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Protein

Cytoskeletal protein syp1

Gene

syp1

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

Multi-functional protein that contributes to the endocytic process, but also to events that occur at the neck during cytokinesis. Plays a role as an endocytic adapters with membrane-tubulation activity that associates with transmembrane cargo proteins and initiates the formation of endocytic sites. Contributes to the stabilization of the nascent clathrin-coated pit. Plays also a role in late endocytosis by mediating vesiculation. Involved in the regulation of cell cycle-dependent dynamics of the septin cytoskeleton by promoting septin turnover in different cell cycle stages (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoskeletal protein syp1
Gene namesi
Name:syp1
ORF Names:SPBC4C3.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC4C3.06.
PomBaseiSPBC4C3.06. syp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 818818Cytoskeletal protein syp1PRO_0000303951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei463 – 4631Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43059.

PTM databases

iPTMnetiO43059.

Interactioni

Subunit structurei

Interacts with dil1.1 Publication

Protein-protein interaction databases

BioGridi277379. 7 interactions.
MINTiMINT-4674979.

Structurei

3D structure databases

ProteinModelPortaliO43059.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 269263F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini551 – 807257MHDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the SYP1 family.Curated
Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

InParanoidiO43059.
KOiK20042.
OrthoDBiEOG76HQ90.
PhylomeDBiO43059.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF10291. muHD. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
[Graphical view]
PROSITEiPS51741. F_BAR. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43059-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESLTKTEYV DAFLSNYSPN DSMSIFRQRL EQVRLDNDML SQWIRERMDI
60 70 80 90 100
ERQYSDQLHK LAMNMQEKNN SSFAFNYAWK QLEGETLEIS RYHSQIIGQI
110 120 130 140 150
ASQVYKPLID YYTSSPQTAT LRRLAERLST VAEEMASSSV PGLKGLKKKG
160 170 180 190 200
RDADTKSQND LTASRATWDS DAPLAFEKLQ IVDEERLLIL KQVYLTIASL
210 220 230 240 250
ETDTALKQQE FFSKSMAVYS DLPIEGEIRQ FMNSTSKVMS SASANKPSKS
260 270 280 290 300
SGFHINNGKS KEEKSHGENE SGGKLKNKMS TLFRRKTIMP KKDKKPSHKS
310 320 330 340 350
NGRPNKLTAF FNKNSKASSI SSAEEHPSNI DDSSIERRHY DSNHSSQIRD
360 370 380 390 400
HPSTNNNASS YQNFNETSDE GEDNDATIRA NNVRSSFLEA PLPVQPNVQA
410 420 430 440 450
ETVTPKISSK ASPFNKPNSV HSEASRNTPS SIDRENASHS NPIMMHGNDF
460 470 480 490 500
GGNFNNMQSR STTTSPTSAV ASPAPTENED SNAAIERVAN TLRKNPTISR
510 520 530 540 550
RTRRAGTMDR YATASSDYME SNLGSLPNLS TLSLQSGPDS TATWHPEFPN
560 570 580 590 600
SSGLSASIVE KYSGELSEDG LLHPSCSGHI FMKYTSDFNT PPPEMGVRVA
610 620 630 640 650
SEFPMSFTHL NDHAVKYGPS ENTLSLIPEL LLSPIKVTDF NLHLDSINGA
660 670 680 690 700
SCIPLTVVQK WKHDESSSSM IAFVKPNPVW RNLGSSLHIE KLVIIVYLGE
710 720 730 740 750
NVLVKSCQSS PAGEFSRKTS KLKLHLSNIN ISSSGFKILA KFAISPSAAI
760 770 780 790 800
RKPVIEFRIR MVDSSNNPGL TKLFLKPDMF DTTSSSGGSQ LESAYEETKV
810
PTSYGIHVRE CSVFADMS
Length:818
Mass (Da):90,757
Last modified:June 1, 1998 - v1
Checksum:iA4B658DC2CACBC36
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA16828.1.
PIRiT40491.
RefSeqiNP_596299.1. NM_001022220.2.

Genome annotation databases

EnsemblFungiiSPBC4C3.06.1; SPBC4C3.06.1:pep; SPBC4C3.06.
GeneIDi2540862.
KEGGispo:SPBC4C3.06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA16828.1.
PIRiT40491.
RefSeqiNP_596299.1. NM_001022220.2.

3D structure databases

ProteinModelPortaliO43059.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277379. 7 interactions.
MINTiMINT-4674979.

PTM databases

iPTMnetiO43059.

Proteomic databases

MaxQBiO43059.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC4C3.06.1; SPBC4C3.06.1:pep; SPBC4C3.06.
GeneIDi2540862.
KEGGispo:SPBC4C3.06.

Organism-specific databases

EuPathDBiFungiDB:SPBC4C3.06.
PomBaseiSPBC4C3.06. syp1.

Phylogenomic databases

InParanoidiO43059.
KOiK20042.
OrthoDBiEOG76HQ90.
PhylomeDBiO43059.

Miscellaneous databases

PROiO43059.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF10291. muHD. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
[Graphical view]
PROSITEiPS51741. F_BAR. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "High-throughput knockout screen in Schizosaccharomyces pombe identifies a novel gene required for efficient homolog disjunction during meiosis I."
    Rumpf C., Cipak L., Novatchkova M., Li Z., Polakova S., Dudas A., Kovacikova I., Miadokova E., Ammerer G., Gregan J.
    Cell Cycle 9:1802-1808(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DIL1.

Entry informationi

Entry nameiSYP1_SCHPO
AccessioniPrimary (citable) accession number: O43059
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 93 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

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.