Reviewed, UniProtKB/Swiss-Prot Q10235 (ALP11_SCHPO)

Names and origin

Protein names

Recommended name:
    Cell polarity protein alp11
Alternative name(s):
    Altered polarity protein 11

Gene names

Name:	alp11
ORF Names:	SPAC13D6.05, SPAC4G9.01

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for microtubule function and cell polarity. Involved in the proper folding of alpha-tubulin.
Subunit structure	Binds to monomeric alpha-tubulin. Interacts with alp21.
Subcellular location	Cytoplasm › cytoskeleton.
Sequence similarities	Belongs to the TBCB family. Contains 1 CAP-Gly domain. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	alpha-tubulin folding Ref.1 Traceable author statement. Source: GeneDB_SPombe post-chaperonin tubulin folding pathway Non-traceable author statement. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	alpha-tubulin binding Ref.1 Inferred from physical interaction. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 234	234	Cell polarity protein alp11		PRO_0000083512
Regions
	Domain	4 – 88	85	Ubiquitin-like
	Domain	174 – 216	43	CAP-Gly
Amino acid modifications
	Modified residue	213	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	Q10235-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 7E4D8B5C3D9D5981	FASTA	234	26,672
	10 20 30 40 50 60 MNEITLFIKS SSANAERRIN PQWTVSQLKT KLVPIVGTPE QYQKLTYEPA SSTVPGHVFT 70 80 90 100 110 120 SEEENLDLGE FKLQPLGTIV VEDTRPPHLR LDFDDLSQVD KYVMPREQYE NRTDSVYAWK 130 140 150 160 170 180 KRNQLGRFNP DFEASKASRQ ESLKRELVDL QKNLNSRCCA AGERYGTIRY IGLVPEINND 190 200 210 220 230 NLWVGVEFDE PVGKNDGTVS GKRYFNAKNK HGSFLRSSEV EVGDFPPEDI LEGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterisation of fission yeast alp11 mutants defines three functional domains within tubulin-folding cofactor B." Radcliffe P.A., Toda T. Mol. Gen. Genet. 263:752-760(2000) [PubMed: 10905343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast." Radcliffe P.A., Hirata D., Vardy L., Toda T. Mol. Biol. Cell 10:2987-3001(1999) [PubMed: 10473641] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH ALPHA-TUBULIN AND ALP21, 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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB008750 Genomic DNA. Translation: BAA23375.1. CU329670 Genomic DNA. Translation: CAB59431.1.
PIR	T43283.
RefSeq	NP_593683.2.
3D structure databases
HSSP	HSSP built from PDB template 1LPL based on UniProtKB Q20728.
ModBase	Search...
Genome annotation databases
GeneID	2542814.
KEGG	spo:SPAC13D6.05.
Organism-specific databases
GeneDB_Spombe	SPAC13D6.05.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001940-MON.
Gene expression databases
ArrayExpress	Q10235.
Family and domain databases
InterPro	IPR000938. Cytoskel-assoc-prot_CAP-Gly. IPR000626. Ubiquitin. [Graphical view]
Pfam	PF01302. CAP_GLY. 1 hit. [Graphical view]
SMART	SM00213. UBQ. 1 hit. [Graphical view]
PROSITE	PS00845. CAP_GLY_1. 1 hit. PS50245. CAP_GLY_2. 1 hit. PS50053. UBIQUITIN_2. 1 hit. [Graphical view]
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

ALP11_SCHPO

Accession

Primary (citable) accession number: Q10235
Secondary accession number(s): Q9UTM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	July 22, 2008
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)