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Q9NRY4

- RHG35_HUMAN

UniProt

Q9NRY4 - RHG35_HUMAN

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Protein

Rho GTPase-activating protein 35

Gene

ARHGAP35

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

Functioni

Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May participate in the regulation of retinal development and degeneration. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor.1 Publication

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. GTP binding Source: InterPro
  3. Rho GTPase activator activity Source: Reactome
  4. transcription corepressor activity Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Reactome
  2. camera-type eye development Source: Ensembl
  3. forebrain development Source: Ensembl
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. negative regulation of vascular permeability Source: Ensembl
  6. neural tube closure Source: Ensembl
  7. positive regulation of Rho GTPase activity Source: GOC
  8. regulation of cell shape Source: Ensembl
  9. regulation of small GTPase mediated signal transduction Source: Reactome
  10. small GTPase mediated signal transduction Source: Reactome
  11. transcription, DNA-templated Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
SignaLinkiQ9NRY4.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 35
Alternative name(s):
Glucocorticoid receptor DNA-binding factor 1
Glucocorticoid receptor repression factor 1
Short name:
GRF-1
Rho GAP p190A
Short name:
p190-A
Gene namesi
Name:ARHGAP35
Synonyms:GRF1, GRLF1, KIAA1722
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:4591. ARHGAP35.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA28988.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14991499Rho GTPase-activating protein 35PRO_0000056730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei308 – 3081Phosphotyrosine1 Publication
Modified residuei589 – 5891Phosphoserine4 Publications
Modified residuei773 – 7731Phosphoserine1 Publication
Modified residuei970 – 9701Phosphoserine2 Publications
Modified residuei975 – 9751Phosphoserine2 Publications
Modified residuei1072 – 10721Phosphoserine1 Publication
Modified residuei1087 – 10871Phosphotyrosine1 Publication
Modified residuei1105 – 11051Phosphotyrosine; by ABL2 and PTK62 Publications
Modified residuei1134 – 11341Phosphoserine2 Publications
Modified residuei1150 – 11501Phosphoserine2 Publications
Modified residuei1179 – 11791Phosphoserine6 Publications

Post-translational modificationi

Phosphorylation of Tyr-1105 by PTK6 promotes the association with RASA1, inactivating RHOA while activating RAS. Phosphorylation at Tyr-308 by PDGFRA inhibits binding to GTF2I.8 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NRY4.
PaxDbiQ9NRY4.
PRIDEiQ9NRY4.

PTM databases

PhosphoSiteiQ9NRY4.

Expressioni

Gene expression databases

BgeeiQ9NRY4.
CleanExiHS_GRLF1.
ExpressionAtlasiQ9NRY4. baseline and differential.
GenevestigatoriQ9NRY4.

Organism-specific databases

HPAiCAB037311.

Interactioni

Subunit structurei

Interacts with RASA1. Interacts with the general transcription factor GTF2I, the interaction sequesters GTF2I in the cytoplasm.1 Publication

Protein-protein interaction databases

BioGridi109166. 9 interactions.
IntActiQ9NRY4. 1 interaction.
STRINGi9606.ENSP00000385720.

Structurei

Secondary structure

1
1499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 218Combined sources
Turni25 – 306Combined sources
Helixi35 – 439Combined sources
Turni47 – 493Combined sources
Helixi60 – 634Combined sources
Turni66 – 705Combined sources
Beta strandi72 – 798Combined sources
Beta strandi91 – 966Combined sources
Turni102 – 1043Combined sources
Helixi110 – 1123Combined sources
Helixi116 – 1205Combined sources
Beta strandi123 – 1264Combined sources
Helixi136 – 1383Combined sources
Helixi142 – 1443Combined sources
Helixi151 – 1533Combined sources
Beta strandi154 – 1563Combined sources
Beta strandi159 – 1657Combined sources
Helixi174 – 19017Combined sources
Beta strandi195 – 2006Combined sources
Helixi202 – 2043Combined sources
Helixi207 – 21812Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi225 – 2273Combined sources
Turni230 – 2334Combined sources
Helixi236 – 24813Combined sources
Turni268 – 2714Combined sources
Helixi272 – 28413Combined sources
Beta strandi286 – 2883Combined sources
Helixi292 – 2998Combined sources
Helixi303 – 3119Combined sources
Helixi314 – 33017Combined sources
Helixi1251 – 12544Combined sources
Beta strandi1257 – 12593Combined sources
Helixi1263 – 127513Combined sources
Turni1280 – 12845Combined sources
Helixi1289 – 130113Combined sources
Helixi1308 – 13103Combined sources
Helixi1314 – 132714Combined sources
Beta strandi1328 – 13303Combined sources
Helixi1335 – 134410Combined sources
Helixi1350 – 136213Combined sources
Helixi1366 – 138318Combined sources
Helixi1386 – 13894Combined sources
Helixi1393 – 140513Combined sources
Beta strandi1409 – 14124Combined sources
Helixi1414 – 143017Combined sources
Helixi1432 – 14365Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K85NMR-A267-331[»]
3C5HX-ray1.80A13-249[»]
3FK2X-ray2.80A/B/C/D1212-1439[»]
ProteinModelPortaliQ9NRY4.
SMRiQ9NRY4. Positions 13-249, 267-331, 1242-1437.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NRY4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini270 – 32758FF 1Add
BLAST
Domaini368 – 42255FF 2Add
BLAST
Domaini429 – 48355FF 3Add
BLAST
Domaini485 – 55066FF 4Add
BLAST
Domaini1249 – 1436188Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1440 – 149051Pro-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG241832.
GeneTreeiENSGT00760000118863.
HOVERGENiHBG051844.
InParanoidiQ9NRY4.
KOiK05732.
OMAiVLYRTRC.
OrthoDBiEOG779NWX.
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.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 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]

