P57740 (NU107_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear pore complex protein Nup107

Alternative name(s):
107 kDa nucleoporin
Nucleoporin Nup107

Gene names

Name:

NUP107

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

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

General annotation (Comments)

Function	Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. Ref.6 Ref.7
Subunit structure	Part of the nuclear pore complex (NPC). 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. Does not interact with TPR. Ref.3 Ref.4 Ref.7
Subcellular location	Nucleus membrane. Nucleus › nuclear pore complex. Chromosome › centromere › kinetochore. Note: Located on both the cytoplasmic and nuclear sides of the NPC core structure. During mitosis, localizes to the kinetochores. Dissociates from the dissasembled NPC structure late during prophase of mitosis. Ref.3 Ref.4 Ref.5 Ref.7
Sequence similarities	Belongs to the nucleoporin Nup84/Nup107 family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Centromere Chromosome Kinetochore Membrane Nuclear pore complex Nucleus
PTM	Acetylation Phosphoprotein
Technical term	3D-structure 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 export from nucleus Inferred from direct assay Ref.4. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome nuclear pore complex assembly Inferred from mutant phenotype Ref.7. Source: UniProtKB 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	condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome nuclear membrane Inferred from direct assay Ref.5Ref.7. Source: UniProtKB nuclear periphery Inferred from direct assay Ref.7. Source: UniProtKB nuclear pore outer ring Inferred from direct assay PubMed 17360435. Source: UniProtKB
Molecular_function	nucleocytoplasmic transporter activity Inferred from direct assay Ref.4. Source: UniProtKB structural constituent of nuclear pore Inferred from mutant phenotype Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NUP133	Q8WUM0	5	EBI-295687,EBI-295695

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

1

1

N-acetylmethionine Ref.14

Modified residue

4

1

Phosphoserine Ref.12 Ref.14

Modified residue

11

1

Phosphoserine Ref.12 Ref.14

Modified residue

37

1

Phosphoserine Ref.10 Ref.12 Ref.13

Modified residue

46

1

Phosphothreonine Ref.9 Ref.12 Ref.13 Ref.14

Modified residue

55

1

Phosphothreonine Ref.12

Modified residue

58

1

Phosphoserine Ref.12

Modified residue

64

1

Phosphothreonine Ref.12

Modified residue

69

1

Phosphoserine Ref.12

Modified residue

86

1

Phosphoserine Ref.8 Ref.12 Ref.16

Experimental info

Sequence conflict

845

1

Q → R in AAH43343. Ref.2

Secondary structure

1

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925

Helix Strand Turn

Details...

Helix

668 – 680

13

Helix

682 – 684

3

Helix

685 – 701

17

Helix

705 – 714

10

Helix

719 – 723

5

Helix

738 – 767

30

Helix

782 – 821

40

Turn

824 – 826

3

Helix

840 – 867

28

Helix

871 – 875

5

Helix

877 – 882

6

Turn

884 – 886

3

Helix

888 – 891

4

Helix

894 – 912

19

Turn

913 – 915

3

Sequences

	Sequence		Length	Mass (Da)
	P57740 [UniParc]. Last modified January 11, 2001. Version 1. Checksum: CE1E4DA6C832A5A5	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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[5]	"Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex." Hase M.E., Cordes V.C. Mol. Biol. Cell 14:1923-1940(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ABSENCE OF INTERACTION WITH TPR, SUBCELLULAR LOCATION.
[6]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket." Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C. Mol. Biol. Cell 15:4261-4277(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION.
[8]	"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-86, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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 THR-46, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"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-4; SER-11; SER-37; THR-46; THR-55; SER-58; THR-64; SER-69 AND SER-86, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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-37 AND THR-46, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-11 AND THR-46, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"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-86, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

IPI

IPI00028005.

RefSeq

NP_065134.1. NM_020401.2.

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	[»]

ProteinModelPortal

P57740.

ModBase

Search...

Protein-protein interaction databases

IntAct

P57740. 5 interactions.

MINT

MINT-3021765.

STRING

9606.ENSP00000229179.

PTM databases

PhosphoSite

P57740.

Polymorphism databases

DMDM

12230339.

Proteomic databases

PaxDb

P57740.

PeptideAtlas

P57740.

PRIDE

P57740.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000229179; ENSP00000229179; ENSG00000111581.

GeneID

57122.

KEGG

hsa:57122.

UCSC

uc001suf.3. human.

Organism-specific databases

CTD

57122.

GeneCards

GC12P069080.

HGNC

HGNC:29914. NUP107.

HPA

HPA024141.

MIM

607617. gene.

neXtProt

NX_P57740.

PharmGKB

PA134890486.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG258212.

HOGENOM

HOG000006750.

HOVERGEN

HBG052677.

InParanoid

P57740.

KO

K14301.

OMA

NEKHTNL.

OrthoDB

EOG4JHCF2.

PhylomeDB

P57740.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6900. Immune System.

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. PTHR13003. 1 hit.

Pfam

PF04121. Nup84_Nup100. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P57740.

GenomeRNAi

57122.

NextBio

63009.

SOURCE

Search...

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:	May 1, 2013
This is version 108 of the entry and version 1 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.