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Protein

ADP-ribosylation factor GTPase-activating protein 1

Gene

ARFGAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri22 – 4524C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • GTPase activator activity Source: MGI
  • zinc ion binding Source: InterPro

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

ReactomeiREACT_11096. COPI Mediated Transport.
REACT_18273. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor GTPase-activating protein 1
Short name:
ARF GAP 1
Alternative name(s):
ADP-ribosylation factor 1 GTPase-activating protein
Short name:
ARF1 GAP
ARF1-directed GTPase-activating protein
Gene namesi
Name:ARFGAP1
Synonyms:ARF1GAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15852. ARFGAP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164741246.

Polymorphism and mutation databases

DMDMi27923731.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406ADP-ribosylation factor GTPase-activating protein 1PRO_0000074190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei135 – 1351Phosphothreonine2 Publications
Modified residuei150 – 1501Phosphoserine1 Publication
Modified residuei189 – 1891Phosphothreonine4 Publications
Modified residuei231 – 2311N6-acetyllysine1 Publication
Modified residuei304 – 3041Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8N6T3.
PaxDbiQ8N6T3.
PRIDEiQ8N6T3.

PTM databases

PhosphoSiteiQ8N6T3.

Expressioni

Gene expression databases

BgeeiQ8N6T3.
CleanExiHS_ARFGAP1.
ExpressionAtlasiQ8N6T3. baseline and differential.
GenevestigatoriQ8N6T3.

Organism-specific databases

HPAiHPA051019.
HPA056273.

Interactioni

Subunit structurei

Interacts with ARF1. Interacts with the COPI coat proteins, KDELR1 and TMED2. The interaction with TMED2 inhibits the GAP activity (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FOSQ6FG413EBI-716933,EBI-10198738
GABARAPL2P605203EBI-716933,EBI-720116
GRNP287993EBI-716933,EBI-747754
KRTAP10-9P604113EBI-716933,EBI-10172052
KRTAP3-2Q9BYR73EBI-716933,EBI-751260
KRTAP9-2Q9BYQ43EBI-716933,EBI-1044640
LRRK2Q5S0076EBI-6288865,EBI-5323863
TRIM23P364063EBI-716933,EBI-740098

Protein-protein interaction databases

BioGridi120856. 38 interactions.
IntActiQ8N6T3. 27 interactions.
MINTiMINT-1409968.
STRINGi9606.ENSP00000314615.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Turni17 – 204Combined sources
Turni23 – 253Combined sources
Beta strandi32 – 343Combined sources
Turni35 – 384Combined sources
Beta strandi39 – 413Combined sources
Helixi43 – 5210Combined sources
Turni54 – 563Combined sources
Beta strandi59 – 624Combined sources
Helixi69 – 779Combined sources
Helixi80 – 889Combined sources
Helixi99 – 1035Combined sources
Helixi106 – 11914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWDX-ray2.40A/B1-128[»]
3O47X-ray2.80A/B1-140[»]
ProteinModelPortaliQ8N6T3.
SMRiQ8N6T3. Positions 3-153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N6T3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 124118Arf-GAPPROSITE-ProRule annotationAdd
BLAST

Domaini

The region downstream of Arf-GAP domain is essential to GAP activity in vivo. This region may be required for its targeting to Golgi membranes (By similarity).By similarity

Sequence similaritiesi

Contains 1 Arf-GAP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri22 – 4524C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00670000098104.
HOGENOMiHOG000008494.
HOVERGENiHBG050562.
InParanoidiQ8N6T3.
KOiK12492.
OMAiFQNSTID.
OrthoDBiEOG7C8GH3.
PhylomeDBiQ8N6T3.
TreeFamiTF105931.

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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N6T3-1) [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
MASPRTRKVL KEVRVQDENN VCFECGAFNP QWVSVTYGIW ICLECSGRHR
60 70 80 90 100
GLGVHLSFVR SVTMDKWKDI ELEKMKAGGN AKFREFLESQ EDYDPCWSLQ
110 120 130 140 150
EKYNSRAAAL FRDKVVALAE GREWSLESSP AQNWTPPQPR TLPSMVHRVS
160 170 180 190 200
GQPQSVTASS DKAFEDWLND DLGSYQGAQG NRYVGFGNTP PPQKKEDDFL
210 220 230 240 250
NNAMSSLYSG WSSFTTGASR FASAAKEGAT KFGSQASQKA SELGHSLNEN
260 270 280 290 300
VLKPAQEKVK EGKIFDDVSS GVSQLASKVQ GVGSKGWRDV TTFFSGKAEG
310 320 330 340 350
PLDSPSEGHS YQNSGLDHFQ NSNIDQSFWE TFGSAEPTKT RKSPSSDSWT
360 370 380 390 400
CADTSTERRS SDSWEVWGSA STNRNSNSDG GEGGEGTKKA VPPAVPTDDG

WDNQNW
Length:406
Mass (Da):44,668
Last modified:January 27, 2003 - v2
Checksum:iCAE41828DE660621
GO
Isoform 2 (identifier: Q8N6T3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     239-239: K → KFWGHKQQPEP
     279-280: Missing.

Note: No experimental confirmation available.

Show »
Length:414
Mass (Da):45,676
Checksum:iBD081C6CE6CF0A18
GO
Isoform 3 (identifier: Q8N6T3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     279-406: VQGVGSKGWR...TDDGWDNQNW → CQRRLCCHQS...AVWTTSKTAT

Show »
Length:403
Mass (Da):44,467
Checksum:i0C695741E21D0F6F
GO
Isoform 4 (identifier: Q8N6T3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MASPRTRKVLKEVRVQDENNVCFECGAFNPQWVS → MLSSESSWSLRRITILAGPCRRSTTAEPRPSLGI
     35-147: Missing.

Note: No experimental confirmation available.

Show »
Length:293
Mass (Da):31,476
Checksum:iC0EEFC7461FF6CB3
GO
Isoform 5 (identifier: Q8N6T3-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: MASPRTRKVLKEVRVQDENNVCFECGAFNPQWVSVTYGIWICLECSGRHRGLGVHLS → MRTT
     239-239: K → KFWGHKQQPEP
     279-280: Missing.

Show »
Length:361
Mass (Da):39,705
Checksum:iD34FF3C257C7E8FB
GO

Sequence cautioni

The sequence BAB55009.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB55113.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB70901.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741Q → R in BAB55009 (PubMed:14702039).Curated
Sequence conflicti358 – 3581R → G in BAH12326 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti184 – 1841V → M.
Corresponds to variant rs2273499 [ dbSNP | Ensembl ].
VAR_015187

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5757MASPR…GVHLS → MRTT in isoform 5. 1 PublicationVSP_055739Add
BLAST
Alternative sequencei1 – 3434MASPR…PQWVS → MLSSESSWSLRRITILAGPC RRSTTAEPRPSLGI in isoform 4. 1 PublicationVSP_055379Add
BLAST
Alternative sequencei35 – 147113Missing in isoform 4. 1 PublicationVSP_055380Add
BLAST
Alternative sequencei239 – 2391K → KFWGHKQQPEP in isoform 2 and isoform 5. 2 PublicationsVSP_000298
Alternative sequencei279 – 406128VQGVG…DNQNW → CQRRLCCHQSHCSAGHLGRA FCPVSWHEALCGQTGREEQA SLLPPKHVVGALEVCARGCP RCHVPHTPGTAAEWPGRLCL SRESVVRDGGTSPPFFRGKQ RAPWTAPRRATVIRTAVWTT SKTAT in isoform 3. 1 PublicationVSP_021818Add
BLAST
Alternative sequencei279 – 2802Missing in isoform 2 and isoform 5. 2 PublicationsVSP_000299

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001629 mRNA. Translation: BAA91796.1.
AK027268 mRNA. Translation: BAB55009.1. Different initiation.
AK296351 mRNA. Translation: BAH12326.1.
AK027441 mRNA. Translation: BAB55113.1. Different initiation.
AK303454 mRNA. Translation: BAH13964.1.
AL121827 Genomic DNA. Translation: CAX12645.1.
CH471077 Genomic DNA. Translation: EAW75292.1.
CH471077 Genomic DNA. Translation: EAW75294.1.
BC000786 mRNA. Translation: AAH00786.1.
BC006085 mRNA. Translation: AAH06085.1.
BC011876 mRNA. Translation: AAH11876.1.
BC028233 mRNA. Translation: AAH28233.1.
AL137744 mRNA. Translation: CAB70901.1. Sequence problems.
AB015340 mRNA. Translation: BAA88117.1.
CCDSiCCDS13515.1. [Q8N6T3-1]
CCDS13516.1. [Q8N6T3-2]
CCDS63326.1. [Q8N6T3-3]
CCDS63327.1. [Q8N6T3-5]
CCDS63328.1. [Q8N6T3-4]
PIRiT46298.
RefSeqiNP_001268411.1. NM_001281482.1. [Q8N6T3-3]
NP_001268412.1. NM_001281483.1. [Q8N6T3-5]
NP_001268413.1. NM_001281484.1. [Q8N6T3-4]
NP_060679.1. NM_018209.3. [Q8N6T3-1]
NP_783202.1. NM_175609.2. [Q8N6T3-2]
UniGeneiHs.25584.

Genome annotation databases

EnsembliENST00000353546; ENSP00000314615; ENSG00000101199. [Q8N6T3-2]
ENST00000370275; ENSP00000359298; ENSG00000101199. [Q8N6T3-3]
ENST00000370283; ENSP00000359306; ENSG00000101199. [Q8N6T3-1]
ENST00000519273; ENSP00000443716; ENSG00000101199. [Q8N6T3-4]
ENST00000519604; ENSP00000430500; ENSG00000101199. [Q8N6T3-5]
GeneIDi55738.
KEGGihsa:55738.
UCSCiuc002yel.3. human. [Q8N6T3-2]
uc002yem.3. human. [Q8N6T3-1]
uc011aat.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001629 mRNA. Translation: BAA91796.1.
AK027268 mRNA. Translation: BAB55009.1. Different initiation.
AK296351 mRNA. Translation: BAH12326.1.
AK027441 mRNA. Translation: BAB55113.1. Different initiation.
AK303454 mRNA. Translation: BAH13964.1.
AL121827 Genomic DNA. Translation: CAX12645.1.
CH471077 Genomic DNA. Translation: EAW75292.1.
CH471077 Genomic DNA. Translation: EAW75294.1.
BC000786 mRNA. Translation: AAH00786.1.
BC006085 mRNA. Translation: AAH06085.1.
BC011876 mRNA. Translation: AAH11876.1.
BC028233 mRNA. Translation: AAH28233.1.
AL137744 mRNA. Translation: CAB70901.1. Sequence problems.
AB015340 mRNA. Translation: BAA88117.1.
CCDSiCCDS13515.1. [Q8N6T3-1]
CCDS13516.1. [Q8N6T3-2]
CCDS63326.1. [Q8N6T3-3]
CCDS63327.1. [Q8N6T3-5]
CCDS63328.1. [Q8N6T3-4]
PIRiT46298.
RefSeqiNP_001268411.1. NM_001281482.1. [Q8N6T3-3]
NP_001268412.1. NM_001281483.1. [Q8N6T3-5]
NP_001268413.1. NM_001281484.1. [Q8N6T3-4]
NP_060679.1. NM_018209.3. [Q8N6T3-1]
NP_783202.1. NM_175609.2. [Q8N6T3-2]
UniGeneiHs.25584.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWDX-ray2.40A/B1-128[»]
3O47X-ray2.80A/B1-140[»]
ProteinModelPortaliQ8N6T3.
SMRiQ8N6T3. Positions 3-153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120856. 38 interactions.
IntActiQ8N6T3. 27 interactions.
MINTiMINT-1409968.
STRINGi9606.ENSP00000314615.

PTM databases

PhosphoSiteiQ8N6T3.

Polymorphism and mutation databases

DMDMi27923731.

Proteomic databases

MaxQBiQ8N6T3.
PaxDbiQ8N6T3.
PRIDEiQ8N6T3.

Protocols and materials databases

DNASUi55738.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353546; ENSP00000314615; ENSG00000101199. [Q8N6T3-2]
ENST00000370275; ENSP00000359298; ENSG00000101199. [Q8N6T3-3]
ENST00000370283; ENSP00000359306; ENSG00000101199. [Q8N6T3-1]
ENST00000519273; ENSP00000443716; ENSG00000101199. [Q8N6T3-4]
ENST00000519604; ENSP00000430500; ENSG00000101199. [Q8N6T3-5]
GeneIDi55738.
KEGGihsa:55738.
UCSCiuc002yel.3. human. [Q8N6T3-2]
uc002yem.3. human. [Q8N6T3-1]
uc011aat.1. human.

Organism-specific databases

CTDi55738.
GeneCardsiGC20P061904.
H-InvDBHIX0174713.
HGNCiHGNC:15852. ARFGAP1.
HPAiHPA051019.
HPA056273.
MIMi608377. gene.
neXtProtiNX_Q8N6T3.
PharmGKBiPA164741246.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00670000098104.
HOGENOMiHOG000008494.
HOVERGENiHBG050562.
InParanoidiQ8N6T3.
KOiK12492.
OMAiFQNSTID.
OrthoDBiEOG7C8GH3.
PhylomeDBiQ8N6T3.
TreeFamiTF105931.

Enzyme and pathway databases

ReactomeiREACT_11096. COPI Mediated Transport.
REACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSiARFGAP1. human.
EvolutionaryTraceiQ8N6T3.
GeneWikiiARFGAP1.
GenomeRNAii55738.
NextBioi35479321.
PROiQ8N6T3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N6T3.
CleanExiHS_ARFGAP1.
ExpressionAtlasiQ8N6T3. baseline and differential.
GenevestigatoriQ8N6T3.

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. "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] (ISOFORMS 1; 4 AND 5).
    Tissue: Thymus.
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 2 AND 3).
    Tissue: Brain and Fetal brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 240-406 (ISOFORM 1).
    Tissue: Testis.
  6. "HRI NTT human fetal brain cDNA project."
    Ueki N.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 299-406 (ISOFORM 1).
    Tissue: Fetal brain.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND THR-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: 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-150 AND THR-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Crystal structure of the ARFGAP domain of human ARFGAP1."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-128 IN COMPLEX WITH ZINC IONS.

Entry informationi

Entry nameiARFG1_HUMAN
AccessioniPrimary (citable) accession number: Q8N6T3
Secondary accession number(s): B7Z3U0
, B7Z8H8, B7ZBI3, E1P5I9, E7EV62, Q6PK71, Q96KC4, Q96T02, Q9NSU3, Q9NVF6, Q9UIL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 27, 2003
Last modified: May 27, 2015
This is version 132 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.