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O75689 (ADAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arf-GAP with dual PH domain-containing protein 1
Alternative name(s):
Centaurin-alpha-1
Short name=Cnt-a1
Putative MAPK-activating protein PM25
Gene names
Name:ADAP1
Synonyms:CENTA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase-activating protein for the ADP ribosylation factor family Probable. Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). Ref.1 Ref.2

Subunit structure

Interacts with PRKCA, PRKCI and PRKCZ. Interacts with the N-terminal region of PRKD1. Ref.9

Subcellular location

Nucleus. Cytoplasm. Note: Recruited to the plasma membrane upon epidermal growth factor-dependent activation of phosphatidylinositol 4,5-diphosphate (PtdInsP2) 3-kinase. Ref.1 Ref.2

Tissue specificity

Expressed at highest levels in brain and at lower levels in peripheral blood leukocytes. Ref.1

Post-translational modification

Phosphorylated by PRKCA, PRKCI, PRKCZ and PRKD1 in vitro. Ref.9

Sequence similarities

Contains 1 Arf-GAP domain.

Contains 2 PH domains.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75689-1)

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 2 (identifier: O75689-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: MAKERRRAVLELLQRPGNARCADCGAP → MFQFVFSRVYCINPARRKWKEFEKMLGCAEEGHASLGR
Isoform 3 (identifier: O75689-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 374374Arf-GAP with dual PH domain-containing protein 1
PRO_0000074205

Regions

Domain7 – 126120Arf-GAP
Domain129 – 230102PH 1
Domain252 – 356105PH 2
Zinc finger21 – 4424C4-type

Amino acid modifications

Modified residue871Phosphoserine; by PKC Ref.9
Modified residue2721N6-acetyllysine Ref.10
Modified residue2761Phosphothreonine; by PKC Ref.9

Natural variations

Alternative sequence1 – 7272Missing in isoform 3.
VSP_054793
Alternative sequence1 – 2727MAKER…DCGAP → MFQFVFSRVYCINPARRKWK EFEKMLGCAEEGHASLGR in isoform 2.
VSP_054794
Natural variant2411G → S. Ref.2 Ref.3 Ref.4 Ref.8
Corresponds to variant rs10256887 [ dbSNP | Ensembl ].
VAR_047470

Experimental info

Mutagenesis211C → A: Loss of GTPase-activating activity. Ref.1 Ref.2
Mutagenesis241C → A: Loss of GTPase-activating activity. Ref.1 Ref.2
Mutagenesis1491R → C: 40-45% reduction in PtdInsP2 3-kinase dependent membrane localization. Almost complete loss of PtdInsP2 3-kinase dependent membrane localization; when associated with C-273. Ref.1 Ref.2
Mutagenesis2731R → C: 70% reduction in PtdInsP2 3-kinase dependent membrane localization. Almost complete loss of PtdInsP2 3-kinase dependent membrane localization; when associated with C-149. Ref.1 Ref.2
Sequence conflict2151G → R in BAG52556. Ref.5

Secondary structure

.......................................................................... 374
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 38547281FB09D9B9

FASTA37443,395
        10         20         30         40         50         60 
MAKERRRAVL ELLQRPGNAR CADCGAPDPD WASYTLGVFI CLSCSGIHRN IPQVSKVKSV 

        70         80         90        100        110        120 
RLDAWEEAQV EFMASHGNDA ARARFESKVP SFYYRPTPSD CQLLREQWIR AKYERQEFIY 

       130        140        150        160        170        180 
PEKQEPYSAG YREGFLWKRG RDNGQFLSRK FVLTEREGAL KYFNRNDAKE PKAVMKIEHL 

       190        200        210        220        230        240 
NATFQPAKIG HPHGLQVTYL KDNSTRNIFI YHEDGKEIVD WFNALRAARF HYLQVAFPGA 

       250        260        270        280        290        300 
GDADLVPKLS RNYLKEGYME KTGPKQTEGF RKRWFTMDDR RLMYFKDPLD AFARGEVFIG 

       310        320        330        340        350        360 
SKESGYTVLH GFPPSTQGHH WPHGITIVTP DRKFLFACET ESDQREWVAA FQKAVDRPML 

       370 
PQEYAVEAHF KHKP 

« Hide

Isoform 2 [UniParc].

Checksum: 67ACBB2A85819D46
Show »

FASTA38544,936
Isoform 3 [UniParc].

