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Protein

Rho GTPase-activating protein 5

Gene

ARHGAP5

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

Functioni

GTPase-activating protein for Rho family members. May play a role in the reduction of the p21rasGTPase-activating potential of RASA1/p120GAP.

GO - Molecular functioni

  • GTPase activator activity Source: Reactome
  • GTPase activity Source: ProtInc
  • GTP binding Source: InterPro
  • SH2 domain binding Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: ProtInc
  • mammary gland development Source: Ensembl
  • positive regulation of GTPase activity Source: GOC
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • Rho protein signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.
SignaLinkiQ13017.
SIGNORiQ13017.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 5
Alternative name(s):
Rho-type GTPase-activating protein 5
p190-B
Gene namesi
Name:ARHGAP5
Synonyms:RHOGAP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:675. ARHGAP5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24959.

Polymorphism and mutation databases

BioMutaiARHGAP5.
DMDMi190358871.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15021502Rho GTPase-activating protein 5PRO_0000056702Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei550 – 5501Nitrated tyrosineCombined sources
Modified residuei765 – 7651PhosphoserineCombined sources
Modified residuei951 – 9511PhosphoserineCombined sources
Modified residuei968 – 9681PhosphoserineCombined sources
Modified residuei1115 – 11151PhosphoserineCombined sources
Modified residuei1173 – 11731PhosphoserineCombined sources
Modified residuei1176 – 11761PhosphoserineCombined sources
Modified residuei1195 – 11951PhosphoserineCombined sources
Modified residuei1202 – 12021PhosphoserineCombined sources
Modified residuei1218 – 12181PhosphoserineCombined sources

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

EPDiQ13017.
MaxQBiQ13017.
PaxDbiQ13017.
PRIDEiQ13017.

PTM databases

iPTMnetiQ13017.
PhosphoSiteiQ13017.

Miscellaneous databases

PMAP-CutDBQ13017.

Expressioni

Tissue specificityi

Expressed in kidney, brain, liver and lung.

Gene expression databases

BgeeiQ13017.
CleanExiHS_ARHGAP5.
ExpressionAtlasiQ13017. baseline and differential.
GenevisibleiQ13017. HS.

Organism-specific databases

HPAiHPA046993.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Rnd3P615882EBI-7237884,EBI-6930266From a different organism.

GO - Molecular functioni

  • SH2 domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106887. 13 interactions.
IntActiQ13017. 2 interactions.
MINTiMINT-1191615.
STRINGi9606.ENSP00000371897.

Structurei

Secondary structure

1
1502
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1258 – 12625Combined sources
Helixi1264 – 12674Combined sources
Helixi1276 – 128712Combined sources
Turni1293 – 12975Combined sources
Helixi1302 – 131413Combined sources
Helixi1320 – 13234Combined sources
Helixi1327 – 134014Combined sources
Beta strandi1341 – 13433Combined sources
Turni1348 – 13503Combined sources
Helixi1351 – 13588Combined sources
Helixi1363 – 137311Combined sources
Turni1374 – 13763Combined sources
Helixi1381 – 139717Combined sources
Helixi1399 – 14024Combined sources
Helixi1406 – 141712Combined sources
Beta strandi1425 – 14273Combined sources
Helixi1434 – 144310Combined sources
Helixi1445 – 14484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EE4NMR-A1255-1456[»]
2EE5NMR-A1245-1456[»]
ProteinModelPortaliQ13017.
SMRiQ13017. Positions 12-248, 1245-1456.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13017.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 32559FF 1Add
BLAST
Domaini366 – 42055FF 2Add
BLAST
Domaini427 – 48155FF 3Add
BLAST
Domaini482 – 54867FF 4Add
BLAST
Domaini1262 – 1449188Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1225 – 124521Lys-richAdd
BLAST

Sequence similaritiesi

Contains 4 FF domains.Curated
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4271. Eukaryota.
ENOG410XR4E. LUCA.
GeneTreeiENSGT00840000129684.
HOVERGENiHBG051844.
InParanoidiQ13017.
KOiK13709.
OMAiDQDHNIS.
OrthoDBiEOG779NWX.
PhylomeDBiQ13017.
TreeFamiTF324451.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR032835. RhoGAP-FF1.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
PF16512. RhoGAP-FF1. 1 hit.
[Graphical view]
SMARTiSM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEiPS51676. FF. 4 hits.
PS50238. RHOGAP. 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: Q13017-1) [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
MMAKNKEPRP PSYTISIVGL SGTEKDKGNC GVGKSCLCNR FVRSKADEYY
60 70 80 90 100
PEHTSVLSTI DFGGRVVNND HFLYWGDIIQ NSEDGVECKI HVIEQTEFID
110 120 130 140 150
DQTFLPHRST NLQPYIKRAA ASKLQSAEKL MYICTDQLGL EQDFEQKQMP
160 170 180 190 200
EGKLNVDGFL LCIDVSQGCN RKFDDQLKFV NNLFVQLSKS KKPVIIAATK
210 220 230 240 250
CDECVDHYLR EVQAFASNKK NLLVVETSAR FNVNIETCFT ALVQMLDKTR
260 270 280 290 300
SKPKIIPYLD AYKTQRQLVV TATDKFEKLV QTVRDYHATW KTVSNKLKNH
310 320 330 340 350
PDYEEYINLE GTRKARNTFS KHIEQLKQEH IRKRREEYIN TLPRAFNTLL
360 370 380 390 400
PNLEEIEHLN WSEALKLMEK RADFQLCFVV LEKTPWDETD HIDKINDRRI
410 420 430 440 450
PFDLLSTLEA EKVYQNHVQH LISEKRRVEM KEKFKKTLEK IQFISPGQPW
460 470 480 490 500
EEVMCFVMED EAYKYITEAD SKEVYGRHQR EIVEKAKEEF QEMLFEHSEL
510 520 530 540 550
FYDLDLNATP SSDKMSEIHT VLSEEPRYKA LQKLAPDRES LLLKHIGFVY
560 570 580 590 600
HPTKETCLSG QNCTDIKVEQ LLASSLLQLD HGRLRLYHDS TNIDKVNLFI
610 620 630 640 650
LGKDGLAQEL ANEIRTQSTD DEYALDGKIY ELDLRPVDAK SPYFLSQLWT
660 670 680 690 700
AAFKPHGCFC VFNSIESLSF IGEFIGKIRT EASQIRKDKY MANLPFTLIL
710 720 730 740 750
ANQRDSISKN LPILRHQGQQ LANKLQCPFV DVPAGTYPRK FNETQIKQAL
760 770 780 790 800
RGVLESVKHN LDVVSPIPAN KDLSEADLRI VMCAMCGDPF SVDLILSPFL
810 820 830 840 850
DSHSCSAAQA GQNNSLMLDK IIGEKRRRIQ ITILSYHSSI GVRKDELVHG
860 870 880 890 900
YILVYSAKRK ASMGMLRAFL SEVQDTIPVQ LVAVTDSQAD FFENEAIKEL
910 920 930 940 950
MTEGEHIATE ITAKFTALYS LSQYHRQTEV FTLFFSDVLE KKNMIENSYL
960 970 980 990 1000
SDNTRESTHQ SEDVFLPSPR DCFPYNNYPD SDDDTEAPPP YSPIGDDVQL
1010 1020 1030 1040 1050
LPTPSDRSRY RLDLEGNEYP IHSTPNCHDH ERNHKVPPPI KPKPVVPKTN
1060 1070 1080 1090 1100
VKKLDPNLLK TIEAGIGKNP RKQTSRVPLA HPEDMDPSDN YAEPIDTIFK
1110 1120 1130 1140 1150
QKGYSDEIYV VPDDSQNRIK IRNSFVNNTQ GDEENGFSDR TSKSHGERRP
1160 1170 1180 1190 1200
SKYKYKSKTL FSKAKSYYRR THSDASDDEA FTTSKTKRKG RHRGSEEDPL
1210 1220 1230 1240 1250
LSPVETWKGG IDNPAITSDQ ELDDKKMKKK THKVKEDKKQ KKKTKNFNPP
1260 1270 1280 1290 1300
TRRNWESNYF GMPLQDLVTA EKPIPLFVEK CVEFIEDTGL CTEGLYRVSG
1310 1320 1330 1340 1350
NKTDQDNIQK QFDQDHNINL VSMEVTVNAV AGALKAFFAD LPDPLIPYSL
1360 1370 1380 1390 1400
HPELLEAAKI PDKTERLHAL KEIVKKFHPV NYDVFRYVIT HLNRVSQQHK
1410 1420 1430 1440 1450
INLMTADNLS ICFWPTLMRP DFENREFLST TKIHQSVVET FIQQCQFFFY
1460 1470 1480 1490 1500
NGEIVETTNI VAPPPPSNPG QLVEPMVPLQ LPPPLQPQLI QPQLQTDPLG

II
Length:1,502
Mass (Da):172,460
Last modified:June 10, 2008 - v2
Checksum:i2E01B5B1D007984D
GO
Isoform 2 (identifier: Q13017-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1240-1240: Missing.

Note: No experimental confirmation available.
Show »
Length:1,501
Mass (Da):172,332
Checksum:i801C2D39400ACA51
GO
Isoform 3 (identifier: Q13017-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1265: Missing.
     1266-1288: DLVTAEKPIPLFVEKCVEFIEDT → MSLPPPPPGPLPLRRRRRRPTLL

Note: No experimental confirmation available.
Show »
Length:237
Mass (Da):26,979
Checksum:iC5044B056AC7297A
GO
Isoform 4 (identifier: Q13017-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1261: Missing.

Note: No experimental confirmation available.
Show »
Length:241
Mass (Da):27,411
Checksum:i63966DC0890DDB5E
GO

Sequence cautioni

The sequence AAA95963.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAH32723.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801Q → R in AAH50059 (PubMed:15489334).Curated
Sequence conflicti409 – 4091E → G in BAF85655 (PubMed:14702039).Curated
Sequence conflicti541 – 5411L → F in BAD92988 (Ref. 5) Curated
Sequence conflicti620 – 6201D → G in BAF85655 (PubMed:14702039).Curated
Sequence conflicti1383 – 13831D → G in AAH50059 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171I → V.
Corresponds to variant rs17386818 [ dbSNP | Ensembl ].
VAR_043980

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 12651265Missing in isoform 3. 1 PublicationVSP_034164Add
BLAST
Alternative sequencei1 – 12611261Missing in isoform 4. 1 PublicationVSP_034165Add
BLAST
Alternative sequencei1240 – 12401Missing in isoform 2. 1 PublicationVSP_034166
Alternative sequencei1266 – 128823DLVTA…FIEDT → MSLPPPPPGPLPLRRRRRRP TLL in isoform 3. 1 PublicationVSP_034167Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17032 mRNA. Translation: AAA95963.1. Frameshift.
CH471078 Genomic DNA. Translation: EAW65935.1.
CH471078 Genomic DNA. Translation: EAW65936.1.
CH471078 Genomic DNA. Translation: EAW65937.1.
CH471078 Genomic DNA. Translation: EAW65938.1.
BC032723 mRNA. Translation: AAH32723.1. Sequence problems.
BC050059 mRNA. Translation: AAH50059.1.
BC075799 mRNA. Translation: AAH75799.1.
BC129928 mRNA. Translation: AAI29929.1.
BC129929 mRNA. Translation: AAI29930.1.
AK292966 mRNA. Translation: BAF85655.1.
AB209751 mRNA. Translation: BAD92988.1.
CCDSiCCDS32062.1. [Q13017-1]
CCDS45095.1. [Q13017-2]
PIRiB59431.
RefSeqiNP_001025226.1. NM_001030055.1. [Q13017-1]
NP_001164.2. NM_001173.2. [Q13017-2]
XP_005267692.1. XM_005267635.2. [Q13017-1]
XP_005267693.1. XM_005267636.2. [Q13017-1]
UniGeneiHs.592313.

Genome annotation databases

EnsembliENST00000345122; ENSP00000371897; ENSG00000100852. [Q13017-1]
ENST00000396582; ENSP00000379827; ENSG00000100852. [Q13017-3]
ENST00000433497; ENSP00000407395; ENSG00000100852. [Q13017-4]
ENST00000539826; ENSP00000441692; ENSG00000100852. [Q13017-1]
ENST00000556611; ENSP00000452222; ENSG00000100852. [Q13017-2]
GeneIDi394.
KEGGihsa:394.
UCSCiuc001wrl.4. human. [Q13017-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17032 mRNA. Translation: AAA95963.1. Frameshift.
CH471078 Genomic DNA. Translation: EAW65935.1.
CH471078 Genomic DNA. Translation: EAW65936.1.
CH471078 Genomic DNA. Translation: EAW65937.1.
CH471078 Genomic DNA. Translation: EAW65938.1.
BC032723 mRNA. Translation: AAH32723.1. Sequence problems.
BC050059 mRNA. Translation: AAH50059.1.
BC075799 mRNA. Translation: AAH75799.1.
BC129928 mRNA. Translation: AAI29929.1.
BC129929 mRNA. Translation: AAI29930.1.
AK292966 mRNA. Translation: BAF85655.1.
AB209751 mRNA. Translation: BAD92988.1.
CCDSiCCDS32062.1. [Q13017-1]
CCDS45095.1. [Q13017-2]
PIRiB59431.
RefSeqiNP_001025226.1. NM_001030055.1. [Q13017-1]
NP_001164.2. NM_001173.2. [Q13017-2]
XP_005267692.1. XM_005267635.2. [Q13017-1]
XP_005267693.1. XM_005267636.2. [Q13017-1]
UniGeneiHs.592313.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EE4NMR-A1255-1456[»]
2EE5NMR-A1245-1456[»]
ProteinModelPortaliQ13017.
SMRiQ13017. Positions 12-248, 1245-1456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106887. 13 interactions.
IntActiQ13017. 2 interactions.
MINTiMINT-1191615.
STRINGi9606.ENSP00000371897.

