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Q15438 (CYH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytohesin-1
Alternative name(s):
PH, SEC7 and coiled-coil domain-containing protein 1
SEC7 homolog B2-1
Gene names
Name:CYTH1
Synonyms:D17S811E, PSCD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP. Ref.4 Ref.9

Subunit structure

Interacts with TRIM23 and CYTIP. Ref.5 Ref.6

Subcellular location

Cell membrane; Peripheral membrane protein. Cytoplasmcytosol By similarity Ref.7.

Tissue specificity

Ubiquitous.

Domain

Binds via its PH domain to the inositol head group of phosphatidylinositol 3,4,5-trisphosphate By similarity.

Autoinhibited by its C-terminal basic region By similarity.

Sequence similarities

Contains 1 PH domain.

Contains 1 SEC7 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CYTIPO607592EBI-997830,EBI-997814

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15438-1)

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: Q15438-2)

The sequence of this isoform differs from the canonical sequence as follows:
     273-273: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Cytohesin-1
PRO_0000120194

Regions

Domain73 – 202130SEC7
Domain260 – 377118PH
Region269 – 2779Phosphatidylinositol 3,4,5-trisphosphate binding By similarity
Region388 – 3969C-terminal autoinhibitory region By similarity
Coiled coil10 – 6758 Potential

Sites

Binding site2811Phosphatidylinositol 3,4,5-trisphosphate By similarity
Binding site2921Phosphatidylinositol 3,4,5-trisphosphate By similarity
Binding site3021Phosphatidylinositol 3,4,5-trisphosphate By similarity
Binding site3511Phosphatidylinositol 3,4,5-trisphosphate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8

Natural variations

Alternative sequence2731Missing in isoform 2.
VSP_006034

Experimental info

Mutagenesis1571E → A or K: Reduces guanine exchange factor activity by over 90%. Ref.9
Mutagenesis1871Y → A: Reduces guanine exchange factor activity by over 90%. Ref.9
Mutagenesis1951M → A: Reduces guanine exchange factor activity by over 90%. Ref.9
Sequence conflict353 – 3619TVYRISAPT → MFTGSQLRR in AAF37737. Ref.4
Sequence conflict353 – 3619TVYRISAPT → MFTGSQLRR in AAF37738. Ref.4

Secondary structure

............................ 398
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: 067FEE0FEA7A4C86

FASTA39846,413
        10         20         30         40         50         60 
MEEDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKDE IAEVANEIEN LGSTEERKNM 

        70         80         90        100        110        120 
QRNKQVAMGR KKFNMDPKKG IQFLIENDLL KNTCEDIAQF LYKGEGLNKT AIGDYLGERD 

       130        140        150        160        170        180 
EFNIQVLHAF VELHEFTDLN LVQALRQFLW SFRLPGEAQK IDRMMEAFAQ RYCQCNNGVF 

       190        200        210        220        230        240 
QSTDTCYVLS FAIIMLNTSL HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK 

       250        260        270        280        290        300 
NEPFKIPEDD GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE 

       310        320        330        340        350        360 
PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG NHTVYRISAP 

       370        380        390 
TPEEKEEWIK CIKAAISRDP FYEMLAARKK KVSSTKRH 

« Hide

Isoform 2 [UniParc].

Checksum: CBD984BC348E6B15
Show »

FASTA39746,356

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7."
Liu L., Pohajdak B.
Biochim. Biophys. Acta 1132:75-78(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 and Testis.
[4]"Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors."
Ogasawara M., Kim S.C., Adamik R., Togawa A., Ferrans V.J., Takeda K., Kirby M., Moss J., Vaughan M.
J. Biol. Chem. 275:3221-3230(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-398, FUNCTION, ALTERNATIVE SPLICING.
[5]"Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)."
Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W., Moss J., Vaughan M.
J. Biol. Chem. 275:21331-21339(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM23.
[6]"Cybr, a cytokine-inducible protein that binds cytohesin-1 and regulates its activity."
Tang P., Cheng T.P., Agnello D., Wu C.-Y., Hissong B.D., Watford W.T., Ahn H.-J., Galon J., Moss J., Vaughan M., O'Shea J.J., Gadina M.
Proc. Natl. Acad. Sci. U.S.A. 99:2625-2629(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CYTIP.
[7]"The Arl4 family of small G proteins can recruit the cytohesin Arf6 exchange factors to the plasma membrane."
Hofmann I., Thompson A., Sanderson C.M., Munro S.
Curr. Biol. 17:711-716(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1."
Betz S.F., Schnuchel A., Wang H., Olejniczak E.T., Meadows R.P., Lipsky B.P., Harris E.A., Staunton D.E., Fesik S.W.
Proc. Natl. Acad. Sci. U.S.A. 95:7909-7914(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 58-256, FUNCTION, MUTAGENESIS OF GLU-157; TYR-187 AND MET-195.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M85169 mRNA. Translation: AAA36602.1.
AC022966 Genomic DNA. No translation available.
BC038385 mRNA. Translation: AAH38385.1.
BC050452 mRNA. Translation: AAH50452.1.
AF125362 expand/collapse EMBL AC list , AF125350, AF125351, AF125352, AF125353, AF125354, AF125355, AF125356, AF125357, AF125359, AF125360, AF125361 Genomic DNA. Translation: AAF37737.1.
AF125362 expand/collapse EMBL AC list , AF125350, AF125351, AF125352, AF125353, AF125354, AF125355, AF125356, AF125357, AF125358, AF125359, AF125360, AF125361 Genomic DNA. Translation: AAF37738.1.
CCDSCCDS32754.1. [Q15438-2]
CCDS42392.2. [Q15438-1]
PIRS24168.
RefSeqNP_004753.1. NM_004762.3. [Q15438-1]
NP_059430.2. NM_017456.3. [Q15438-2]
UniGeneHs.191215.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BC9NMR-A58-256[»]
4A4PX-ray2.00A/B63-248[»]
ProteinModelPortalQ15438.
SMRQ15438. Positions 58-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114688. 12 interactions.
IntActQ15438. 2 interactions.
MINTMINT-3031502.
STRING9606.ENSP00000354398.

PTM databases

PhosphoSiteQ15438.

Polymorphism databases

DMDM2498175.

Proteomic databases

MaxQBQ15438.
PaxDbQ15438.
PRIDEQ15438.

Protocols and materials databases

DNASU9267.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361101; ENSP00000354398; ENSG00000108669. [Q15438-1]
ENST00000446868; ENSP00000389095; ENSG00000108669. [Q15438-1]
ENST00000591455; ENSP00000465665; ENSG00000108669. [Q15438-2]
GeneID9267.
KEGGhsa:9267.
UCSCuc002jvw.3. human. [Q15438-2]
uc010wtw.1. human. [Q15438-1]

Organism-specific databases

CTD9267.
GeneCardsGC17M076670.
HGNCHGNC:9501. CYTH1.
HPAHPA047498.
MIM182115. gene.
neXtProtNX_Q15438.
PharmGKBPA164718528.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5307.
HOGENOMHOG000253023.
HOVERGENHBG002647.
OMAVGLHEFT.
OrthoDBEOG7RBZ9C.
PhylomeDBQ15438.
TreeFamTF352091.

Gene expression databases

ArrayExpressQ15438.
BgeeQ15438.
CleanExHS_CYTH1.
GenevestigatorQ15438.

Family and domain databases

Gene3D1.10.1000.11. 1 hit.
2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view]
PfamPF00169. PH. 1 hit.
PF01369. Sec7. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMSSF48425. SSF48425. 1 hit.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50190. SEC7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCYTH1. human.
EvolutionaryTraceQ15438.
GeneWikiCYTH1.
GenomeRNAi9267.
NextBio34739.
PROQ15438.
SOURCESearch...

Entry information

Entry nameCYH1_HUMAN
AccessionPrimary (citable) accession number: Q15438
Secondary accession number(s): A6NFW7, Q9P123, Q9P124
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 136 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM