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Protein

Arf-GAP domain and FG repeat-containing protein 1

Gene

AGFG1

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

Functioni

Required for vesicle docking or fusion during acrosome biogenesis (By similarity). May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication.By similarity3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri29 – 5224C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • GTPase activator activity Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • RNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, mRNA transport, Spermatogenesis, Transport

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Arf-GAP domain and FG repeat-containing protein 1
Alternative name(s):
HIV-1 Rev-binding protein
Nucleoporin-like protein RIP
Rev-interacting protein
Rev/Rex activation domain-binding protein
Gene namesi
Name:AGFG1
Synonyms:HRB, RAB, RIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5175. AGFG1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29449.

Polymorphism and mutation databases

BioMutaiAGFG1.
DMDMi26007019.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 562562Arf-GAP domain and FG repeat-containing protein 1PRO_0000204904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei177 – 1771PhosphothreonineCombined sources
Modified residuei181 – 1811PhosphoserineCombined sources
Glycosylationi367 – 3671O-linked (GlcNAc)By similarity

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP52594.
MaxQBiP52594.
PaxDbiP52594.
PRIDEiP52594.

PTM databases

iPTMnetiP52594.
PhosphoSiteiP52594.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiP52594.
CleanExiHS_AGFG1.
ExpressionAtlasiP52594. baseline and differential.
GenevisibleiP52594. HS.

Organism-specific databases

HPAiHPA008741.

Interactioni

Subunit structurei

Interacts with EPS15R and EPS15. Interacts with FCHO1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NYAP2Q9P2423EBI-996560,EBI-10269689
POLE2P562823EBI-996560,EBI-713847
VAMP7P518097EBI-996560,EBI-1052205

Protein-protein interaction databases

BioGridi109503. 38 interactions.
DIPiDIP-35546N.
IntActiP52594. 9 interactions.
MINTiMINT-1651458.
STRINGi9606.ENSP00000387282.

Structurei

Secondary structure

1
562
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2118Combined sources
Helixi24 – 274Combined sources
Turni30 – 323Combined sources
Beta strandi39 – 413Combined sources
Turni42 – 454Combined sources
Beta strandi46 – 483Combined sources
Helixi50 – 567Combined sources
Beta strandi59 – 613Combined sources
Beta strandi65 – 673Combined sources
Turni68 – 703Combined sources
Helixi75 – 839Combined sources
Helixi85 – 939Combined sources
Turni94 – 963Combined sources
Turni99 – 1013Combined sources
Helixi110 – 12112Combined sources
Helixi130 – 1345Combined sources
Beta strandi157 – 1593Combined sources
Helixi160 – 1645Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9LNMR-A14-134[»]
2OLMX-ray1.48A4-141[»]
2VX8X-ray2.20A/B/C/D136-175[»]
ProteinModelPortaliP52594.
SMRiP52594. Positions 14-134, 153-186.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52594.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 135125Arf-GAPPROSITE-ProRule annotationAdd
BLAST

Domaini

Contains FG repeats. The FG repeat region is required for acting as a cofactor of HIV-1 Rev.

Sequence similaritiesi

Contains 1 Arf-GAP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri29 – 5224C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IUMA. Eukaryota.
COG5347. LUCA.
GeneTreeiENSGT00560000077249.
HOGENOMiHOG000253009.
HOVERGENiHBG006551.
InParanoidiP52594.
KOiK15044.
OMAiSSCSFGE.
OrthoDBiEOG7W9RW0.
PhylomeDBiP52594.
TreeFamiTF325357.

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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P52594-1) [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
MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT
60 70 80 90 100
SCSGSLRGLN PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR
110 120 130 140 150
SSAIPDFRDP QKVKEFLQEK YEKKRWYVPP EQAKVVASVH ASISGSSASS
160 170 180 190 200
TSSTPEVKPL KSLLGDSAPT LHLNKGTPSQ SPVVGRSQGQ QQEKKQFDLL
210 220 230 240 250
SDLGSDIFAA PAPQSTATAN FANFAHFNSH AAQNSANADF ANFDAFGQSS
260 270 280 290 300
GSSNFGGFPT ASHSPFQPQT TGGSAASVNA NFAHFDNFPK SSSADFGTFN
310 320 330 340 350
TSQSHQTASA VSKVSTNKAG LQTADKYAAL ANLDNIFSAG QGGDQGSGFG
360 370 380 390 400
TTGKAPVGSV VSVPSQSSAS SDKYAALAEL DSVFSSAATS SNAYTSTSNA
410 420 430 440 450
SSNVFGTVPV VASAQTQPAS SSVPAPFGAT PSTNPFVAAA GPSVASSTNP
460 470 480 490 500
FQTNARGATA ATFGTASMSM PTGFGTPAPY SLPTSFSGSF QQPAFPAQAA
510 520 530 540 550
FPQQTAFSQQ PNGAGFAAFG QTKPVVTPFG QVAAAGVSSN PFMTGAPTGQ
560
FPTGSSSTNP FL
Length:562
Mass (Da):58,260
Last modified:November 28, 2002 - v2
Checksum:i9A2242217F53B4D9
GO
Isoform 2 (identifier: P52594-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     232-271: Missing.

Show »
Length:522
Mass (Da):54,182
Checksum:iDE779347F13D2557
GO
Isoform 3 (identifier: P52594-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     513-514: Missing.

Show »
Length:560
Mass (Da):58,132
Checksum:iAE7E67C63C6830ED
GO
Isoform 4 (identifier: P52594-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     272-272: G → AFRMLSSSCSFGEFTSAFPLQATHS
     513-514: Missing.

Note: No experimental confirmation available.
Show »
Length:584
Mass (Da):60,767
Checksum:i4D508894C0FFE3F6
GO

Sequence cautioni

The sequence BAG53473.1 differs from that shown.Aberrant splicing within exon 1.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251H → R in CAA61667 (PubMed:7637788).Curated
Sequence conflicti429 – 4291A → R in CAA61667 (PubMed:7637788).Curated
Sequence conflicti542 – 5421F → S in BAG53473 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei232 – 27140Missing in isoform 2. 1 PublicationVSP_017600Add
BLAST
Alternative sequencei272 – 2721G → AFRMLSSSCSFGEFTSAFPL QATHS in isoform 4. 1 PublicationVSP_046186
Alternative sequencei513 – 5142Missing in isoform 3 and isoform 4. 2 PublicationsVSP_017601

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42025 Genomic DNA. Translation: AAC37580.1.
X89478 mRNA. Translation: CAA61667.1.
AK097451 mRNA. Translation: BAG53473.1. Sequence problems.
AC105286 Genomic DNA. Translation: AAX93270.1.
AC097662 Genomic DNA. Translation: AAY24254.1.
BC030592 mRNA. Translation: AAH30592.1.
BC096272 mRNA. Translation: AAH96272.1.
BC096273 mRNA. Translation: AAH96273.1.
BC096274 mRNA. Translation: AAH96274.1.
BC096275 mRNA. Translation: AAH96275.1.
CCDSiCCDS2467.1. [P52594-1]
CCDS46533.1. [P52594-4]
CCDS46534.1. [P52594-3]
CCDS46535.1. [P52594-2]
PIRiA57088.
RefSeqiNP_001128659.1. NM_001135187.1. [P52594-4]
NP_001128660.1. NM_001135188.1. [P52594-3]
NP_001128661.1. NM_001135189.1. [P52594-2]
NP_004495.2. NM_004504.4. [P52594-1]
UniGeneiHs.352962.

Genome annotation databases

EnsembliENST00000310078; ENSP00000312059; ENSG00000173744. [P52594-1]
ENST00000373671; ENSP00000362775; ENSG00000173744. [P52594-2]
ENST00000409171; ENSP00000387218; ENSG00000173744. [P52594-3]
ENST00000409979; ENSP00000387282; ENSG00000173744. [P52594-4]
GeneIDi3267.
KEGGihsa:3267.
UCSCiuc002vpc.3. human. [P52594-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42025 Genomic DNA. Translation: AAC37580.1.
X89478 mRNA. Translation: CAA61667.1.
AK097451 mRNA. Translation: BAG53473.1. Sequence problems.
AC105286 Genomic DNA. Translation: AAX93270.1.
AC097662 Genomic DNA. Translation: AAY24254.1.
BC030592 mRNA. Translation: AAH30592.1.
BC096272 mRNA. Translation: AAH96272.1.
BC096273 mRNA. Translation: AAH96273.1.
BC096274 mRNA. Translation: AAH96274.1.
BC096275 mRNA. Translation: AAH96275.1.
CCDSiCCDS2467.1. [P52594-1]
CCDS46533.1. [P52594-4]
CCDS46534.1. [P52594-3]
CCDS46535.1. [P52594-2]
PIRiA57088.
RefSeqiNP_001128659.1. NM_001135187.1. [P52594-4]
NP_001128660.1. NM_001135188.1. [P52594-3]
NP_001128661.1. NM_001135189.1. [P52594-2]
NP_004495.2. NM_004504.4. [P52594-1]
UniGeneiHs.352962.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9LNMR-A14-134[»]
2OLMX-ray1.48A4-141[»]
2VX8X-ray2.20A/B/C/D136-175[»]
ProteinModelPortaliP52594.
SMRiP52594. Positions 14-134, 153-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109503. 38 interactions.
DIPiDIP-35546N.
IntActiP52594. 9 interactions.
MINTiMINT-1651458.
STRINGi9606.ENSP00000387282.

PTM databases

iPTMnetiP52594.
PhosphoSiteiP52594.

Polymorphism and mutation databases

BioMutaiAGFG1.
DMDMi26007019.

Proteomic databases

EPDiP52594.
MaxQBiP52594.
PaxDbiP52594.
PRIDEiP52594.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310078; ENSP00000312059; ENSG00000173744. [P52594-1]
ENST00000373671; ENSP00000362775; ENSG00000173744. [P52594-2]
ENST00000409171; ENSP00000387218; ENSG00000173744. [P52594-3]
ENST00000409979; ENSP00000387282; ENSG00000173744. [P52594-4]
GeneIDi3267.
KEGGihsa:3267.
UCSCiuc002vpc.3. human. [P52594-1]

Organism-specific databases

CTDi3267.
GeneCardsiAGFG1.
HGNCiHGNC:5175. AGFG1.
HPAiHPA008741.
MIMi600862. gene.
neXtProtiNX_P52594.
PharmGKBiPA29449.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IUMA. Eukaryota.
COG5347. LUCA.
GeneTreeiENSGT00560000077249.
HOGENOMiHOG000253009.
HOVERGENiHBG006551.
InParanoidiP52594.
KOiK15044.
OMAiSSCSFGE.
OrthoDBiEOG7W9RW0.
PhylomeDBiP52594.
TreeFamiTF325357.

Miscellaneous databases

ChiTaRSiAGFG1. human.
EvolutionaryTraceiP52594.
GeneWikiiHRB_(gene).
GenomeRNAii3267.
NextBioi12971.
PROiP52594.
SOURCEiSearch...

Gene expression databases

BgeeiP52594.
CleanExiHS_AGFG1.
ExpressionAtlasiP52594. baseline and differential.
GenevisibleiP52594. HS.

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. "Identification of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory proteins."
    Bogerd H.P., Fridell R.A., Madore S., Cullen B.R.
    Cell 82:485-494(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1), INTERACTION WITH HIV-1 REV AND HTLV-1 REX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "A human nucleoporin-like protein that specifically interacts with HIV Rev."
    Fritz C.C., Zapp M.L., Green M.R.
    Nature 376:530-533(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HIV-1 REV.
    Tissue: Placenta.
  3. "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] (ISOFORM 4).
    Tissue: Testis.
  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; 2 AND 3).
    Tissue: Testis.
  6. "The eps15 homology (EH) domain-based interaction between eps15 and hrb connects the molecular machinery of endocytosis to that of nucleocytosolic transport."
    Doria M., Salcini A.E., Colombo E., Parslow T.G., Pelicci P.G., Di Fiore P.P.
    J. Cell Biol. 147:1379-1384(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EPS15, FUNCTION.
  7. "hRIP, a cellular cofactor for Rev function, promotes release of HIV RNAs from the perinuclear region."
    Sanchez-Velar N., Udofia E.B., Yu Z., Zapp M.L.
    Genes Dev. 18:23-34(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The cellular HIV-1 Rev cofactor hRIP is required for viral replication."
    Yu Z., Sanchez-Velar N., Catrina I.E., Kittler E.L., Udofia E.B., Zapp M.L.
    Proc. Natl. Acad. Sci. U.S.A. 102:4027-4032(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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 SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
    Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
    Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCHO1.
  18. "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-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Solution structure of the ARFGAP domain of human RIP."
    RIKEN structural genomics initiative (RSGI)
    Submitted (DEC-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 14-134.

Entry informationi

Entry nameiAGFG1_HUMAN
AccessioniPrimary (citable) accession number: P52594
Secondary accession number(s): B3KUL1
, E9PHX7, Q15277, Q4VAS0, Q4VAS1, Q4VAS3, Q53QT8, Q53R11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 28, 2002
Last modified: May 11, 2016
This is version 153 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.