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P57740

- NU107_HUMAN

UniProt

P57740 - NU107_HUMAN

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Protein

Nuclear pore complex protein Nup107

Gene

NUP107

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. nucleocytoplasmic transporter activity Source: UniProtKB
  2. structural constituent of nuclear pore Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cytokine-mediated signaling pathway Source: Reactome
  3. glucose transport Source: Reactome
  4. hexose transport Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. mitotic nuclear envelope disassembly Source: Reactome
  7. mRNA export from nucleus Source: UniProtKB
  8. nuclear pore complex assembly Source: UniProtKB
  9. protein transport Source: UniProtKB-KW
  10. regulation of glucose transport Source: Reactome
  11. small molecule metabolic process Source: Reactome
  12. transmembrane transport Source: Reactome
  13. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
REACT_682. Mitotic Prometaphase.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_9395. Nuclear import of Rev protein.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear pore complex protein Nup107
Alternative name(s):
107 kDa nucleoporin
Nucleoporin Nup107
Gene namesi
Name:NUP107
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:29914. NUP107.

Subcellular locationi

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.

GO - Cellular componenti

  1. centrosome Source: HPA
  2. cytosol Source: Reactome
  3. kinetochore Source: UniProtKB-KW
  4. membrane Source: UniProtKB
  5. nuclear envelope Source: Reactome
  6. nuclear membrane Source: UniProtKB
  7. nuclear periphery Source: UniProtKB
  8. nuclear pore Source: UniProtKB
  9. nuclear pore outer ring Source: UniProtKB
  10. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134890486.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 925925Nuclear pore complex protein Nup107PRO_0000204831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei4 – 41Phosphoserine2 Publications
Modified residuei11 – 111Phosphoserine2 Publications
Modified residuei37 – 371Phosphoserine3 Publications
Modified residuei46 – 461Phosphothreonine4 Publications
Modified residuei55 – 551Phosphothreonine1 Publication
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei64 – 641Phosphothreonine1 Publication
Modified residuei69 – 691Phosphoserine1 Publication
Modified residuei86 – 861Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP57740.
PaxDbiP57740.
PeptideAtlasiP57740.
PRIDEiP57740.

PTM databases

PhosphoSiteiP57740.

Expressioni

Gene expression databases

BgeeiP57740.
CleanExiHS_NUP107.
ExpressionAtlasiP57740. baseline and differential.
GenevestigatoriP57740.

Organism-specific databases

HPAiHPA024141.
HPA031679.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NUP133Q8WUM06EBI-295687,EBI-295695

Protein-protein interaction databases

BioGridi121386. 36 interactions.
IntActiP57740. 10 interactions.
MINTiMINT-3021765.
STRINGi9606.ENSP00000229179.

Structurei

Secondary structure

1
925
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi668 – 68013Combined sources
Helixi682 – 6843Combined sources
Helixi685 – 70117Combined sources
Helixi705 – 71410Combined sources
Helixi719 – 7235Combined sources
Helixi738 – 76730Combined sources
Helixi782 – 82140Combined sources
Turni824 – 8263Combined sources
Helixi840 – 86728Combined sources
Helixi871 – 8755Combined sources
Helixi877 – 8826Combined sources
Turni884 – 8863Combined sources
Helixi888 – 8914Combined sources
Helixi894 – 91219Combined sources
Turni913 – 9153Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQCX-ray2.53A658-925[»]
3CQGX-ray3.00A658-771[»]
A802-925[»]
3I4RX-ray3.53A658-925[»]
ProteinModelPortaliP57740.
SMRiP57740. Positions 324-580, 667-924.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP57740.

Family & Domainsi

Sequence similaritiesi

Belongs to the nucleoporin Nup84/Nup107 family.Curated

Phylogenomic databases

eggNOGiNOG258212.
GeneTreeiENSGT00390000012080.
HOGENOMiHOG000006750.
HOVERGENiHBG052677.
InParanoidiP57740.
KOiK14301.
OMAiYLETNWT.
OrthoDBiEOG773XFG.
PhylomeDBiP57740.
TreeFamiTF324259.

Family and domain databases

InterProiIPR007252. Nup84_Nup100.
[Graphical view]
PANTHERiPTHR13003. PTHR13003. 1 hit.
PfamiPF04121. Nup84_Nup100. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P57740-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDRSGFGEIS SPVIREAEVT RTARKQSAQK RVLLQASQDE NFGNTTPRNQ
60 70 80 90 100
VIPRTPSSFR QPFTPTSRSL LRQPDISCIL GTGGKSPRLT QSSGFFGNLS
110 120 130 140 150
MVTNLDDSNW AAAFSSQRSG LFTNTEPHSI TEDVTISAVM LREDDPGEAA
160 170 180 190 200
SMSMFSDFLQ SFLKHSSSTV FDLVEEYENI CGSQVNILSK IVSRATPGLQ
210 220 230 240 250
KFSKTASMLW LLQQEMVTWR LLASLYRDRI QSALEEESVF AVTAVNASEK
260 270 280 290 300
TVVEALFQRD SLVRQSQLVV DWLESIAKDE IGEFSDNIEF YAKSVYWENT
310 320 330 340 350
LHTLKQRQLT SYVGSVRPLV TELDPDAPIR QKMPLDDLDR EDEVRLLKYL
360 370 380 390 400
FTLIRAGMTE EAQRLCKRCG QAWRAATLEG WKLYHDPNVN GGTELEPVEG
410 420 430 440 450
NPYRRIWKIS CWRMAEDELF NRYERAIYAA LSGNLKQLLP VCDTWEDTVW
460 470 480 490 500
AYFRVMVDSL VEQEIQTSVA TLDETEELPR EYLGANWTLE KVFEELQATD
510 520 530 540 550
KKRVLEENQE HYHIVQKFLI LGDIDGLMDE FSKWLSKSRN NLPGHLLRFM
560 570 580 590 600
THLILFFRTL GLQTKEEVSI EVLKTYIQLL IREKHTNLIA FYTCHLPQDL
610 620 630 640 650
AVAQYALFLE SVTEFEQRHH CLELAKEADL DVATITKTVV ENIRKKDNGE
660 670 680 690 700
FSHHDLAPAL DTGTTEEDRL KIDVIDWLVF DPAQRAEALK QGNAIMRKFL
710 720 730 740 750
ASKKHEAAKE VFVKIPQDSI AEIYNQCEEQ GMESPLPAED DNAIREHLCI
760 770 780 790 800
RAYLEAHETF NEWFKHMNSV PQKPALIPQP TFTEKVAHEH KEKKYEMDFG
810 820 830 840 850
IWKGHLDALT ADVKEKMYNV LLFVDGGWMV DVREDAKEDH ERTHQMVLLR
860 870 880 890 900
KLCLPMLCFL LHTILHSTGQ YQECLQLADM VSSERHKLYL VFSKEELRKL
910 920
LQKLRESSLM LLDQGLDPLG YEIQL
Length:925
Mass (Da):106,374
Last modified:January 11, 2001 - v1
Checksum:iCE1E4DA6C832A5A5
GO
Isoform 2 (identifier: P57740-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-63: MDRSGFGEIS...RTPSSFRQPF → MKILVILHQETRLSLELLAHFDSLVLSTNLLFIV

Note: No experimental confirmation available.

Show »
Length:896
Mass (Da):103,175
Checksum:i5F39C26B982CE197
GO
Isoform 3 (identifier: P57740-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.
     579-666: Missing.

Note: No experimental confirmation available.

Show »
Length:686
Mass (Da):79,971
Checksum:iBC61E0588F57AA4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti845 – 8451Q → R in AAH43343. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 151151Missing in isoform 3. 1 PublicationVSP_054262Add
BLAST
Alternative sequencei1 – 6363MDRSG…FRQPF → MKILVILHQETRLSLELLAH FDSLVLSTNLLFIV in isoform 2. 1 PublicationVSP_054263Add
BLAST
Alternative sequencei579 – 66688Missing in isoform 3. 1 PublicationVSP_054264Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8985.1. [P57740-1]
RefSeqiNP_065134.1. NM_020401.2. [P57740-1]
UniGeneiHs.524574.

Genome annotation databases

EnsembliENST00000229179; ENSP00000229179; ENSG00000111581. [P57740-1]
ENST00000378905; ENSP00000368185; ENSG00000111581. [P57740-3]
ENST00000539906; ENSP00000441448; ENSG00000111581. [P57740-2]
GeneIDi57122.
KEGGihsa:57122.
UCSCiuc001suf.3. human. [P57740-1]
uc001sug.3. human.
uc010stj.2. human.

Polymorphism databases

DMDMi12230339.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS8985.1. [P57740-1 ]
RefSeqi NP_065134.1. NM_020401.2. [P57740-1 ]
UniGenei Hs.524574.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CQC X-ray 2.53 A 658-925 [» ]
3CQG X-ray 3.00 A 658-771 [» ]
A 802-925 [» ]
3I4R X-ray 3.53 A 658-925 [» ]
ProteinModelPortali P57740.
SMRi P57740. Positions 324-580, 667-924.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121386. 36 interactions.
IntActi P57740. 10 interactions.
MINTi MINT-3021765.
STRINGi 9606.ENSP00000229179.

PTM databases

PhosphoSitei P57740.

Polymorphism databases

DMDMi 12230339.

Proteomic databases

MaxQBi P57740.
PaxDbi P57740.
PeptideAtlasi P57740.
PRIDEi P57740.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229179 ; ENSP00000229179 ; ENSG00000111581 . [P57740-1 ]
ENST00000378905 ; ENSP00000368185 ; ENSG00000111581 . [P57740-3 ]
ENST00000539906 ; ENSP00000441448 ; ENSG00000111581 . [P57740-2 ]
GeneIDi 57122.
KEGGi hsa:57122.
UCSCi uc001suf.3. human. [P57740-1 ]
uc001sug.3. human.
uc010stj.2. human.

Organism-specific databases

CTDi 57122.
GeneCardsi GC12P069080.
HGNCi HGNC:29914. NUP107.
HPAi HPA024141.
HPA031679.
MIMi 607617. gene.
neXtProti NX_P57740.
PharmGKBi PA134890486.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258212.
GeneTreei ENSGT00390000012080.
HOGENOMi HOG000006750.
HOVERGENi HBG052677.
InParanoidi P57740.
KOi K14301.
OMAi YLETNWT.
OrthoDBi EOG773XFG.
PhylomeDBi P57740.
TreeFami TF324259.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
REACT_682. Mitotic Prometaphase.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_9395. Nuclear import of Rev protein.

Miscellaneous databases

ChiTaRSi NUP107. human.
EvolutionaryTracei P57740.
GeneWikii NUP107.
GenomeRNAii 57122.
NextBioi 35476405.
PROi P57740.
SOURCEi Search...

Gene expression databases

Bgeei P57740.
CleanExi HS_NUP107.
ExpressionAtlasi P57740. baseline and differential.
Genevestigatori P57740.

Family and domain databases

InterProi IPR007252. Nup84_Nup100.
[Graphical view ]
PANTHERi PTHR13003. PTHR13003. 1 hit.
Pfami PF04121. Nup84_Nup100. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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].

Entry informationi

Entry nameiNU107_HUMAN
AccessioniPrimary (citable) accession number: P57740
Secondary accession number(s): B4DZ67, Q6PJE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: November 26, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3