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Protein

Tip elongation protein 1

Gene

tip1

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

Functioni

Has a role in stabilizing and targeting the growing tips of the microtubules along the long axis of the cell, directing them to the ends of the cell. Acts as a cargo for tea2.2 Publications

GO - Molecular functioni

  • microtubule plus-end binding Source: PomBase

GO - Biological processi

  • ascospore formation Source: PomBase
  • cellular protein localization Source: PomBase
  • establishment of cell polarity Source: PomBase
  • establishment or maintenance of cell polarity regulating cell shape Source: PomBase
  • microtubule cytoskeleton organization Source: PomBase
  • regulation of filamentous growth Source: PomBase
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Tip elongation protein 1
Alternative name(s):
Protein noc1
Gene namesi
Name:tip1
Synonyms:noc1
ORF Names:SPAC3C7.12
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC3C7.12.
PomBaseiSPAC3C7.12. tip1.

Subcellular locationi

GO - Cellular componenti

  • cell cortex of cell tip Source: PomBase
  • cell tip Source: PomBase
  • cytosol Source: PomBase
  • microtubule Source: UniProtKB-KW
  • microtubule cytoskeleton Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Tip elongation protein 1PRO_0000083544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821Phosphoserine1 Publication
Modified residuei84 – 841Phosphoserine1 Publication
Modified residuei289 – 2891Phosphoserine1 Publication
Modified residuei294 – 2941Phosphoserine1 Publication
Modified residuei305 – 3051Phosphoserine1 Publication
Modified residuei367 – 3671Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP79065.

PTM databases

iPTMnetiP79065.

Interactioni

Subunit structurei

Monomer. Interacts with tea1 and tea2. Interacts with tea4 in the presence of tea1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
peg1O428744EBI-1102463,EBI-1112382
tea1P870614EBI-1102463,EBI-875376
tea2Q1MTQ14EBI-1102463,EBI-1107767

GO - Molecular functioni

  • microtubule plus-end binding Source: PomBase

Protein-protein interaction databases

BioGridi279479. 108 interactions.
DIPiDIP-35371N.
IntActiP79065. 8 interactions.
MINTiMINT-4692021.

Structurei

3D structure databases

ProteinModelPortaliP79065.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 6948CAP-GlyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili134 – 418285Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi77 – 11943Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 CAP-Gly domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

InParanoidiP79065.
OMAiPYENDIF.
OrthoDBiEOG7HF1VC.
PhylomeDBiP79065.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
[Graphical view]
PfamiPF01302. CAP_GLY. 1 hit.
[Graphical view]
SMARTiSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMiSSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P79065-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPLGSVVEV ITGERGFVRY AGEVENRKGV YVGLELLPEF AEFGKNRGVV
60 70 80 90 100
DGREYFKTKN NEKTGIFVPF DKCKLASSIS SSPSPKIDGT AASIGMGFPP
110 120 130 140 150
MSPNLQSSIP RLTNVSSSSN LSMNTISSTA LTPTEKILQK RIEDLLYERQ
160 170 180 190 200
NHQQQLEEVL ATVDQLQSLV TNFNDQQDEV DELRERITLK EERIQQMRNE
210 220 230 240 250
ASQRRFEFKT TIECLEESSN RAIETYENRI AELEAQLEMY MSGKSEDDLL
260 270 280 290 300
FSLQQERDYA LNQVEILQER VDTLMKQKAN SSTANEKLSH MESSSPTLTN
310 320 330 340 350
ASFESPKRGK GSNDLPENHP QRRQTLEFYE IEIEVLREKV EKLQALSDEK
360 370 380 390 400
DFYISKLEKS LDRNDTTPVP SDEKLSNYAA EKENLVSRIS ELEHTIEQLT
410 420 430 440 450
INNERDNERM SPAEFELETT QEVEENDSDS HDDEETWCEV CETNNHSLQE
460
CPTVFGSTDE A
Length:461
Mass (Da):52,607
Last modified:May 1, 1997 - v1
Checksum:i66CCDB96146F86D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59915 mRNA. Translation: AAC33366.1.
CU329670 Genomic DNA. Translation: CAB16742.1.
PIRiT38698.
RefSeqiNP_593613.1. NM_001019044.2.

Genome annotation databases

EnsemblFungiiSPAC3C7.12.1; SPAC3C7.12.1:pep; SPAC3C7.12.
GeneIDi2543044.
KEGGispo:SPAC3C7.12.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59915 mRNA. Translation: AAC33366.1.
CU329670 Genomic DNA. Translation: CAB16742.1.
PIRiT38698.
RefSeqiNP_593613.1. NM_001019044.2.

3D structure databases

ProteinModelPortaliP79065.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279479. 108 interactions.
DIPiDIP-35371N.
IntActiP79065. 8 interactions.
MINTiMINT-4692021.

PTM databases

iPTMnetiP79065.

Proteomic databases

MaxQBiP79065.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC3C7.12.1; SPAC3C7.12.1:pep; SPAC3C7.12.
GeneIDi2543044.
KEGGispo:SPAC3C7.12.

Organism-specific databases

EuPathDBiFungiDB:SPAC3C7.12.
PomBaseiSPAC3C7.12. tip1.

Phylogenomic databases

InParanoidiP79065.
OMAiPYENDIF.
OrthoDBiEOG7HF1VC.
PhylomeDBiP79065.

Miscellaneous databases

PROiP79065.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
[Graphical view]
PfamiPF01302. CAP_GLY. 1 hit.
[Graphical view]
SMARTiSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMiSSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A Schizosaccharomyces pombe gene encoding a novel polypeptide with a predicted alpha-helical rod structure found in the myosin and intermediate-filament families of proteins."
    Jannatipour M., Rokeach L.A.
    Biochim. Biophys. Acta 1399:67-72(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
  2. "CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast."
    Brunner D., Nurse P.
    Cell 102:695-704(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
  3. "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.
  4. "Tea2p kinesin is involved in spatial microtubule organization by transporting tip1p on microtubules."
    Busch K.E., Hayles J., Nurse P., Brunner D.
    Dev. Cell 6:831-843(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TEA2, SUBCELLULAR LOCATION.
  5. "Tea4p links microtubule plus ends with the formin for3p in the establishment of cell polarity."
    Martin S.G., McDonald W.H., Yates J.R. III, Chang F.
    Dev. Cell 8:479-491(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TEA1 AND TEA4.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-289; SER-294; SER-305 AND THR-367, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTIP1_SCHPO
AccessioniPrimary (citable) accession number: P79065
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 119 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.