Nuclear pore complex protein Nup107

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Reviewed, UniProtKB/Swiss-Prot P57740 (NU107_HUMAN)

Last modified January 19, 2010. Version 81. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Nuclear pore complex protein Nup107
Alternative name(s):
    Nucleoporin Nup107
    107 kDa nucleoporin

Gene names

Name:

NUP107

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	925 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Essential component of nuclear pore complex. Required for the assembly of peripheral proteins into the nuclear pore complex. Ref.5
Subunit structure	Forms part of the Nup160 subcomplex in the nuclear pore which is composed of Nup160, Nup133, Nup107 and Nup96. This complex plays a role in RNA export and in tethering Nup98 and Nup153 to the nucleus. Ref.3 Ref.4
Subcellular location	Nucleus › nuclear pore complex. Kinetochore. Note: Located on both the cytoplasmic and nuclear sides of the nuclear pore. During mitosis, localizes to the kinetochores. Ref.3 Ref.4
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17
Sequence similarities	Belongs to the nucleoporin Nup84/Nup107 family.

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Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Kinetochore Nuclear pore complex Nucleus
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	mRNA export from nucleus Ref.4 Inferred from direct assay. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW transmembrane transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Nup107-160 complex Inferred from direct assay. Source: UniProtKB condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nucleocytoplasmic transporter activity Ref.4 Inferred from direct assay. Source: UniProtKB protein binding Ref.3 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
NUP133	Q8WUM0	1	EBI-295687,EBI-295695

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 925

925

Nuclear pore complex protein Nup107

PRO_0000204831

Amino acid modifications

Modified residue

N-acetylmethionine Ref.16

Modified residue

Phosphoserine Ref.8 Ref.13

Modified residue

Phosphoserine Ref.16

Modified residue

Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17

Modified residue

Phosphoserine Ref.10 Ref.13 Ref.17

Modified residue

Phosphothreonine Ref.7 Ref.8 Ref.13 Ref.17

Modified residue

Phosphothreonine Ref.8 Ref.11 Ref.13

Modified residue

Phosphoserine Ref.8 Ref.13

Modified residue

Phosphothreonine Ref.8 Ref.13

Modified residue

Phosphoserine Ref.13

Modified residue

Phosphoserine Ref.13

Modified residue

Phosphoserine Ref.6 Ref.13

Experimental info

Sequence conflict

845

Q → R in AAH43343. Ref.2

Secondary structure

925

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P57740-1 [UniParc].

Last modified January 11, 2001. Version 1.
Checksum: CE1E4DA6C832A5A5
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FASTA

925

106,374

        10         20         30         40         50         60 
MDRSGFGEIS SPVIREAEVT RTARKQSAQK RVLLQASQDE NFGNTTPRNQ VIPRTPSSFR 

        70         80         90        100        110        120 
QPFTPTSRSL LRQPDISCIL GTGGKSPRLT QSSGFFGNLS MVTNLDDSNW AAAFSSQRSG 

       130        140        150        160        170        180 
LFTNTEPHSI TEDVTISAVM LREDDPGEAA SMSMFSDFLQ SFLKHSSSTV FDLVEEYENI 

       190        200        210        220        230        240 
CGSQVNILSK IVSRATPGLQ KFSKTASMLW LLQQEMVTWR LLASLYRDRI QSALEEESVF 

       250        260        270        280        290        300 
AVTAVNASEK TVVEALFQRD SLVRQSQLVV DWLESIAKDE IGEFSDNIEF YAKSVYWENT 

       310        320        330        340        350        360 
LHTLKQRQLT SYVGSVRPLV TELDPDAPIR QKMPLDDLDR EDEVRLLKYL FTLIRAGMTE 

       370        380        390        400        410        420 
EAQRLCKRCG QAWRAATLEG WKLYHDPNVN GGTELEPVEG NPYRRIWKIS CWRMAEDELF 

       430        440        450        460        470        480 
NRYERAIYAA LSGNLKQLLP VCDTWEDTVW AYFRVMVDSL VEQEIQTSVA TLDETEELPR 

       490        500        510        520        530        540 
EYLGANWTLE KVFEELQATD KKRVLEENQE HYHIVQKFLI LGDIDGLMDE FSKWLSKSRN 

       550        560        570        580        590        600 
NLPGHLLRFM THLILFFRTL GLQTKEEVSI EVLKTYIQLL IREKHTNLIA FYTCHLPQDL 

       610        620        630        640        650        660 
AVAQYALFLE SVTEFEQRHH CLELAKEADL DVATITKTVV ENIRKKDNGE FSHHDLAPAL 

       670        680        690        700        710        720 
DTGTTEEDRL KIDVIDWLVF DPAQRAEALK QGNAIMRKFL ASKKHEAAKE VFVKIPQDSI 

       730        740        750        760        770        780 
AEIYNQCEEQ GMESPLPAED DNAIREHLCI RAYLEAHETF NEWFKHMNSV PQKPALIPQP 

       790        800        810        820        830        840 
TFTEKVAHEH KEKKYEMDFG IWKGHLDALT ADVKEKMYNV LLFVDGGWMV DVREDAKEDH 

       850        860        870        880        890        900 
ERTHQMVLLR KLCLPMLCFL LHTILHSTGQ YQECLQLADM VSSERHKLYL VFSKEELRKL 

       910        920 
LQKLRESSLM LLDQGLDPLG YEIQL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequential assembly of structural modules forming the vertebrate nuclear pore complex." Cordes V.C., Hunziker A., Mueller-Pillasch F. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pancreatic cancer.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[3]	"An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells." Belgareh N., Rabut G., Bai S.W., van Overbeek M., Beaudouin J., Daigle N., Zatsepina O.V., Pasteau F., Labas V., Fromont-Racine M., Ellenberg J., Doye V. J. Cell Biol. 154:1147-1160(2001) [PubMed: 11564755] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[4]	"Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export." Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J. J. Cell Biol. 155:339-354(2001) [PubMed: 11684705] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[5]	"Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex." Boehmer T., Enninga J., Dales S., Blobel G., Zhong H. Proc. Natl. Acad. Sci. U.S.A. 100:981-985(2003) [PubMed: 12552102] [Abstract] Cited for: FUNCTION.
[6]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-11; THR-46; THR-55; SER-58 AND THR-64, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY.
[11]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND THR-55, MASS SPECTROMETRY.
[12]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, MASS SPECTROMETRY.
[13]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-11; SER-37; THR-46; THR-55; SER-58; THR-64; SER-69; SER-77 AND SER-86, MASS SPECTROMETRY.
[14]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, MASS SPECTROMETRY.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-11, MASS SPECTROMETRY.
[17]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-37 AND THR-46, MASS SPECTROMETRY. Tissue: T-cell.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ295745 mRNA. Translation: CAC03716.1.
BC043343 mRNA. Translation: AAH43343.1.

IPI

IPI00028005.

RefSeq

NP_065134.1.

UniGene

Hs.524574

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CQC	X-ray	2.53	A	658-925	[»]
3CQG	X-ray	3.00	A	658-925	[»]
3I4R	X-ray	3.53	A	658-925	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P57740. 3 interactions.

STRING

P57740.

PTM databases

PhosphoSite

P57740.

Proteomic databases

PeptideAtlas

P57740.

PRIDE

P57740.

Genome annotation databases

Ensembl

ENST00000229179; ENSP00000229179; ENSG00000111581; Homo sapiens. [Genome view]

GeneID

57122.

KEGG

hsa:57122.

UCSC

uc001suf.1. human.

Organism-specific databases

CTD

57122.

GeneCards

GC12P067366.

H-InvDB

HIX0010802.

HGNC

HGNC:29914. NUP107.

HPA

HPA024141.

MIM

607617. gene.

PharmGKB

PA134890486.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16353.

HOGENOM

HBG356874.

HOVERGEN

P57740.

InParanoid

P57740.

OMA

EYLEANW.

OrthoDB

EOG94J54F.

PhylomeDB

P57740.

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpress

P57740.

Bgee

P57740.

CleanEx

HS_NUP107.

Genevestigator

P57740.

GermOnline

ENSG00000111581. Homo sapiens.

Family and domain databases

InterPro

IPR007252. Nup84_Nup100.
[Graphical view]

PANTHER

PTHR13003. Nup84_Nup100. 1 hit.

Pfam

PF04121. Nup84_Nup100. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

63009.

SOURCE

Search...

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Entry information

Entry name

NU107_HUMAN

Accession

Primary (citable) accession number: P57740

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 11, 2001
Last modified:	January 19, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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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Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents