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Q9NRR3 (C42S2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CDC42 small effector protein 2
Alternative name(s):
Small effector of CDC42 protein 2
Gene names
Name:CDC42SE2
Synonyms:SPEC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length84 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T-cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages. Ref.1 Ref.5

Subunit structure

Interacts with CDC42 (in GTP-bound form). Interacts weakly with RAC1 and not at all with RHOA. Ref.1

Subcellular location

Cytoplasmcytoskeleton. Cell membrane; Lipid-anchor. Cell projectionphagocytic cup. Note: Recruited to the activated TCR prior actin polymerization. Localizes at the phagocytic cup of macrophages. Ref.1 Ref.5 Ref.6

Tissue specificity

Widely expressed. Expressed at higher level in T-lymphocytes. Highly expressed in CCRF-CEM T-lymphocytes, Jurkat T-lymphocytes, and Raji B-lymphocytes compared (at protein level). Ref.5

Domain

The CRIB domain mediates interaction with CDC42.

Miscellaneous

CDC42SE2 is mapped in the genomic region associated with schizophrenia.

Sequence similarities

Belongs to the CDC42SE/SPEC family.

Contains 1 CRIB domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8484CDC42 small effector protein 2
PRO_0000334639

Regions

Domain29 – 4214CRIB
Compositional bias20 – 234Poly-Arg

Amino acid modifications

Lipidation101S-palmitoyl cysteine Ref.5
Lipidation111S-palmitoyl cysteine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9NRR3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 98C5E82176DA990A

FASTA849,223
        10         20         30         40         50         60 
MSEFWLCFNC CIAEQPQPKR RRRIDRSMIG EPTNFVHTAH VGSGDLFSGM NSVSSIQNQM 

        70         80 
QSKGGYGGGM PANVQMQLVD TKAG 

« Hide

References

« Hide 'large scale' references
[1]"SPECs, small binding proteins for Cdc42."
Pirone D.M., Fukuhara S., Gutkind J.S., Burbelo P.D.
J. Biol. Chem. 275:22650-22656(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDC42.
[2]"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].
Tissue: Brain.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The role of SPECs, small Cdc42-binding proteins, in F-actin accumulation at the immunological synapse."
Ching K.H., Kisailus A.E., Burbelo P.D.
J. Biol. Chem. 280:23660-23667(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PALMITOYLATION AT CYS-10 AND CYS-11.
[6]"Biochemical characterization of distinct regions of SPEC molecules and their role in phagocytosis."
Ching K.H., Kisailus A.E., Burbelo P.D.
Exp. Cell Res. 313:10-21(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Haplotypes spanning SPEC2, PDZ-GEF2 and ACSL6 genes are associated with schizophrenia."
Chen X., Wang X., Hossain S., O'Neill F.A., Walsh D., Pless L., Chowdari K.V., Nimgaonkar V.L., Schwab S.G., Wildenauer D.B., Sullivan P.F., van den Oord E., Kendler K.S.
Hum. Mol. Genet. 15:3329-3342(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE SUSCEPTIBILITY TO SCHIZOPHRENIA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF189692 mRNA. Translation: AAF87598.1.
AK312406 mRNA. Translation: BAG35319.1.
CH471062 Genomic DNA. Translation: EAW62373.1.
BC096703 mRNA. Translation: AAH96703.1.
BC096738 mRNA. Translation: AAH96738.1.
BC098349 mRNA. Translation: AAH98349.1.
CCDSCCDS34224.1.
RefSeqNP_001033791.1. NM_001038702.1.
NP_064625.1. NM_020240.2.
UniGeneHs.508829.
Hs.713870.

3D structure databases

ProteinModelPortalQ9NRR3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121306. 5 interactions.
STRING9606.ENSP00000353706.

PTM databases

PhosphoSiteQ9NRR3.

Polymorphism databases

DMDM74719133.

Proteomic databases

MaxQBQ9NRR3.
PaxDbQ9NRR3.
PRIDEQ9NRR3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360515; ENSP00000353706; ENSG00000158985.
ENST00000395246; ENSP00000378667; ENSG00000158985.
ENST00000505065; ENSP00000427421; ENSG00000158985.
GeneID56990.
KEGGhsa:56990.
UCSCuc003kvh.3. human.

Organism-specific databases

CTD56990.
GeneCardsGC05P130581.
H-InvDBHIX0005148.
HGNCHGNC:18547. CDC42SE2.
HPAHPA038624.
neXtProtNX_Q9NRR3.
PharmGKBPA133787056.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG78697.
HOGENOMHOG000006512.
HOVERGENHBG107546.
InParanoidQ9NRR3.
OMAISANVQM.
PhylomeDBQ9NRR3.
TreeFamTF323815.

Enzyme and pathway databases

SignaLinkQ9NRR3.

Gene expression databases

ArrayExpressQ9NRR3.
BgeeQ9NRR3.
CleanExHS_CDC42SE2.
GenevestigatorQ9NRR3.

Family and domain databases

Gene3D3.90.810.10. 1 hit.
InterProIPR000095. CRIB_dom.
[Graphical view]
PfamPF00786. PBD. 1 hit.
[Graphical view]
PROSITEPS50108. CRIB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi56990.
NextBio62683.
PROQ9NRR3.

Entry information

Entry nameC42S2_HUMAN
AccessionPrimary (citable) accession number: Q9NRR3
Secondary accession number(s): B2R622, Q4KMT9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 95 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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM