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Q8IYI6

- EXOC8_HUMAN

UniProt

Q8IYI6 - EXOC8_HUMAN

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Protein
Exocyst complex component 8
Gene
EXOC8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. cellular protein localization Source: Ensembl
  2. cellular protein metabolic process Source: Reactome
  3. exocytosis Source: UniProtKB-KW
  4. membrane organization Source: Reactome
  5. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_15550. Insulin processing.

Names & Taxonomyi

Protein namesi
Recommended name:
Exocyst complex component 8
Alternative name(s):
Exocyst complex 84 kDa subunit
Gene namesi
Name:EXOC8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:24659. EXOC8.

Subcellular locationi

Cytoplasm. Cell projectiongrowth cone By similarity
Note: Redistributes to growing neurites and growth cones during cell differentiation By similarity. Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. exocyst Source: Ensembl
  3. growth cone Source: UniProtKB-SubCell
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134991382.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Exocyst complex component 8
PRO_0000227550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei142 – 1421Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8IYI6.
PaxDbiQ8IYI6.
PRIDEiQ8IYI6.

PTM databases

PhosphoSiteiQ8IYI6.

Expressioni

Gene expression databases

BgeeiQ8IYI6.
CleanExiHS_EXOC8.
GenevestigatoriQ8IYI6.

Organism-specific databases

HPAiHPA027438.

Interactioni

Subunit structurei

The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with the GTP-bound forms of RALA and RALB via its PH domain.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BECN1Q144574EBI-742102,EBI-949378
USHBP1Q8N6Y02EBI-742102,EBI-739895
WASH1A8K0Z33EBI-742102,EBI-6160405

Protein-protein interaction databases

BioGridi127206. 32 interactions.
IntActiQ8IYI6. 22 interactions.
MINTiMINT-1449731.
STRINGi9606.ENSP00000353564.

Structurei

3D structure databases

ProteinModelPortaliQ8IYI6.
SMRiQ8IYI6. Positions 180-292.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini182 – 282101PH
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi108 – 11710Poly-Ala
Compositional biasi316 – 3194Poly-Glu

Sequence similaritiesi

Belongs to the EXO84 family.
Contains 1 PH domain.

Phylogenomic databases

eggNOGiNOG331886.
HOGENOMiHOG000006737.
HOVERGENiHBG081489.
InParanoidiQ8IYI6.
OMAiRNFEQYT.
OrthoDBiEOG7NSB1Q.
PhylomeDBiQ8IYI6.
TreeFamiTF105819.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR016159. Cullin_repeat-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF74788. SSF74788. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8IYI6-1 [UniParc]FASTAAdd to Basket

« Hide

MAMAMSDSGA SRLRRQLESG GFEARLYVKQ LSQQSDGDRD LQEHRQRIQA    50
LAEETAQNLK RNVYQNYRQF IETAREISYL ESEMYQLSHL LTEQKSSLES 100
IPLTLLPAAA AAGAAAASGG EEGVGGAGGR DHLRGQAGFF STPGGASRDG 150
SGPGEEGKQR TLTTLLEKVE GCRHLLETPG QYLVYNGDLV EYDADHMAQL 200
QRVHGFLMND CLLVATWLPQ RRGMYRYNAL YSLDGLAVVN VKDNPPMKDM 250
FKLLMFPESR IFQAENAKIK REWLEVLEDT KRALSEKRRR EQEEAAAPRG 300
PPQVTSKATN PFEDDEEEEP AVPEVEEEKV DLSMEWIQEL PEDLDVCIAQ 350
RDFEGAVDLL DKLNHYLEDK PSPPPVKELR AKVEERVRQL TEVLVFELSP 400
DRSLRGGPKA TRRAVSQLIR LGQCTKACEL FLRNRAAAVH TAIRQLRIEG 450
ATLLYIHKLC HVFFTSLLET AREFEIDFAG TDSGCYSAFV VWARSAMGMF 500
VDAFSKQVFD SKESLSTAAE CVKVAKEHCQ QLGDIGLDLT FIIHALLVKD 550
IQGALHSYKE IIIEATKHRN SEEMWRRMNL MTPEALGKLK EEMKSCGVSN 600
FEQYTGDDCW VNLSYTVVAF TKQTMGFLEE ALKLYFPELH MVLLESLVEI 650
ILVAVQHVDY SLRCEQDPEK KAFIRQNASF LYETVLPVVE KRFEEGVGKP 700
AKQLQDLRNA SRLIRVNPES TTSVV 725
Length:725
Mass (Da):81,799
Last modified:July 5, 2004 - v2
Checksum:iF4E5E344EF24FDCA
GO

Sequence cautioni

The sequence CAI23095.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK096460 mRNA. Translation: BAG53295.1.
AL117352 Genomic DNA. Translation: CAI23095.1. Different initiation.
CH471098 Genomic DNA. Translation: EAW69955.1.
BC035763 mRNA. Translation: AAH35763.2.
CCDSiCCDS1593.1.
RefSeqiNP_787072.2. NM_175876.3.
UniGeneiHs.356198.

Genome annotation databases

EnsembliENST00000360394; ENSP00000353564; ENSG00000116903.
GeneIDi149371.
KEGGihsa:149371.
UCSCiuc001huq.3. human.

Polymorphism databases

DMDMi74750763.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK096460 mRNA. Translation: BAG53295.1 .
AL117352 Genomic DNA. Translation: CAI23095.1 . Different initiation.
CH471098 Genomic DNA. Translation: EAW69955.1 .
BC035763 mRNA. Translation: AAH35763.2 .
CCDSi CCDS1593.1.
RefSeqi NP_787072.2. NM_175876.3.
UniGenei Hs.356198.

3D structure databases

ProteinModelPortali Q8IYI6.
SMRi Q8IYI6. Positions 180-292.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127206. 32 interactions.
IntActi Q8IYI6. 22 interactions.
MINTi MINT-1449731.
STRINGi 9606.ENSP00000353564.

PTM databases

PhosphoSitei Q8IYI6.

Polymorphism databases

DMDMi 74750763.

Proteomic databases

MaxQBi Q8IYI6.
PaxDbi Q8IYI6.
PRIDEi Q8IYI6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360394 ; ENSP00000353564 ; ENSG00000116903 .
GeneIDi 149371.
KEGGi hsa:149371.
UCSCi uc001huq.3. human.

Organism-specific databases

CTDi 149371.
GeneCardsi GC01M231469.
HGNCi HGNC:24659. EXOC8.
HPAi HPA027438.
MIMi 615283. gene.
neXtProti NX_Q8IYI6.
PharmGKBi PA134991382.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG331886.
HOGENOMi HOG000006737.
HOVERGENi HBG081489.
InParanoidi Q8IYI6.
OMAi RNFEQYT.
OrthoDBi EOG7NSB1Q.
PhylomeDBi Q8IYI6.
TreeFami TF105819.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_15550. Insulin processing.

Miscellaneous databases

GeneWikii EXOC8.
GenomeRNAii 149371.
NextBioi 86129.
PROi Q8IYI6.
SOURCEi Search...

Gene expression databases

Bgeei Q8IYI6.
CleanExi HS_EXOC8.
Genevestigatori Q8IYI6.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR016159. Cullin_repeat-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
[Graphical view ]
SUPFAMi SSF74788. SSF74788. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: Tongue.
  2. "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].
  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].
    Tissue: Lymph.
  5. "Ral GTPases regulate exocyst assembly through dual subunit interactions."
    Moskalenko S., Tong C., Rosse C., Mirey G., Formstecher E., Daviet L., Camonis J., White M.A.
    J. Biol. Chem. 278:51743-51748(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EXOC2; RALA AND RALB.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEXOC8_HUMAN
AccessioniPrimary (citable) accession number: Q8IYI6
Secondary accession number(s): B3KU33, Q5TE82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 100 of the entry and version 2 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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