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Protein

CDC42 small effector protein 2

Gene

CDC42SE2

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. structural molecule activity Source: UniProtKB

GO - Biological processi

  1. phagocytosis Source: UniProtKB-KW
  2. regulation of cell shape Source: UniProtKB-KW
  3. regulation of signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell shape, Phagocytosis

Enzyme and pathway databases

SignaLinkiQ9NRR3.

Names & Taxonomyi

Protein namesi
Recommended name:
CDC42 small effector protein 2
Alternative name(s):
Small effector of CDC42 protein 2
Gene namesi
Name:CDC42SE2
Synonyms:SPEC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:18547. CDC42SE2.

Subcellular locationi

  1. Cytoplasmcytoskeleton
  2. Cell membrane; Lipid-anchor
  3. Cell projectionphagocytic cup

  4. Note: Recruited to the activated TCR prior actin polymerization. Localizes at the phagocytic cup of macrophages.

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProtKB
  5. phagocytic cup Source: UniProtKB-SubCell
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA133787056.

Polymorphism and mutation databases

BioMutaiCDC42SE2.
DMDMi74719133.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8484CDC42 small effector protein 2PRO_0000334639Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi10 – 101S-palmitoyl cysteine1 Publication
Lipidationi11 – 111S-palmitoyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ9NRR3.
PaxDbiQ9NRR3.
PRIDEiQ9NRR3.

PTM databases

PhosphoSiteiQ9NRR3.

Expressioni

Tissue specificityi

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).1 Publication

Gene expression databases

BgeeiQ9NRR3.
CleanExiHS_CDC42SE2.
ExpressionAtlasiQ9NRR3. baseline and differential.
GenevestigatoriQ9NRR3.

Organism-specific databases

HPAiHPA038624.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi121306. 8 interactions.
STRINGi9606.ENSP00000353706.

Structurei

3D structure databases

ProteinModelPortaliQ9NRR3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 4214CRIBPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi20 – 234Poly-Arg

Domaini

The CRIB domain mediates interaction with CDC42.

Sequence similaritiesi

Belongs to the CDC42SE/SPEC family.Curated
Contains 1 CRIB domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG78697.
GeneTreeiENSGT00390000010375.
HOGENOMiHOG000006512.
HOVERGENiHBG107546.
InParanoidiQ9NRR3.
OMAiHHQRLRI.
PhylomeDBiQ9NRR3.
TreeFamiTF323815.

Family and domain databases

Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
[Graphical view]
PROSITEiPS50108. CRIB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NRR3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEFWLCFNC CIAEQPQPKR RRRIDRSMIG EPTNFVHTAH VGSGDLFSGM
60 70 80
NSVSSIQNQM QSKGGYGGGM PANVQMQLVD TKAG
Length:84
Mass (Da):9,223
Last modified:October 1, 2000 - v1
Checksum:i98C5E82176DA990A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34224.1.
RefSeqiNP_001033791.1. NM_001038702.1.
NP_064625.1. NM_020240.2.
UniGeneiHs.508829.
Hs.713870.

Genome annotation databases

EnsembliENST00000360515; ENSP00000353706; ENSG00000158985.
ENST00000395246; ENSP00000378667; ENSG00000158985.
ENST00000505065; ENSP00000427421; ENSG00000158985.
GeneIDi56990.
KEGGihsa:56990.
UCSCiuc003kvh.3. human.

Polymorphism and mutation databases

BioMutaiCDC42SE2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34224.1.
RefSeqiNP_001033791.1. NM_001038702.1.
NP_064625.1. NM_020240.2.
UniGeneiHs.508829.
Hs.713870.

3D structure databases

ProteinModelPortaliQ9NRR3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121306. 8 interactions.
STRINGi9606.ENSP00000353706.

PTM databases

PhosphoSiteiQ9NRR3.

Polymorphism and mutation databases

BioMutaiCDC42SE2.
DMDMi74719133.

Proteomic databases

MaxQBiQ9NRR3.
PaxDbiQ9NRR3.
PRIDEiQ9NRR3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360515; ENSP00000353706; ENSG00000158985.
ENST00000395246; ENSP00000378667; ENSG00000158985.
ENST00000505065; ENSP00000427421; ENSG00000158985.
GeneIDi56990.
KEGGihsa:56990.
UCSCiuc003kvh.3. human.

Organism-specific databases

CTDi56990.
GeneCardsiGC05P130581.
H-InvDBHIX0005148.
HGNCiHGNC:18547. CDC42SE2.
HPAiHPA038624.
neXtProtiNX_Q9NRR3.
PharmGKBiPA133787056.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG78697.
GeneTreeiENSGT00390000010375.
HOGENOMiHOG000006512.
HOVERGENiHBG107546.
InParanoidiQ9NRR3.
OMAiHHQRLRI.
PhylomeDBiQ9NRR3.
TreeFamiTF323815.

Enzyme and pathway databases

SignaLinkiQ9NRR3.

Miscellaneous databases

ChiTaRSiCDC42SE2. human.
GenomeRNAii56990.
NextBioi62683.
PROiQ9NRR3.

Gene expression databases

BgeeiQ9NRR3.
CleanExiHS_CDC42SE2.
ExpressionAtlasiQ9NRR3. baseline and differential.
GenevestigatoriQ9NRR3.

Family and domain databases

Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
[Graphical view]
PROSITEiPS50108. CRIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. Cited for: POSSIBLE SUSCEPTIBILITY TO SCHIZOPHRENIA.

Entry informationi

Entry nameiC42S2_HUMAN
AccessioniPrimary (citable) accession number: Q9NRR3
Secondary accession number(s): B2R622, Q4KMT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 1, 2000
Last modified: April 29, 2015
This is version 101 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

Miscellaneous

CDC42SE2 is mapped in the genomic region associated with schizophrenia.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.