P38181 (NU170_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleoporin NUP170

Alternative name(s):
Nuclear pore protein NUP170

Gene names

Name:	NUP170
Synonyms:	NLE3
Ordered Locus Names:	YBL079W
ORF Names:	YBL0725

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1502 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. NUP170 probably plays an important role in NPC assembly and organization. In addition it is required for chromosome transmission fidelity. Ref.5 Ref.6 Ref.7 Ref.10 Ref.11
Subunit structure	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. During mitosis NUP53 changes its binding partner within the NPC from NUP170 to NIC96, exposing a high affinity binding site for the karyopherin PSE1, and retaining it in the NPC. Ref.9
Subcellular location	Nucleus › nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Note: Central core structure of the nuclear pore complex.
Miscellaneous	Present with 1560 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the non-repetitive/WGA-negative nucleoporin family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Membrane Nuclear pore complex Nucleus
Domain	Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	NLS-bearing substrate import into nucleus Traceable author statement. Source: SGD chromosome segregation Inferred from mutant phenotype Ref.10. Source: SGD mRNA export from nucleus Traceable author statement. Source: SGD mRNA-binding (hnRNP) protein import into nucleus Traceable author statement. Source: SGD nuclear pore complex assembly Inferred from genetic interaction. Source: SGD protein export from nucleus Traceable author statement. Source: SGD protein targeting to membrane Inferred from mutant phenotype. Source: SGD rRNA export from nucleus Traceable author statement. Source: SGD ribosomal protein import into nucleus Traceable author statement. Source: SGD snRNA export from nucleus Traceable author statement. Source: SGD snRNP protein import into nucleus Traceable author statement. Source: SGD tRNA export from nucleus Traceable author statement. Source: SGD
Cellular component	nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Inferred from direct assay Ref.9. Source: SGD
Molecular function	structural constituent of nuclear pore Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1502

1502

Nucleoporin NUP170

PRO_0000204854

Regions

Transmembrane

225 – 245

21

Helical; Potential

Transmembrane

1383 – 1403

21

Helical; Potential

Transmembrane

1410 – 1430

21

Helical; Potential

Domain

233 – 261

29

Leucine-zipper Potential

Amino acid modifications

Modified residue

1247

1

Phosphoserine Ref.13

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1502

Helix Strand Turn

Details...

