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Nuclear pore glycoprotein p62 (62 kDa nucleoporin) (Nucleoporin Nup62)

 NUP62_HUMAN             Reviewed;         522 AA.
P37198; B3KWU5; Q503A4; Q6GTM2; Q96C43; Q9NSL1;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 3.
27-SEP-2017, entry version 187.
RecName: Full=Nuclear pore glycoprotein p62;
AltName: Full=62 kDa nucleoporin;
AltName: Full=Nucleoporin Nup62;
Name=NUP62;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
VARIANT THR-283.
PubMed=1915414;
Carmo-Fonseca M., Kern H., Hurt E.C.;
"Human nucleoporin p62 and the essential yeast nuclear pore protein
NSP1 show sequence homology and a similar domain organization.";
Eur. J. Cell Biol. 55:17-30(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-283.
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-283.
TISSUE=Pancreas, Skin, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH CAPG.
PubMed=18266911; DOI=10.1111/j.1600-0854.2008.00720.x;
Van Impe K., Hubert T., De Corte V., Vanloo B., Boucherie C.,
Vandekerckhove J., Gettemans J.;
"A new role for nuclear transport factor 2 and Ran: nuclear import of
CapG.";
Traffic 9:695-707(2008).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
INTERACTION WITH OSBPL8.
PubMed=21698267; DOI=10.1371/journal.pone.0021078;
Zhou T., Li S., Zhong W., Vihervaara T., Beaslas O., Perttila J.,
Luo W., Jiang Y., Lehto M., Olkkonen V.M., Yan D.;
"OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid
levels and interacts with the nucleoporin Nup62.";
PLoS ONE 6:E21078-E21078(2011).
[14]
INTERACTION WITH HIKESHI.
PubMed=22541429; DOI=10.1016/j.cell.2012.02.058;
Kose S., Furuta M., Imamoto N.;
"Hikeshi, a nuclear import carrier for hsp70s, protects cells from
heat shock-induced nuclear damage.";
Cell 149:578-589(2012).
[15]
INTERACTION WITH EPSTEIN-BARR VIRUS BGLF4.
PubMed=22623767; DOI=10.1128/JVI.01058-12;
Chang C.W., Lee C.P., Huang Y.H., Yang P.W., Wang J.T., Chen M.R.;
"Epstein-Barr virus protein kinase BGLF4 targets the nucleus through
interaction with nucleoporins.";
J. Virol. 86:8072-8085(2012).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
FUNCTION, INTERACTION WITH SAS6 AND TUBG1, AND SUBCELLULAR LOCATION.
PubMed=24107630; DOI=10.4161/cc.26671;
Hashizume C., Moyori A., Kobayashi A., Yamakoshi N., Endo A.,
Wong R.W.;
"Nucleoporin Nup62 maintains centrosome homeostasis.";
Cell Cycle 12:3804-3816(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-418, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
VARIANT SNDI PRO-391.
PubMed=16786527; DOI=10.1002/ana.20902;
Basel-Vanagaite L., Muncher L., Straussberg R., Pasmanik-Chor M.,
Yahav M., Rainshtein L., Walsh C.A., Magal N., Taub E., Drasinover V.,
Shalev H., Attia R., Rechavi G., Simon A.J., Shohat M.;
"Mutated nup62 causes autosomal recessive infantile bilateral striatal
necrosis.";
Ann. Neurol. 60:214-222(2006).
-!- FUNCTION: Essential component of the nuclear pore complex
(PubMed:1915414). The N-terminal is probably involved in
nucleocytoplasmic transport (PubMed:1915414). The C-terminal is
involved in protein-protein interaction probably via coiled-coil
formation, promotes its association with centrosomes and may
function in anchorage of p62 to the pore complex (PubMed:1915414,
PubMed:24107630). Plays a role in mitotic cell cycle progression
by regulating centrosome segregation, centriole maturation and
spindle orientation (PubMed:24107630). It might be involved in
protein recruitment to the centrosome after nuclear breakdown
(PubMed:24107630). {ECO:0000269|PubMed:1915414,
ECO:0000269|PubMed:24107630}.
-!- SUBUNIT: Component of the p62 complex, a complex at least composed
of NUP62, NUP54, and NUP58 (By similarity). Interacts with NUTF2
(By similarity). Interacts with HIKESHI (PubMed:22541429).
Interacts with OSBPL8 (PubMed:21698267). Interacts with CAPG
(PubMed:18266911). Interacts with SAS6 and TUBG1 at the centrosome
(PubMed:24107630). {ECO:0000250|UniProtKB:P17955,
ECO:0000269|PubMed:18266911, ECO:0000269|PubMed:21698267,
ECO:0000269|PubMed:22541429, ECO:0000269|PubMed:24107630}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-barr virus
BGLF4; this interaction allows BGLF4 nuclear entry.
{ECO:0000269|PubMed:22623767}.
-!- INTERACTION:
Q9H614:-; NbExp=3; IntAct=EBI-347978, EBI-10249899;
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-347978, EBI-743598;
Q13444:ADAM15; NbExp=3; IntAct=EBI-347978, EBI-77818;
Q8TD06:AGR3; NbExp=5; IntAct=EBI-347978, EBI-3925742;
O15265:ATXN7; NbExp=2; IntAct=EBI-347978, EBI-708350;
Q12934:BFSP1; NbExp=3; IntAct=EBI-347978, EBI-10227494;
Q9UL45:BLOC1S6; NbExp=5; IntAct=EBI-347978, EBI-465781;
Q8TAB5:C1orf216; NbExp=5; IntAct=EBI-347978, EBI-747505;
P53829:CAF40 (xeno); NbExp=3; IntAct=EBI-347978, EBI-28306;
Q6ZUS5:CCDC121; NbExp=4; IntAct=EBI-347978, EBI-2836982;
Q8IYE0:CCDC146; NbExp=4; IntAct=EBI-347978, EBI-10749669;
Q8IYE0-2:CCDC146; NbExp=3; IntAct=EBI-347978, EBI-10247802;
Q8NCX0:CCDC150; NbExp=3; IntAct=EBI-347978, EBI-10269342;
Q494R4:CCDC153; NbExp=3; IntAct=EBI-347978, EBI-10241443;
Q8TD31-3:CCHCR1; NbExp=5; IntAct=EBI-347978, EBI-10175300;
P31384:CCR4 (xeno); NbExp=3; IntAct=EBI-347978, EBI-4396;
Q71F23:CENPU; NbExp=3; IntAct=EBI-347978, EBI-2515234;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-347978, EBI-10181988;
Q9UGL9:CRCT1; NbExp=5; IntAct=EBI-347978, EBI-713677;
O60941:DTNB; NbExp=4; IntAct=EBI-347978, EBI-740402;
P05413:FABP3; NbExp=6; IntAct=EBI-347978, EBI-704216;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-347978, EBI-2514791;
A0A024R8L2:hCG_1987119; NbExp=4; IntAct=EBI-347978, EBI-14103818;
Q03933:HSF2; NbExp=3; IntAct=EBI-347978, EBI-2556750;
Q03933-2:HSF2; NbExp=3; IntAct=EBI-347978, EBI-10223348;
Q8IY31:IFT20; NbExp=3; IntAct=EBI-347978, EBI-744203;
Q70UQ0:IKBIP; NbExp=3; IntAct=EBI-347978, EBI-2557212;
Q9H1K1:ISCU; NbExp=5; IntAct=EBI-347978, EBI-1047335;
Q7Z3B3:KANSL1; NbExp=4; IntAct=EBI-347978, EBI-740244;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-347978, EBI-2125614;
Q5THT1:KLHL32; NbExp=3; IntAct=EBI-347978, EBI-10247181;
P52292:KPNA2; NbExp=3; IntAct=EBI-347978, EBI-349938;
P04264:KRT1; NbExp=6; IntAct=EBI-347978, EBI-298429;
P35900:KRT20; NbExp=5; IntAct=EBI-347978, EBI-742094;
P25791:LMO2; NbExp=3; IntAct=EBI-347978, EBI-739696;
Q7Z3B4:NUP54; NbExp=8; IntAct=EBI-347978, EBI-741048;
P48837:NUP57 (xeno); NbExp=3; IntAct=EBI-347978, EBI-12324;
Q9BVL2:NUP58; NbExp=5; IntAct=EBI-347978, EBI-2811583;
P40368:NUP82 (xeno); NbExp=3; IntAct=EBI-347978, EBI-12331;
P61970:NUTF2; NbExp=5; IntAct=EBI-347978, EBI-591778;
Q9UBU9:NXF1; NbExp=9; IntAct=EBI-347978, EBI-398874;
O43482:OIP5; NbExp=5; IntAct=EBI-347978, EBI-536879;
E5LBS6:ORF10 (xeno); NbExp=2; IntAct=EBI-347978, EBI-14033439;
Q96BD5:PHF21A; NbExp=5; IntAct=EBI-347978, EBI-745085;
Q13526:PIN1; NbExp=5; IntAct=EBI-347978, EBI-714158;
Q969G3:SMARCE1; NbExp=3; IntAct=EBI-347978, EBI-455078;
O75971:SNAPC5; NbExp=3; IntAct=EBI-347978, EBI-749483;
P48232:SNN1 (xeno); NbExp=3; IntAct=EBI-347978, EBI-28775;
P40014:SPC25 (xeno); NbExp=3; IntAct=EBI-347978, EBI-22458;
A1L4H1:SSC5D; NbExp=5; IntAct=EBI-347978, EBI-10172867;
P51687:SUOX; NbExp=5; IntAct=EBI-347978, EBI-3921347;
Q06707:SWC7 (xeno); NbExp=3; IntAct=EBI-347978, EBI-32671;
Q9NVV9:THAP1; NbExp=11; IntAct=EBI-347978, EBI-741515;
P40222:TXLNA; NbExp=5; IntAct=EBI-347978, EBI-359793;
P10238:UL54 (xeno); NbExp=3; IntAct=EBI-347978, EBI-6883946;
Q9Y3C0:WASHC3; NbExp=7; IntAct=EBI-347978, EBI-712969;
Q96QU8-2:XPO6; NbExp=3; IntAct=EBI-347978, EBI-10293124;
Q02831:YPL077C (xeno); NbExp=3; IntAct=EBI-347978, EBI-31828;
-!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
{ECO:0000269|PubMed:1915414}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000269|PubMed:24107630}. Nucleus envelope
{ECO:0000269|PubMed:24107630}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000269|PubMed:24107630}. Note=Central region of the nuclear
pore, within the transporter (PubMed:1915414). During mitotic cell
division, it associates with the poles of the mitotic spindle
(PubMed:24107630). {ECO:0000269|PubMed:1915414,
ECO:0000269|PubMed:24107630}.
-!- DOMAIN: Contains FG repeats.
-!- PTM: O-glycosylated. Contains about 10 N-acetylglucosamine side
chain sites predicted for the entire protein, among which only one
in the C-terminal. {ECO:0000305}.
-!- PTM: 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. {ECO:0000250}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:16786527}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the nucleoporin NSP1/NUP62 family.
{ECO:0000305}.
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EMBL; X58521; CAA41411.1; -; mRNA.
EMBL; AL162061; CAB82399.1; -; mRNA.
EMBL; AK125857; BAG54257.1; -; mRNA.
EMBL; CR541721; CAG46522.1; -; mRNA.
EMBL; AC011452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471177; EAW52576.1; -; Genomic_DNA.
EMBL; BC003663; AAH03663.1; -; mRNA.
EMBL; BC014842; AAH14842.1; -; mRNA.
EMBL; BC050717; AAH50717.1; -; mRNA.
EMBL; BC095410; AAH95410.1; -; mRNA.
EMBL; BC101104; AAI01105.1; -; mRNA.
EMBL; BC101105; AAI01106.1; -; mRNA.
EMBL; BC101106; AAI01107.1; -; mRNA.
EMBL; BC101107; AAI01108.1; -; mRNA.
CCDS; CCDS12788.1; -.
PIR; S41819; S41819.
RefSeq; NP_001180286.1; NM_001193357.1.
RefSeq; NP_036478.2; NM_012346.4.
RefSeq; NP_057637.2; NM_016553.4.
RefSeq; NP_714940.1; NM_153718.3.
RefSeq; NP_714941.1; NM_153719.3.
UniGene; Hs.574492; -.
PDB; 2H4D; Model; -; A=1-522.
PDB; 5IJN; EM; 21.40 A; H/N/T/Z=1-522.
PDB; 5IJO; EM; 21.40 A; H/N/T/Z=1-522.
PDBsum; 2H4D; -.
PDBsum; 5IJN; -.
PDBsum; 5IJO; -.
ProteinModelPortal; P37198; -.
SMR; P37198; -.
BioGrid; 117165; 168.
DIP; DIP-29749N; -.
IntAct; P37198; 106.
MINT; MINT-121394; -.
STRING; 9606.ENSP00000305503; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P37198; -.
PhosphoSitePlus; P37198; -.
UniCarbKB; P37198; -.
BioMuta; NUP62; -.
DMDM; 134047855; -.
EPD; P37198; -.
MaxQB; P37198; -.
PaxDb; P37198; -.
PeptideAtlas; P37198; -.
PRIDE; P37198; -.
DNASU; 23636; -.
Ensembl; ENST00000352066; ENSP00000305503; ENSG00000213024.
Ensembl; ENST00000422090; ENSP00000407331; ENSG00000213024.
Ensembl; ENST00000596217; ENSP00000471191; ENSG00000213024.
Ensembl; ENST00000597029; ENSP00000473192; ENSG00000213024.
GeneID; 23636; -.
KEGG; hsa:23636; -.
UCSC; uc002pqy.5; human.
CTD; 23636; -.
DisGeNET; 23636; -.
EuPathDB; HostDB:ENSG00000213024.11; -.
GeneCards; NUP62; -.
H-InvDB; HIX0016974; -.
HGNC; HGNC:8066; NUP62.
HPA; CAB020724; -.
HPA; HPA005435; -.
MalaCards; NUP62; -.
MIM; 271930; phenotype.
MIM; 605815; gene.
neXtProt; NX_P37198; -.
OpenTargets; ENSG00000213024; -.
Orphanet; 225154; Familial infantile bilateral striatal necrosis.
PharmGKB; PA31854; -.
eggNOG; KOG2196; Eukaryota.
eggNOG; ENOG410XT5X; LUCA.
GeneTree; ENSGT00730000111010; -.
HOGENOM; HOG000007693; -.
HOVERGEN; HBG052699; -.
InParanoid; P37198; -.
KO; K14306; -.
OMA; DEMMSKQ; -.
OrthoDB; EOG091G0KV9; -.
PhylomeDB; P37198; -.
TreeFam; TF324795; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
Reactome; R-HSA-180746; Nuclear import of Rev protein.
Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
Reactome; R-HSA-191859; snRNP Assembly.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-6784531; tRNA processing in the nucleus.
GeneWiki; Nucleoporin_62; -.
GenomeRNAi; 23636; -.
PRO; PR:P37198; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000213024; -.
CleanEx; HS_NUP62; -.
ExpressionAtlas; P37198; baseline and differential.
Genevisible; P37198; HS.
GO; GO:0005642; C:annulate lamellae; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
GO; GO:0005487; F:nucleocytoplasmic transporter activity; IBA:GO_Central.
GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
GO; GO:0051425; F:PTB domain binding; IEA:Ensembl.
GO; GO:0030159; F:receptor signaling complex scaffold activity; IDA:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
GO; GO:0046966; F:thyroid hormone receptor binding; IPI:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
GO; GO:0007569; P:cell aging; IEA:Ensembl.
GO; GO:0008219; P:cell death; IMP:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
GO; GO:0098534; P:centriole assembly; IMP:UniProtKB.
GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
GO; GO:0009755; P:hormone-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0007100; P:mitotic centrosome separation; IMP:UniProtKB.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0043069; P:negative regulation of programmed cell death; IDA:UniProtKB.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:Ensembl.
GO; GO:0046601; P:positive regulation of centriole replication; IMP:UniProtKB.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; NAS:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; IMP:UniProtKB.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:UniProtKB.
GO; GO:1904781; P:positive regulation of protein localization to centrosome; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl.
GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:0006110; P:regulation of glycolytic process; TAS:Reactome.
GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
GO; GO:0042306; P:regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:0046578; P:regulation of Ras protein signal transduction; NAS:UniProtKB.
GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB.
GO; GO:0071426; P:ribonucleoprotein complex export from nucleus; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006409; P:tRNA export from nucleus; TAS:Reactome.
GO; GO:0016032; P:viral process; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
InterPro; IPR026010; NSP1/NUP62.
InterPro; IPR007758; Nucleoporin_NSP1_C.
InterPro; IPR033072; NUP62_met.
PANTHER; PTHR12084; PTHR12084; 1.
PANTHER; PTHR12084:SF6; PTHR12084:SF6; 1.
Pfam; PF05064; Nsp1_C; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Disease mutation; Disulfide bond; Glycoprotein;
Host-virus interaction; mRNA transport; Nuclear pore complex; Nucleus;
Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
Repeat; Translocation; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 522 Nuclear pore glycoprotein p62.
/FTId=PRO_0000204880.
REPEAT 6 7 1.
REPEAT 44 45 2.
REPEAT 76 77 3.
REPEAT 114 115 4.
REPEAT 142 143 5.
REGION 6 143 5 X 2 AA repeats of F-G.
REGION 328 458 Required for centrosome localization.
{ECO:0000269|PubMed:24107630}.
COILED 328 458 {ECO:0000255}.
COMPBIAS 9 288 Thr-rich.
COMPBIAS 176 331 Ala-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 373 373 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 468 468 O-linked (GlcNAc) serine. {ECO:0000250}.
DISULFID 475 475 Interchain (with NUP155). {ECO:0000250}.
DISULFID 506 506 Interchain (with NUP155). {ECO:0000250}.
VARIANT 139 139 G -> S (in dbSNP:rs3745489).
/FTId=VAR_028064.
VARIANT 233 233 A -> S (in dbSNP:rs2290772).
/FTId=VAR_013467.
VARIANT 283 283 S -> T (in dbSNP:rs1062798).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:1915414}.
/FTId=VAR_028065.
VARIANT 391 391 Q -> P (in SNDI; dbSNP:rs121917865).
{ECO:0000269|PubMed:16786527}.
/FTId=VAR_034904.
CONFLICT 418 419 SG -> RA (in Ref. 1; CAA41411).
{ECO:0000305}.
CONFLICT 431 431 E -> Q (in Ref. 1; CAA41411).
{ECO:0000305}.
CONFLICT 507 507 E -> V (in Ref. 1; CAA41411).
{ECO:0000305}.
SEQUENCE 522 AA; 53255 MW; 1FF65018452719A3 CRC64;
MSGFNFGGTG APTGGFTFGT AKTATTTPAT GFSFSTSGTG GFNFGAPFQP ATSTPSTGLF
SLATQTPATQ TTGFTFGTAT LASGGTGFSL GIGASKLNLS NTAATPAMAN PSGFGLGSSN
LTNAISSTVT SSQGTAPTGF VFGPSTTSVA PATTSGGFSF TGGSTAQPSG FNIGSAGNSA
QPTAPATLPF TPATPAATTA GATQPAAPTP TATITSTGPS LFASIATAPT SSATTGLSLC
TPVTTAGAPT AGTQGFSLKA PGAASGTSTT TSTAATATAT TTSSSSTTGF ALNLKPLAPA
GIPSNTAAAV TAPPGPGAAA GAAASSAMTY AQLESLINKW SLELEDQERH FLQQATQVNA
WDRTLIENGE KITSLHREVE KVKLDQKRLD QELDFILSQQ KELEDLLSPL EELVKEQSGT
IYLQHADEER EKTYKLAENI DAQLKRMAQD LKDIIEHLNT SGAPADTSDP LQQICKILNA
HMDSLQWIDQ NSALLQRKVE EVTKVCEGRR KEQERSFRIT FD


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