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Q9H4E5 (RHOJ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho-related GTP-binding protein RhoJ
Alternative name(s):
Ras-like protein family member 7B
Tc10-like GTP-binding protein
Gene names
Name:RHOJ
Synonyms:ARHJ, RASL7B, RHOI, TCL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

GTP-binding protein with GTPase activity. Elicits the formation of F-actin-rich structures in fibroblasts and is involved in the regulation of cell morphology By similarity.

Subunit structure

Interacts with the CRIB domains of proteins such as Pak1 and Was/Wasp By similarity.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Sequence caution

The sequence BAB55013.1 differs from that shown. Reason: Frameshift at position 143.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H4E5-1)

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.
Isoform 2 (identifier: Q9H4E5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     113-134: Missing.
Note: No experimental confirmation available. Could be created by usage of an unusual splicing donor site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Rho-related GTP-binding protein RhoJ
PRO_0000198869
Propeptide212 – 2143Removed in mature form By similarity
PRO_0000281220

Regions

Nucleotide binding28 – 358GTP By similarity
Nucleotide binding75 – 795GTP By similarity
Nucleotide binding133 – 1364GTP By similarity
Motif50 – 589Effector region Potential

Amino acid modifications

Modified residue2111Cysteine methyl ester By similarity
Lipidation2111S-farnesyl cysteine By similarity

Natural variations

Alternative sequence113 – 13422Missing in isoform 2.
VSP_007231

Experimental info

Sequence conflict31C → R in BAB55013. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: AAD2E2CED036F48C

FASTA21423,821
        10         20         30         40         50         60 
MNCKEGTDSS CGCRGNDEKK MLKCVVVGDG AVGKTCLLMS YANDAFPEEY VPTVFDHYAV 

        70         80         90        100        110        120 
TVTVGGKQHL LGLYDTAGQE DYNQLRPLSY PNTDVFLICF SVVNPASYHN VQEEWVPELK 

       130        140        150        160        170        180 
DCMPHVPYVL IGTQIDLRDD PKTLARLLYM KEKPLTYEHG VKLAKAIGAQ CYLECSALTQ 

       190        200        210 
KGLKAVFDEA ILTIFHPKKK KKRCSEGHSC CSII 

« Hide

Isoform 2 [UniParc].

Checksum: F20844F6EC738489
Show »

FASTA19221,255

References

« Hide 'large scale' references
[1]"Characterization of TCL, a new GTPase of the Rho family related to TC10 and Cdc42."
Vignal E., De Toledo M., Comunale F., Ladopoulou A., Gauthier-Rouviere C., Blangy A., Fort P.
J. Biol. Chem. 275:36457-36464(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A novel Rho GTPase (RhoI) induces loss of stress-fibers and results in apical actin reorganization."
Allen M., Halford S., Daniels H., McIntosh B., Kanuga N., Greenwood J., Carey A.H., Adamson P.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Tissue: Embryo.
[4]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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 1).
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ276567 mRNA. Translation: CAC06611.1.
AF309563 mRNA. Translation: AAL09440.1.
AK027278 mRNA. Translation: BAB55013.1. Frameshift.
AK027351 mRNA. Translation: BAB55055.1.
AF498977 mRNA. Translation: AAM21124.1.
BC062575 mRNA. Translation: AAH62575.1.
CCDSCCDS9757.1. [Q9H4E5-1]
RefSeqNP_065714.1. NM_020663.4. [Q9H4E5-1]
UniGeneHs.656339.

3D structure databases

ProteinModelPortalQ9H4E5.
SMRQ9H4E5. Positions 21-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121499. 2 interactions.
IntActQ9H4E5. 2 interactions.
STRING9606.ENSP00000316729.

PTM databases

PhosphoSiteQ9H4E5.

Polymorphism databases

DMDM24418646.

Proteomic databases

MaxQBQ9H4E5.
PaxDbQ9H4E5.
PRIDEQ9H4E5.

Protocols and materials databases

DNASU57381.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316754; ENSP00000316729; ENSG00000126785. [Q9H4E5-1]
GeneID57381.
KEGGhsa:57381.
UCSCuc001xgb.2. human. [Q9H4E5-1]

Organism-specific databases

CTD57381.
GeneCardsGC14P063671.
HGNCHGNC:688. RHOJ.
HPAHPA003050.
MIM607653. gene.
neXtProtNX_Q9H4E5.
PharmGKBPA24981.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOVERGENHBG009351.
InParanoidQ9H4E5.
KOK07864.
OMAARMNCKE.
PhylomeDBQ9H4E5.
TreeFamTF101109.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9H4E5.
BgeeQ9H4E5.
CleanExHS_RHOJ.
GenevestigatorQ9H4E5.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRHOJ. human.
GeneWikiRHOJ.
GenomeRNAi57381.
NextBio63486.
PROQ9H4E5.
SOURCESearch...

Entry information

Entry nameRHOJ_HUMAN
AccessionPrimary (citable) accession number: Q9H4E5
Secondary accession number(s): Q96KC1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM