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Q9UPQ3

- AGAP1_HUMAN

UniProt

Q9UPQ3 - AGAP1_HUMAN

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Protein
Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1
Gene
AGAP1, CENTG2, KIAA1099
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-dependent trafficking of proteins in the endosomal-lysosomal system.1 Publication

Enzyme regulationi

GAP activity stimulated by phosphatidylinositol 3,4,5-trisphosphate (PIP3) and, to a lesser extent, by phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidic acid potentiates PIP2 stimulation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi78 – 858GTP Reviewed prediction
Nucleotide bindingi122 – 1265GTP Reviewed prediction
Nucleotide bindingi178 – 1814GTP Reviewed prediction
Zinc fingeri624 – 64724C4-type
Add
BLAST

GO - Molecular functioni

  1. ARF GTPase activator activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. phospholipid binding Source: FlyBase
  4. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
  2. regulation of ARF GTPase activity Source: InterPro
  3. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1
Short name:
AGAP-1
Alternative name(s):
Centaurin-gamma-2
Short name:
Cnt-g2
GTP-binding and GTPase-activating protein 1
Short name:
GGAP1
Gene namesi
Name:AGAP1
Synonyms:CENTG2, KIAA1099
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:16922. AGAP1.

Subcellular locationi

Cytoplasm
Note: Associates with the endocytic compartment.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi647 – 6471C → S: Loss of GAP activity. 1 Publication
Mutagenesisi652 – 6521R → K: Loss of GAP activity. No effect on AP-3-binding. 1 Publication

Organism-specific databases

PharmGKBiPA26412.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 857857Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1
PRO_0000074218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei836 – 8361Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated on tyrosines.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UPQ3.
PaxDbiQ9UPQ3.
PRIDEiQ9UPQ3.

PTM databases

PhosphoSiteiQ9UPQ3.

Expressioni

Tissue specificityi

Widely expressed.4 Publications

Gene expression databases

ArrayExpressiQ9UPQ3.
BgeeiQ9UPQ3.
CleanExiHS_AGAP1.
GenevestigatoriQ9UPQ3.

Organism-specific databases

HPAiHPA051405.

Interactioni

Subunit structurei

Homodimer. Interacts with several subunits of the AP-3 protein complex: AP3M1, AP3S1 and AP3S2. Interacts with GUCY1A3 and GUCY1B3.2 Publications

Protein-protein interaction databases

BioGridi125550. 4 interactions.
IntActiQ9UPQ3. 3 interactions.
MINTiMINT-6783717.
STRINGi9606.ENSP00000307634.

Structurei

3D structure databases

ProteinModelPortaliQ9UPQ3.
SMRiQ9UPQ3. Positions 70-233, 344-422, 530-592, 612-854.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini346 – 588243PH
Add
BLAST
Domaini609 – 729121Arf-GAP
Add
BLAST
Repeati768 – 79730ANK 1
Add
BLAST
Repeati801 – 83030ANK 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 276211Small GTPase-like
Add
BLAST

Domaini

The PH domain mediates AP-3 binding.

Sequence similaritiesi

Contains 2 ANK repeats.
Contains 1 Arf-GAP domain.
Contains 1 PH domain.

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
HOGENOMiHOG000007233.
HOVERGENiHBG054045.
KOiK12491.
OMAiEVENNIS.
OrthoDBiEOG72VH5V.
PhylomeDBiQ9UPQ3.
TreeFamiTF317762.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
2.30.29.30. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF08477. Miro. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 2 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS51419. RAB. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UPQ3-1) [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

MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERVEEP VLQNQIREHV    50
IAIEDAFVNS QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE 100
SPEGGRFKKE IVVDGQSYLL LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI 150
SFQTVYHYYS RMANYRNTSE IPLVLVGTQD AISSANPRVI DDARARKLSN 200
DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI GPCKSLPNSP 250
SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT 300
ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ 350
GMLLKRSGKS LNKEWKKKYV TLCDNGVLTY HPSLHDYMQN VHGKEIDLLR 400
TTVKVPGKRP PRATSACAPI SSPKTNGLSK DMSSLHISPN SGNVTSASGS 450
QMASGISLVS FNSRPDGMHQ RSYSVSSADQ WSEATVIANS AISSDTGLGD 500
SVCSSPSISS TTSPKLDPPP SPHANRKKHR RKKSTSNFKA DGLSGTAEEQ 550
EENFEFIIVS LTGQTWHFEA TTYEERDAWV QAIESQILAS LQSCESSKNK 600
SRLTSQSEAM ALQSIRNMRG NSHCVDCETQ NPNWASLNLG ALMCIECSGI 650
HRNLGTHLSR VRSLDLDDWP VELIKVMSSI GNELANSVWE ESSQGRTKPS 700
VDSTREEKER WIRAKYEQKL FLAPLPCTEL SLGQHLLRAT ADEDLRTAIL 750
LLAHGSRDEV NETCGEGDGR TALHLACRKG NVVLAQLLIW YGVDVTARDA 800
HGNTALAYAR QASSQECIDV LLQYGCPDER FVLMATPNLS RRNNNRNNSS 850
GRVPTII 857
Length:857
Mass (Da):94,470
Last modified:November 13, 2007 - v4
Checksum:iBBFDB8DA0ECD55E8
GO
Isoform 2 (identifier: Q9UPQ3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     442-494: Missing.

Show »
Length:804
Mass (Da):89,066
Checksum:i6014F37974C24A52
GO
Isoform 3 (identifier: Q9UPQ3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     352-405: MLLKRSGKSL...IDLLRTTVKV → LPFFVLALTA...SAQLSGAMMN
     406-857: Missing.

Note: No experimental confirmation available.

Show »
Length:405
Mass (Da):44,512
Checksum:i0B179759420981A9
GO

Sequence cautioni

The sequence AAH60814.1 differs from that shown. Reason: A 4-nucleotides insertion of unknown origin disrupts the reading frame.
The sequence BAA83051.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAA91862.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821S → G in an autistic patient. 1 Publication
VAR_026446
Natural varianti148 – 1481D → G.1 Publication
Corresponds to variant rs17855721 [ dbSNP | Ensembl ].
VAR_026447
Natural varianti522 – 5221P → L.
Corresponds to variant rs17840725 [ dbSNP | Ensembl ].
VAR_048331
Natural varianti671 – 6711V → I.5 Publications
Corresponds to variant rs2034648 [ dbSNP | Ensembl ].
VAR_026448
Natural varianti798 – 7981R → G in an autistic patient. 1 Publication
VAR_026449
Natural varianti829 – 8291E → K.
Corresponds to variant rs15718 [ dbSNP | Ensembl ].
VAR_019550
Natural varianti854 – 8541P → T in a family with an autistic patient. 1 Publication
VAR_026450

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei352 – 40554MLLKR…TTVKV → LPFFVLALTASTYLRPAGAR ARQSSPWPGPRGGQTSPHCA EGPQSAQLSGAMMN in isoform 3.
VSP_011181Add
BLAST
Alternative sequencei406 – 857452Missing in isoform 3.
VSP_011182Add
BLAST
Alternative sequencei442 – 49453Missing in isoform 2.
VSP_011183Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti288 – 2881T → I in AAK56506. 1 Publication
Sequence conflicti288 – 2881T → I in AAL04172. 1 Publication
Sequence conflicti288 – 2881T → I in BAA83051. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY033765 mRNA. Translation: AAK56506.1.
AF413078 mRNA. Translation: AAL04172.1.
AB029022 mRNA. Translation: BAA83051.2. Different initiation.
AC012305 Genomic DNA. No translation available.
AC019047 Genomic DNA. No translation available.
AC064874 Genomic DNA. No translation available.
AC073989 Genomic DNA. No translation available.
AC079400 Genomic DNA. No translation available.
BC060814 mRNA. Translation: AAH60814.1. Sequence problems.
BC140856 mRNA. Translation: AAI40857.1.
AK001722 mRNA. Translation: BAA91862.1. Different initiation.
CCDSiCCDS2514.1. [Q9UPQ3-2]
CCDS33408.1. [Q9UPQ3-1]
CCDS58756.1. [Q9UPQ3-3]
RefSeqiNP_001032208.1. NM_001037131.2. [Q9UPQ3-1]
NP_001231817.1. NM_001244888.1. [Q9UPQ3-3]
NP_055729.2. NM_014914.4. [Q9UPQ3-2]
UniGeneiHs.435039.

Genome annotation databases

EnsembliENST00000304032; ENSP00000307634; ENSG00000157985. [Q9UPQ3-1]
ENST00000336665; ENSP00000338378; ENSG00000157985. [Q9UPQ3-2]
ENST00000409457; ENSP00000387174; ENSG00000157985. [Q9UPQ3-3]
GeneIDi116987.
KEGGihsa:116987.
UCSCiuc002vvs.3. human. [Q9UPQ3-1]
uc002vvt.3. human. [Q9UPQ3-2]
uc021vyp.1. human. [Q9UPQ3-3]

Polymorphism databases

DMDMi160332373.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY033765 mRNA. Translation: AAK56506.1 .
AF413078 mRNA. Translation: AAL04172.1 .
AB029022 mRNA. Translation: BAA83051.2 . Different initiation.
AC012305 Genomic DNA. No translation available.
AC019047 Genomic DNA. No translation available.
AC064874 Genomic DNA. No translation available.
AC073989 Genomic DNA. No translation available.
AC079400 Genomic DNA. No translation available.
BC060814 mRNA. Translation: AAH60814.1 . Sequence problems.
BC140856 mRNA. Translation: AAI40857.1 .
AK001722 mRNA. Translation: BAA91862.1 . Different initiation.
CCDSi CCDS2514.1. [Q9UPQ3-2 ]
CCDS33408.1. [Q9UPQ3-1 ]
CCDS58756.1. [Q9UPQ3-3 ]
RefSeqi NP_001032208.1. NM_001037131.2. [Q9UPQ3-1 ]
NP_001231817.1. NM_001244888.1. [Q9UPQ3-3 ]
NP_055729.2. NM_014914.4. [Q9UPQ3-2 ]
UniGenei Hs.435039.

