NUP60_SCHPO
ID NUP60_SCHPO Reviewed; 736 AA.
AC O74500;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Nucleoporin nup60;
DE AltName: Full=Nuclear pore protein nup60;
GN Name=nup60; ORFNames=SPCC285.13c;
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 [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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-161 AND
RP SER-162, 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: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. Active directional transport is assured by both, a Phe-Gly
CC (FG) repeat affinity gradient for these transport factors across the
CC NPC and a transport cofactor concentration gradient across the nuclear
CC envelope (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. {ECO:0000250|UniProtKB:P39705}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic
CC side {ECO:0000250}.
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DR EMBL; CU329672; CAA20852.1; -; Genomic_DNA.
DR PIR; T41259; T41259.
DR RefSeq; NP_588341.1; NM_001023332.2.
DR AlphaFoldDB; O74500; -.
DR BioGRID; 275382; 108.
DR STRING; 4896.SPCC285.13c.1; -.
DR iPTMnet; O74500; -.
DR MaxQB; O74500; -.
DR PaxDb; O74500; -.
DR PRIDE; O74500; -.
DR EnsemblFungi; SPCC285.13c.1; SPCC285.13c.1:pep; SPCC285.13c.
DR GeneID; 2538801; -.
DR KEGG; spo:SPCC285.13c; -.
DR PomBase; SPCC285.13c; nup60.
DR VEuPathDB; FungiDB:SPCC285.13c; -.
DR eggNOG; ENOG502T5TJ; Eukaryota.
DR HOGENOM; CLU_381375_0_0_1; -.
DR InParanoid; O74500; -.
DR OMA; TMAHAPL; -.
DR PRO; PR:O74500; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0140512; C:mitotic nuclear bridge midzone; IDA:PomBase.
DR GO; GO:0140599; C:mitotic nuclear bridge midzone membrane domain; IDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IEA:InterPro.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISO:PomBase.
DR GO; GO:0008298; P:intracellular mRNA localization; IBA:GO_Central.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IBA:GO_Central.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; ISO:PomBase.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IBA:GO_Central.
DR InterPro; IPR034432; Nup60.
DR PANTHER; PTHR28284; PTHR28284; 1.
PE 1: Evidence at protein level;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..736
FT /note="Nucleoporin nup60"
FT /id="PRO_0000350997"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 736 AA; 80253 MW; DA4D0C3A440ADA0F CRC64;
MSSGPIRTLH KGKAARNRTP YDRIAASKDG NHSNGPQTPS KSIFQRAKEW LTPSSWKKAI
SIFSSPVVNK HEDSFDSKTD EEYLQNVSTT TEDVSMLINT PVTEKYEQEH RDTSAQATPS
IVEQSPNQML ANFFSKKGKT PLNEIEKEGI ISILNKSASP SSSVISPAAS LNRFQTPRAA
AISKRESGVS SEPRARTSSL TPGNTPNSAK QWSAFRSTFS PLREQDQLST ISPNSLLPAQ
RLSYYGPTLS TPYNRRLRHK RHSTTPISLS NSIAPSLSFQ PKKARYESAN VSFNDTSFTN
VPTSSPLHQS TTANHPEKTP SRAAASLLSI LDSKEKNTPS ITAKAGSPQS APSKASYISP
YARPGITTSR RRHDQIRPSS EKSEPEKKEP SAFETLEKSS NVQTYKPSLM PEFLEKASTH
GSFAKQKEGE QTSLSEKTAL SEPENKTPVF SFKAPSATTD KPSPPVSSIF SFNAPSAAST
KPSPAVSSTF SFNAPTTTPS ATSFSIINKE KPARSPNETI DVDLEEEGSG ISAEVEVANE
GEDLQKNATE VKASTSEKPV FRFEAVTDEK NSEVSSSNQA SSSTMISQPN TGFSFGSFNK
PAGQEEKPQQ RSLFSASFTT QKPELPAAKI EPEVQMTNVA IDQRSFEQAE KSPISVSEST
SLVEVEKPSA EGTNEHKQDA TMTLEKTDKQ GSLEEEPFPK FSFTVLPKEN GENLSTMEST
QELPKFSFSV LKEEKN