Sequencei

Sequence statusi: Complete.

Q9NRY4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF
60 70 80 90 100
HLDHTSVLST SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI
110 120 130 140 150
DDQTFQPHRS TALQPYIKRA AATKLASAEK LMYFCTDQLG LEQDFEQKQM
160 170 180 190 200
PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF VSNLYNQLAK TKKPIVVVLT
210 220 230 240 250
KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF STLVQLIDKS
260 270 280 290 300
RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWLSVSRKMQ
310 320 330 340 350
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA
360 370 380 390 400
LIPNLDEIDH LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE
410 420 430 440 450
RIPFDLMDTV PAEQLYEAHL EKLRNERKRV EMRRAFKENL ETSPFITPGK
460 470 480 490 500
PWEEARSFIM NEDFYQWLEE SVYMDIYGKH QKQIIDKAKE EFQELLLEYS
510 520 530 540 550
ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER DALILKHIHF
560 570 580 590 600
VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDPNIDRINL
610 620 630 640 650
VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS
660 670 680 690 700
FQTPTFQPHG CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL
710 720 730 740 750
ILVNKRGDTS GETLHSLIQQ GQQIASKLQC VFLDPASAGI GYGRNINEKQ
760 770 780 790 800
ISQVLKGLLD SKRNLNLVSS TASIKDLADV DLRIVMCLMC GDPFSADDIL
810 820 830 840 850
FPVLQSQTCK SSHCGSNNSV LLELPIGLHK KRIELSVLSY HSSFSIRKSR
860 870 880 890 900
LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAVDVLDNDL
910 920 930 940 950
SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LEIFHPFFKD VVEKKNIIEA
960 970 980 990 1000
THMYDNAAEA CSTTEEVFNS PRAGSPLCNS NLQDSEEDIE PSYSLFREDT
1010 1020 1030 1040 1050
SLPSLSKDHS KLSMELEGND GLSFIMSNFE SKLNNKVPPP VKPKPPVHFE
1060 1070 1080 1090 1100
ITKGDLSYLD QGHRDGQRKS VSSSPWLPQD GFDPSDYAEP MDAVVKPRNE
1110 1120 1130 1140 1150
EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT SSLERGRKVS
1160 1170 1180 1190 1200
IVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG
1210 1220 1230 1240 1250
DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP
1260 1270 1280 1290 1300
LTTVVTPEKP IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD
1310 1320 1330 1340 1350
QDHNLDLAEK DFTVNTVAGA MKSFFSELPD PLVPYNMQID LVEAHKINDR
1360 1370 1380 1390 1400
EQKLHALKEV LKKFPKENHE VFKYVISHLN KVSHNNKVNL MTSENLSICF
1410 1420 1430 1440 1450
WPTLMRPDFS TMDALTATRT YQTIIELFIQ QCPFFFYNRP ITEPPGARPS
1460 1470 1480 1490
SPSAVASTVP FLTSTPVTSQ PSPPQSPPPT PQSPMQPLLP SQLQAEHTL
Length:1,499
Mass (Da):170,514
Last modified:October 3, 2012 - v3
Checksum:i8CCB493414A7E3E6
GO

Sequence cautioni

The sequence AAA58618.1 differs from that shown. Reason: Frameshift at positions 389, 533, 540, 607, 614, 1167, 1241, 1292, 1334 and 1446. Curated
The sequence AAF80386.1 differs from that shown. Reason: Unlikely isoform. Aberrant splice sites.Curated
The sequence AAF80386.1 differs from that shown. Reason: Frameshift at positions 533, 540, 607 and 614. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511R → P in AAF80386. (PubMed:11054565)Curated
Sequence conflicti309 – 3091V → D in AAF80386. (PubMed:11054565)Curated
Sequence conflicti362 – 3621S → G in AAF80386. (PubMed:11054565)Curated
Sequence conflicti414 – 4141Q → A in AAF80386. (PubMed:11054565)Curated
Sequence conflicti414 – 4141Q → A in AAA58618. (PubMed:1894621)Curated
Sequence conflicti474 – 4741M → T in AAF80386. (PubMed:11054565)Curated
Sequence conflicti474 – 4741M → T in AAA58618. (PubMed:1894621)Curated
Sequence conflicti978 – 9781C → S in AAF80386. (PubMed:11054565)Curated
Sequence conflicti1292 – 12921M → I in AAF80386. (PubMed:11054565)Curated
Sequence conflicti1452 – 14532PS → RN in AAA58618. (PubMed:1894621)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051509 mRNA. Translation: BAB21813.2.
CH471126 Genomic DNA. Translation: EAW57450.1.
BC150257 mRNA. Translation: AAI50258.1.
AF159851 mRNA. Translation: AAF80386.1. Sequence problems.
M73077 mRNA. Translation: AAA58618.1. Frameshift.
CCDSiCCDS46127.1.
RefSeqiNP_004482.4. NM_004491.4.
UniGeneiHs.509447.