Helix

1262 – 1264

3

Helix

1265 – 1268

4

Helix

1275 – 1281

7

Helix

1287 – 1297

11

Helix

1304 – 1310

7

Turn

1311 – 1316

6

Helix

1318 – 1327

10

Helix

1333 – 1349

17

Helix

1357 – 1373

17

Turn

1382 – 1384

3

Helix

1387 – 1401

15

Helix

1404 – 1406

3

Helix

1413 – 1418

6

Helix

1423 – 1436

14

Helix

1442 – 1458

17

Helix

1460 – 1463

4

Helix

1468 – 1472

5

Turn

1479 – 1481

3

Helix

1483 – 1490

8

Sequences

	Sequence		Length	Mass (Da)
	P38181 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 3BEA65DAA2A5F99A	FASTA	1,502	169,475
	10 20 30 40 50 60 MFQSFFHNNG PAAAGETFSD SRSYPLTNHQ EVPRNGLNEL ASSATKAQQQ PTHILNSYPI 70 80 90 100 110 120 TGSNPLMRAS AMGATSGSIN PNMSNMNEHI RVSGMGTSKP LDLAGKYIDH LQHKDSNTPV 130 140 150 160 170 180 LDERSYYNSG VDYNFSREKN GLGAFTPFEK QDVFNIPDEI LHEFSTSQTK TDMGIFPELN 190 200 210 220 230 240 RCWITIDNKL ILWNINNDNE YQVVDDMKHT IQKVALVRPK PNTFVPAVKH LLLISTTMEL 250 260 270 280 290 300 FMFAISLDKA TNELSVFNTH LSVPVQGIDV IDIVSHERSG RIFFAGQASG LNIWELHYSG 310 320 330 340 350 360 SDDWFNSKCS KVCLTKSALL SLLPTNMLSQ IPGVDFIQAL FEDNSNGNGG FSQETITQLT 370 380 390 400 410 420 IDQQRGIIYS LSSKSTIRAY VITEKSLEGP MSIEPAYISR IIGTTTARAA PILGPKYLKI 430 440 450 460 470 480 VKISSVAPEE NNNLFLVALT VGGVRLYFNG SMGRFNIEAL RLESIKFPPS SVTPEVIQQE 490 500 510 520 530 540 LLHQQQEQAK RSFPFFSNLM SSEPVLLKFQ KKSSVLLETT KASTIISPGI FFSAVIKSSQ 550 560 570 580 590 600 QTHQQEKKEN SSVTGTTATA GSKTVKQQPV TLQHKLFVSV PDYGILKTHG KYVENATFLE 610 620 630 640 650 660 TAGPVQQIIP LSGLFNATTK PQGFANEFAT QYTSETLRVA VLTSTSIEIY KYRTPDEIFE 670 680 690 700 710 720 DLIDNPLPFV LNYGAAEACS TALFVTCKSN KSEKLRSNAL TFLTMGIPGV VDIKPVYNRY 730 740 750 760 770 780 SVSTVSSLLS KPTLSTATTN LQQSITGFSK PSPANKEDFD LDDVILSPRF YGIALLITRL 790 800 810 820 830 840 LRDIWGRHVF MTFTDNRVTS HAFISSSDPI TPSINNLKSD EISQNRNIIS KVSISKDCIE 850 860 870 880 890 900 YYLSSINILN EFFITYGDSI SQISAPYVLA NNSNGRVIDK TEEVANQAES IAINAMIKMV 910 920 930 940 950 960 QSIKEGLSFL NVLYEESEVE GFDNQYLGFK DIISFVSLDV QKDLVKLDFK DLFAPNDKTK 970 980 990 1000 1010 1020 SLIREILLSI INRNITKGAS IEYTATALQE RCGSFCSASD ILGFRAIEHL RRAKEIGLRN 1030 1040 1050 1060 1070 1080 YDSLNYHLKN ATALLEQIVD DLSIEKLKEA VSMMLSVNYY PKSIEFLLNI ANSMDKGKLA 1090 1100 1110 1120 1130 1140 CQYVANGFLE NDDRKQYYDK RILVYDLVFD TLIKVDELAE KKQSSKTQNQ ISISNDDEVK 1150 1160 1170 1180 1190 1200 LRQKSYEAAL KYNDRLFHYH MYDWLVSQNR EEKLLDIETP FILPYLMEKA GSSLKISNIL 1210 1220 1230 1240 1250 1260 WVYYSRRSKF FESAEILYRL ATSNFDITLF ERIEFLSRAN GFCNSVSPLS QKQRIVQLAS 1270 1280 1290 1300 1310 1320 RIQDACEVAG IQGDILSLVY TDARIDSAIK DELIKTLDGK ILSTSELFND FAVPLSYHEI 1330 1340 1350 1360 1370 1380 ALFIFKIADF RDHEVIMAKW DELFQSLRME FNNTGKKEDS MNFINLLSNV LIKIGKNVQD 1390 1400 1410 1420 1430 1440 SEFIFPIFEL FPIVCNFFYE TLPKEHIVSG SIVSIFITAG VSFNKMYYIL KELIETSDSD 1450 1460 1470 1480 1490 1500 NSVFNKEMTW LIHEWYKSDR KFRDIISYND IIHLKEYKID NDPIEKYVKN SGNNLGICFY KE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II." Obermaier B., Gassenhuber J., Piravandi E., Domdey H. Yeast 11:1103-1112(1995) [PubMed: 7502586] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p." Aitchison J.D., Rout M.P., Marelli M., Blobel G., Wozniak R.W. J. Cell Biol. 131:1133-1148(1995) [PubMed: 8522578] [Abstract] Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 117-133 AND 153-166.
[5]	"Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p." Marelli M., Aitchison J.D., Wozniak R.W. J. Cell Biol. 143:1813-1830(1998) [PubMed: 9864357] [Abstract] Cited for: FUNCTION, SUBCOMPLEX WITH NUP59 AND NUP53.
[6]	"Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes." Lusk C.P., Makhnevych T., Marelli M., Aitchison J.D., Wozniak R.W. J. Cell Biol. 159:267-278(2002) [PubMed: 12403813] [Abstract] Cited for: FUNCTION, COMPETITION WITH NUP53 FOR PSE1 BINDING.
[7]	"Cell cycle regulated transport controlled by alterations in the nuclear pore complex." Makhnevych T., Lusk C.P., Anderson A.M., Aitchison J.D., Wozniak R.W. Cell 115:813-823(2003) [PubMed: 14697200] [Abstract] Cited for: FUNCTION, MITOTIC PSE1 TRANSPORT INHIBITION, NPC ASSEMBLY.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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: 10684247] [Abstract] Cited for: CHARACTERIZATION, NPC SUBUNIT LOCATION.
[10]	"Novel role for a Saccharomyces cerevisiae nucleoporin, Nup170p, in chromosome segregation." Kerscher O., Hieter P., Winey M., Basrai M.A. Genetics 157:1543-1553(2001) [PubMed: 11290711] [Abstract] Cited for: FUNCTION, CHROMOSOME TRANSMISSION FIDELITY.
[11]	"The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint." Iouk T., Kerscher O., Scott R.J., Basrai M.A., Wozniak R.W. J. Cell Biol. 159:807-819(2002) [PubMed: 12473689] [Abstract] Cited for: FUNCTION, INTERACTION WITH NUP157 AND NUP53.
[12]	"Peering through the pore: nuclear pore complex structure, assembly, and function." Suntharalingam M., Wente S.R. Dev. Cell 4:775-789(2003) [PubMed: 12791264] [Abstract] Cited for: REVIEW.
[13]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X79489 Genomic DNA. Translation: CAA56029.1.
Z35840 Genomic DNA. Translation: CAA84900.1.
BK006936 Genomic DNA. Translation: DAA07044.1.

PIR

S45429.

RefSeq

NP_009474.1. NM_001178319.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3I5P	X-ray	3.20	A	980-1502	[»]
3I5Q	X-ray	2.20	A/B	1253-1502	[»]

ProteinModelPortal

P38181.

SMR

P38181. Positions 1000-1502.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2450N.

IntAct

P38181. 18 interactions.

MINT

MINT-2788627.

STRING

P38181.

Protein family/group databases

TCDB

9.A.14.1.1. nuclear pore complex (NPC) family.

Proteomic databases

PeptideAtlas

P38181.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YBL079W; YBL079W; YBL079W.

GeneID

852199.

KEGG

sce:YBL079W.

NMPDR

fig|4932.3.peg.160.

Organism-specific databases

CYGD

YBL079w.

SGD

S000000175. NUP170.

Phylogenomic databases

eggNOG

fuNOG04081.

GeneTree

EFGT00050000004270.

HOGENOM

HBG395947.

OMA

LREGCPS.

OrthoDB

EOG41ZJJZ.

Gene expression databases

ArrayExpress

P38181.

Genevestigator

P38181.

GermOnline

YBL079W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR007187. Nucleoporin_Nup133/Nup155_C.
IPR014908. Nucleoporin_Nup133/Nup155_N.
IPR004870. Nucleoporin_Nup155.
[Graphical view]

KO

K14312.

PANTHER

PTHR10350. Nup_nucleoporin. 1 hit.

Pfam

PF03177. Nucleoporin_C. 1 hit.
PF08801. Nucleoporin_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

970691.

Entry information

Entry name

NU170_YEAST

Accession

Primary (citable) accession number: P38181
Secondary accession number(s): D6VPS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program