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Protein

Nucleoporin NUP145

Gene

NUP145

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export. It is also required for normal NPC distribution (probably through interactions with MLP1 and MLP2) and NPC assembly, as well as for normal nuclear envelope organization.9 Publications

GO - Molecular functioni

  • hydrolase activity Source: UniProtKB-KW
  • nucleocytoplasmic transporter activity Source: SGD
  • RNA binding Source: SGD
  • structural constituent of nuclear pore Source: SGD

GO - Biological processi

  • double-strand break repair Source: SGD
  • maintenance of chromatin silencing at telomere Source: SGD
  • NLS-bearing protein import into nucleus Source: SGD
  • nuclear pore distribution Source: SGD
  • poly(A)+ mRNA export from nucleus Source: SGD
  • positive regulation of transcription, DNA-templated Source: SGD
  • posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
  • protein import into nucleus Source: SGD
  • protein targeting to nuclear inner membrane Source: SGD
  • regulation of nucleocytoplasmic transport Source: SGD
  • telomere tethering at nuclear periphery Source: SGD
  • tRNA export from nucleus Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30592-MONOMER.

Protein family/group databases

MEROPSiS59.002.
TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP145 (EC:3.4.21.-)
Alternative name(s):
Nuclear pore protein NUP145
Cleaved into the following 2 chains:
Nucleoporin NUP145N
Short name:
N-NUP145
Nucleoporin NUP145C
Short name:
C-NUP145
Gene namesi
Name:NUP145
Synonyms:RAT10
Ordered Locus Names:YGL092W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL092W.
SGDiS000003060. NUP145.

Subcellular locationi

Nucleoporin NUP145N :

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • nuclear membrane Source: UniProtKB-SubCell
  • nuclear pore Source: SGD
  • nuclear pore central transport channel Source: SGD
  • nuclear pore outer ring Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi604 – 6041H → P: Loss of autocatalytic cleavage; when associated with L-608. 1 Publication
Mutagenesisi605 – 6051F → S: Loss of autocatalytic cleavage; when associated with R-608. 1 Publication
Mutagenesisi606 – 6061S → A: Loss of autocatalytic cleavage. 1 Publication
Mutagenesisi608 – 6081W → L: Loss of autocatalytic cleavage; when associated with P-604. 1 Publication
Mutagenesisi608 – 6081W → R: Loss of autocatalytic cleavage; when associated with F-605. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 605605Nucleoporin NUP145NPRO_0000019927Add
BLAST
Chaini606 – 1317712Nucleoporin NUP145CPRO_0000019928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei273 – 2731PhosphoserineCombined sources
Modified residuei403 – 4031PhosphoserineCombined sources
Modified residuei404 – 4041PhosphoserineCombined sources
Modified residuei414 – 4141PhosphoserineCombined sources
Modified residuei667 – 6671PhosphoserineCombined sources
Modified residuei679 – 6791PhosphoserineCombined sources
Modified residuei689 – 6891PhosphoserineCombined sources
Modified residuei751 – 7511PhosphothreonineCombined sources

Post-translational modificationi

NUP145 is autocatalytically cleaved in NUP145N and NUP145C.1 Publication

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein

Proteomic databases

MaxQBiP49687.

PTM databases

iPTMnetiP49687.

Miscellaneous databases

PMAP-CutDBP49687.

Interactioni

Subunit structurei

The nuclear pore complex (NPC) constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. The 55-60 MDa NPC is composed of at least 31 different subunits: ASM4, CDC31, GLE1, GLE2, NDC1, NIC96, NSP1, NUP1, NUP2, NUP100, NUP116, NUP120, NUP133, NUP145, NUP157, NUP159, NUP170, NUP188, NUP192, NUP42, NUP49, NUP53, NUP57, NUP60, NUP82, NUP84, NUP85, POM152, POM34, SEH1 and SEC1. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP145C is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1). NUP145N may bind homopolymeric RNA and interacts through its FG repeats with karyopherins. Interacts with MLP1 and MLP2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NUP120P357293EBI-11730,EBI-11713
NUP84P528915EBI-11730,EBI-12337
NUP85P466733EBI-11730,EBI-12345
SEC13P557359EBI-11730,EBI-1046596From a different organism.
SEC13Q044918EBI-11730,EBI-16529

Protein-protein interaction databases

BioGridi33159. 49 interactions.
DIPiDIP-2074N.
IntActiP49687. 17 interactions.
MINTiMINT-508825.

Structurei

Secondary structure

1
1317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi454 – 4585Combined sources
Beta strandi461 – 4655Combined sources
Helixi467 – 4715Combined sources
Helixi477 – 4793Combined sources
Beta strandi480 – 4834Combined sources
Beta strandi485 – 4884Combined sources
Turni489 – 4913Combined sources
Beta strandi492 – 4987Combined sources
Helixi503 – 5053Combined sources
Helixi509 – 5135Combined sources
Turni515 – 5173Combined sources
Beta strandi518 – 5214Combined sources
Turni522 – 5243Combined sources
Beta strandi525 – 5284Combined sources
Turni532 – 5343Combined sources
Beta strandi546 – 5527Combined sources
Turni558 – 5603Combined sources
Helixi570 – 58213Combined sources
Beta strandi584 – 5929Combined sources
Turni593 – 5964Combined sources
Beta strandi597 – 6037Combined sources
Turni731 – 7333Combined sources
Helixi738 – 7469Combined sources
Turni747 – 7493Combined sources
Beta strandi757 – 7593Combined sources
Turni761 – 7633Combined sources
Beta strandi765 – 7695Combined sources
Beta strandi772 – 7754Combined sources
Helixi788 – 7914Combined sources
Helixi793 – 8019Combined sources
Beta strandi803 – 8075Combined sources
Beta strandi809 – 8124Combined sources
Beta strandi814 – 8196Combined sources
Helixi823 – 8275Combined sources
Helixi835 – 84612Combined sources
Helixi859 – 88123Combined sources
Helixi883 – 8919Combined sources
Helixi896 – 9049Combined sources
Turni905 – 9073Combined sources
Helixi909 – 91810Combined sources
Helixi922 – 93110Combined sources
Helixi936 – 94813Combined sources
Turni950 – 9523Combined sources
Helixi958 – 96811Combined sources
Beta strandi971 – 9744Combined sources
Helixi979 – 9835Combined sources
Helixi987 – 99610Combined sources
Turni997 – 10026Combined sources
Helixi1005 – 101511Combined sources
Helixi1023 – 103210Combined sources
Helixi1034 – 10363Combined sources
Helixi1037 – 10459Combined sources
Helixi1053 – 106412Combined sources
Helixi1073 – 108917Combined sources
Helixi1093 – 11008Combined sources
Helixi1106 – 111914Combined sources
Helixi1122 – 11243Combined sources
Turni1126 – 11294Combined sources
Helixi1132 – 11354Combined sources
Helixi1140 – 115718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BG0X-ray3.15B/C/F/G731-1158[»]
3BG1X-ray3.00B/C/F/G731-1158[»]
3IKOX-ray3.20B/E/H731-1158[»]
3KEPX-ray1.82A/B442-605[»]
3KESX-ray2.10A/B442-605[»]
4XMMX-ray7.38B680-1317[»]
4XMNX-ray7.60B680-1317[»]
ProteinModelPortaliP49687.
SMRiP49687. Positions 459-605, 736-1317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49687.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati12 – 132FG 1
Repeati39 – 424GLFG 1
Repeati79 – 802FG 2
Repeati89 – 924GLFG 2
Repeati106 – 1072FG 3
Repeati136 – 1394GLFG 3
Repeati154 – 1574GLFG 4
Repeati168 – 1714GLFG 5
Repeati181 – 1844GLFG 6
Repeati193 – 1964GLFG 7; approximate
Repeati206 – 2094GLFG 8
Domaini458 – 605148Peptidase S59PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni398 – 523126Required for autocatalytic cleavageAdd
BLAST
Regioni460 – 604145Nucleoporin RNA-binding motif (NRM)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi369 – 38517Bipartite nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi43 – 145103Asn-richAdd
BLAST
Compositional biasi140 – 1456Poly-Asn

Domaini

Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side: GLFG repeats are especially abundant in NUPs in the central region (lacking a charged environment but are enriched in Ser, Thr, Gln, and Asn).

Sequence similaritiesi

Belongs to the nucleoporin GLFG family.Curated
Contains 1 peptidase S59 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00550000074799.
HOGENOMiHOG000113874.
InParanoidiP49687.
KOiK18720.
OMAiGMEFVTY.
OrthoDBiEOG7Z95VP.

Family and domain databases

Gene3Di3.30.1610.10. 1 hit.
InterProiIPR025574. Nucleoporin_FG_rpt.
IPR021967. Nup96.
IPR007230. Peptidase_S59.
[Graphical view]
PfamiPF04096. Nucleoporin2. 1 hit.
PF13634. Nucleoporin_FG. 3 hits.
PF12110. Nup96. 1 hit.
[Graphical view]
SUPFAMiSSF82215. SSF82215. 1 hit.
PROSITEiPS51434. NUP_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNKSVNSGF TFGNQNTSTP TSTPAQPSSS LQFPQKSTGL FGNVNVNANT
60 70 80 90 100
STPSPSGGLF NANSNANSIS QQPANNSLFG NKPAQPSGGL FGATNNTTSK
110 120 130 140 150
SAGSLFGNNN ATANSTGSTG LFSGSNNIAS STQNGGLFGN SNNNNITSTT
160 170 180 190 200
QNGGLFGKPT TTPAGAGGLF GNSSSTNSTT GLFGSNNTQS STGIFGQKPG
210 220 230 240 250
ASTTGGLFGN NGASFPRSGE TTGTMSTNPY GINISNVPMA VADMPRSITS
260 270 280 290 300
SLSDVNGKSD AEPKPIENRR TYSFSSSVSG NAPLPLASQS SLVSRLSTRL
310 320 330 340 350
KATQKSTSPN EIFSPSYSKP WLNGAGSAPL VDDFFSSKMT SLAPNENSIF
360 370 380 390 400
PQNGFNFLSS QRADLTELRK LKIDSNRSAA KKLKLLSGTP AITKKHMQDE
410 420 430 440 450
QDSSENEPIA NADSVTNIDR KENRDNNLDN TYLNGKEQSN NLNKQDGENT
460 470 480 490 500
LQHEKSSSFG YWCSPSPEQL ERLSLKQLAA VSNFVIGRRG YGCITFQHDV
510 520 530 540 550
DLTAFTKSFR EELFGKIVIF RSSKTVEVYP DEATKPMIGH GLNVPAIITL
560 570 580 590 600
ENVYPVDKKT KKPMKDTTKF AEFQVFDRKL RSMREMNYIS YNPFGGTWTF
610 620 630 640 650
KVNHFSIWGL VNEEDAEIDE DDLSKQEDGG EQPLRKVRTL AQSKPSDKEV
660 670 680 690 700
ILKTDGTFGT LSGKDDSIVE EKAYEPDLSD ADFEGIEASP KLDVSKDWVE
710 720 730 740 750
QLILAGSSLR SVFATSKEFD GPCQNEIDLL FSECNDEIDN AKLIMKERRF
760 770 780 790 800
TASYTFAKFS TGSMLLTKDI VGKSGVSIKR LPTELQRKFL FDDVYLDKEI
810 820 830 840 850
EKVTIEARKS NPYPQISESS LLFKDALDYM EKTSSDYNLW KLSSILFDPV
860 870 880 890 900
SYPYKTDNDQ VKMALLKKER HCRLTSWIVS QIGPEIEEKI RNSSNEIEQI
910 920 930 940 950
FLYLLLNDVV RASKLAIESK NGHLSVLISY LGSNDPRIRD LAELQLQKWS
960 970 980 990 1000
TGGCSIDKNI SKIYKLLSGS PFEGLFSLKE LESEFSWLCL LNLTLCYGQI
1010 1020 1030 1040 1050
DEYSLESLVQ SHLDKFSLPY DDPIGVIFQL YAANENTEKL YKEVRQRTNA
1060 1070 1080 1090 1100
LDVQFCWYLI QTLRFNGTRV FSKETSDEAT FAFAAQLEFA QLHGHSLFVS
1110 1120 1130 1140 1150
CFLNDDKAAE DTIKRLVMRE ITLLRASTND HILNRLKIPS QLIFNAQALK
1160 1170 1180 1190 1200
DRYEGNYLSE VQNLLLGSSY DLAEMAIVTS LGPRLLLSNN PVQNNELKTL
1210 1220 1230 1240 1250
REILNEFPDS ERDKWSVSIN VFEVYLKLVL DNVETQETID SLISGMKIFY
1260 1270 1280 1290 1300
DQYKHCREVA ACCNVMSQEI VSKILEKNNP SIGDSKAKLL ELPLGQPEKA
1310
YLRGEFAQDL MKCTYKI
Length:1,317
Mass (Da):145,661
Last modified:February 1, 1996 - v1
Checksum:i59399D86BB553030
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 2822NA → QR in CAA83584 (PubMed:8195299).Curated
Sequence conflicti1142 – 11421L → S in CAA83584 (PubMed:8195299).Curated
Sequence conflicti1310 – 13167LMKCTYK → FEVYI (PubMed:8195299).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76557 Genomic DNA. Translation: CAA54057.1.
Z32672 Genomic DNA. Translation: CAA83584.1.
Z72614 Genomic DNA. Translation: CAA96798.1.
BK006941 Genomic DNA. Translation: DAA08014.1.
PIRiA54831.
RefSeqiNP_011423.1. NM_001180957.1.

Genome annotation databases

EnsemblFungiiYGL092W; YGL092W; YGL092W.
GeneIDi852788.
KEGGisce:YGL092W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76557 Genomic DNA. Translation: CAA54057.1.
Z32672 Genomic DNA. Translation: CAA83584.1.
Z72614 Genomic DNA. Translation: CAA96798.1.
BK006941 Genomic DNA. Translation: DAA08014.1.
PIRiA54831.
RefSeqiNP_011423.1. NM_001180957.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BG0X-ray3.15B/C/F/G731-1158[»]
3BG1X-ray3.00B/C/F/G731-1158[»]
3IKOX-ray3.20B/E/H731-1158[»]
3KEPX-ray1.82A/B442-605[»]
3KESX-ray2.10A/B442-605[»]
4XMMX-ray7.38B680-1317[»]
4XMNX-ray7.60B680-1317[»]
ProteinModelPortaliP49687.
SMRiP49687. Positions 459-605, 736-1317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33159. 49 interactions.
DIPiDIP-2074N.
IntActiP49687. 17 interactions.
MINTiMINT-508825.

Protein family/group databases

MEROPSiS59.002.
TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiP49687.

Proteomic databases

MaxQBiP49687.

Protocols and materials databases

DNASUi852788.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL092W; YGL092W; YGL092W.
GeneIDi852788.
KEGGisce:YGL092W.

Organism-specific databases

EuPathDBiFungiDB:YGL092W.
SGDiS000003060. NUP145.

Phylogenomic databases

GeneTreeiENSGT00550000074799.
HOGENOMiHOG000113874.
InParanoidiP49687.
KOiK18720.
OMAiGMEFVTY.
OrthoDBiEOG7Z95VP.

Enzyme and pathway databases

BioCyciYEAST:G3O-30592-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP49687.
NextBioi972282.
PMAP-CutDBP49687.
PROiP49687.

Family and domain databases

Gene3Di3.30.1610.10. 1 hit.
InterProiIPR025574. Nucleoporin_FG_rpt.
IPR021967. Nup96.
IPR007230. Peptidase_S59.
[Graphical view]
PfamiPF04096. Nucleoporin2. 1 hit.
PF13634. Nucleoporin_FG. 3 hits.
PF12110. Nup96. 1 hit.
[Graphical view]
SUPFAMiSSF82215. SSF82215. 1 hit.
PROSITEiPS51434. NUP_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif."
    Fabre E., Boelens W.C., Wimmer C., Mattaj I.W., Hurt E.C.
    Cell 78:275-289(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN NUCLEAR MRNA EXPORT.
  2. "NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure."
    Wente S.R., Blobel G.
    J. Cell Biol. 125:955-969(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN NPC ASSEMBLY AND DISTRIBUTION.
    Strain: ATCC 26109 / X2180.
  3. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Yeast nucleoporin mutants are defective in pre-tRNA splicing."
    Sharma K., Fabre E., Tekotte H., Hurt E.C., Tollervey D.
    Mol. Cell. Biol. 16:294-301(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NUCLEAR TRNA EXPORT.
  7. "Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins."
    Teixeira M.T., Siniossoglou S., Podtelejnikov S., Benichou J.C., Mann M., Dujon B., Hurt E.C., Fabre E.
    EMBO J. 16:5086-5097(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CLEAVAGE, MUTAGENESIS OF HIS-604; PHE-605 AND TRP-608.
  8. "Self-catalyzed cleavage of the yeast nucleoporin Nup145p precursor."
    Teixeira M.T., Fabre E., Dujon B.
    J. Biol. Chem. 274:32439-32444(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF SER-606.
  9. "Nuclear pore complexes in the organization of silent telomeric chromatin."
    Galy V., Olivo-Marin J.-C., Scherthan H., Doye V., Rascalou N., Nehrbass U.
    Nature 403:108-112(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MLP1 AND MLP2.
  10. "The yeast nuclear pore complex: composition, architecture, and transport mechanism."
    Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.
    J. Cell Biol. 148:635-651(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, NPC SUBUNIT LOCATION.
  11. "Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins."
    Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C.
    EMBO J. 21:387-397(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded."
    Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.
    Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FG REPEAT STRUCTURE.
  14. "Minimal nuclear pore complexes define FG repeat domains essential for transport."
    Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.
    Nat. Cell Biol. 6:197-206(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FG REPEATS IN NPC TRANSPORT.
  15. "Peering through the pore: nuclear pore complex structure, assembly, and function."
    Suntharalingam M., Wente S.R.
    Dev. Cell 4:775-789(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  17. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-679; SER-689 AND THR-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-403; SER-404; SER-414; SER-667; SER-679 AND SER-689, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Architecture of a coat for the nuclear pore membrane."
    Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.
    Cell 131:1313-1326(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 731-1158 IN COMPLEX WITH HUMAN SEC13.

Entry informationi

Entry nameiNU145_YEAST
AccessioniPrimary (citable) accession number: P49687
Secondary accession number(s): D6VU53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4630 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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.