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P37198

- NUP62_HUMAN

UniProt

P37198 - NUP62_HUMAN

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Protein

Nuclear pore glycoprotein p62

Gene

NUP62

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

Functioni

Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is probably involved in protein-protein interaction via coiled-coil formation and may function in anchorage of p62 to the pore complex.

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. receptor signaling complex scaffold activity Source: UniProtKB
  3. SH2 domain binding Source: UniProtKB
  4. structural constituent of nuclear pore Source: InterPro
  5. thyroid hormone receptor binding Source: UniProtKB
  6. ubiquitin binding Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cell aging Source: Ensembl
  3. cell death Source: UniProtKB
  4. cell surface receptor signaling pathway Source: UniProtKB
  5. cytokine-mediated signaling pathway Source: Reactome
  6. glucose transport Source: Reactome
  7. hexose transport Source: Reactome
  8. hormone-mediated signaling pathway Source: UniProtKB
  9. mitotic cell cycle Source: Reactome
  10. mitotic nuclear envelope disassembly Source: Reactome
  11. mRNA transport Source: UniProtKB-KW
  12. negative regulation of apoptotic process Source: UniProtKB
  13. negative regulation of cell proliferation Source: UniProtKB
  14. negative regulation of epidermal growth factor receptor signaling pathway Source: Ensembl
  15. negative regulation of MAP kinase activity Source: Ensembl
  16. negative regulation of programmed cell death Source: UniProtKB
  17. negative regulation of Ras protein signal transduction Source: Ensembl
  18. nucleocytoplasmic transport Source: GOC
  19. positive regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  20. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  21. positive regulation of transcription, DNA-templated Source: UniProtKB
  22. protein transport Source: UniProtKB-KW
  23. regulation of glucose transport Source: Reactome
  24. regulation of Ras protein signal transduction Source: UniProtKB
  25. regulation of signal transduction Source: UniProtKB
  26. small molecule metabolic process Source: Reactome
  27. transcription, DNA-templated Source: UniProtKB
  28. transmembrane transport Source: Reactome
  29. 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_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_7991. Vpr-mediated nuclear import of PICs.
REACT_9395. Nuclear import of Rev protein.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear pore glycoprotein p62
Alternative name(s):
62 kDa nucleoporin
Nucleoporin Nup62
Gene namesi
Name:NUP62
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:8066. NUP62.

Subcellular locationi

Nucleusnuclear pore complex. Cytoplasmcytoskeletonspindle pole
Note: Central region of the nuclear pore, within the transporter. During mitotic cell division, it associates with the poles of the mitotic spindle.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. intracellular membrane-bounded organelle Source: HPA
  4. nuclear envelope Source: UniProtKB
  5. nuclear membrane Source: HPA
  6. nuclear pore Source: UniProtKB
  7. nucleocytoplasmic shuttling complex Source: UniProtKB
  8. pore complex Source: UniProtKB
  9. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nuclear pore complex, Nucleus

Pathology & Biotechi

Involvement in diseasei

Infantile striatonigral degeneration (SNDI) [MIM:271930]: Neurological disorder characterized by symmetrical degeneration of the caudate nucleus, putamen, and occasionally the globus pallidus, with little involvement of the rest of the brain. The clinical features include developmental regression, choreoathetosis, dystonia, spasticity, dysphagia, failure to thrive, nystagmus, optic atrophy, and mental retardation.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti391 – 3911Q → P in SNDI. 1 Publication
VAR_034904

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi271930. phenotype.
Orphaneti225154. Familial infantile bilateral striatal necrosis.
PharmGKBiPA31854.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 522521Nuclear pore glycoprotein p62PRO_0000204880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Glycosylationi373 – 3731O-linked (GlcNAc)By similarity
Modified residuei408 – 4081Phosphoserine2 Publications
Glycosylationi468 – 4681O-linked (GlcNAc)By similarity
Disulfide bondi475 – 475Interchain (with NUP155)By similarity
Disulfide bondi506 – 506Interchain (with NUP155)By similarity

Post-translational modificationi

O-glycosylated. Contains about 10 N-acetylglucosamine side chain sites predicted for the entire protein, amongst which only one in the C-terminal.
The the inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP37198.
PaxDbiP37198.
PRIDEiP37198.

PTM databases

PhosphoSiteiP37198.
UniCarbKBiP37198.

Expressioni

Gene expression databases

BgeeiP37198.
CleanExiHS_NUP62.
ExpressionAtlasiP37198. baseline and differential.
GenevestigatoriP37198.

Organism-specific databases

HPAiCAB020724.
HPA005435.

Interactioni

Subunit structurei

Component of the p62 complex, a complex at least composed of NUP62, NUP54, and NUPL1 (By similarity). Interacts with C11orf73/Hikeshi.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ATXN7O152652EBI-347978,EBI-708350
NXF1Q9UBU93EBI-347978,EBI-398874
UL54P102383EBI-347978,EBI-6883946From a different organism.

