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Protein

Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1

Gene

AGAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 858GTPSequence Analysis
Nucleotide bindingi122 – 1265GTPSequence Analysis
Nucleotide bindingi178 – 1814GTPSequence Analysis
Zinc fingeri624 – 64724C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • GTP binding Source: UniProtKB-KW
  • phospholipid binding Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:16922. AGAP1.

Subcellular locationi

GO - Cellular componenti

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.

Polymorphism and mutation databases

BioMutaiAGAP1.
DMDMi160332373.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei521 – 5211Phosphoserine1 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

BgeeiQ9UPQ3.
CleanExiHS_AGAP1.
ExpressionAtlasiQ9UPQ3. baseline and differential.
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. 10 interactions.
IntActiQ9UPQ3. 3 interactions.
MINTiMINT-6783717.
STRINGi9606.ENSP00000307634.

Structurei

3D structure databases

ProteinModelPortaliQ9UPQ3.
SMRiQ9UPQ3. Positions 70-233, 344-422, 530-592, 612-825.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

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

Domaini

The PH domain mediates AP-3 binding.

Sequence similaritiesi

Belongs to the centaurin gamma-like family.Curated
Contains 2 ANK repeats.PROSITE-ProRule annotation
Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri624 – 64724C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000007233.
HOVERGENiHBG054045.
InParanoidiQ9UPQ3.
KOiK12491.
OMAiDGMQQRS.
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. AlignAdd to basket

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

        10         20         30         40         50
MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERVEEP VLQNQIREHV
60 70 80 90 100
IAIEDAFVNS QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE
110 120 130 140 150
SPEGGRFKKE IVVDGQSYLL LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI
160 170 180 190 200
SFQTVYHYYS RMANYRNTSE IPLVLVGTQD AISSANPRVI DDARARKLSN
210 220 230 240 250
DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI GPCKSLPNSP
260 270 280 290 300
SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT
310 320 330 340 350
ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ
360 370 380 390 400
GMLLKRSGKS LNKEWKKKYV TLCDNGVLTY HPSLHDYMQN VHGKEIDLLR
410 420 430 440 450
TTVKVPGKRP PRATSACAPI SSPKTNGLSK DMSSLHISPN SGNVTSASGS
460 470 480 490 500
QMASGISLVS FNSRPDGMHQ RSYSVSSADQ WSEATVIANS AISSDTGLGD
510 520 530 540 550
SVCSSPSISS TTSPKLDPPP SPHANRKKHR RKKSTSNFKA DGLSGTAEEQ
560 570 580 590 600
EENFEFIIVS LTGQTWHFEA TTYEERDAWV QAIESQILAS LQSCESSKNK
610 620 630 640 650
SRLTSQSEAM ALQSIRNMRG NSHCVDCETQ NPNWASLNLG ALMCIECSGI
660 670 680 690 700
HRNLGTHLSR VRSLDLDDWP VELIKVMSSI GNELANSVWE ESSQGRTKPS
710 720 730 740 750
VDSTREEKER WIRAKYEQKL FLAPLPCTEL SLGQHLLRAT ADEDLRTAIL
760 770 780 790 800
LLAHGSRDEV NETCGEGDGR TALHLACRKG NVVLAQLLIW YGVDVTARDA
810 820 830 840 850
HGNTALAYAR QASSQECIDV LLQYGCPDER FVLMATPNLS RRNNNRNNSS

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti288 – 2881T → I in AAK56506 (PubMed:12640130).Curated
Sequence conflicti288 – 2881T → I in AAL04172 (Ref. 2) Curated
Sequence conflicti288 – 2881T → I in BAA83051 (PubMed:10470851).Curated

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. 1 PublicationVSP_011181Add
BLAST
Alternative sequencei406 – 857452Missing in isoform 3. 1 PublicationVSP_011182Add
BLAST
Alternative sequencei442 – 49453Missing in isoform 2. 3 PublicationsVSP_011183Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9UPQ3.
SMRiQ9UPQ3. Positions 70-233, 344-422, 530-592, 612-825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125550. 10 interactions.
IntActiQ9UPQ3. 3 interactions.
MINTiMINT-6783717.
STRINGi9606.ENSP00000307634.

PTM databases

PhosphoSiteiQ9UPQ3.

Polymorphism and mutation databases

BioMutaiAGAP1.
DMDMi160332373.

Proteomic databases

MaxQBiQ9UPQ3.
PaxDbiQ9UPQ3.
PRIDEiQ9UPQ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi116987.
GeneCardsiGC02P236402.
HGNCiHGNC:16922. AGAP1.
HPAiHPA051405.
MIMi608651. gene.
neXtProtiNX_Q9UPQ3.
PharmGKBiPA26412.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000007233.
HOVERGENiHBG054045.
InParanoidiQ9UPQ3.
KOiK12491.
OMAiDGMQQRS.
OrthoDBiEOG72VH5V.
PhylomeDBiQ9UPQ3.
TreeFamiTF317762.

Miscellaneous databases

ChiTaRSiAGAP1. human.
GeneWikiiCENTG2.
GenomeRNAii116987.
NextBioi80074.
PROiQ9UPQ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UPQ3.
CleanExiHS_AGAP1.
ExpressionAtlasiQ9UPQ3. baseline and differential.
GenevestigatoriQ9UPQ3.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. 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: May 27, 2015
This is version 153 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

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 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.