.Curated

Phylogenomic databases

eggNOGiKOG4076. Eukaryota.
ENOG4112586. LUCA.
GeneTreeiENSGT00390000010139.
HOGENOMiHOG000232115.
HOVERGENiHBG000297.
InParanoidiP56211.
OrthoDBiEOG7JT702.
PhylomeDBiP56211.
TreeFamiTF314718.

Family and domain databases

InterProiIPR006760. Endosulphine.
[Graphical view]
PfamiPF04667. Endosulfine. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform ARPP-19 (identifier: P56211-1) [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
MSAEVPEAAS AEEQKEMEDK VTSPEKAEEA KLKARYPHLG QKPGGSDFLR
60 70 80 90 100
KRLQKGQKYF DSGDYNMAKA KMKNKQLPTA APDKTEVTGD HIPTPQDLPQ
110
RKPSLVASKL AG
Length:112
Mass (Da):12,323
Last modified:January 23, 2007 - v2
Checksum:iF19652B545C839AB
GO
Isoform ARPP-16 (identifier: P56211-2) [UniParc]FASTAAdd to basket

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

Show »
Length:96
Mass (Da):10,635
Checksum:iE29FF03CFF5DB609
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1616Missing in isoform ARPP-16. 1 PublicationVSP_018555Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32242.1. [P56211-1]
RefSeqiNP_001293120.1. NM_001306191.1.
NP_001293124.1. NM_001306195.1. [P56211-1]
NP_001293125.1. NM_001306196.1.
NP_006619.1. NM_006628.5. [P56211-1]
UniGeneiHs.512908.

Genome annotation databases

EnsembliENST00000249822; ENSP00000249822; ENSG00000128989. [P56211-1]
ENST00000561650; ENSP00000454234; ENSG00000128989. [P56211-2]
ENST00000563277; ENSP00000455986; ENSG00000128989. [P56211-2]
ENST00000563566; ENSP00000457631; ENSG00000128989. [P56211-2]
ENST00000566423; ENSP00000455625; ENSG00000128989. [P56211-1]
ENST00000567669; ENSP00000455151; ENSG00000128989. [P56211-1]
ENST00000568196; ENSP00000457805; ENSG00000128989. [P56211-2]
ENST00000569281; ENSP00000454297; ENSG00000128989. [P56211-1]
GeneIDi10776.
KEGGihsa:10776.
UCSCiuc002acd.2. human. [P56211-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32242.1. [P56211-1]
RefSeqiNP_001293120.1. NM_001306191.1.
NP_001293124.1. NM_001306195.1. [P56211-1]
NP_001293125.1. NM_001306196.1.
NP_006619.1. NM_006628.5. [P56211-1]
UniGeneiHs.512908.

3D structure databases

ProteinModelPortaliP56211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115994. 8 interactions.
IntActiP56211. 1 interaction.
STRINGi9606.ENSP00000249822.

PTM databases

iPTMnetiP56211.
PhosphoSiteiP56211.

Polymorphism and mutation databases

BioMutaiARPP19.

Proteomic databases

EPDiP56211.
MaxQBiP56211.
PaxDbiP56211.
PRIDEiP56211.

Protocols and materials databases

DNASUi10776.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249822; ENSP00000249822; ENSG00000128989. [P56211-1]
ENST00000561650; ENSP00000454234; ENSG00000128989. [P56211-2]
ENST00000563277; ENSP00000455986; ENSG00000128989. [P56211-2]
ENST00000563566; ENSP00000457631; ENSG00000128989. [P56211-2]
ENST00000566423; ENSP00000455625; ENSG00000128989. [P56211-1]
ENST00000567669; ENSP00000455151; ENSG00000128989. [P56211-1]
ENST00000568196; ENSP00000457805; ENSG00000128989. [P56211-2]
ENST00000569281; ENSP00000454297; ENSG00000128989. [P56211-1]
GeneIDi10776.
KEGGihsa:10776.
UCSCiuc002acd.2. human. [P56211-1]

Organism-specific databases

CTDi10776.
GeneCardsiARPP19.
HGNCiHGNC:16967. ARPP19.
HPAiHPA056851.
MIMi605487. gene.
neXtProtiNX_P56211.
PharmGKBiPA165478498.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4076. Eukaryota.
ENOG4112586. LUCA.
GeneTreeiENSGT00390000010139.
HOGENOMiHOG000232115.
HOVERGENiHBG000297.
InParanoidiP56211.
OrthoDBiEOG7JT702.
PhylomeDBiP56211.
TreeFamiTF314718.

Enzyme and pathway databases

ReactomeiR-HSA-2465910. MASTL Facilitates Mitotic Progression.
SIGNORiP56211.

Miscellaneous databases

ChiTaRSiARPP19. human.
GeneWikiiARPP-19.
GenomeRNAii10776.
PROiP56211.
SOURCEiSearch...

Gene expression databases

BgeeiP56211.
ExpressionAtlasiP56211. baseline and differential.
GenevisibleiP56211. HS.

Family and domain databases

InterProiIPR006760. Endosulphine.
[Graphical view]
PfamiPF04667. Endosulfine. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ARPP-19).
    Tissue: Amygdala.
  6. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ARPP-19).
    Tissue: Placenta.
  10. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNCA.
  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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "miR-451 enhances erythroid differentiation in K562 cells."
    Bruchova-Votavova H., Yoon D., Prchal J.T.
    Leuk. Lymphoma 51:686-693(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARP19_HUMAN
AccessioniPrimary (citable) accession number: P56211
Secondary accession number(s): B2R497
, Q6IAM2, Q86TA6, Q9UD70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 143 of the entry and version 2 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 15
    Human chromosome 15: 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.