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P53901

- INN1_YEAST

UniProt

P53901 - INN1_YEAST

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Protein

Ingression protein 1

Gene

INN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Required for the ingression of the plasma membrane into the bud neck at the end of cytokinesis, leading to the separation of the mother and daughter cells. Stimulates the synthesis of the primary septum (PS) by CHS2.3 Publications

GO - Molecular functioni

  1. enzyme regulator activity Source: SGD
  2. phospholipid binding Source: SGD

GO - Biological processi

  1. barrier septum assembly Source: SGD
  2. chromosome organization Source: SGD
  3. mitotic cytokinesis Source: SGD
  4. mitotic nuclear division Source: UniProtKB-KW
  5. regulation of catalytic activity Source: GOC
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

BioCyciYEAST:G3O-33169-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ingression protein 1
Gene namesi
Name:INN1
Ordered Locus Names:YNL152W
ORF Names:N1765
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNL152w.
SGDiS000005096. INN1.

Subcellular locationi

Bud neck 4 Publications
Note: Localizes at the contractile actinomyosin ring at the end of cytokinesis. Recruitment to the bud neck requires either CYK2 or CYK3.

GO - Cellular componenti

  1. cellular bud neck contractile ring Source: SGD
  2. HICS complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi28 – 281K → A: Impairs plasma membrane ingression; when associated with A-31. 1 Publication
Mutagenesisi31 – 311K → A: Impairs plasma membrane ingression; when associated with A-28. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409Ingression protein 1PRO_0000203419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei392 – 3921Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53901.
PaxDbiP53901.
PeptideAtlasiP53901.

Expressioni

Gene expression databases

GenevestigatoriP53901.

Interactioni

Subunit structurei

Interacts with CYK2, CYK3 and IQG1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HOF1Q050805EBI-28955,EBI-5412
PEX13P806672EBI-28955,EBI-13206

Protein-protein interaction databases

BioGridi35677. 20 interactions.
DIPiDIP-4339N.
IntActiP53901. 9 interactions.
MINTiMINT-496500.
STRINGi4932.YNL152W.

Structurei

3D structure databases

ProteinModelPortaliP53901.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 134134C2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi303 – 3108Poly-Asp

Domaini

The C2 domain is essential for membrane ingression during cytokinesis, but not for recruitment to the actomyosin ring.1 Publication

Sequence similaritiesi

Belongs to the INN1/fic1 family.Curated
Contains 1 C2 domain.Curated

Phylogenomic databases

eggNOGiNOG305949.
HOGENOMiHOG000142049.
InParanoidiP53901.
OMAiINIFKNP.
OrthoDBiEOG7P5TC4.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.

Sequencei

Sequence statusi: Complete.

P53901-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEEVWNGNQ GILSVYVSKA RDLPNLNKLD KQNVMLRLRI AHMTRASNTL
60 70 80 90 100
HRAGQNPVFH YLEKFDITPE IKPLMYVEVY CDRRKKSPLP IGRCEIDLLN
110 120 130 140 150
AIRADPKEGY CTWYELKRSG DEFAGTIFIE LTFTPKVPRL NRDDLNKEMD
160 170 180 190 200
RLDSSMAMRP IPPLPTESEY DYVHGSTMRQ ITPQCVSTSH EDKDEGQPYR
210 220 230 240 250
NGNVFSMSSK SDTAVLANSN DPIILPPTFS ASMGTTSTLE TNDTAISNTS
260 270 280 290 300
NTKFHFANLR KLKEKINIFK NPDSSTNNCQ NESNKVDIEA LQKAIGVTSL
310 320 330 340 350
SYDEDDDDDD ENDAFYSSSH RVSHNYNQPP LPPIPTRDDM SNYSSSRNTP
360 370 380 390 400
LVRRDRPSRL DSSSPNSHPH PSGLNSPKLP PLPTTSNSNF NSRKNSMSPT

RKRPPPRLS
Length:409
Mass (Da):46,226
Last modified:October 1, 1996 - v1
Checksum:i66C2B81D21CE5520
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti221 – 2211D → G in AAS56352. (PubMed:9169873)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92517 Genomic DNA. Translation: CAA63287.1.
Z71428 Genomic DNA. Translation: CAA96039.1.
AY558026 Genomic DNA. Translation: AAS56352.1.
BK006947 Genomic DNA. Translation: DAA10397.1.
PIRiS60975.
RefSeqiNP_014247.1. NM_001182990.1.

Genome annotation databases

EnsemblFungiiYNL152W; YNL152W; YNL152W.
GeneIDi855570.
KEGGisce:YNL152W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92517 Genomic DNA. Translation: CAA63287.1 .
Z71428 Genomic DNA. Translation: CAA96039.1 .
AY558026 Genomic DNA. Translation: AAS56352.1 .
BK006947 Genomic DNA. Translation: DAA10397.1 .
PIRi S60975.
RefSeqi NP_014247.1. NM_001182990.1.

3D structure databases

ProteinModelPortali P53901.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35677. 20 interactions.
DIPi DIP-4339N.
IntActi P53901. 9 interactions.
MINTi MINT-496500.
STRINGi 4932.YNL152W.

Proteomic databases

MaxQBi P53901.
PaxDbi P53901.
PeptideAtlasi P53901.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YNL152W ; YNL152W ; YNL152W .
GeneIDi 855570.
KEGGi sce:YNL152W.

Organism-specific databases

CYGDi YNL152w.
SGDi S000005096. INN1.

Phylogenomic databases

eggNOGi NOG305949.
HOGENOMi HOG000142049.
InParanoidi P53901.
OMAi INIFKNP.
OrthoDBi EOG7P5TC4.

Enzyme and pathway databases

BioCyci YEAST:G3O-33169-MONOMER.

Miscellaneous databases

NextBioi 979682.

Gene expression databases

Genevestigatori P53901.

Family and domain databases

Gene3Di 2.60.40.150. 1 hit.
InterProi IPR000008. C2_dom.
[Graphical view ]
Pfami PF00168. C2. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24 complete open reading frames: 18 correspond to new genes, one of which encodes a protein similar to the human myotonic dystrophy kinase."
    Nasr F., Becam A.-M., Herbert C.J.
    Yeast 12:169-175(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Inn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast."
    Sanchez-Diaz A., Marchesi V., Murray S., Jones R., Pereira G., Edmondson R., Allen T., Labib K.
    Nat. Cell Biol. 10:395-406(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH CYK2 AND IQG1, MUTAGENESIS OF LYS-28 AND LYS-31.
  6. "Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae."
    Nishihama R., Schreiter J.H., Onishi M., Vallen E.A., Hanna J., Moravcevic K., Lippincott M.F., Han H., Lemmon M.A., Pringle J.R., Bi E.
    J. Cell Biol. 185:995-1012(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CYK2 AND CYK3.
  7. "Cyk3 acts in actomyosin ring independent cytokinesis by recruiting Inn1 to the yeast bud neck."
    Jendretzki A., Ciklic I., Rodicio R., Schmitz H.P., Heinisch J.J.
    Mol. Genet. Genomics 282:437-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CYK3.
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Targeted localization of Inn1, Cyk3 and Chs2 by the mitotic-exit network regulates cytokinesis in budding yeast."
    Meitinger F., Petrova B., Lombardi I.M., Bertazzi D.T., Hub B., Zentgraf H., Pereira G.
    J. Cell Sci. 123:1851-1861(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiINN1_YEAST
AccessioniPrimary (citable) accession number: P53901
Secondary accession number(s): D6W131, Q6Q5J6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3