Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nucleoporin NSP1

Gene

NSP1

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). NSP1 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, pre-ribosome, signal recognition particle (SRP), and protein transport.13 Publications

GO - Molecular functioni

  • nucleocytoplasmic transporter activity Source: SGD
  • phospholipid binding Source: SGD
  • structural constituent of nuclear pore Source: SGD

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • ncRNA export from nucleus Source: SGD
  • NLS-bearing protein import into nucleus Source: SGD
  • poly(A)+ mRNA export from nucleus Source: SGD
  • protein import into nucleus Source: SGD
  • ribosomal large subunit export from nucleus Source: SGD
  • ribosomal small subunit export from nucleus Source: SGD
  • tRNA export from nucleus Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-31506-MONOMER.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NSP1
Alternative name(s):
Nuclear pore protein NSP1
Nucleoskeletal-like protein
p110
Gene namesi
Name:NSP1
Ordered Locus Names:YJL041W
ORF Names:J1207
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL041W.
SGDiS000003577. NSP1.

Subcellular locationi

GO - Cellular componenti

  • nuclear membrane Source: UniProtKB-SubCell
  • nuclear pore Source: SGD
  • nuclear pore central transport channel Source: SGD
  • nuclear pore nuclear basket Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 823823Nucleoporin NSP1PRO_0000204865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei238 – 2381PhosphoserineCombined sources
Modified residuei361 – 3611PhosphoserineCombined sources
Modified residuei456 – 4561PhosphoserineCombined sources
Modified residuei631 – 6311PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP14907.

PTM databases

iPTMnetiP14907.

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. NSP1 interacts alternatively with NUP82 or NUP57 through its C-terminal coiled coil in two distinct NPC subcomplexes, the NUP82 subcomplex (NUP82, NSP1, NUP159) and the NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57). The NUP82 subcomplex is the base for interactions with NUP116 and GLE2 and with NUP42 and GLE1. Interacts through its FG repeats with karyopherins, such as KAP95, KAP123, PSE1, LOS1, NTF2, the heterodimeric mRNA transport factor MEX67/MTR2, and GSP1.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KAP95Q061423EBI-12265,EBI-9145
KPNB1Q149742EBI-12265,EBI-286758From a different organism.
NUP57P488374EBI-12265,EBI-12324
NUP82P403688EBI-12265,EBI-12331

Protein-protein interaction databases

BioGridi33717. 73 interactions.
DIPiDIP-1484N.
IntActiP14907. 36 interactions.
MINTiMINT-405423.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O6OX-ray2.80D/E/F497-608[»]
ProteinModelPortaliP14907.
SMRiP14907. Positions 637-770.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14907.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati13 – 164FSFG 1
Repeati36 – 372FG 1
Repeati43 – 442FG 2
Repeati64 – 652FG 3
Repeati74 – 752FG 4
Repeati84 – 852FG 5
Repeati94 – 952FG 6
Repeati104 – 1052FG 7
Repeati123 – 1242FG 8
Repeati142 – 1432FG 9
Repeati147 – 1482FG 10
Repeati168 – 1692FG 11
Repeati179 – 1824FSFG 2
Repeati217 – 2204FSFG 3
Repeati239 – 2402FG 12
Repeati268 – 2692FG 13
Repeati284 – 2874FSFG 4
Repeati303 – 3064FSFG 5
Repeati322 – 3254FSFG 6
Repeati341 – 3444FSFG 7
Repeati360 – 3634FSFG 8
Repeati379 – 3824FSFG 9
Repeati398 – 4014FSFG 10
Repeati417 – 4204FSFG 11
Repeati436 – 4394FSFG 12
Repeati455 – 4584FSFG 13
Repeati474 – 4774FSFG 14
Repeati493 – 4964FSFG 15
Repeati512 – 5154FSFG 16
Repeati531 – 5344FSFG 17
Repeati550 – 5534FSFG 18
Repeati571 – 5722FG 14
Repeati588 – 5914FSFG 19; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni673 – 73866Competitive binding site of NUP57 and NUP82Add
BLAST
Regioni740 – 82384Required for association with NUP57 subcomplexAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili630 – 823194Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 175174Asn-richAdd
BLAST
Compositional biasi308 – 628321Lys-richAdd
BLAST

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.1 Publication

Sequence similaritiesi

Belongs to the nucleoporin NSP1/NUP62 family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

GeneTreeiENSGT00730000111010.
HOGENOMiHOG000000808.
InParanoidiP14907.
KOiK14306.
OMAiKDDNSSK.
OrthoDBiEOG7BW0ST.

Family and domain databases

InterProiIPR026010. NSP1/NUP62.
IPR007758. Nucleoporin_NSP1_C.
[Graphical view]
PANTHERiPTHR12084. PTHR12084. 3 hits.
PfamiPF05064. Nsp1_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14907-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFNTPQQNK TPFSFGTANN NSNTTNQNSS TGAGAFGTGQ STFGFNNSAP
60 70 80 90 100
NNTNNANSSI TPAFGSNNTG NTAFGNSNPT SNVFGSNNST TNTFGSNSAG
110 120 130 140 150
TSLFGSSSAQ QTKSNGTAGG NTFGSSSLFN NSTNSNTTKP AFGGLNFGGG
160 170 180 190 200
NNTTPSSTGN ANTSNNLFGA TANANKPAFS FGATTNDDKK TEPDKPAFSF
210 220 230 240 250
NSSVGNKTDA QAPTTGFSFG SQLGGNKTVN EAAKPSLSFG SGSAGANPAG
260 270 280 290 300
ASQPEPTTNE PAKPALSFGT ATSDNKTTNT TPSFSFGAKS DENKAGATSK
310 320 330 340 350
PAFSFGAKPE EKKDDNSSKP AFSFGAKSNE DKQDGTAKPA FSFGAKPAEK
360 370 380 390 400
NNNETSKPAF SFGAKSDEKK DGDASKPAFS FGAKPDENKA SATSKPAFSF
410 420 430 440 450
GAKPEEKKDD NSSKPAFSFG AKSNEDKQDG TAKPAFSFGA KPAEKNNNET
460 470 480 490 500
SKPAFSFGAK SDEKKDGDAS KPAFSFGAKS DEKKDSDSSK PAFSFGTKSN
510 520 530 540 550
EKKDSGSSKP AFSFGAKPDE KKNDEVSKPA FSFGAKANEK KESDESKSAF
560 570 580 590 600
SFGSKPTGKE EGDGAKAAIS FGAKPEEQKS SDTSKPAFTF GAQKDNEKKT
610 620 630 640 650
EESSTGKSTA DVKSSDSLKL NSKPVELKPV SLDNKTLDDL VTKWTNQLTE
660 670 680 690 700
SASHFEQYTK KINSWDQVLV KGGEQISQLY SDAVMAEHSQ NKIDQSLQYI
710 720 730 740 750
ERQQDELENF LDNFETKTEA LLSDVVSTSS GAAANNNDQK RQQAYKTAQT
760 770 780 790 800
LDENLNSLSS NLSSLIVEIN NVSNTFNKTT NIDINNEDEN IQLIKILNSH
810 820
FDALRSLDDN STSLEKQINS IKK
Length:823
Mass (Da):86,516
Last modified:April 1, 1990 - v1
Checksum:iA258003CB1917810
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37160 Genomic DNA. Translation: AAA34821.1.
Z49316 Genomic DNA. Translation: CAA89332.1.
Z49314 Genomic DNA. Translation: CAA89331.1.
BK006943 Genomic DNA. Translation: DAA08759.1.
PIRiS14055.
RefSeqiNP_012494.3. NM_001181474.3.

Genome annotation databases

EnsemblFungiiYJL041W; YJL041W; YJL041W.
GeneIDi853409.
KEGGisce:YJL041W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37160 Genomic DNA. Translation: AAA34821.1.
Z49316 Genomic DNA. Translation: CAA89332.1.
Z49314 Genomic DNA. Translation: CAA89331.1.
BK006943 Genomic DNA. Translation: DAA08759.1.
PIRiS14055.
RefSeqiNP_012494.3. NM_001181474.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O6OX-ray2.80D/E/F497-608[»]
ProteinModelPortaliP14907.
SMRiP14907. Positions 637-770.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33717. 73 interactions.
DIPiDIP-1484N.
IntActiP14907. 36 interactions.
MINTiMINT-405423.

Protein family/group databases

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

PTM databases

iPTMnetiP14907.

Proteomic databases

MaxQBiP14907.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL041W; YJL041W; YJL041W.
GeneIDi853409.
KEGGisce:YJL041W.

Organism-specific databases

EuPathDBiFungiDB:YJL041W.
SGDiS000003577. NSP1.

Phylogenomic databases

GeneTreeiENSGT00730000111010.
HOGENOMiHOG000000808.
InParanoidiP14907.
KOiK14306.
OMAiKDDNSSK.
OrthoDBiEOG7BW0ST.

Enzyme and pathway databases

BioCyciYEAST:G3O-31506-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14907.
PROiP14907.

Family and domain databases

InterProiIPR026010. NSP1/NUP62.
IPR007758. Nucleoporin_NSP1_C.
[Graphical view]
PANTHERiPTHR12084. PTHR12084. 3 hits.
PfamiPF05064. Nsp1_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel nucleoskeletal-like protein located at the nuclear periphery is required for the life cycle of Saccharomyces cerevisiae."
    Hurt E.C.
    EMBO J. 7:4323-4334(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "NSP1: a yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxy-terminal domain."
    Nehrbass U., Kern H., Mutvei A., Horstmann H., Marshallsay B., Hurt E.C.
    Cell 61:979-989(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
  5. "In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsp1p, Nup49p, and Nup57p."
    Schlaich N.L., Haener M., Lustig A., Aebi U., Hurt E.C.
    Mol. Biol. Cell 8:33-46(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NUP57 NPC SUBCOMPLEX.
  6. "Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNA."
    Hellmuth K., Lau D.M., Bischoff F.R., Kuenzler M., Hurt E.C., Simos G.
    Mol. Cell. Biol. 18:6374-6386(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LOS1.
  7. "The small GTPase Gsp1p binds to the repeat domain of the nucleoporin Nsp1p."
    Stochaj U., Hejazi M., Belhumeur P.
    Biochem. J. 330:421-427(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GSP1.
  8. "Functional characterization of a Nup159p-containing nuclear pore subcomplex."
    Belgareh N., Snay-Hodge C., Pasteau F., Dagher S., Cole C.N., Doye V.
    Mol. Biol. Cell 9:3475-3492(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP159.
  9. "Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase."
    Seedorf M., Damelin M., Kahana J., Taura T., Silver P.A.
    Mol. Cell. Biol. 19:1547-1557(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PSE1.
  10. "The mechanism of ran import into the nucleus by nuclear transport factor 2."
    Quimby B.B., Lamitina T., L'Hernault S.W., Corbett A.H.
    J. Biol. Chem. 275:28575-28582(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NTF2.
  11. "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.
  12. "Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export."
    Straesser K., Bassler J., Hurt E.C.
    J. Cell Biol. 150:695-706(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MEX67/MTR2 HETERODIMER.
  13. "Proteomic analysis of nucleoporin interacting proteins."
    Allen N.P., Huang L., Burlingame A., Rexach M.
    J. Biol. Chem. 276:29268-29274(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NUCLEOPORIN INTERACTING PROTEINS.
  14. "Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex."
    Gleizes P.-E., Noaillac-Depeyre J., Leger-Silvestre I., Teulieres F., Dauxois J.-Y., Pommet D., Azum-Gelade M.-C., Gas N.
    J. Cell Biol. 155:923-936(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PRE-RIBOSOME EXPORT.
  15. "Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export."
    Grosshans H., Deinert K., Hurt E.C., Simos G.
    J. Cell Biol. 153:745-762(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NUCLEAR SRP EXPORT.
  16. "The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport."
    Bailer S.M., Balduf C., Hurt E.C.
    Mol. Cell. Biol. 21:7944-7955(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCOMPLEX ASSEMBLY, INTERACTION WITH NUP57 AND NUP82.
  17. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  18. "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.
  19. "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.
  20. "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.
  21. "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-238; SER-361 AND SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta."
    Bayliss R., Littlewood T., Strawn L.A., Wente S.R., Stewart M.
    J. Biol. Chem. 277:50597-50606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 511-516 IN COMPLEX WITH HUMAN IMPORTIN BETA-1 SUBUNIT, STRUCTURAL BASIS OF FG REPEAT INTERACTION, INTERACTION WITH KAP95.

Entry informationi

Entry nameiNSP1_YEAST
AccessioniPrimary (citable) accession number: P14907
Secondary accession number(s): D6VWE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 6, 2016
This is version 166 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 2400 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. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.