Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Septation protein imp2

Gene

imp2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Required for normal septation. Involved in the disassembly of the medial ring during septation.1 Publication

GO - Biological processi

  • mitotic actomyosin contractile ring assembly Source: PomBase
  • mitotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Septation protein imp2
Gene namesi
Name:imp2
ORF Names:SPBC11C11.02
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC11C11.02.
PomBaseiSPBC11C11.02.

Subcellular locationi

  • Cytoplasmcytoskeleton 1 Publication

  • Note: Associates with the medial ring during septation.

GO - Cellular componenti

  • actomyosin contractile ring Source: PomBase
  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 670670Septation protein imp2PRO_0000084186Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei397 – 3971Phosphoserine1 Publication
Modified residuei503 – 5031Phosphoserine1 Publication
Modified residuei531 – 5311Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ10199.

Interactioni

Protein-protein interaction databases

BioGridi276649. 19 interactions.
MINTiMINT-4697729.
STRINGi4896.SPBC11C11.02-1.

Structurei

3D structure databases

ProteinModelPortaliQ10199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 269254F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini607 – 67064SH3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG303711.
InParanoidiQ10199.
OMAiFAKSWNS.
OrthoDBiEOG7F7WKS.
PhylomeDBiQ10199.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10199-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQQLSFNAS SAKPDKSFSN YFWGANDEGY HALLSRFSDV KHINEELRSF
60 70 80 90 100
YHERANIEED YAKRMAKLSR TTFSSLETGC LKESVQVMKA EVDNMAKSHL
110 120 130 140 150
QISQLLQDDV ENAFTRYAAS LKDKKKMIVS GIEKVHKDKL SKHQALVKAQ
160 170 180 190 200
DKYHYLCKKV NYYVSQQNML FGKELEKNNA KLNKTQNAIT ASSSDYQSAV
210 220 230 240 250
AAVRDSYARW TNEWRSTCDK LQDIEEERRH FLKSVMWTFT LLISRSCFND
260 270 280 290 300
DQACERIRKN LEQCSVSQDV LEFIDAKSTG TGIPQPPKFY DYYKGEVPDD
310 320 330 340 350
SVELVQANFQ RAQTKIENDN MPLNRPYVLS ATARNESSFE NTLPNTPSAI
360 370 380 390 400
QSLTTVSSNS SQNGRSSPKK SFLSKFKLTS RPSTPNVGNT APDALSSPRN
410 420 430 440 450
DSPLTSAADE QMKHLSLQEE PKQNPTPAAP GAFPNSNTLP PRYNELGSLP
460 470 480 490 500
SPNSVSFTED SRPNVNTPSR RQQIQEEFGS VLQMENRAVS PVYDSRKNGS
510 520 530 540 550
RSSFTLRKSR SPKRPSSSLS QNASRLPRSL TPGNLEPNYD FGVRVDPASG
560 570 580 590 600
TAPTDDEPYT DRDSSFVDDT INTKATGNTS NRLSLPAYPT DGGDTSIDNP
610 620 630 640 650
TSTDGQRILG YVSALYDYDA AIPEEISFRK GDTIAVLKLY EDGWWEGFVV
660 670
GEDDHNRGQF PSNFVREIEV
Length:670
Mass (Da):75,167
Last modified:October 1, 1996 - v1
Checksum:i03551FBB56FC91AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20684.1.
PIRiT39317. S67383.
RefSeqiNP_596391.1. NM_001022312.2.

Genome annotation databases

EnsemblFungiiSPBC11C11.02.1; SPBC11C11.02.1:pep; SPBC11C11.02.
GeneIDi2540112.
KEGGispo:SPBC11C11.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20684.1.
PIRiT39317. S67383.
RefSeqiNP_596391.1. NM_001022312.2.

3D structure databases

ProteinModelPortaliQ10199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276649. 19 interactions.
MINTiMINT-4697729.
STRINGi4896.SPBC11C11.02-1.

Proteomic databases

MaxQBiQ10199.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC11C11.02.1; SPBC11C11.02.1:pep; SPBC11C11.02.
GeneIDi2540112.
KEGGispo:SPBC11C11.02.

Organism-specific databases

EuPathDBiFungiDB:SPBC11C11.02.
PomBaseiSPBC11C11.02.

Phylogenomic databases

eggNOGiNOG303711.
InParanoidiQ10199.
OMAiFAKSWNS.
OrthoDBiEOG7F7WKS.
PhylomeDBiQ10199.

Miscellaneous databases

NextBioi20801248.
PROiQ10199.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "imp2, a new component of the actin ring in the fission yeast Schizosaccharomyces pombe."
    Demeter J., Sazer S.
    J. Cell Biol. 143:415-427(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-503 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiIMP2_SCHPO
AccessioniPrimary (citable) accession number: Q10199
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 27, 2015
This is version 105 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.