PTM databases

iPTMnetiQ13017.
PhosphoSiteiQ13017.

Polymorphism and mutation databases

BioMutaiARHGAP5.
DMDMi190358871.

Proteomic databases

EPDiQ13017.
MaxQBiQ13017.
PaxDbiQ13017.
PRIDEiQ13017.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000345122; ENSP00000371897; ENSG00000100852. [Q13017-1]
ENST00000396582; ENSP00000379827; ENSG00000100852. [Q13017-3]
ENST00000433497; ENSP00000407395; ENSG00000100852. [Q13017-4]
ENST00000539826; ENSP00000441692; ENSG00000100852. [Q13017-1]
ENST00000556611; ENSP00000452222; ENSG00000100852. [Q13017-2]
GeneIDi394.
KEGGihsa:394.
UCSCiuc001wrl.4. human. [Q13017-1]

Organism-specific databases

CTDi394.
GeneCardsiARHGAP5.
HGNCiHGNC:675. ARHGAP5.
HPAiHPA046993.
MIMi602680. gene.
neXtProtiNX_Q13017.
PharmGKBiPA24959.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4271. Eukaryota.
ENOG410XR4E. LUCA.
GeneTreeiENSGT00840000129684.
HOVERGENiHBG051844.
InParanoidiQ13017.
KOiK13709.
OMAiDQDHNIS.
OrthoDBiEOG779NWX.
PhylomeDBiQ13017.
TreeFamiTF324451.

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.
SignaLinkiQ13017.
SIGNORiQ13017.

Miscellaneous databases

ChiTaRSiARHGAP5. human.
EvolutionaryTraceiQ13017.
GeneWikiiARHGAP5.
GenomeRNAii394.
PMAP-CutDBQ13017.
PROiQ13017.
SOURCEiSearch...

Gene expression databases

BgeeiQ13017.
CleanExiHS_ARHGAP5.
ExpressionAtlasiQ13017. baseline and differential.
GenevisibleiQ13017. HS.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR032835. RhoGAP-FF1.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
PF16512. RhoGAP-FF1. 1 hit.
[Graphical view]
SMARTiSM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEiPS51676. FF. 4 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "p190-B, a new member of the Rho GAP family, and Rho are induced to cluster after integrin cross-linking."
    Burbelo P.D., Miyamoto S., Utani A., Brill S., Yamada K.M., Hall A., Yamada Y.
    J. Biol. Chem. 270:30919-30926(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mesangial cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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; 3 AND 4).
    Tissue: Brain, Testis and Uterus.
  4. "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] OF 1-1239 (ISOFORM 1).
    Tissue: Trachea.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 364-1499 (ISOFORM 2).
    Tissue: Brain.
  6. "Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry."
    Zhan X., Desiderio D.M.
    Anal. Biochem. 354:279-289(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-550, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary adenoma.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765 AND SER-1202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968; SER-1115; SER-1176; SER-1195; SER-1202 AND SER-1218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "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-1195 AND SER-1202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-765; SER-951 AND SER-1202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-1173 AND SER-1176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-1173 AND SER-1195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Solution structure of the N-terminus extended RhoGAP domain from human Rho GTPase activating protein 5 variant."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1245-1456.

Entry informationi

Entry nameiRHG05_HUMAN
AccessioniPrimary (citable) accession number: Q13017
Secondary accession number(s): A1L375
, A1L376, A8KAA1, D3DS89, D3DS90, Q05BE8, Q05BU8, Q59ER0, Q6DHZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: June 10, 2008
Last modified: June 8, 2016
This is version 146 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 14
    Human chromosome 14: 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

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.