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Protein

Rho-GTPase-activating protein 8

Gene

rga8

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts in signal transduction. Negatively regulates the pak1/shk1 control pathway.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-GTPase-activating protein 8
Gene namesi
Name:rga8
ORF Names:SPAC13A11.01c, SPAC2F7.18c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC13A11.01c.
PomBaseiSPAC13A11.01c. rga8.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Localizes to the cell ends during interphase and to the septum-forming region during cytokinesis.

GO - Cellular componenti

  • cell cortex of cell tip Source: PomBase
  • cell division site Source: PomBase
  • cytoplasm Source: PomBase
  • medial cortex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 777777Rho-GTPase-activating protein 8PRO_0000097316Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei676 – 6761Phosphoserine1 Publication
Modified residuei680 – 6801Phosphoserine1 Publication
Modified residuei682 – 6821Phosphothreonine1 Publication
Modified residuei686 – 6861Phosphoserine1 Publication
Modified residuei694 – 6941Phosphothreonine1 Publication
Modified residuei698 – 6981Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by pak1/shk1.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ09697.

PTM databases

iPTMnetiQ09697.

Interactioni

Subunit structurei

Interacts with pak1/shk1.1 Publication

Protein-protein interaction databases

BioGridi279071. 59 interactions.
MINTiMINT-4694186.

Structurei

3D structure databases

ProteinModelPortaliQ09697.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 420418F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini213 – 29684DEPPROSITE-ProRule annotationAdd
BLAST
Domaini454 – 650197Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili117 – 17256Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 DEP domain.PROSITE-ProRule annotation
Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000180209.
InParanoidiQ09697.
OMAiPCILRPR.
OrthoDBiEOG7W6WV5.
PhylomeDBiQ09697.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.555.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR031160. F_BAR.
IPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00610. DEP. 1 hit.
PF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00049. DEP. 1 hit.
SM00055. FCH. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48350. SSF48350. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09697-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISSFSNGFW SKDYATGVKK LFDCLDNGVE ENEQVKNLLK LYKEANEEFG
60 70 80 90 100
EKLQEITKEC LKGKKPENTE DGATSNKAFE GLRSEIANQG KQHIRIAKDL
110 120 130 140 150
ETLIIAPFSK MSIDHSQKLQ TSQQVLTNQI KSYEKKYYTL KKTKSAYYNK
160 170 180 190 200
CRNLEDYEEE SKESNETTSE AITDLTTVSS PQQQSLLEND DDLIQLGFME
210 220 230 240 250
FRPEELKEVL AQVLQEIPLQ DYRVPILGTY PNTCSGNIIV SWLQENLPVP
260 270 280 290 300
TLVAAEAFGQ DLIAQGFLRH MGVGGSFVNS TNFHYQWKDK AFQFAGLNSV
310 320 330 340 350
DSLVENAKAL PLVGEYLSDY ISHRKLYSSE TQSQRLKREV LDANKIYSES
360 370 380 390 400
VVDLDKCRTL VEETIADHLQ FLQKCETDRV LYYKDFFMDL STIISNFLPS
410 420 430 440 450
MKLLADQIVV YQEIIQPESD IRYILESAAT GPFLPRVEIY EDYYNDIKDQ
460 470 480 490 500
IFGVDVEFLS HRDKKRVPII VSTILSYLDL LYPTLASDEV RQNIWLVNSP
510 520 530 540 550
LSSVHQLREA LNHSSSVTKE VLSQYTPSVV IGVLKLYFLE LPDSIVPSSA
560 570 580 590 600
FELIRSIYMN HSNDTPYRLR LLQNLLSQLR RVNLATLSAI ITHLNRLITL
610 620 630 640 650
TPNKETFTIN LANSLSLCIS RPATWNLGIQ HDKHPTKFME DLLTYGPSIF
660 670 680 690 700
EELRKLNSSK RVSDRVLYQS SATPRSTDVS PTRPDSISSV RSHTAVESPR
710 720 730 740 750
SSFEELQPSE IPAESEFTLE NVPTSLIRSS YALNTRKTRR NFSHSSASNE
760 770
SAAIFIDQDA KIVNEAVASR DSSLSGS
Length:777
Mass (Da):88,208
Last modified:November 1, 1995 - v1
Checksum:i707F64DCCADEDAE6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY375444 mRNA. Translation: AAR21285.1.
CU329670 Genomic DNA. Translation: CAA90505.1.
PIRiT38566. S58162.
RefSeqiNP_592988.2. NM_001018388.2.

Genome annotation databases

EnsemblFungiiSPAC13A11.01c.1; SPAC13A11.01c.1:pep; SPAC13A11.01c.
GeneIDi2542617.
KEGGispo:SPAC13A11.01c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY375444 mRNA. Translation: AAR21285.1.
CU329670 Genomic DNA. Translation: CAA90505.1.
PIRiT38566. S58162.
RefSeqiNP_592988.2. NM_001018388.2.

3D structure databases

ProteinModelPortaliQ09697.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279071. 59 interactions.
MINTiMINT-4694186.

PTM databases

iPTMnetiQ09697.

Proteomic databases

MaxQBiQ09697.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC13A11.01c.1; SPAC13A11.01c.1:pep; SPAC13A11.01c.
GeneIDi2542617.
KEGGispo:SPAC13A11.01c.

Organism-specific databases

EuPathDBiFungiDB:SPAC13A11.01c.
PomBaseiSPAC13A11.01c. rga8.

Phylogenomic databases

HOGENOMiHOG000180209.
InParanoidiQ09697.
OMAiPCILRPR.
OrthoDBiEOG7W6WV5.
PhylomeDBiQ09697.

Miscellaneous databases

NextBioi20803666.
PROiQ09697.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.555.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR031160. F_BAR.
IPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00610. DEP. 1 hit.
PF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00049. DEP. 1 hit.
SM00055. FCH. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48350. SSF48350. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The novel Rho GTPase-activating protein family protein, Rga8, provides a potential link between Cdc42/p21-activated kinase and Rho signaling pathways in the fission yeast, Schizosaccharomyces pombe."
    Yang P., Qyang Y., Bartholomeusz G., Zhou X., Marcus S.
    J. Biol. Chem. 278:48821-48830(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PAK1, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676; SER-680; THR-682; SER-686; THR-694 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRGA8_SCHPO
AccessioniPrimary (citable) accession number: Q09697
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 13, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.