Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ADP-ribosylation factor GTPase-activating protein 3

Gene

Arfgap3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes (By similarity).By similarity

Enzyme regulationi

GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri25 – 4824C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor GTPase-activating protein 3
Short name:
ARF GAP 3
Gene namesi
Name:Arfgap3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1913501. Arfgap3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 523523ADP-ribosylation factor GTPase-activating protein 3PRO_0000074194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei231 – 2311PhosphoserineBy similarity
Modified residuei241 – 2411PhosphoserineCombined sources
Modified residuei270 – 2701PhosphoserineBy similarity
Modified residuei274 – 2741PhosphoserineBy similarity
Modified residuei331 – 3311PhosphoserineCombined sources
Modified residuei377 – 3771PhosphoserineBy similarity
Modified residuei435 – 4351PhosphoserineBy similarity
Modified residuei458 – 4581PhosphoserineBy similarity
Modified residuei460 – 4601PhosphoserineBy similarity
Modified residuei462 – 4621PhosphoserineBy similarity
Modified residuei464 – 4641PhosphoserineBy similarity
Modified residuei465 – 4651PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9D8S3.
MaxQBiQ9D8S3.
PaxDbiQ9D8S3.
PeptideAtlasiQ9D8S3.
PRIDEiQ9D8S3.

PTM databases

iPTMnetiQ9D8S3.
PhosphoSiteiQ9D8S3.

Expressioni

Gene expression databases

BgeeiQ9D8S3.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064893.

Structurei

3D structure databases

ProteinModelPortaliQ9D8S3.
SMRiQ9D8S3. Positions 3-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 126117Arf-GAPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi348 – 40861Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 Arf-GAP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri25 – 4824C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0706. Eukaryota.
COG5347. LUCA.
HOGENOMiHOG000162970.
HOVERGENiHBG050563.
InParanoidiQ9D8S3.
KOiK12493.
OrthoDBiEOG7B8S42.
PhylomeDBiQ9D8S3.
TreeFamiTF313985.

Family and domain databases

InterProiIPR001164. ArfGAP.
[Graphical view]
PfamiPF01412. ArfGap. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00105. ArfGap. 1 hit.
[Graphical view]
PROSITEiPS50115. ARFGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D8S3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDPSKQDIL AIFKRLRSVP TNKVCFDCGA KNPSWASISY GVFLCIDCSG
60 70 80 90 100
SHRSLGVHLS FIRSTELDSN WSWFQLRCMQ VGGNSNASSF FHQHGCATKD
110 120 130 140 150
TNAKYNSRAA QLYREKIKTL ATQATRRHGT DLWLDSCAAP PVSPPPKEED
160 170 180 190 200
FFASHASLEV SGAMQASAQP ESASSTPWGL ETTPEKHEGG PGQGPSVEGL
210 220 230 240 250
NTPGKAAPEV SSIIKKKPNQ AKKGLGAKKG SLGAQKLTNT SFTEIEKQAQ
260 270 280 290 300
AVDKRKEQED LARGAPKEES IVSSLRLAYK DLEISRKKDE RLNLSGQKKV
310 320 330 340 350
EAERLGMGFG SCRSGISHSV TSDMQTIEQE SPTLAKPRRK YQEDPEDSYF
360 370 380 390 400
SSSSKWSEQS SRYFDDPMEL RSSSFSSWDD GADSYWKKDS SRDPEPAMRS
410 420 430 440 450
TGSSDRPSAR RKPEYEPIGS TDEAQKKFGN VKAISSDMYF GIQAQTDFET
460 470 480 490 500
RARLERLSTS SSISSADLFD EQRKQTAGNY NLSNVLPNAP DMAQFKQGVR
510 520
SVAGKLSVFA NGVMTSIQDR YGS
Length:523
Mass (Da):57,456
Last modified:January 15, 2008 - v2
Checksum:iFC093B11DB765BC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081P → PA in BAB25220 (PubMed:16141072).Curated
Sequence conflicti361 – 3611S → SS in BAB25220 (PubMed:16141072).Curated
Sequence conflicti361 – 3611S → SS in BAC26229 (PubMed:16141072).Curated
Sequence conflicti361 – 3611S → SS in AAH04081 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007732 mRNA. Translation: BAB25220.1.
AK028990 mRNA. Translation: BAC26229.1.
AK075788 mRNA. Translation: BAC35959.1.
AK169107 mRNA. Translation: BAE40889.1.
BC004081 mRNA. Translation: AAH04081.1.
BC060369 mRNA. Translation: AAH60369.1.
RefSeqiNP_079721.2. NM_025445.4.
XP_006521316.2. XM_006521253.2.
XP_006521318.2. XM_006521255.2.
UniGeneiMm.258910.

Genome annotation databases

GeneIDi66251.
KEGGimmu:66251.
UCSCiuc007xag.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007732 mRNA. Translation: BAB25220.1.
AK028990 mRNA. Translation: BAC26229.1.
AK075788 mRNA. Translation: BAC35959.1.
AK169107 mRNA. Translation: BAE40889.1.
BC004081 mRNA. Translation: AAH04081.1.
BC060369 mRNA. Translation: AAH60369.1.
RefSeqiNP_079721.2. NM_025445.4.
XP_006521316.2. XM_006521253.2.
XP_006521318.2. XM_006521255.2.
UniGeneiMm.258910.

3D structure databases

ProteinModelPortaliQ9D8S3.
SMRiQ9D8S3. Positions 3-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064893.

PTM databases

iPTMnetiQ9D8S3.
PhosphoSiteiQ9D8S3.

Proteomic databases

EPDiQ9D8S3.
MaxQBiQ9D8S3.
PaxDbiQ9D8S3.
PeptideAtlasiQ9D8S3.
PRIDEiQ9D8S3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi66251.
KEGGimmu:66251.
UCSCiuc007xag.1. mouse.

Organism-specific databases

CTDi26286.
MGIiMGI:1913501. Arfgap3.

Phylogenomic databases

eggNOGiKOG0706. Eukaryota.
COG5347. LUCA.
HOGENOMiHOG000162970.
HOVERGENiHBG050563.
InParanoidiQ9D8S3.
KOiK12493.
OrthoDBiEOG7B8S42.
PhylomeDBiQ9D8S3.
TreeFamiTF313985.

Miscellaneous databases

ChiTaRSiArfgap3. mouse.
PROiQ9D8S3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8S3.

Family and domain databases

InterProiIPR001164. ArfGAP.
[Graphical view]
PfamiPF01412. ArfGap. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00105. ArfGap. 1 hit.
[Graphical view]
PROSITEiPS50115. ARFGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Amnion, Pancreas and Skin.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland and Olfactory epithelium.
  3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiARFG3_MOUSE
AccessioniPrimary (citable) accession number: Q9D8S3
Secondary accession number(s): Q544V6, Q8BW06, Q99KN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: January 15, 2008
Last modified: July 6, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.