Genome annotation databases

GeneIDi2909.
KEGGihsa:2909.
UCSCiuc010ekv.3. human.

Polymorphism databases

DMDMi408360250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051509 mRNA. Translation: BAB21813.2 .
CH471126 Genomic DNA. Translation: EAW57450.1 .
BC150257 mRNA. Translation: AAI50258.1 .
AF159851 mRNA. Translation: AAF80386.1 . Sequence problems.
M73077 mRNA. Translation: AAA58618.1 . Frameshift.
CCDSi CCDS46127.1.
RefSeqi NP_004482.4. NM_004491.4.
UniGenei Hs.509447.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K85 NMR - A 267-331 [» ]
3C5H X-ray 1.80 A 13-249 [» ]
3FK2 X-ray 2.80 A/B/C/D 1212-1439 [» ]
ProteinModelPortali Q9NRY4.
SMRi Q9NRY4. Positions 13-249, 267-331, 1242-1437.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109166. 9 interactions.
IntActi Q9NRY4. 1 interaction.
STRINGi 9606.ENSP00000385720.

PTM databases

PhosphoSitei Q9NRY4.

Polymorphism databases

DMDMi 408360250.

Proteomic databases

MaxQBi Q9NRY4.
PaxDbi Q9NRY4.
PRIDEi Q9NRY4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2909.
KEGGi hsa:2909.
UCSCi uc010ekv.3. human.

Organism-specific databases

CTDi 2909.
GeneCardsi GC19P047422.
H-InvDB HIX0015264.
HGNCi HGNC:4591. ARHGAP35.
HPAi CAB037311.
MIMi 605277. gene.
neXtProti NX_Q9NRY4.
PharmGKBi PA28988.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG241832.
GeneTreei ENSGT00760000118863.
HOVERGENi HBG051844.
InParanoidi Q9NRY4.
KOi K05732.
OMAi VLYRTRC.
OrthoDBi EOG779NWX.
TreeFami TF324451.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
SignaLinki Q9NRY4.

Miscellaneous databases

ChiTaRSi ARHGAP35. human.
EvolutionaryTracei Q9NRY4.
GeneWikii GRLF1.
GenomeRNAii 2909.
NextBioi 11533.
PROi Q9NRY4.
SOURCEi Search...

Gene expression databases

Bgeei Q9NRY4.
CleanExi HS_GRLF1.
ExpressionAtlasi Q9NRY4. baseline and differential.
Genevestigatori Q9NRY4.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view ]
Pfami PF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view ]
SMARTi SM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEi PS51676. FF. 4 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "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.
  3. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "p190-A, a human tumor suppressor gene, maps to the chromosomal region 19q13.3 that is reportedly deleted in some gliomas."
    Tikoo A., Czekay S., Viars C., White S., Heath J.K., Arden K., Maruta H.
    Gene 257:23-31(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1491.
    Tissue: Mammary cancer.
  6. "Molecular cloning and characterization of a factor that binds the human glucocorticoid receptor gene and represses its expression."
    LeClerc S., Palaniswami R., Xie B.X., Govindan M.V.
    J. Biol. Chem. 266:17333-17340(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 377-1453, FUNCTION.
    Tissue: Mammary cancer.
  7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "Breast tumor kinase phosphorylates p190RhoGAP to regulate rho and ras and promote breast carcinoma growth, migration, and invasion."
    Shen C.H., Chen H.Y., Lin M.S., Li F.Y., Chang C.C., Kuo M.L., Settleman J., Chen R.H.
    Cancer Res. 68:7779-7787(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-1105.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-970 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-970; SER-975; SER-1150 AND SER-1179, 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-589; SER-773; SER-975; SER-1072; TYR-1087; TYR-1105; SER-1134 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-589 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-589; SER-1134; SER-1150 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "NMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding."
    Bonet R., Ruiz L., Aragon E., Martin-Malpartida P., Macias M.J.
    J. Mol. Biol. 389:230-237(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 267-331, PHOSPHORYLATION AT TYR-308, INTERACTION WITH GTF2I.

Entry informationi

Entry nameiRHG35_HUMAN
AccessioniPrimary (citable) accession number: Q9NRY4
Secondary accession number(s): A7E2A4, Q14452, Q9C0E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: October 3, 2012
Last modified: November 26, 2014
This is version 145 of the entry and version 3 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3