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Q5VV41

- ARHGG_HUMAN

UniProt

Q5VV41 - ARHGG_HUMAN

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Protein

Rho guanine nucleotide exchange factor 16

Gene

ARHGEF16

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

Functioni

Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 and mediate activation of CDC42 by the viral protein HPV16 E6.1 Publication

GO - Molecular functioni

  1. PDZ domain binding Source: BHF-UCL
  2. receptor tyrosine kinase binding Source: UniProtKB
  3. Rho GTPase binding Source: UniProtKB
  4. Rho guanyl-nucleotide exchange factor activity Source: UniProtKB

GO - Biological processi

  1. activation of Cdc42 GTPase activity Source: BHF-UCL
  2. activation of Rac GTPase activity Source: UniProtKB
  3. apoptotic signaling pathway Source: Reactome
  4. cell chemotaxis Source: UniProtKB
  5. neurotrophin TRK receptor signaling pathway Source: Reactome
  6. positive regulation of apoptotic process Source: Reactome
  7. positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  8. regulation of small GTPase mediated signal transduction Source: Reactome
  9. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 16
Alternative name(s):
Ephexin-4
Gene namesi
Name:ARHGEF16
Synonyms:EPHEXIN4, NBR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:15515. ARHGEF16.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24971.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 709708Rho guanine nucleotide exchange factor 16PRO_0000233690Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei41 – 411Phosphoserine2 Publications
Modified residuei107 – 1071Phosphoserine4 Publications
Modified residuei174 – 1741Phosphoserine1 Publication
Modified residuei191 – 1911Phosphoserine1 Publication
Modified residuei208 – 2081Phosphoserine2 Publications
Modified residuei227 – 2271Phosphoserine1 Publication
Modified residuei230 – 2301Phosphoserine2 Publications
Modified residuei240 – 2401Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5VV41.
PaxDbiQ5VV41.
PRIDEiQ5VV41.

PTM databases

PhosphoSiteiQ5VV41.

Expressioni

Inductioni

Up-regulated by HPV16 E6 (at protein level).1 Publication

Gene expression databases

BgeeiQ5VV41.
CleanExiHS_ARHGEF16.
ExpressionAtlasiQ5VV41. baseline and differential.
GenevestigatoriQ5VV41.

Organism-specific databases

HPAiHPA010609.

Interactioni

Subunit structurei

Interacts with ELMO2, EPHA2, RAC1 and RHOG; mediates activation of RAC1 by EPHA2. Interacts with TAX1BP3 (via PDZ domain). May interact with CDC42; stimulated by HPV16 E6.2 Publications

Protein-protein interaction databases

BioGridi118085. 3 interactions.
IntActiQ5VV41. 2 interactions.
MINTiMINT-3295714.
STRINGi9606.ENSP00000367629.

Structurei

Secondary structure

1
709
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi633 – 6386Combined sources
Beta strandi644 – 6474Combined sources
Beta strandi654 – 6629Combined sources
Beta strandi665 – 6706Combined sources
Turni671 – 6733Combined sources
Beta strandi676 – 6794Combined sources
Helixi681 – 6833Combined sources
Beta strandi685 – 6873Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X6BNMR-A622-687[»]
ProteinModelPortaliQ5VV41.
SMRiQ5VV41. Positions 276-618, 628-688.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5VV41.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini284 – 468185DHPROSITE-ProRule annotationAdd
BLAST
Domaini501 – 620120PHPROSITE-ProRule annotationAdd
BLAST
Domaini629 – 68961SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni275 – 481207Required for RHOG activation and mediates interaction with EPHA2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi707 – 7093PDZ-binding motif

Domaini

The PDZ-binding motif mediates interaction with TAX1BP3.

