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Protein

ADP-ribosylation factor GTPase-activating protein 2

Gene

Arfgap2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). May regulate coatomer-mediated protein transport from the Golgi complex to the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri26 – 4924C4-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

Enzyme and pathway databases

ReactomeiR-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor GTPase-activating protein 2
Short name:
ARF GAP 2
Alternative name(s):
GTPase-activating protein ZNF289
Zinc finger protein 289
Gene namesi
Name:Arfgap2
Synonyms:Zfp289, Znf289
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1924288. Arfgap2.

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
Initiator methionineiRemovedBy similarity
Chaini2 – 520519ADP-ribosylation factor GTPase-activating protein 2PRO_0000278469Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei145 – 1451PhosphoserineCombined sources
Modified residuei200 – 2001PhosphoserineBy similarity
Modified residuei236 – 2361PhosphoserineBy similarity
Modified residuei239 – 2391PhosphoserineCombined sources
Modified residuei333 – 3331PhosphoserineBy similarity
Modified residuei339 – 3391PhosphoserineCombined sources
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei432 – 4321PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99K28.
MaxQBiQ99K28.
PaxDbiQ99K28.
PRIDEiQ99K28.

PTM databases

iPTMnetiQ99K28.
PhosphoSiteiQ99K28.

Expressioni

Tissue specificityi

Highly expressed in liver, heart and kidney. Low expression in skeletal muscle and spleen.1 Publication

Developmental stagei

High levels in mammary glands of virgin mice and in mammary glands of pregnant mice associated with extensive proliferation of ductal cells and lobulo-alveolar development. Expression declines at the beginning of lactation when the glands fully differentiate. No expression after day 2 of lactation until day 21. Expression may be controlled by ID1.1 Publication

Gene expression databases

BgeeiQ99K28.
GenevisibleiQ99K28. MM.

Interactioni

Subunit structurei

Interacts with the coatomer complex. Interacts with the C-terminal appendage domain of COPG1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi218475. 1 interaction.
IntActiQ99K28. 1 interaction.
MINTiMINT-1836442.
STRINGi10090.ENSMUSP00000028691.

Structurei

3D structure databases

ProteinModelPortaliQ99K28.
SMRiQ99K28. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 127117Arf-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 520424Required for interaction with coatomerBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili241 – 30767Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 Arf-GAP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri26 – 4924C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG0706. Eukaryota.
COG5347. LUCA.
GeneTreeiENSGT00390000005436.
HOGENOMiHOG000162970.
HOVERGENiHBG050563.
InParanoidiQ99K28.
KOiK12493.
OMAiAHNCSST.
OrthoDBiEOG7B8S42.
PhylomeDBiQ99K28.
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]

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 1 (identifier: Q99K28-1) [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
MAASPSKTEI QTIFKRLRAI PTNKACFDCG AKSPSWASIT YGVFLCIDCS
60 70 80 90 100
GVHRSLGVHL SFIRSTELDS NWSWLQLRCM QVGGNANATA FFRQHGCMAN
110 120 130 140 150
DANTKYTSRA AQMYREKIRQ LGSAALTRHG TDLWIDSMNS APSHSPEKKD
160 170 180 190 200
SDFFTEHTQA PAWDTAATDP SGTQQPALPS ESSSLAQPEQ GPNTDLLGTS
210 220 230 240 250
PQASLELKSS IIGKKKPAAA KKGLGAKKGL GAQKVSNQSF TEIERQAQVA
260 270 280 290 300
EKLREQQAAD AKKQAEESMV ASMRLAYQEL QIDRKKEEKK LQNLEGKKRE
310 320 330 340 350
QAERLGMGLV SRSSISHSVL SEMQMIEQET PLSAKSSRSQ LDLFDDVGTF
360 370 380 390 400
ASGPPKYKDN PFSLGETFGS RWDSDAAWGM DRVEEKEPEV TISSIRPISE
410 420 430 440 450
RTASRREVET RSSGLESSEA RQKFAGAKAI SSDMFFGREV DSEYEARSRL
460 470 480 490 500
QQLSGSSAIS SSDLFGNMDG AHGGGTVSLG NVLPTADIAQ FKQGVKSVAG
510 520
KMAVLANGVM NSLQDRYGSY
Length:520
Mass (Da):56,598
Last modified:June 1, 2001 - v1
Checksum:i9B06038602F15014
GO
Isoform 2 (identifier: Q99K28-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     206-206: E → ESMYLSAKGPSCTRE