Checksum: 8197A42910488E1E
Show »

FASTA30235,353

References

« Hide 'large scale' references
[1]"Molecular cloning and functional characterization of a human homologue of centaurin-alpha."
Venkateswarlu K., Cullen P.J.
Biochem. Biophys. Res. Commun. 262:237-244(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-149 AND ARG-273.
Tissue: Blood.
[2]"Identification of centaurin-alpha1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1."
Venkateswarlu K., Oatey P.B., Tavare J.M., Jackson T.R., Cullen P.J.
Biochem. J. 340:359-363(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-21; CYS-24; ARG-149 AND ARG-273, VARIANT SER-241.
Tissue: Peripheral blood.
[3]"Molecular identification of a high-affinity Ins(1,3,4,5)tetrakisphosphate/phosphatidylinositol(3,4, 5)trisphosphate binding protein from human brain, p42IP4."
Horstmeyer A., Reiser G.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-241.
Tissue: Brain.
[4]"Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-241.
Tissue: Lung fibroblast.
[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. expand/collapse author list , 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] (ISOFORMS 2 AND 3).
Tissue: Small intestine.
[6]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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].
[8]"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 1), VARIANT SER-241.
Tissue: Brain.
[9]"Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C."
Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D., Wakefield R.I.D., Johannes F.-J., Aitken A.
Biochem. Biophys. Res. Commun. 307:459-465(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKCA; PRKCI; PRKCZ AND PRKD1, PHOSPHORYLATION AT SER-87 AND THR-276.
[10]"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-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Crystal structure of full length centaurin alpha-1."
Structural genomics consortium (SGC)
Submitted (DEC-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-370.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ006422 mRNA. Translation: CAA07024.1.
AF082324 mRNA. Translation: AAD11414.1.
AB097049 mRNA. Translation: BAC77402.1.
AK300999 mRNA. Translation: BAG62618.1.
AC073957 Genomic DNA. No translation available.
AK092471 mRNA. Translation: BAG52556.1.
CH236965 Genomic DNA. Translation: EAL23709.1.
CH471144 Genomic DNA. Translation: EAW87183.1.
CH471144 Genomic DNA. Translation: EAW87184.1.
BC033747 mRNA. Translation: AAH33747.1.
CCDSCCDS5318.1.
PIRJC7091.
RefSeqNP_001271237.1. NM_001284308.1.
NP_001271238.1. NM_001284309.1.
NP_001271239.1. NM_001284310.1.
NP_001271240.1. NM_001284311.1.
NP_006860.1. NM_006869.3.
UniGeneHs.602573.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FEHX-ray1.90A3-370[»]
3FM8X-ray2.30C/D1-374[»]
3LJUX-ray1.70X3-370[»]
3MDBX-ray2.95C/D1-374[»]
ProteinModelPortalO75689.
SMRO75689. Positions 2-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116222. 13 interactions.
DIPDIP-41731N.
IntActO75689. 5 interactions.
MINTMINT-193767.
STRING9606.ENSP00000265846.

PTM databases

PhosphoSiteO75689.

Proteomic databases

MaxQBO75689.
PaxDbO75689.
PRIDEO75689.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265846; ENSP00000265846; ENSG00000105963.
ENST00000449296; ENSP00000407267; ENSG00000105963.
ENST00000539900; ENSP00000442682; ENSG00000105963.
GeneID11033.
KEGGhsa:11033.
UCSCuc003sjm.4. human. [O75689-1]

Organism-specific databases

CTD11033.
GeneCardsGC07M000905.
HGNCHGNC:16486. ADAP1.
HPAHPA007033.
HPA012049.
MIM608114. gene.
neXtProtNX_O75689.
PharmGKBPA26404.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5347.
HOGENOMHOG000006719.
HOVERGENHBG050888.
InParanoidO75689.
OrthoDBEOG71K62W.
PhylomeDBO75689.
TreeFamTF324540.

Gene expression databases

BgeeO75689.
CleanExHS_ADAP1.
GenevestigatorO75689.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR001164. ArfGAP.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF01412. ArfGap. 1 hit.
[Graphical view]
PRINTSPR00405. REVINTRACTNG.
SMARTSM00105. ArfGap. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
PROSITEPS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSADAP1. human.
EvolutionaryTraceO75689.
GeneWikiCentaurin,_alpha_1.
GenomeRNAi11033.
NextBio35469618.
PROO75689.
SOURCESearch...

Entry information

Entry nameADAP1_HUMAN
AccessionPrimary (citable) accession number: O75689
Secondary accession number(s): A4D2Q2 expand/collapse secondary AC list , B3KRZ4, B4DVA6, F6XZ68, H7C2Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM