Nuclear pore complex protein Nup88 - Homo sapiens (Human)

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Q99567 (NUP88_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nuclear pore complex protein Nup88

Alternative name(s):
88 kDa nucleoporin
Nucleoporin Nup88

Gene names

Name:

NUP88

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	741 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential component of nuclear pore complex.
Subunit structure	Interacts with NUP214/CAN. Ref.1
Subcellular location	Nucleus › nuclear pore complex.
Tissue specificity	Ubiquitous.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Nuclear pore complex Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome cytokine-mediated signaling pathway Traceable author statement. Source: Reactome glucose transport Traceable author statement. Source: Reactome mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of glucose transport Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear pore Traceable author statement Ref.1. Source: ProtInc
Molecular_function	transporter activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 741

741

Nuclear pore complex protein Nup88

PRO_0000204887

Regions

Coiled coil

585 – 651

Potential

Amino acid modifications

Modified residue

Phosphoserine Ref.7

Modified residue

Phosphoserine Ref.7

Modified residue

517

Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11

Modified residue

525

Phosphothreonine Ref.5 Ref.6 Ref.7 Ref.9

Modified residue

540

Phosphoserine Ref.9

Natural variations

Natural variant

289

N → S.
Corresponds to variant rs1806245 [ dbSNP | Ensembl ].

VAR_029340

Experimental info

Sequence conflict

247

A → D in CAA69904. Ref.1

Sequence conflict

291 – 301

GKLLGPLPMHP → WKAVGSIAHAS in CAA69904. Ref.1

Sequence conflict

456

K → R in CAA69904. Ref.1

Sequence conflict

518

P → S in CAA69904. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q99567 [UniParc].

Last modified November 8, 2002. Version 2.
Checksum: 954A8E2E203BC20B
Show »

FASTA

741

83,542

        10         20         30         40         50         60 
MAAAEGPVGD GELWQTWLPN HVVFLRLREG LKNQSPTEAE KPASSSLPSS PPPQLLTRNV 

        70         80         90        100        110        120 
VFGLGGELFL WDGEDSSFLV VRLRGPSGGG EEPALSQYQR LLCINPPLFE IYQVLLSPTQ 

       130        140        150        160        170        180 
HHVALIGIKG LMVLELPKRW GKNSEFEGGK STVNCSTTPV AERFFTSSTS LTLKHAAWYP 

       190        200        210        220        230        240 
SEILDPHVVL LTSDNVIRIY SLREPQTPTN VIILSEAEEE SLVLNKGRAY TASLGETAVA 

       250        260        270        280        290        300 
FDFGPLAAVP KTLFGQNGKD EVVAYPLYIL YENGETFLTY ISLLHSPGNI GKLLGPLPMH 

       310        320        330        340        350        360 
PAAEDNYGYD ACAVLCLPCV PNILVIATES GMLYHCVVLE GEEEDDHTSE KSWDSRIDLI 

       370        380        390        400        410        420 
PSLYVFECVE LELALKLASG EDDPFDSDFS CPVKLHRDPK CPSRYHCTHE AGVHSVGLTW 

       430        440        450        460        470        480 
IHKLHKFLGS DEEDKDSLQE LSTEQKCFVE HILCTKPLPC RQPAPIRGFW IVPDILGPTM 

       490        500        510        520        530        540 
ICITSTYECL IWPLLSTVHP ASPPLLCTRE DVEVAESPLR VLAETPDSFE KHIRSILQRS 

       550        560        570        580        590        600 
VANPAFLKAS EKDIAPPPEE CLQLLSRATQ VFREQYILKQ DLAKEEIQRR VKLLCDQKKK 

       610        620        630        640        650        660 
QLEDLSYCRE ERKSLREMAE RLADKYEEAK EKQEDIMNRM KKLLHSFHSE LPVLSDSERD 

       670        680        690        700        710        720 
MKKELQLIPD QLRHLGNAIK QVTMKKDYQQ QKMEKVLSLP KPTIILSAYQ RKCIQSILKE 

       730        740 
EGEHIREMVK QINDIRNHVN F

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and the novel nuclear pore component Nup88." Fornerod M., van Deursen J.M., van Baal S., Reynolds A., Davis D., Murti K.G., Fransen J., Grosveld G. EMBO J. 16:807-816(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NUP214/CAN. Tissue: Placenta.
[2]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND THR-525, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND THR-525, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-50; SER-517 AND THR-525, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; THR-525 AND SER-540, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y08612 mRNA. Translation: CAA69904.1. CH471108 Genomic DNA. Translation: EAW90340.1. CH471108 Genomic DNA. Translation: EAW90342.1. BC000335 mRNA. Translation: AAH00335.1.
IPI	IPI00001738.
RefSeq	NP_002523.2. NM_002532.4.
UniGene	Hs.584784.
3D structure databases
ProteinModelPortal	Q99567.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99567. 11 interactions.
MINT	MINT-191368.
STRING	9606.ENSP00000225696.
PTM databases
PhosphoSite	Q99567.
Polymorphism databases
DMDM	25008854.
Proteomic databases
PaxDb	Q99567.
PeptideAtlas	Q99567.
PRIDE	Q99567.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000573584; ENSP00000458954; ENSG00000108559.
GeneID	4927.
KEGG	hsa:4927.
UCSC	uc002gbo.2. human.
Organism-specific databases
CTD	4927.
GeneCards	GC17M005180.
HGNC	HGNC:8067. NUP88.
HPA	CAB002209. HPA021816.
MIM	602552. gene.
neXtProt	NX_Q99567.
PharmGKB	PA31855.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG274278.
HOGENOM	HOG000234330.
HOVERGEN	HBG052700.
InParanoid	Q99567.
KO	K14318.
OMA	PLYILYE.
OrthoDB	EOG43R3M9.
PhylomeDB	Q99567.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease. REACT_15518. Transmembrane transport of small molecules. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q99567.
Bgee	Q99567.
CleanEx	HS_NUP88.
Genevestigator	Q99567.
GermOnline	ENSG00000108559. Homo sapiens.
Family and domain databases
InterPro	IPR019321. Nucleoporin_Nup88. [Graphical view]
Pfam	PF10168. Nup88. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NUP88. human.
GenomeRNAi	4927.
NextBio	18975.
SOURCE	Search...

Entry information

Entry name

NUP88_HUMAN

Accession

Primary (citable) accession number: Q99567
Secondary accession number(s): D3DTM2, Q9BWE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	November 8, 2002
Last modified:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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List of human entries with polymorphisms or disease mutations

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Index of human polymorphisms and disease mutations

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents