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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
  • nuclear localization sequence binding Source: GO_Central
  • 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 cytoplasmic filaments Source: GO_Central
  • nuclear pore outer ring Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi604H → P: Loss of autocatalytic cleavage; when associated with L-608. 1 Publication1
Mutagenesisi605F → S: Loss of autocatalytic cleavage; when associated with R-608. 1 Publication1
Mutagenesisi606S → A: Loss of autocatalytic cleavage. 1 Publication1
Mutagenesisi608W → L: Loss of autocatalytic cleavage; when associated with P-604. 1 Publication1
Mutagenesisi608W → R: Loss of autocatalytic cleavage; when associated with F-605. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000199271 – 605Nucleoporin NUP145NAdd BLAST605
ChainiPRO_0000019928606 – 1317Nucleoporin NUP145CAdd BLAST712

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei273PhosphoserineCombined sources1
Modified residuei403PhosphoserineCombined sources1
Modified residuei404PhosphoserineCombined sources1
Modified residuei414PhosphoserineCombined sources1
Modified residuei667PhosphoserineCombined sources1
Modified residuei679PhosphoserineCombined sources1
Modified residuei689PhosphoserineCombined sources1
Modified residuei751PhosphothreonineCombined sources1

Post-translational modificationi

NUP145 is autocatalytically cleaved in NUP145N and NUP145C.1 Publication

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein

Proteomic databases

MaxQBiP49687.
PRIDEiP49687.

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
NUP120P3572914EBI-11730,EBI-11713
NUP84P5289110EBI-11730,EBI-12337
NUP85P466738EBI-11730,EBI-12345
SEC13P5573515EBI-11730,EBI-1046596From a different organism.
SEC13Q0449112EBI-11730,EBI-16529

Protein-protein interaction databases

BioGridi33159. 49 interactors.
DIPiDIP-2074N.
IntActiP49687. 21 interactors.
MINTiMINT-508825.

Structurei

Secondary structure

11317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi454 – 458Combined sources5
Beta strandi461 – 465Combined sources5
Helixi467 – 471Combined sources5
Helixi477 – 479Combined sources3
Beta strandi480 – 483Combined sources4
Beta strandi485 – 488Combined sources4
Turni489 – 491Combined sources3
Beta strandi492 – 498Combined sources7
Helixi503 – 505Combined sources3
Helixi509 – 513Combined sources5
Turni515 – 517Combined sources3
Beta strandi518 – 521Combined sources4
Turni522 – 524Combined sources3
Beta strandi525 – 528Combined sources4
Turni532 – 534Combined sources3
Beta strandi546 – 552Combined sources7
Turni558 – 560Combined sources3
Helixi570 – 582Combined sources13
Beta strandi584 – 592Combined sources9
Turni593 – 596Combined sources4
Beta strandi597 – 603Combined sources7
Turni731 – 733Combined sources3
Helixi738 – 746Combined sources9
Turni747 – 749Combined sources3
Beta strandi757 – 759Combined sources3
Turni761 – 763Combined sources3
Beta strandi765 – 769Combined sources5
Beta strandi772 – 775Combined sources4
Helixi788 – 791Combined sources4
Helixi793 – 801Combined sources9
Beta strandi803 – 807Combined sources5
Beta strandi809 – 812Combined sources4
Beta strandi814 – 819Combined sources6
Helixi823 – 827Combined sources5
Helixi835 – 846Combined sources12
Helixi859 – 881Combined sources23
Helixi883 – 891Combined sources9
Helixi896 – 904Combined sources9
Turni905 – 907Combined sources3
Helixi909 – 918Combined sources10
Helixi922 – 931Combined sources10
Helixi936 – 948Combined sources13
Turni950 – 952Combined sources3
Helixi958 – 968Combined sources11
Beta strandi971 – 974Combined sources4
Helixi979 – 983Combined sources5
Helixi987 – 996Combined sources10
Turni997 – 1002Combined sources6
Helixi1005 – 1015Combined sources11
Helixi1023 – 1032Combined sources10
Helixi1034 – 1036Combined sources3
Helixi1037 – 1045Combined sources9
Helixi1053 – 1064Combined sources12
Helixi1073 – 1089Combined sources17
Helixi1093 – 1100Combined sources8
Helixi1106 – 1119Combined sources14
Helixi1122 – 1124Combined sources3
Turni1126 – 1129Combined sources4
Helixi1132 – 1135Combined sources4
Helixi1140 – 1157Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49687.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati12 – 13FG 12
Repeati39 – 42GLFG 14
Repeati79 – 80FG 22
Repeati89 – 92GLFG 24
Repeati106 – 107FG 32
Repeati136 – 139GLFG 34
Repeati154 – 157GLFG 44
Repeati168 – 171GLFG 54
Repeati181 – 184GLFG 64
Repeati193 – 196GLFG 7; approximate4
Repeati206 – 209GLFG 84
Domaini458 – 605Peptidase S59PROSITE-ProRule annotationAdd BLAST148

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni398 – 523Required for autocatalytic cleavageAdd BLAST126
Regioni460 – 604Nucleoporin RNA-binding motif (NRM)Add BLAST145

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi369 – 385Bipartite nuclear localization signalSequence analysisAdd BLAST17

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi43 – 145Asn-richAdd BLAST103
Compositional biasi140 – 145Poly-Asn6

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.
OrthoDBiEOG092C0BHV.

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. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti281 – 282NA → QR in CAA83584 (PubMed:8195299).Curated2
Sequence conflicti1142L → S in CAA83584 (PubMed:8195299).Curated1
Sequence conflicti1310 – 1316LMKCTYK → FEVYI (PubMed:8195299).Curated7

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33159. 49 interactors.
DIPiDIP-2074N.
IntActiP49687. 21 interactors.
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.
PRIDEiP49687.

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.
OrthoDBiEOG092C0BHV.

Enzyme and pathway databases

BioCyciYEAST:G3O-30592-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP49687.
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. 1 hit.
PF12110. Nup96. 1 hit.
[Graphical view]
SUPFAMiSSF82215. SSF82215. 1 hit.
PROSITEiPS51434. NUP_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 164 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.