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiCOG5422.
GeneTreeiENSGT00550000074493.
HOGENOMiHOG000007536.
HOVERGENiHBG059167.
InParanoidiQ5VV41.
OMAiQTEHHHL.
OrthoDBiEOG73NG2P.
PhylomeDBiQ5VV41.
TreeFamiTF316357.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5VV41-1) [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
MAQRHSDSSL EEKLLGHRFH SELRLDAGGN PASGLPMVRG SPRVRDDAAF
60 70 80 90 100
QPQVPAPPQP RPPGHEEPWP IVLSTESPAA LKLGTQQLIP KSLAVASKAK
110 120 130 140 150
TPARHQSFGA AVLSREAARR DPKLLPAPSF SLDDMDVDKD PGGMLRRNLR
160 170 180 190 200
NQSYRAAMKG LGKPGGQGDA IQLSPKLQAL AEEPSQPHTR SPAKNKKTLG
210 220 230 240 250
RKRGHKGSFK DDPQLYQEIQ ERGLNTSQES DDDILDESSS PEGTQKVDAT
260 270 280 290 300
IVVKSYRPAQ VTWSQLPEVV ELGILDQLST EERKRQEAMF EILTSEFSYQ
310 320 330 340 350
HSLSILVEEF LQSKELRATV TQMEHHHLFS NILDVLGASQ RFFEDLEQRH
360 370 380 390 400
KAQVLVEDIS DILEEHAEKH FHPYIAYCSN EVYQQRTLQK LISSNAAFRE
410 420 430 440 450
ALREIERRPA CGGLPMLSFL ILPMQRVTRL PLLMDTLCLK TQGHSERYKA
460 470 480 490 500
ASRALKAISK LVRQCNEGAH RMERMEQMYT LHTQLDFSKV KSLPLISASR
510 520 530 540 550
WLLKRGELFL VEETGLFRKI ASRPTCYLFL FNDVLVVTKK KSEESYMVQD
560 570 580 590 600
YAQMNHIQVE KIEPSELPLP GGGNRSSSVP HPFQVTLLRN SEGRQEQLLL
610 620 630 640 650
SSDSASDRAR WIVALTHSER QWQGLSSKGD LPQVEITKAF FAKQADEVTL
660 670 680 690 700
QQADVVLVLQ QEDGWLYGER LRDGETGWFP EDFARFITSR VAVEGNVRRM

ERLRVETDV
Length:709
Mass (Da):80,105
Last modified:December 7, 2004 - v1
Checksum:i9672AB3C92311BEB
GO
Isoform 2 (identifier: Q5VV41-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-288: Missing.

Show »
Length:421
Mass (Da):48,629
Checksum:i7A75C46922C40EA4
GO

Sequence cautioni

The sequence AAH02681.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1582AM → RG in AAH02681. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371V → M.
Corresponds to variant rs3806164 [ dbSNP | Ensembl ].
VAR_059796
Natural varianti370 – 3701H → Y.3 Publications
Corresponds to variant rs2185639 [ dbSNP | Ensembl ].
VAR_059797
Natural varianti681 – 6811E → K.
Corresponds to variant rs56309807 [ dbSNP | Ensembl ].
VAR_061796

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 288288Missing in isoform 2. 3 PublicationsVSP_018149Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89016 mRNA. Translation: BAA13745.1.
BT007270 mRNA. Translation: AAP35934.1.
AL512413 Genomic DNA. Translation: CAH70832.1.
AL512413 Genomic DNA. Translation: CAH70833.1.
BC002681 mRNA. Translation: AAH02681.1. Different initiation.
BC051838 mRNA. Translation: AAH51838.1.
CCDSiCCDS46.2. [Q5VV41-1]
RefSeqiNP_055263.2. NM_014448.3. [Q5VV41-1]
XP_006710641.1. XM_006710578.1. [Q5VV41-1]
UniGeneiHs.87435.

Genome annotation databases

EnsembliENST00000378371; ENSP00000367622; ENSG00000130762. [Q5VV41-2]
ENST00000378373; ENSP00000367624; ENSG00000130762. [Q5VV41-2]
ENST00000378378; ENSP00000367629; ENSG00000130762. [Q5VV41-1]
GeneIDi27237.
KEGGihsa:27237.
UCSCiuc001akg.4. human. [Q5VV41-1]

Polymorphism databases

DMDMi74747198.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89016 mRNA. Translation: BAA13745.1 .
BT007270 mRNA. Translation: AAP35934.1 .
AL512413 Genomic DNA. Translation: CAH70832.1 .
AL512413 Genomic DNA. Translation: CAH70833.1 .
BC002681 mRNA. Translation: AAH02681.1 . Different initiation.
BC051838 mRNA. Translation: AAH51838.1 .
CCDSi CCDS46.2. [Q5VV41-1 ]
RefSeqi NP_055263.2. NM_014448.3. [Q5VV41-1 ]
XP_006710641.1. XM_006710578.1. [Q5VV41-1 ]
UniGenei Hs.87435.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X6B NMR - A 622-687 [» ]
ProteinModelPortali Q5VV41.
SMRi Q5VV41. Positions 276-618, 628-688.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118085. 3 interactions.
IntActi Q5VV41. 2 interactions.
MINTi MINT-3295714.
STRINGi 9606.ENSP00000367629.

PTM databases

PhosphoSitei Q5VV41.

Polymorphism databases

DMDMi 74747198.

Proteomic databases

MaxQBi Q5VV41.
PaxDbi Q5VV41.
PRIDEi Q5VV41.

Protocols and materials databases

DNASUi 27237.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378371 ; ENSP00000367622 ; ENSG00000130762 . [Q5VV41-2 ]
ENST00000378373 ; ENSP00000367624 ; ENSG00000130762 . [Q5VV41-2 ]
ENST00000378378 ; ENSP00000367629 ; ENSG00000130762 . [Q5VV41-1 ]
GeneIDi 27237.
KEGGi hsa:27237.
UCSCi uc001akg.4. human. [Q5VV41-1 ]

Organism-specific databases

CTDi 27237.
GeneCardsi GC01P003370.
HGNCi HGNC:15515. ARHGEF16.
HPAi HPA010609.
neXtProti NX_Q5VV41.
PharmGKBi PA24971.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5422.
GeneTreei ENSGT00550000074493.
HOGENOMi HOG000007536.
HOVERGENi HBG059167.
InParanoidi Q5VV41.
OMAi QTEHHHL.
OrthoDBi EOG73NG2P.
PhylomeDBi Q5VV41.
TreeFami TF316357.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.

Miscellaneous databases

ChiTaRSi ARHGEF16. human.
EvolutionaryTracei Q5VV41.
GenomeRNAii 27237.
NextBioi 50111.
PROi Q5VV41.

Gene expression databases

Bgeei Q5VV41.
CleanExi HS_ARHGEF16.
ExpressionAtlasi Q5VV41. baseline and differential.
Genevestigatori Q5VV41.

Family and domain databases

Gene3Di 1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEi PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a candidate gene for human neuroblastoma mapped to 1p36.3, NBR: a new member of the Rho/Rac GEF family."
    Sasaki S., Takei Y., Ito M., Nakagawara A., Fujiwara T., Takahashi E., Muto T., Tokino T., Nakamura Y.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT TYR-370.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT TYR-370.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-709, VARIANT TYR-370.
    Tissue: PNS.
  5. "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-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-107; SER-208; SER-227; SER-230 AND SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent mechanism."
    Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S., Negishi M., Katoh H.
    J. Cell Biol. 190:461-477(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ELMO2; EPHA2; RAC1 AND RHOG.
  9. "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-41; SER-107; SER-174 AND SER-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which activates Cdc42."
    Oliver A.W., He X., Borthwick K., Donne A.J., Hampson L., Hampson I.N.
    Br. J. Cancer 104:324-331(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC42 AND TAX1BP3, INDUCTION BY HPV16 E6.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-107; SER-208 AND SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "Solution structures of the SH3 domain of human rho guanine exchange factor (GEF) 16."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: STRUCTURE BY NMR OF 622-687.

Entry informationi

Entry nameiARHGG_HUMAN
AccessioniPrimary (citable) accession number: Q5VV41
Secondary accession number(s): Q86TF0, Q99434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: December 7, 2004
Last modified: November 26, 2014
This is version 106 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3