P52594 (AGFG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arf-GAP domain and FG repeats-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 names

Name:	AGFG1
Synonyms:	HRB, RAB, RIP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6 Ref.7
Subunit structure	Interacts with EPS15R and EPS15. Ref.1 Ref.2 Ref.5
Subcellular location	Nucleus. Cytoplasmic vesicle Ref.1 Ref.5.
Tissue specificity	Ubiquitously expressed. Ref.1
Domain	Contains FG repeats. The FG repeat region is required for acting as a cofactor of HIV-1 Rev.
Post-translational modification	O-glycosylated By similarity.
Sequence similarities	Contains 1 Arf-GAP domain.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis Transport mRNA transport
Cellular component	Cytoplasmic vesicle Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Developmental protein
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW mRNA export from nucleus Traceable author statement. Source: ProtInc multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW regulation of ARF GTPase activity Inferred from electronic annotation. Source: InterPro spermatogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Traceable author statement. Source: ProtInc
Molecular function	ARF GTPase activator activity Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VAMP7	P51809	7	EBI-996560,EBI-1052205

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P52594-1)

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.

Isoform 2 (identifier: P52594-2)

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

Isoform 3 (identifier: P52594-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 562

562

Arf-GAP domain and FG repeats-containing protein 1

PRO_0000204904

Regions

Domain

11 – 135

125

Arf-GAP

Zinc finger

29 – 52

24

C4-type

Amino acid modifications

Modified residue

177

1

Phosphothreonine Ref.8 Ref.9 Ref.10 Ref.11

Modified residue

179

1

Phosphoserine By similarity

Modified residue

181

1

Phosphoserine Ref.8 Ref.9 Ref.10

Glycosylation

367

1

O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence

232 – 271

40

Missing in isoform 2.

VSP_017600

Alternative sequence

513 – 514

2

Missing in isoform 3.

VSP_017601

Experimental info

Sequence conflict

25

1

H → R in CAA61667. Ref.2

Sequence conflict

429

1

A → R in CAA61667. Ref.2

Secondary structure

1

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562

Helix Strand Turn

Details...

Helix

4 – 21

18

Helix

24 – 27

4

Turn

30 – 32

3

Beta strand

39 – 41

3

Turn

42 – 45

4

Beta strand

46 – 48

3

Helix

50 – 56

7

Beta strand

59 – 61

3

Beta strand

65 – 67

3

Turn

68 – 70

3

Helix

75 – 83

9

Helix

85 – 93

9

Turn

94 – 96

3

Turn

99 – 101

3

Helix

110 – 121

12

Helix

130 – 134

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2002. Version 2. Checksum: 9A2242217F53B4D9	FASTA	562	58,260
	10 20 30 40 50 60 MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT SCSGSLRGLN 70 80 90 100 110 120 PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR SSAIPDFRDP QKVKEFLQEK 130 140 150 160 170 180 YEKKRWYVPP EQAKVVASVH ASISGSSASS TSSTPEVKPL KSLLGDSAPT LHLNKGTPSQ 190 200 210 220 230 240 SPVVGRSQGQ QQEKKQFDLL SDLGSDIFAA PAPQSTATAN FANFAHFNSH AAQNSANADF 250 260 270 280 290 300 ANFDAFGQSS GSSNFGGFPT ASHSPFQPQT TGGSAASVNA NFAHFDNFPK SSSADFGTFN 310 320 330 340 350 360 TSQSHQTASA VSKVSTNKAG LQTADKYAAL ANLDNIFSAG QGGDQGSGFG TTGKAPVGSV 370 380 390 400 410 420 VSVPSQSSAS SDKYAALAEL DSVFSSAATS SNAYTSTSNA SSNVFGTVPV VASAQTQPAS 430 440 450 460 470 480 SSVPAPFGAT PSTNPFVAAA GPSVASSTNP FQTNARGATA ATFGTASMSM PTGFGTPAPY 490 500 510 520 530 540 SLPTSFSGSF QQPAFPAQAA FPQQTAFSQQ PNGAGFAAFG QTKPVVTPFG QVAAAGVSSN 550 560 PFMTGAPTGQ FPTGSSSTNP FL
	Isoform 2 [UniParc]. Checksum: DE779347F13D2557	FASTA	522	54,182
	10 20 30 40 50 60 MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT SCSGSLRGLN 70 80 90 100 110 120 PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR SSAIPDFRDP QKVKEFLQEK 130 140 150 160 170 180 YEKKRWYVPP EQAKVVASVH ASISGSSASS TSSTPEVKPL KSLLGDSAPT LHLNKGTPSQ 190 200 210 220 230 240 SPVVGRSQGQ QQEKKQFDLL SDLGSDIFAA PAPQSTATAN FANFAHFNSH AGGSAASVNA 250 260 270 280 290 300 NFAHFDNFPK SSSADFGTFN TSQSHQTASA VSKVSTNKAG LQTADKYAAL ANLDNIFSAG 310 320 330 340 350 360 QGGDQGSGFG TTGKAPVGSV VSVPSQSSAS SDKYAALAEL DSVFSSAATS SNAYTSTSNA 370 380 390 400 410 420 SSNVFGTVPV VASAQTQPAS SSVPAPFGAT PSTNPFVAAA GPSVASSTNP FQTNARGATA 430 440 450 460 470 480 ATFGTASMSM PTGFGTPAPY SLPTSFSGSF QQPAFPAQAA FPQQTAFSQQ PNGAGFAAFG 490 500 510 520 QTKPVVTPFG QVAAAGVSSN PFMTGAPTGQ FPTGSSSTNP FL
	Isoform 3 [UniParc]. Checksum: AE7E67C63C6830ED	FASTA	560	58,132
	10 20 30 40 50 60 MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT SCSGSLRGLN 70 80 90 100 110 120 PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR SSAIPDFRDP QKVKEFLQEK 130 140 150 160 170 180 YEKKRWYVPP EQAKVVASVH ASISGSSASS TSSTPEVKPL KSLLGDSAPT LHLNKGTPSQ 190 200 210 220 230 240 SPVVGRSQGQ QQEKKQFDLL SDLGSDIFAA PAPQSTATAN FANFAHFNSH AAQNSANADF 250 260 270 280 290 300 ANFDAFGQSS GSSNFGGFPT ASHSPFQPQT TGGSAASVNA NFAHFDNFPK SSSADFGTFN 310 320 330 340 350 360 TSQSHQTASA VSKVSTNKAG LQTADKYAAL ANLDNIFSAG QGGDQGSGFG TTGKAPVGSV 370 380 390 400 410 420 VSVPSQSSAS SDKYAALAEL DSVFSSAATS SNAYTSTSNA SSNVFGTVPV VASAQTQPAS 430 440 450 460 470 480 SSVPAPFGAT PSTNPFVAAA GPSVASSTNP FQTNARGATA ATFGTASMSM PTGFGTPAPY 490 500 510 520 530 540 SLPTSFSGSF QQPAFPAQAA FPQQTAFSQQ PNGFAAFGQT KPVVTPFGQV AAAGVSSNPF 550 560 MTGAPTGQFP TGSSSTNPFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7634337] [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: 7637788] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HIV-1 REV. Tissue: Placenta.
[3]	"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: 15815621] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Testis.
[5]	"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: 10613896] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EPS15, FUNCTION.
[6]	"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: 14701878] [Abstract] Cited for: FUNCTION.
[7]	"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: 15749819] [Abstract] Cited for: FUNCTION.
[8]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, MASS SPECTROMETRY. Tissue: Platelet.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42025 Genomic DNA. Translation: AAC37580.1.
X89478 mRNA. Translation: CAA61667.1.
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.

IPI

IPI00304693.
IPI00607616.
IPI00736669.

PIR

A57088.

RefSeq

NP_001128660.1. NM_001135188.1.
NP_001128661.1. NM_001135189.1.
NP_004495.2. NM_004504.4.

UniGene

Hs.352962.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D9L	NMR	-	A	14-134	[»]
2OLM	X-ray	1.48	A	4-141	[»]
2VX8	X-ray	2.20	A/B/C/D	136-176	[»]

ProteinModelPortal

P52594.

SMR

P52594. Positions 14-134, 153-186.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52594. 3 interactions.

STRING

P52594.

PTM databases

PhosphoSite

P52594.

Polymorphism databases

DMDM

26007019.

Proteomic databases

PRIDE

P52594.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310078; ENSP00000312059; ENSG00000173744.

GeneID

3267.

KEGG

hsa:3267.

UCSC

uc002vpc.1. human.
uc002vpd.1. human.
uc002vpf.1. human.

Organism-specific databases

CTD

3267.

GeneCards

GC02P228336.

H-InvDB

HIX0002896.

HGNC

HGNC:5175. AGFG1.

HPA

HPA008741.

MIM

600862. gene.

neXtProt

NX_P52594.

PharmGKB

PA29449.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10553.

GeneTree

ENSGT00560000077249.

HOVERGEN

HBG006551.

PhylomeDB

P52594.

Gene expression databases

ArrayExpress

P52594.

Bgee

P52594.

CleanEx

HS_AGFG1.

Genevestigator

P52594.

GermOnline

ENSG00000173744. Homo sapiens.

Family and domain databases

InterPro

IPR001164. ArfGAP.
[Graphical view]

KO

K15044.

Pfam

PF01412. ArfGap. 1 hit.
[Graphical view]

PRINTS

PR00405. REVINTRACTNG.

SMART

SM00105. ArfGap. 1 hit.
[Graphical view]

SUPFAM

SSF57863. ArfGAP. 1 hit.

PROSITE

PS50115. ARFGAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

12971.

SOURCE

Search...

Entry information

Entry name

AGFG1_HUMAN

Accession

Primary (citable) accession number: P52594
Secondary accession number(s): Q15277 , Q4VAS0, Q4VAS1, Q4VAS3, Q53QT8, Q53R11

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 28, 2002
Last modified:	January 25, 2012
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.