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P46060

- RAGP1_HUMAN

UniProt

P46060 - RAGP1_HUMAN

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Protein

Ran GTPase-activating protein 1

Gene

RANGAP1

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

Functioni

GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei562 – 5621Hydrophobic interaction with UBC9By similarity
Sitei565 – 5651Hydrophobic interaction with UBC9By similarity

GO - Molecular functioni

  1. Ran GTPase activator activity Source: ProtInc

GO - Biological processi

  1. mitotic cell cycle Source: Reactome
  2. negative regulation of protein export from nucleus Source: BHF-UCL
  3. positive regulation of Ran GTPase activity Source: GOC
  4. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Ran GTPase-activating protein 1
Short name:
RanGAP1
Gene namesi
Name:RANGAP1
Synonyms:KIAA1835, SD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:9854. RANGAP1.

Subcellular locationi

Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle 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.

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytoskeleton Source: UniProtKB-KW
  3. cytosol Source: Reactome
  4. kinetochore Source: UniProtKB-KW
  5. nuclear pore Source: ProtInc
  6. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi524 – 5241K → R: No association with mitotic spindles during mitosis. 1 Publication

Organism-specific databases

PharmGKBiPA34216.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 587586Ran GTPase-activating protein 1PRO_0000056737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)
Modified residuei358 – 3581Phosphoserine1 Publication
Modified residuei409 – 4091Phosphothreonine; by CDK21 Publication
Modified residuei428 – 4281Phosphoserine4 Publications
Modified residuei435 – 4351Phosphoserine1 Publication
Modified residuei436 – 4361Phosphothreonine1 Publication
Modified residuei442 – 4421Phosphoserine6 Publications
Modified residuei524 – 5241N6-acetyllysine; alternate1 Publication
Cross-linki524 – 524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternate

Post-translational modificationi

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.6 Publications
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 UBC9.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP46060.
PaxDbiP46060.
PRIDEiP46060.

PTM databases

PhosphoSiteiP46060.

Expressioni

Tissue specificityi

Highly expressed in brain, thymus and testis.1 Publication

Gene expression databases

BgeeiP46060.
CleanExiHS_RANGAP1.
ExpressionAtlasiP46060. baseline and differential.
GenevestigatoriP46060.

Organism-specific databases

HPAiCAB004293.
HPA050110.

Interactioni

Subunit structurei

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 TRAF6.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SUMO1P631655EBI-396091,EBI-80140
UBE2IP632795EBI-396091,EBI-80168

Protein-protein interaction databases

BioGridi111840. 77 interactions.
DIPiDIP-29079N.
IntActiP46060. 17 interactions.
MINTiMINT-3016328.
STRINGi9606.ENSP00000348577.

Structurei

Secondary structure

1
587
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi434 – 4396Combined sources
Helixi443 – 4486Combined sources
Helixi453 – 4597Combined sources
Helixi466 – 47712Combined sources
Helixi484 – 50219Combined sources
Beta strandi503 – 5075Combined sources
Helixi509 – 51911Combined sources
Helixi536 – 54510Combined sources
Beta strandi548 – 5514Combined sources
Helixi553 – 5553Combined sources
Helixi556 – 5649Combined sources
Helixi568 – 5714Combined sources
Helixi574 – 58613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z5SX-ray3.01C418-587[»]
2GRNX-ray1.80B419-587[»]
2GROX-ray1.70B419-587[»]
2GRPX-ray2.05B419-587[»]
2GRQX-ray1.70B419-587[»]
2GRRX-ray1.30B419-587[»]
2IO2X-ray2.90C418-587[»]
2IO3X-ray3.20C418-587[»]
2IY0X-ray2.77C432-587[»]
3UINX-ray2.60C419-587[»]
3UIOX-ray2.60C419-587[»]
3UIPX-ray2.29C419-587[»]
ProteinModelPortaliP46060.
SMRiP46060. Positions 21-349, 431-587.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46060.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati48 – 7124LRR 1Add
BLAST
Repeati111 – 13424LRR 2Add
BLAST
Repeati207 – 23024LRR 3Add
BLAST
Repeati235 – 25824LRR 4Add
BLAST
Repeati292 – 31928LRR 5Add
BLAST
Repeati320 – 34324LRR 6Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi523 – 5264SUMO conjugation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi359 – 39941Asp/Glu-rich (highly acidic)Add
BLAST
Compositional biasi359 – 39739Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Belongs to the RNA1 family.Curated
Contains 6 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG5238.
GeneTreeiENSGT00440000039203.
HOGENOMiHOG000195026.
HOVERGENiHBG017720.
InParanoidiP46060.
KOiK14319.
OMAiSFNSNAF.
OrthoDBiEOG70W3DV.
PhylomeDBiP46060.
TreeFamiTF318283.

Family and domain databases

Gene3Di1.25.40.200. 1 hit.
InterProiIPR009109. Ran_GTPase_activating_1_C.
IPR027038. RanGap.
[Graphical view]
PANTHERiPTHR24113. PTHR24113. 1 hit.
PfamiPF07834. RanGAP1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69099. SSF69099. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46060-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASEDIAKLA ETLAKTQVAG GQLSFKGKSL KLNTAEDAKD VIKEIEDFDS
60 70 80 90 100
LEALRLEGNT VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRTEIPPAL
110 120 130 140 150
ISLGEGLITA GAQLVELDLS DNAFGPDGVQ GFEALLKSSA CFTLQELKLN
160 170 180 190 200
NCGMGIGGGK ILAAALTECH RKSSAQGKPL ALKVFVAGRN RLENDGATAL
210 220 230 240 250
AEAFRVIGTL EEVHMPQNGI NHPGITALAQ AFAVNPLLRV INLNDNTFTE
260 270 280 290 300
KGAVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAIRG GLPKLKELNL
310 320 330 340 350
SFCEIKRDAA LAVAEAMADK AELEKLDLNG NTLGEEGCEQ LQEVLEGFNM
360 370 380 390 400
AKVLASLSDD EDEEEEEEGE EEEEEAEEEE EEDEEEEEEE EEEEEEEPQQ
410 420 430 440 450
RGQGEKSATP SRKILDPNTG EPAPVLSSPP PADVSTFLAF PSPEKLLRLG
460 470 480 490 500
PKSSVLIAQQ TDTSDPEKVV SAFLKVSSVF KDEATVRMAV QDAVDALMQK
510 520 530 540 550
AFNSSSFNSN TFLTRLLVHM GLLKSEDKVK AIANLYGPLM ALNHMVQQDY
560 570 580
FPKALAPLLL AFVTKPNSAL ESCSFARHSL LQTLYKV
Length:587
Mass (Da):63,542
Last modified:November 1, 1995 - v1
Checksum:i3C18068AAC06B98F
GO

Sequence cautioni

The sequence BAB47464.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti133 – 1331E → Q.
Corresponds to variant rs2229752 [ dbSNP | Ensembl ].
VAR_029240

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14012.1.
PIRiJC5300.
RefSeqiNP_001265580.1. NM_001278651.1.
NP_002874.1. NM_002883.3.
XP_006724352.1. XM_006724289.1.
UniGeneiHs.183800.

Genome annotation databases

EnsembliENST00000356244; ENSP00000348577; ENSG00000100401.
ENST00000405486; ENSP00000385866; ENSG00000100401.
ENST00000455915; ENSP00000401470; ENSG00000100401.
GeneIDi5905.
KEGGihsa:5905.
UCSCiuc003azs.3. human.

Polymorphism databases

DMDMi1172922.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS14012.1.
PIRi JC5300.
RefSeqi NP_001265580.1. NM_001278651.1.
NP_002874.1. NM_002883.3.
XP_006724352.1. XM_006724289.1.
UniGenei Hs.183800.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P46060.
SMRi P46060. Positions 21-349, 431-587.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111840. 77 interactions.
DIPi DIP-29079N.
IntActi P46060. 17 interactions.
MINTi MINT-3016328.
STRINGi 9606.ENSP00000348577.

PTM databases

PhosphoSitei P46060.

Polymorphism databases

DMDMi 1172922.

Proteomic databases

MaxQBi P46060.
PaxDbi P46060.
PRIDEi P46060.

Protocols and materials databases

DNASUi 5905.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356244 ; ENSP00000348577 ; ENSG00000100401 .
ENST00000405486 ; ENSP00000385866 ; ENSG00000100401 .
ENST00000455915 ; ENSP00000401470 ; ENSG00000100401 .
GeneIDi 5905.
KEGGi hsa:5905.
UCSCi uc003azs.3. human.

Organism-specific databases

CTDi 5905.
GeneCardsi GC22M041641.
HGNCi HGNC:9854. RANGAP1.
HPAi CAB004293.
HPA050110.
MIMi 602362. gene.
neXtProti NX_P46060.
PharmGKBi PA34216.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5238.
GeneTreei ENSGT00440000039203.
HOGENOMi HOG000195026.
HOVERGENi HBG017720.
InParanoidi P46060.
KOi K14319.
OMAi SFNSNAF.
OrthoDBi EOG70W3DV.
PhylomeDBi P46060.
TreeFami TF318283.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSi RANGAP1. human.
EvolutionaryTracei P46060.
GeneWikii RANGAP1.
GenomeRNAii 5905.
NextBioi 22968.
PROi P46060.
SOURCEi Search...

Gene expression databases

Bgeei P46060.
CleanExi HS_RANGAP1.
ExpressionAtlasi P46060. baseline and differential.
Genevestigatori P46060.

Family and domain databases

Gene3Di 1.25.40.200. 1 hit.
InterProi IPR009109. Ran_GTPase_activating_1_C.
IPR027038. RanGap.
[Graphical view ]
PANTHERi PTHR24113. PTHR24113. 1 hit.
Pfami PF07834. RanGAP1_C. 1 hit.
[Graphical view ]
SUPFAMi SSF69099. SSF69099. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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].
  14. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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.
  17. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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.
  21. "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.

Entry informationi

Entry nameiRAGP1_HUMAN
AccessioniPrimary (citable) accession number: P46060
Secondary accession number(s): Q96JJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 165 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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

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