3D structure databases

ProteinModelPortali Q9UPQ3.
SMRi Q9UPQ3. Positions 70-233, 344-422, 530-592, 612-854.
ModBasei Search...

Protein-protein interaction databases

BioGridi 125550. 4 interactions.
IntActi Q9UPQ3. 3 interactions.
MINTi MINT-6783717.
STRINGi 9606.ENSP00000307634.

PTM databases

PhosphoSitei Q9UPQ3.

Polymorphism databases

DMDMi 160332373.

Proteomic databases

MaxQBi Q9UPQ3.
PaxDbi Q9UPQ3.
PRIDEi Q9UPQ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304032 ; ENSP00000307634 ; ENSG00000157985 . [Q9UPQ3-1 ]
ENST00000336665 ; ENSP00000338378 ; ENSG00000157985 . [Q9UPQ3-2 ]
ENST00000409457 ; ENSP00000387174 ; ENSG00000157985 . [Q9UPQ3-3 ]
GeneIDi 116987.
KEGGi hsa:116987.
UCSCi uc002vvs.3. human. [Q9UPQ3-1 ]
uc002vvt.3. human. [Q9UPQ3-2 ]
uc021vyp.1. human. [Q9UPQ3-3 ]

Organism-specific databases

CTDi 116987.
GeneCardsi GC02P236402.
HGNCi HGNC:16922. AGAP1.
HPAi HPA051405.
MIMi 608651. gene.
neXtProti NX_Q9UPQ3.
PharmGKBi PA26412.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5347.
HOGENOMi HOG000007233.
HOVERGENi HBG054045.
KOi K12491.
OMAi EVENNIS.
OrthoDBi EOG72VH5V.
PhylomeDBi Q9UPQ3.
TreeFami TF317762.

Miscellaneous databases

ChiTaRSi AGAP1. human.
GeneWikii CENTG2.
GenomeRNAii 116987.
NextBioi 80074.
PROi Q9UPQ3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UPQ3.
Bgeei Q9UPQ3.
CleanExi HS_AGAP1.
Genevestigatori Q9UPQ3.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
2.30.29.30. 2 hits.
3.40.50.300. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF08477. Miro. 1 hit.
PF00169. PH. 1 hit.
[Graphical view ]
PRINTSi PR00405. REVINTRACTNG.
SMARTi SM00248. ANK. 2 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS51419. RAB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "GGAPs, a new family of bifunctional GTP-binding and GTPase-activating proteins."
    Xia C., Ma W., Stafford L.J., Liu C., Gong L., Martin J.F., Liu M.
    Mol. Cell. Biol. 23:2476-2488(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ILE-671, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
    Tissue: Heart.
  2. "Kiaa1099 as a member (centaurin gamma2) of the centaurin ArfGAP protein family."
    Hong W.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ILE-671.
  3. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ILE-671.
    Tissue: Brain.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 3), VARIANT GLY-148.
    Tissue: Placenta.
  6. "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] OF 429-857 (ISOFORM 1), VARIANT ILE-671.
    Tissue: Teratocarcinoma.
  7. "AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton."
    Nie Z., Stanley K.T., Stauffer S., Jacques K.M., Hirsch D.S., Takei J., Randazzo P.A.
    J. Biol. Chem. 277:48965-48975(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-647 AND ARG-652.
  8. "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1."
    Nie Z., Boehm M., Boja E.S., Vass W.C., Bonifacino J.S., Fales H.M., Randazzo P.A.
    Dev. Cell 5:513-521(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE AP-3 COMPLEX.
  9. "AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl cyclase."
    Meurer S., Pioch S., Wagner K., Mueller-Esterl W., Gross S.
    J. Biol. Chem. 279:49346-49354(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH GUCY1A3 AND GUCY1B3.
  10. "The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3."
    Nie Z., Fei J., Premont R.T., Randazzo P.A.
    J. Cell Sci. 118:3555-3566(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANTS GLY-82; ILE-671; GLY-798 AND THR-854.

Entry informationi

Entry nameiAGAP1_HUMAN
AccessioniPrimary (citable) accession number: Q9UPQ3
Secondary accession number(s): B2RTX7
, Q541S5, Q6P9D7, Q9NV93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: November 13, 2007
Last modified: September 3, 2014
This is version 147 of the entry and version 4 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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