P46060 (RAGP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ran GTPase-activating protein 1
Short name=RanGAP1

Gene names

Name:	RANGAP1
Synonyms:	KIAA1835, SD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	587 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state.
Subunit structure	Homodimer. Forms a tight complex in association with RANBP2/NUP358 and UBE2I/UBC9, the ubiquitin-conjugating enzyme E2. Interacts with UBE2I; the interaction conjugates SUMO1 to RANGAP1, and subsequently stabilizes interactions of sumoylated RANGAP1 with RANBP2/NUP358. The SUMO1/RANGAP1/UBC9/NUP358 complex associates with nuclear pore complexes. Interacts with TRAF6. Ref.9 Ref.11
Subcellular location	Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Chromosome › centromere › kinetochore By similarity. Cytoplasm › cytoskeleton › spindle pole By similarity. Note: Cytoplasmic during interphase. Targeted to the nuclear rim after sumoylation. During mitosis, associates with mitotic spindles. Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase. Mitotic location also requires sumoylation. Ref.8 Ref.9
Tissue specificity	Highly expressed in brain, thymus and testis. Ref.7
Post-translational modification	Phosphorylated occurs before nuclear envelope breakdown and continues throughout mitosis. Phosphorylated by the M-phase kinase cyclin B/Cdk1, in vitro. Differential timimg of dephosphorylation occurs during phases of mitosis. The phosphorylated form remains associated with RANBP2/NUP358 and the SUMO E2-conjugating enzyme, UBC9, on nuclear pore complex (NPC) diassembly and during mitosis. Ref.9 Sumoylated with SUMO1. Sumoylation is necessary for targeting to the nuclear envelope (NE), and for association with mitotic spindles and kinetochores during mitosis. Also required for interaction with RANBP2 and is mediated by UBC9. Ref.8 Ref.15
Sequence similarities	Belongs to the RNA1 family. Contains 6 LRR (leucine-rich) repeats.
Sequence caution	The sequence BAB47464.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	Leucine-rich repeat Repeat
Molecular function	GTPase activation
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mitotic prometaphase Traceable author statement. Source: Reactome negative regulation of protein export from nucleus Inferred from direct assay PubMed 16449645. Source: BHF-UCL signal transduction Traceable author statement Ref.1. Source: ProtInc
Cellular_component	condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Traceable author statement PubMed 8978815. Source: ProtInc perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	Ran GTPase activator activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SUMO1	P63165	3	EBI-396091,EBI-80140

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 587

586

Ran GTPase-activating protein 1

PRO_0000056737

Regions

Repeat

48 – 71

24

LRR 1

Repeat

111 – 134

24

LRR 2

Repeat

207 – 230

24

LRR 3

Repeat

235 – 258

24

LRR 4

Repeat

292 – 319

28

LRR 5

Repeat

320 – 343

24

LRR 6

Motif

523 – 526

4

SUMO conjugation

Compositional bias

359 – 399

41

Asp/Glu-rich (highly acidic)

Compositional bias

359 – 397

39

Asp/Glu-rich (highly acidic)

Sites

Site

562

1

Hydrophobic interaction with UBC9 By similarity

Site

565

1

Hydrophobic interaction with UBC9 By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.15

Modified residue

358

1

Phosphoserine Ref.12

Modified residue

409

1

Phosphothreonine; by CDK2 Ref.9

Modified residue

428

1

Phosphoserine Ref.9 Ref.12 Ref.13 Ref.16

Modified residue

435

1

Phosphoserine Ref.13

Modified residue

436

1

Phosphothreonine Ref.13

Modified residue

442

1

Phosphoserine Ref.9 Ref.10 Ref.12 Ref.13 Ref.16 Ref.18

Modified residue

524

1

N6-acetyllysine; alternate Ref.14

Cross-link

8

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.15

Cross-link

524

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternate Ref.15

Natural variations

Natural variant

133

1

E → Q.
Corresponds to variant rs2229752 [ dbSNP | Ensembl ].

VAR_029240

Experimental info

Mutagenesis

524

1

K → R: No association with mitotic spindles during mitosis. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

.

.

.

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.

.

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587

Helix Strand Turn

Details...