Protein-protein interaction databases

BioGridi117165. 49 interactions.
DIPiDIP-29749N.
IntActiP37198. 32 interactions.
MINTiMINT-121394.
STRINGi9606.ENSP00000305503.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H4Dmodel-A1-522[»]
ProteinModelPortaliP37198.
SMRiP37198. Positions 361-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati2 – 981
Repeati13 – 2192
Repeati29 – 3793
Repeati39 – 4794
Repeati57 – 6595
Repeati71 – 7996
Repeati85 – 9397
Repeati111 – 11998
Repeati137 – 14599
Repeati155 – 163910
Repeati168 – 176911
Repeati185 – 193912
Repeati234 – 242913
Repeati253 – 261914
Repeati287 – 295915

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 29529415 X 9 AA approximate repeatsAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili328 – 458131Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 288280Thr-richAdd
BLAST
Compositional biasi176 – 331156Ala-richAdd
BLAST

Domaini

Contains F-X-F-G repeats.

Sequence similaritiesi

Belongs to the nucleoporin NSP1/NUP62 family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00730000111010.
HOGENOMiHOG000007693.
HOVERGENiHBG052699.
InParanoidiP37198.
KOiK14306.
OMAiPAMTYAQ.
OrthoDBiEOG7PZRZB.
PhylomeDBiP37198.
TreeFamiTF324795.

Family and domain databases

InterProiIPR026010. NSP1/NUP62.
IPR007758. Nucleoporin_NSP1_C.
[Graphical view]
PANTHERiPTHR12084. PTHR12084. 1 hit.
PfamiPF05064. Nsp1_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37198-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGFNFGGTG APTGGFTFGT AKTATTTPAT GFSFSTSGTG GFNFGAPFQP
60 70 80 90 100
ATSTPSTGLF SLATQTPATQ TTGFTFGTAT LASGGTGFSL GIGASKLNLS
110 120 130 140 150
NTAATPAMAN PSGFGLGSSN LTNAISSTVT SSQGTAPTGF VFGPSTTSVA
160 170 180 190 200
PATTSGGFSF TGGSTAQPSG FNIGSAGNSA QPTAPATLPF TPATPAATTA
210 220 230 240 250
GATQPAAPTP TATITSTGPS LFASIATAPT SSATTGLSLC TPVTTAGAPT
260 270 280 290 300
AGTQGFSLKA PGAASGTSTT TSTAATATAT TTSSSSTTGF ALNLKPLAPA
310 320 330 340 350
GIPSNTAAAV TAPPGPGAAA GAAASSAMTY AQLESLINKW SLELEDQERH
360 370 380 390 400
FLQQATQVNA WDRTLIENGE KITSLHREVE KVKLDQKRLD QELDFILSQQ
410 420 430 440 450
KELEDLLSPL EELVKEQSGT IYLQHADEER EKTYKLAENI DAQLKRMAQD
460 470 480 490 500
LKDIIEHLNT SGAPADTSDP LQQICKILNA HMDSLQWIDQ NSALLQRKVE
510 520
EVTKVCEGRR KEQERSFRIT FD
Length:522
Mass (Da):53,255
Last modified:March 20, 2007 - v3
Checksum:i1FF65018452719A3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti418 – 4192SG → RA in CAA41411. (PubMed:1915414)Curated
Sequence conflicti431 – 4311E → Q in CAA41411. (PubMed:1915414)Curated
Sequence conflicti507 – 5071E → V in CAA41411. (PubMed:1915414)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti139 – 1391G → S.
Corresponds to variant rs3745489 [ dbSNP | Ensembl ].
VAR_028064
Natural varianti233 – 2331A → S.
Corresponds to variant rs2290772 [ dbSNP | Ensembl ].
VAR_013467
Natural varianti283 – 2831S → T.3 Publications
Corresponds to variant rs1062798 [ dbSNP | Ensembl ].
VAR_028065
Natural varianti391 – 3911Q → P in SNDI. 1 Publication
VAR_034904

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58521 mRNA. Translation: CAA41411.1.
AL162061 mRNA. Translation: CAB82399.1.
AK125857 mRNA. Translation: BAG54257.1.
CR541721 mRNA. Translation: CAG46522.1.
AC011452 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52576.1.
BC003663 mRNA. Translation: AAH03663.1.
BC014842 mRNA. Translation: AAH14842.1.
BC050717 mRNA. Translation: AAH50717.1.
BC095410 mRNA. Translation: AAH95410.1.
BC101104 mRNA. Translation: AAI01105.1.
BC101105 mRNA. Translation: AAI01106.1.
BC101106 mRNA. Translation: AAI01107.1.
BC101107 mRNA. Translation: AAI01108.1.
CCDSiCCDS12788.1.
PIRiS41819.
RefSeqiNP_001180286.1. NM_001193357.1.
NP_036478.2. NM_012346.4.
NP_057637.2. NM_016553.4.
NP_714940.1. NM_153718.3.
NP_714941.1. NM_153719.3.
UniGeneiHs.574492.

Genome annotation databases

EnsembliENST00000352066; ENSP00000305503; ENSG00000213024.
ENST00000422090; ENSP00000407331; ENSG00000213024.
ENST00000596217; ENSP00000471191; ENSG00000213024.
ENST00000597029; ENSP00000473192; ENSG00000213024.
GeneIDi23636.
KEGGihsa:23636.
UCSCiuc002pqx.3. human.

Polymorphism databases

DMDMi134047855.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58521 mRNA. Translation: CAA41411.1 .
AL162061 mRNA. Translation: CAB82399.1 .
AK125857 mRNA. Translation: BAG54257.1 .
CR541721 mRNA. Translation: CAG46522.1 .
AC011452 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52576.1 .
BC003663 mRNA. Translation: AAH03663.1 .
BC014842 mRNA. Translation: AAH14842.1 .
BC050717 mRNA. Translation: AAH50717.1 .
BC095410 mRNA. Translation: AAH95410.1 .
BC101104 mRNA. Translation: AAI01105.1 .
BC101105 mRNA. Translation: AAI01106.1 .
BC101106 mRNA. Translation: AAI01107.1 .
BC101107 mRNA. Translation: AAI01108.1 .
CCDSi CCDS12788.1.
PIRi S41819.
RefSeqi NP_001180286.1. NM_001193357.1.
NP_036478.2. NM_012346.4.
NP_057637.2. NM_016553.4.
NP_714940.1. NM_153718.3.
NP_714941.1. NM_153719.3.
UniGenei Hs.574492.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2H4D model - A 1-522 [» ]
ProteinModelPortali P37198.
SMRi P37198. Positions 361-416.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117165. 49 interactions.
DIPi DIP-29749N.
IntActi P37198. 32 interactions.
MINTi MINT-121394.
STRINGi 9606.ENSP00000305503.

PTM databases

PhosphoSitei P37198.
UniCarbKBi P37198.

Polymorphism databases

DMDMi 134047855.

Proteomic databases

MaxQBi P37198.
PaxDbi P37198.
PRIDEi P37198.

Protocols and materials databases

DNASUi 23636.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000352066 ; ENSP00000305503 ; ENSG00000213024 .
ENST00000422090 ; ENSP00000407331 ; ENSG00000213024 .
ENST00000596217 ; ENSP00000471191 ; ENSG00000213024 .
ENST00000597029 ; ENSP00000473192 ; ENSG00000213024 .
GeneIDi 23636.
KEGGi hsa:23636.
UCSCi uc002pqx.3. human.

Organism-specific databases

CTDi 23636.
GeneCardsi GC19M050410.
H-InvDB HIX0016974.
HGNCi HGNC:8066. NUP62.
HPAi CAB020724.
HPA005435.
MIMi 271930. phenotype.
605815. gene.
neXtProti NX_P37198.
Orphaneti 225154. Familial infantile bilateral striatal necrosis.
PharmGKBi PA31854.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00730000111010.
HOGENOMi HOG000007693.
HOVERGENi HBG052699.
InParanoidi P37198.
KOi K14306.
OMAi PAMTYAQ.
OrthoDBi EOG7PZRZB.
PhylomeDBi P37198.
TreeFami TF324795.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
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_7991. Vpr-mediated nuclear import of PICs.
REACT_9395. Nuclear import of Rev protein.

Miscellaneous databases

GeneWikii Nucleoporin_62.
GenomeRNAii 23636.
NextBioi 46419.
PROi P37198.
SOURCEi Search...

Gene expression databases

Bgeei P37198.
CleanExi HS_NUP62.
ExpressionAtlasi P37198. baseline and differential.
Genevestigatori P37198.

Family and domain databases

InterProi IPR026010. NSP1/NUP62.
IPR007758. Nucleoporin_NSP1_C.
[Graphical view ]
PANTHERi PTHR12084. PTHR12084. 1 hit.
Pfami PF05064. Nsp1_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization."
    Carmo-Fonseca M., Kern H., Hurt E.C.
    Eur. J. Cell Biol. 55:17-30(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-283.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-283.
    Tissue: Brain.
  3. "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].
    Tissue: Testis.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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], VARIANT THR-283.
    Tissue: Pancreas, Skin and Urinary bladder.
  8. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "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-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Hikeshi, a nuclear import carrier for hsp70s, protects cells from heat shock-induced nuclear damage."
    Kose S., Furuta M., Imamoto N.
    Cell 149:578-589(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C11ORF73.
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: VARIANT SNDI PRO-391.

Entry informationi

Entry nameiNUP62_HUMAN
AccessioniPrimary (citable) accession number: P37198
Secondary accession number(s): B3KWU5
, Q503A4, Q6GTM2, Q96C43, Q9NSL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: March 20, 2007
Last modified: November 26, 2014
This is version 157 of the entry and version 3 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3