Note: No experimental confirmation available.
Show »
Length:534
Mass (Da):58,110
Checksum:i5711CBFABECB1ECA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti467 – 4671N → D in AAF91258 (PubMed:11278321).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei206 – 2061E → ESMYLSAKGPSCTRE in isoform 2. 1 PublicationVSP_023305

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF229439 mRNA. Translation: AAF91258.1.
AK009565 mRNA. Translation: BAB26362.1.
AK168489 mRNA. Translation: BAE40376.1.
AK169144 mRNA. Translation: BAE40923.1.
AK149837 mRNA. Translation: BAE29114.1.
AL732478 Genomic DNA. Translation: CAM24080.1.
AL732478 Genomic DNA. Translation: CAM24081.1.
BC005495 mRNA. Translation: AAH05495.1.
CCDSiCCDS16430.1. [Q99K28-1]
CCDS50639.1. [Q99K28-2]
RefSeqiNP_001159496.1. NM_001166024.1. [Q99K28-2]
NP_076343.2. NM_023854.2. [Q99K28-1]
UniGeneiMm.386861.
Mm.43636.

Genome annotation databases

EnsembliENSMUST00000028691; ENSMUSP00000028691; ENSMUSG00000027255. [Q99K28-2]
ENSMUST00000080008; ENSMUSP00000078920; ENSMUSG00000027255. [Q99K28-1]
GeneIDi77038.
KEGGimmu:77038.
UCSCiuc008kvq.2. mouse. [Q99K28-1]
uc008kvr.2. mouse. [Q99K28-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF229439 mRNA. Translation: AAF91258.1.
AK009565 mRNA. Translation: BAB26362.1.
AK168489 mRNA. Translation: BAE40376.1.
AK169144 mRNA. Translation: BAE40923.1.
AK149837 mRNA. Translation: BAE29114.1.
AL732478 Genomic DNA. Translation: CAM24080.1.
AL732478 Genomic DNA. Translation: CAM24081.1.
BC005495 mRNA. Translation: AAH05495.1.
CCDSiCCDS16430.1. [Q99K28-1]
CCDS50639.1. [Q99K28-2]
RefSeqiNP_001159496.1. NM_001166024.1. [Q99K28-2]
NP_076343.2. NM_023854.2. [Q99K28-1]
UniGeneiMm.386861.
Mm.43636.

3D structure databases

ProteinModelPortaliQ99K28.
SMRiQ99K28. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218475. 1 interaction.
IntActiQ99K28. 1 interaction.
MINTiMINT-1836442.
STRINGi10090.ENSMUSP00000028691.

PTM databases

iPTMnetiQ99K28.
PhosphoSiteiQ99K28.

Proteomic databases

EPDiQ99K28.
MaxQBiQ99K28.
PaxDbiQ99K28.
PRIDEiQ99K28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028691; ENSMUSP00000028691; ENSMUSG00000027255. [Q99K28-2]
ENSMUST00000080008; ENSMUSP00000078920; ENSMUSG00000027255. [Q99K28-1]
GeneIDi77038.
KEGGimmu:77038.
UCSCiuc008kvq.2. mouse. [Q99K28-1]
uc008kvr.2. mouse. [Q99K28-2]

Organism-specific databases

CTDi84364.
MGIiMGI:1924288. Arfgap2.

Phylogenomic databases

eggNOGiKOG0706. Eukaryota.
COG5347. LUCA.
GeneTreeiENSGT00390000005436.
HOGENOMiHOG000162970.
HOVERGENiHBG050563.
InParanoidiQ99K28.
KOiK12493.
OMAiAHNCSST.
OrthoDBiEOG7B8S42.
PhylomeDBiQ99K28.
TreeFamiTF313985.

Enzyme and pathway databases

ReactomeiR-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Miscellaneous databases

ChiTaRSiArfgap2. mouse.
PROiQ99K28.
SOURCEiSearch...

Gene expression databases

BgeeiQ99K28.
GenevisibleiQ99K28. MM.

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

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a zinc finger protein involved in Id-1-stimulated mammary edithelial cell growth."
    Singh J., Itahana Y., Parrinello S., Murata K., Desprez P.-Y.
    J. Biol. Chem. 276:11852-11858(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Mammary epithelium.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Amnion, Bone marrow and Heart.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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).
    Tissue: Mammary tumor.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-239 AND SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiARFG2_MOUSE
AccessioniPrimary (citable) accession number: Q99K28
Secondary accession number(s): Q9D758, Q9JIH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 121 of the entry and version 1 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.