Helix

434 – 439

6

Helix

443 – 448

6

Helix

450 – 452

3

Helix

453 – 459

7

Helix

466 – 477

12

Helix

484 – 502

19

Beta strand

503 – 507

5

Helix

509 – 519

11

Beta strand

522 – 526

5

Helix

536 – 545

10

Beta strand

548 – 551

4

Helix

553 – 555

3

Helix

556 – 564

9

Helix

568 – 571

4

Helix

574 – 586

13

Sequences

	Sequence		Length	Mass (Da)
	P46060 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 3C18068AAC06B98F	FASTA	587	63,542
	10 20 30 40 50 60 MASEDIAKLA ETLAKTQVAG GQLSFKGKSL KLNTAEDAKD VIKEIEDFDS LEALRLEGNT 70 80 90 100 110 120 VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRTEIPPAL ISLGEGLITA GAQLVELDLS 130 140 150 160 170 180 DNAFGPDGVQ GFEALLKSSA CFTLQELKLN NCGMGIGGGK ILAAALTECH RKSSAQGKPL 190 200 210 220 230 240 ALKVFVAGRN RLENDGATAL AEAFRVIGTL EEVHMPQNGI NHPGITALAQ AFAVNPLLRV 250 260 270 280 290 300 INLNDNTFTE KGAVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAIRG GLPKLKELNL 310 320 330 340 350 360 SFCEIKRDAA LAVAEAMADK AELEKLDLNG NTLGEEGCEQ LQEVLEGFNM AKVLASLSDD 370 380 390 400 410 420 EDEEEEEEGE EEEEEAEEEE EEDEEEEEEE EEEEEEEPQQ RGQGEKSATP SRKILDPNTG 430 440 450 460 470 480 EPAPVLSSPP PADVSTFLAF PSPEKLLRLG PKSSVLIAQQ TDTSDPEKVV SAFLKVSSVF 490 500 510 520 530 540 KDEATVRMAV QDAVDALMQK AFNSSSFNSN TFLTRLLVHM GLLKSEDKVK AIANLYGPLM 550 560 570 580 ALNHMVQQDY FPKALAPLLL AFVTKPNSAL ESCSFARHSL LQTLYKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport." Bischoff F.R., Krebber H., Kempf T., Hermes I., Ponstingl H. Proc. Natl. Acad. Sci. U.S.A. 92:1749-1753(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Brain and Kidney.
[7]	"Ubiquitous expression and testis-specific alternative polyadenylation of mRNA for the human Ran GTPase activator RanGAP1." Krebber H., Ponstingl H. Gene 180:7-11(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles." Joseph J., Tan S.-H., Karpova T.S., McNally J.G., Dasso M. J. Cell Biol. 156:595-602(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-524.
[9]	"RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly." Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F. J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; RANBP2 AND UBE2I.
[10]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification." Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L., Darnay B.G., Ford R.J. J. Biol. Chem. 283:5081-5089(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRAF6.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-428 AND SER-442, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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 SER-428; SER-435; THR-436 AND SER-442, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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-524, MASS SPECTROMETRY.
[15]	"In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification." Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L. J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-8 AND LYS-524, ACETYLATION AT ALA-2. Tissue: Cervix carcinoma.
[16]	"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-428 AND SER-442, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"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-442, MASS SPECTROMETRY.
[19]	"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex." Reverter D., Lima C.D. Nature 435:687-692(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 418-587 IN COMPLEX WITH SUMO1; RANBP2 AND UBE2I.
[20]	"SUMO protease SENP1 induces isomerization of the scissile peptide bond." Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T. Nat. Struct. Mol. Biol. 13:1069-1077(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 432-587 IN COMPLEX WITH SUMO1 AND SENP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X82260 mRNA. Translation: CAA57714.1.
AB058738 mRNA. Translation: BAB47464.1. Different initiation.
CR456557 mRNA. Translation: CAG30443.1.
AL035681 Genomic DNA. Translation: CAB63073.1.
BC014044 mRNA. Translation: AAH14044.1.
BC041396 mRNA. Translation: AAH41396.1.

IPI

IPI00294879.

PIR

JC5300.

RefSeq

NP_002874.1. NM_002883.2.

UniGene

Hs.183800.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z5S	X-ray	3.01	C	418-587	[»]
2GRN	X-ray	1.80	B	419-587	[»]
2GRO	X-ray	1.70	B	419-587	[»]
2GRP	X-ray	2.05	B	419-587	[»]
2GRQ	X-ray	1.70	B	419-587	[»]
2GRR	X-ray	1.30	B	419-587	[»]
2IO2	X-ray	2.90	C	418-587	[»]
2IO3	X-ray	3.20	C	418-587	[»]
2IY0	X-ray	2.77	C	432-587	[»]
3UIN	X-ray	2.60	C	419-587	[»]
3UIO	X-ray	2.60	C	419-587	[»]
3UIP	X-ray	2.29	C	419-587	[»]

ProteinModelPortal

P46060.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29079N.

IntAct

P46060. 14 interactions.

MINT

MINT-3016328.

STRING

9606.ENSP00000348577.

PTM databases

PhosphoSite

P46060.

Polymorphism databases

DMDM

1172922.

Proteomic databases

PaxDb

P46060.

PRIDE

P46060.

Protocols and materials databases

DNASU

5905.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356244; ENSP00000348577; ENSG00000100401.
ENST00000405486; ENSP00000385866; ENSG00000100401.
ENST00000455915; ENSP00000401470; ENSG00000100401.

GeneID

5905.

KEGG

hsa:5905.

UCSC

uc003azs.3. human.

Organism-specific databases

CTD

5905.

GeneCards

GC22M041641.

HGNC

HGNC:9854. RANGAP1.

HPA

CAB004293.

MIM

602362. gene.

neXtProt

NX_P46060.

PharmGKB

PA34216.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5238.

HOGENOM

HOG000195026.

HOVERGEN

HBG017720.

InParanoid

P46060.

KO

K14319.

OMA

SFNSNAF.

OrthoDB

EOG4K0QN7.

Enzyme and pathway databases

Pathway_Interaction_DB

hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
ranbp2pathway. Sumoylation by RanBP2 regulates transcriptional repression.

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpress

P46060.

Bgee

P46060.

CleanEx

HS_RANGAP1.

Genevestigator

P46060.

GermOnline

ENSG00000100401. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.200. 1 hit.

InterPro

IPR009109. Ran_GTPase_activating_1_C.
IPR027038. RanGap.
[Graphical view]

PANTHER

PTHR24113. PTHR24113. 1 hit.

Pfam

PF07834. RanGAP1_C. 1 hit.
[Graphical view]

SUPFAM

SSF69099. RanGAP1_C. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

RANGAP1. human.

EvolutionaryTrace

P46060.

GenomeRNAi

5905.

NextBio

22968.

SOURCE

Search...

Entry information

Entry name

RAGP1_HUMAN

Accession

Primary (citable) accession number: P46060
Secondary accession number(s): Q96JJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 149 of the entry and version 1 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.