HOB1_SCHPO
ID HOB1_SCHPO Reviewed; 466 AA.
AC O74352;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein hob1;
DE AltName: Full=Homolog of Bin1;
GN Name=hob1; ORFNames=SPBC21D10.12;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12569356; DOI=10.1038/sj.onc.1206162;
RA Routhier E.L., Donover P.S., Prendergast G.C.;
RT "hob1+, the fission yeast homolog of Bin1, is dispensable for endocytosis
RT or actin organization, but required for the response to starvation or
RT genotoxic stress.";
RL Oncogene 22:637-648(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-299; SER-301 AND
RP SER-303, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in DNA damage signaling as a part of stress
CC response processes. {ECO:0000269|PubMed:12569356}.
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DR EMBL; AF275637; AAF86458.1; -; mRNA.
DR EMBL; CU329671; CAA20768.1; -; Genomic_DNA.
DR PIR; T11684; T11684.
DR RefSeq; NP_596001.1; NM_001021909.2.
DR AlphaFoldDB; O74352; -.
DR SMR; O74352; -.
DR BioGRID; 277159; 13.
DR STRING; 4896.SPBC21D10.12.1; -.
DR iPTMnet; O74352; -.
DR MaxQB; O74352; -.
DR PaxDb; O74352; -.
DR PRIDE; O74352; -.
DR EnsemblFungi; SPBC21D10.12.1; SPBC21D10.12.1:pep; SPBC21D10.12.
DR GeneID; 2540633; -.
DR KEGG; spo:SPBC21D10.12; -.
DR PomBase; SPBC21D10.12; hob1.
DR VEuPathDB; FungiDB:SPBC21D10.12; -.
DR eggNOG; KOG3771; Eukaryota.
DR HOGENOM; CLU_025518_0_1_1; -.
DR InParanoid; O74352; -.
DR OMA; AEIYKPI; -.
DR PhylomeDB; O74352; -.
DR PRO; PR:O74352; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:1990528; C:Rvs161p-Rvs167p complex; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISM:PomBase.
DR GO; GO:0051666; P:actin cortical patch localization; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:PomBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IGI:PomBase.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..466
FT /note="Protein hob1"
FT /id="PRO_0000192954"
FT DOMAIN 17..269
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 407..466
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 280..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 31..67
FT /evidence="ECO:0000255"
FT COILED 177..204
FT /evidence="ECO:0000255"
FT COMPBIAS 293..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 466 AA; 51392 MW; 441793950D6C2C7E CRC64;
MSWKGFTKAL ARTPQTLRSK FNVGEITKDP IYEDAGRRFK SLETEAKKLA EDAKKYTDAI
NGLLNHQIGF ADACIEIYKP ISGRASDPES YEQEGNAEGI EAAEAYKEIV YDLQKNLASE
MDVINTRIVN PTGELLKIVK DVDKLLLKRD HKQLDYDRHR SSFKKLQEKK DKSLKDEKKL
YEAETAFEQS SQEYEYYNEM LKEELPKLFA LAQSFIAPLF QGFYYMQLNV YYVLYEKMSH
CEIQYFDFNT DILESYERRR GDVKDRAEAL TITKFKTAKP TYKRPGMGPG GKDATASSSS
SFSSKREEAA AEPSSSTATD IPPPYSTPSV AGASDYSTPS AGYQTVQTTT TTTEAAAAQY
PQAAFPPPPV MPQPAAAAVT TPVAAPVAAA AAAVPVPPPA PAPAAAPAAE HVVALYDYAA
QAAGDLSFHA GDRIEVVSRT DNQNEWWIGR LNGAQGQFPG NYVQLE
