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P57740 (NU107_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear pore complex protein Nup107
Alternative name(s):
107 kDa nucleoporin
Nucleoporin Nup107
Gene names
Name:NUP107
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length925 AA.
Sequence statusComplete.
Protein existenceEvidence 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.8 Ref.9

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.5 Ref.6 Ref.9

Subcellular location

Nucleus membrane. Nucleusnuclear pore complex. Chromosomecentromerekinetochore. 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.5 Ref.6 Ref.7 Ref.9

Sequence similarities

Belongs to the nucleoporin Nup84/Nup107 family.

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
   Cellular componentCentromere
Chromosome
Kinetochore
Membrane
Nuclear pore complex
Nucleus
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

glucose transport

Traceable author statement. Source: Reactome

hexose transport

Traceable author statement. Source: Reactome

mRNA export from nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

nuclear pore complex assembly

Inferred from mutant phenotype Ref.9. 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 process

Traceable author statement. Source: Reactome

   Cellular_componentcentrosome

Inferred from direct assay. Source: HPA

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

nuclear envelope

Traceable author statement. Source: Reactome

nuclear membrane

Inferred from direct assay Ref.7Ref.9. Source: UniProtKB

nuclear periphery

Inferred from direct assay Ref.9. Source: UniProtKB

nuclear pore

Inferred from direct assay Ref.5Ref.6Ref.7Ref.9. Source: UniProtKB

nuclear pore outer ring

Inferred from direct assay PubMed 17360435. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionnucleocytoplasmic transporter activity

Inferred from direct assay Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15146057PubMed 17363900. Source: UniProtKB

structural constituent of nuclear pore

Inferred from mutant phenotype Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NUP133Q8WUM06EBI-295687,EBI-295695

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P57740-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P57740-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-63: MDRSGFGEIS...RTPSSFRQPF → MKILVILHQETRLSLELLAHFDSLVLSTNLLFIV
Note: No experimental confirmation available.
Isoform 3 (identifier: P57740-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.
     579-666: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 925925Nuclear pore complex protein Nup107
PRO_0000204831

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16
Modified residue41Phosphoserine Ref.14 Ref.16
Modified residue111Phosphoserine Ref.14 Ref.16
Modified residue371Phosphoserine Ref.12 Ref.14 Ref.15
Modified residue461Phosphothreonine Ref.11 Ref.14 Ref.15 Ref.16
Modified residue551Phosphothreonine Ref.14
Modified residue581Phosphoserine Ref.14
Modified residue641Phosphothreonine Ref.14
Modified residue691Phosphoserine Ref.14
Modified residue861Phosphoserine Ref.10 Ref.14 Ref.18

Natural variations

Alternative sequence1 – 151151Missing in isoform 3.
VSP_054262
Alternative sequence1 – 6363MDRSG…FRQPF → MKILVILHQETRLSLELLAH FDSLVLSTNLLFIV in isoform 2.
VSP_054263
Alternative sequence579 – 66688Missing in isoform 3.
VSP_054264

Experimental info

Sequence conflict8451Q → R in AAH43343. Ref.4

Secondary structure

............................. 925
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

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

FASTA925106,374
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5F39C26B982CE197
Show »

FASTA896103,175
Isoform 3 [UniParc].

Checksum: BC61E0588F57AA4B
Show »

FASTA68679,971

References

« Hide '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] (ISOFORM 1).
Tissue: Pancreatic cancer.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1 AND 3).
Tissue: Uterus.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"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.
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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].
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ295745 mRNA. Translation: CAC03716.1.
AK302773 mRNA. Translation: BAG63979.1.
AC090061 Genomic DNA. No translation available.
AC124890 Genomic DNA. No translation available.
BC017167 mRNA. Translation: AAH17167.1.
BC043343 mRNA. Translation: AAH43343.1.
CCDSCCDS8985.1.
RefSeqNP_065134.1. NM_020401.2. [P57740-1]
UniGeneHs.524574.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQCX-ray2.53A658-925[»]
3CQGX-ray3.00A658-771[»]
A802-925[»]
3I4RX-ray3.53A658-925[»]
ProteinModelPortalP57740.
SMRP57740. Positions 324-580, 667-924.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121386. 32 interactions.
IntActP57740. 9 interactions.
MINTMINT-3021765.
STRING9606.ENSP00000229179.

PTM databases

PhosphoSiteP57740.

Polymorphism databases

DMDM12230339.

Proteomic databases

MaxQBP57740.
PaxDbP57740.
PeptideAtlasP57740.
PRIDEP57740.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229179; ENSP00000229179; ENSG00000111581.
ENST00000378905; ENSP00000368185; ENSG00000111581.
ENST00000539906; ENSP00000441448; ENSG00000111581.
GeneID57122.
KEGGhsa:57122.
UCSCuc001suf.3. human. [P57740-1]

Organism-specific databases

CTD57122.
GeneCardsGC12P069080.
HGNCHGNC:29914. NUP107.
HPAHPA024141.
HPA031679.
MIM607617. gene.
neXtProtNX_P57740.
PharmGKBPA134890486.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258212.
HOGENOMHOG000006750.
HOVERGENHBG052677.
InParanoidP57740.
KOK14301.
OMAYLETNWT.
OrthoDBEOG773XFG.
PhylomeDBP57740.
TreeFamTF324259.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressP57740.
BgeeP57740.
CleanExHS_NUP107.
GenevestigatorP57740.

Family and domain databases

InterProIPR007252. Nup84_Nup100.
[Graphical view]
PANTHERPTHR13003. PTHR13003. 1 hit.
PfamPF04121. Nup84_Nup100. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP57740.
GeneWikiNUP107.
GenomeRNAi57122.
NextBio35476405.
PROP57740.
SOURCESearch...

Entry information

Entry nameNU107_HUMAN
AccessionPrimary (citable) accession number: P57740
Secondary accession number(s): B4DZ67, Q6PJE1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 12

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