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Protein

CDC42 small effector protein 1

Gene

CDC42SE1

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.3 Publications

GO - Molecular functioni

  • GTPase inhibitor activity Source: ProtInc
  • structural molecule activity Source: GO_Central

GO - Biological processi

  • phagocytosis Source: UniProtKB-KW
  • regulation of cell shape Source: UniProtKB-KW
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell shape, Phagocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
CDC42 small effector protein 1
Alternative name(s):
CDC42-binding protein SCIP1
Small effector of CDC42 protein 1
Gene namesi
Name:CDC42SE1
Synonyms:SPEC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17719. CDC42SE1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 112CC → AA: Prevents targeting to the activated TCR. 1 Publication
Mutagenesisi33 – 331P → A: Abolishes interaction with CDC42, induces a decrease in blocking CDC42-induced JNK activation but does not affect targeting to the activated TCR; when associated with A-38 and A-41. 2 Publications
Mutagenesisi38 – 381H → A: Abolishes interaction with CDC42, induces a decrease in blocking CDC42-induced JNK activation but does not affect targeting to the activated TCR; when associated with A-33 and A-41. 2 Publications
Mutagenesisi41 – 411H → A: Abolishes interaction with CDC42, induces a decrease in blocking CDC42-induced JNK activation but does not affect targeting to the activated TCR; when associated with A-33 and A-38. 2 Publications
Mutagenesisi62 – 621Q → A: Abolishes interaction with CDC42 and induces a decrease in blocking CDC42-induced JNK activation; when associated with A-66. 1 Publication
Mutagenesisi66 – 661K → A: Abolishes interaction with CDC42 and induces a decrease in blocking CDC42-induced JNK activation; when associated with A-62. 1 Publication

Organism-specific databases

PharmGKBiPA134875001.

Polymorphism and mutation databases

BioMutaiCDC42SE1.
DMDMi74752924.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7979CDC42 small effector protein 1PRO_0000334629Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ9NRR8.
PaxDbiQ9NRR8.
PeptideAtlasiQ9NRR8.
PRIDEiQ9NRR8.

PTM databases

iPTMnetiQ9NRR8.
PhosphoSiteiQ9NRR8.
SwissPalmiQ9NRR8.

Expressioni

Tissue specificityi

Widely expressed. Expressed at higher level in T-lymphocytes, dendritic and whole blood cells.1 Publication

Gene expression databases

BgeeiQ9NRR8.
CleanExiHS_CDC42SE1.
GenevisibleiQ9NRR8. HS.

Organism-specific databases

HPAiHPA027634.

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

BioGridi121215. 11 interactions.
IntActiQ9NRR8. 1 interaction.
STRINGi9606.ENSP00000349773.

Structurei

3D structure databases

ProteinModelPortaliQ9NRR8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 4314CRIBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 246Mediates phosphoinositide-binding

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

eggNOGiENOG410IYXR. Eukaryota.
ENOG4112BYQ. LUCA.
GeneTreeiENSGT00390000010375.
HOVERGENiHBG107546.
InParanoidiQ9NRR8.
OMAiQMRSKGS.
OrthoDBiEOG74N5KD.
PhylomeDBiQ9NRR8.
TreeFamiTF323815.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NRR8-1) [UniParc]FASTAAdd to basket

Also known as: Alpha

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
MSEFWHKLGC CVVEKPQPKK KRRRIDRTMI GEPMNFVHLT HIGSGEMGAG
60 70
DGLAMTGAVQ EQMRSKGNRD RPWSNSRGL
Length:79
Mass (Da):8,925
Last modified:October 1, 2000 - v1
Checksum:iD1C1DCEBD339EF5B
GO
Isoform 2 (identifier: Q9NRR8-2) [UniParc]FASTAAdd to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     19-79: KKKRRRIDRT...DRPWSNSRGL → VSLPTPHPNPKSSQLLCAVR

Show »
Length:38
Mass (Da):4,245
Checksum:i3B416F3C5ADF4E91
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei19 – 7961KKKRR…NSRGL → VSLPTPHPNPKSSQLLCAVR in isoform 2. 1 PublicationVSP_033717Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF187845 mRNA. Translation: AAF87597.1.
AF286592 mRNA. Translation: AAG17723.1.
AL590133 Genomic DNA. Translation: CAI13349.1.
CH471121 Genomic DNA. Translation: EAW53477.1.
CH471121 Genomic DNA. Translation: EAW53478.1.
CH471121 Genomic DNA. Translation: EAW53479.1.
BC012796 mRNA. Translation: AAH12796.2.
BC041604 mRNA. Translation: AAH41604.1.
AF286041 mRNA. Translation: AAF97248.1.
CCDSiCCDS981.1. [Q9NRR8-1]
RefSeqiNP_001033796.1. NM_001038707.1. [Q9NRR8-1]
NP_064624.1. NM_020239.3. [Q9NRR8-1]
UniGeneiHs.22065.
Hs.656288.

Genome annotation databases

EnsembliENST00000357235; ENSP00000349773; ENSG00000197622. [Q9NRR8-1]
ENST00000439374; ENSP00000475845; ENSG00000197622. [Q9NRR8-1]
ENST00000540998; ENSP00000445647; ENSG00000197622. [Q9NRR8-1]
GeneIDi56882.
KEGGihsa:56882.
UCSCiuc001ewo.4. human. [Q9NRR8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF187845 mRNA. Translation: AAF87597.1.
AF286592 mRNA. Translation: AAG17723.1.
AL590133 Genomic DNA. Translation: CAI13349.1.
CH471121 Genomic DNA. Translation: EAW53477.1.
CH471121 Genomic DNA. Translation: EAW53478.1.
CH471121 Genomic DNA. Translation: EAW53479.1.
BC012796 mRNA. Translation: AAH12796.2.
BC041604 mRNA. Translation: AAH41604.1.
AF286041 mRNA. Translation: AAF97248.1.
CCDSiCCDS981.1. [Q9NRR8-1]
RefSeqiNP_001033796.1. NM_001038707.1. [Q9NRR8-1]
NP_064624.1. NM_020239.3. [Q9NRR8-1]
UniGeneiHs.22065.
Hs.656288.

3D structure databases

ProteinModelPortaliQ9NRR8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121215. 11 interactions.
IntActiQ9NRR8. 1 interaction.
STRINGi9606.ENSP00000349773.

PTM databases

iPTMnetiQ9NRR8.
PhosphoSiteiQ9NRR8.
SwissPalmiQ9NRR8.

Polymorphism and mutation databases

BioMutaiCDC42SE1.
DMDMi74752924.

Proteomic databases

MaxQBiQ9NRR8.
PaxDbiQ9NRR8.
PeptideAtlasiQ9NRR8.
PRIDEiQ9NRR8.

Protocols and materials databases

DNASUi56882.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357235; ENSP00000349773; ENSG00000197622. [Q9NRR8-1]
ENST00000439374; ENSP00000475845; ENSG00000197622. [Q9NRR8-1]
ENST00000540998; ENSP00000445647; ENSG00000197622. [Q9NRR8-1]
GeneIDi56882.
KEGGihsa:56882.
UCSCiuc001ewo.4. human. [Q9NRR8-1]

Organism-specific databases

CTDi56882.
GeneCardsiCDC42SE1.
HGNCiHGNC:17719. CDC42SE1.
HPAiHPA027634.
neXtProtiNX_Q9NRR8.
PharmGKBiPA134875001.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IYXR. Eukaryota.
ENOG4112BYQ. LUCA.
GeneTreeiENSGT00390000010375.
HOVERGENiHBG107546.
InParanoidiQ9NRR8.
OMAiQMRSKGS.
OrthoDBiEOG74N5KD.
PhylomeDBiQ9NRR8.
TreeFamiTF323815.

Miscellaneous databases

ChiTaRSiCDC42SE1. human.
GenomeRNAii56882.
PROiQ9NRR8.

Gene expression databases

BgeeiQ9NRR8.
CleanExiHS_CDC42SE1.
GenevisibleiQ9NRR8. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDC42, MUTAGENESIS OF PRO-33; HIS-38; HIS-41; GLN-62 AND LYS-66.
  2. "The genomic structure of the human SPEC1 gene reveals complex splicing and close promoter proximity to the AF1q translocation gene."
    Pirone D.M., Oberst M.D., Stylianou D., Burbelo P.D.
    Gene 273:295-303(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: Skin.
  6. "Cloning and characterization of a small, CRIB-containing, Cdc42-binding protein."
    Mitina O.V., Serebriiskii I.G., Chernoff J.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-79 (ISOFORM 1).
  7. "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, PROBABLE PALMITOYLATION, MUTAGENESIS OF 10-CYS-CYS-11; PRO-33; HIS-38 AND HIS-41.
  8. "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: FUNCTION, PHOSPHOINOSITIDE-BINDING.

Entry informationi

Entry nameiC42S1_HUMAN
AccessioniPrimary (citable) accession number: Q9NRR8
Secondary accession number(s): D3DV12, Q9HB17, Q9NQR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 116 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

Complete proteome, Reference proteome

Documents

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

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 one 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.