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Protein

Nucleoporin NUP53

Gene

NUP35

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

Functioni

Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs). Can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC.1 Publication

GO - Biological processi

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_264487. Regulation of HSF1-mediated heat shock response.
REACT_268530. Transcriptional regulation by small RNAs.
REACT_355174. SUMOylation of DNA damage response and repair proteins.
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:
Nucleoporin NUP53
Alternative name(s):
35 kDa nucleoporin
Mitotic phosphoprotein 44
Short name:
MP-44
Nuclear pore complex protein Nup53
Nucleoporin Nup35
Gene namesi
Name:NUP35
Synonyms:MP44, NUP53
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:29797. NUP35.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134861481.

Polymorphism and mutation databases

DMDMi74730292.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Nucleoporin NUP53PRO_0000234294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661Phosphoserine1 Publication
Modified residuei73 – 731Phosphoserine3 Publications
Modified residuei99 – 991Phosphoserine1 Publication
Modified residuei100 – 1001Phosphoserine3 Publications
Modified residuei106 – 1061Phosphothreonine2 Publications
Modified residuei121 – 1211Phosphoserine1 Publication
Modified residuei129 – 1291Phosphothreonine1 Publication
Modified residuei138 – 1381Phosphoserine1 Publication
Modified residuei259 – 2591PhosphoserineBy similarity
Modified residuei265 – 2651Phosphothreonine1 Publication
Modified residuei273 – 2731Phosphothreonine3 Publications
Modified residuei275 – 2751Phosphothreonine1 Publication
Modified residuei279 – 2791Phosphoserine2 Publications
Modified residuei280 – 2801Phosphothreonine2 Publications
Modified residuei308 – 3081Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8NFH5.
PaxDbiQ8NFH5.
PeptideAtlasiQ8NFH5.
PRIDEiQ8NFH5.

PTM databases

PhosphoSiteiQ8NFH5.

Expressioni

Gene expression databases

BgeeiQ8NFH5.
CleanExiHS_NUP35.
ExpressionAtlasiQ8NFH5. baseline and differential.
GenevisibleiQ8NFH5. HS.

Organism-specific databases

HPAiHPA018401.
HPA018410.
HPA018441.

Interactioni

Subunit structurei

Interacts with TMEM48/NDC1. Forms a complex with NUP93, NUP155, NUP205 and lamin B; the interaction with NUP93 is direct.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KCTD9Q7L2733EBI-9050429,EBI-4397613

Protein-protein interaction databases

BioGridi126190. 14 interactions.
DIPiDIP-47308N.
IntActiQ8NFH5. 4 interactions.
MINTiMINT-4301788.
STRINGi9606.ENSP00000295119.

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi172 – 1743Combined sources
Beta strandi175 – 1795Combined sources
Helixi183 – 1853Combined sources
Helixi186 – 1938Combined sources
Beta strandi199 – 2046Combined sources
Beta strandi206 – 21712Combined sources
Helixi218 – 2258Combined sources
Turni226 – 2294Combined sources
Beta strandi230 – 2323Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 2427Combined sources
Helixi246 – 2494Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LIRX-ray2.46A/B151-266[»]
ProteinModelPortaliQ8NFH5.
SMRiQ8NFH5. Positions 169-252.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini170 – 25081RRM Nup35-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the Nup53 family.Curated
Contains 1 RRM Nup35-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG253574.
GeneTreeiENSGT00390000005923.
HOGENOMiHOG000231921.
HOVERGENiHBG060396.
InParanoidiQ8NFH5.
KOiK14313.
OMAiSGAQFLP.
PhylomeDBiQ8NFH5.
TreeFamiTF325369.

Family and domain databases

InterProiIPR017389. Nucleoporin_NUP53.
IPR007846. RRM_NUP35_dom.
[Graphical view]
PfamiPF05172. Nup35_RRM. 1 hit.
[Graphical view]
PIRSFiPIRSF038119. Nucleoporin_NUP53. 1 hit.
PROSITEiPS51472. RRM_NUP35. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NFH5-1) [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
MAAFAVEPQG PALGSEPMML GSPTSPKPGV NAQFLPGFLM GDLPAPVTPQ
60 70 80 90 100
PRSISGPSVG VMEMRSPLLA GGSPPQPVVP AHKDKSGAPP VRSIYDDISS
110 120 130 140 150
PGLGSTPLTS RRQPNISVMQ SPLVGVTSTP GTGQSMFSPA SIGQPRKTTL
160 170 180 190 200
SPAQLDPFYT QGDSLTSEDH LDDSWVTVFG FPQASASYIL LQFAQYGNIL
210 220 230 240 250
KHVMSNTGNW MHIRYQSKLQ ARKALSKDGR IFGESIMIGV KPCIDKSVME
260 270 280 290 300
SSDRCALSSP SLAFTPPIKT LGTPTQPGST PRISTMRPLA TAYKASTSDY
310 320
QVISDRQTPK KDESLVSKAM EYMFGW
Length:326
Mass (Da):34,774
Last modified:October 1, 2002 - v1
Checksum:i6420B0EF1AE31013
GO
Isoform 2 (identifier: Q8NFH5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.

Note: No experimental confirmation available.
Show »
Length:309
Mass (Da):33,120
Checksum:iBA43C9E8B0BD3BD1
GO
Isoform 3 (identifier: Q8NFH5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: Missing.

Note: No experimental confirmation available.
Show »
Length:191
Mass (Da):21,142
Checksum:i96265A68DC195F33
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131E → G in AAL86379 (Ref. 2) Curated
Sequence conflicti318 – 3181K → Q in AAL86379 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 135135Missing in isoform 3. 1 PublicationVSP_056210Add
BLAST
Alternative sequencei1 – 1717Missing in isoform 2. 1 PublicationVSP_056211Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF514993 mRNA. Translation: AAM76704.1.
AF411516 mRNA. Translation: AAL86379.1.
AK298199 mRNA. Translation: BAG60469.1.
AK302350 mRNA. Translation: BAG63676.1.
AC064871 Genomic DNA. Translation: AAY24198.1.
AC079249 Genomic DNA. Translation: AAX88896.1.
BC047029 mRNA. Translation: AAH47029.1.
BC061698 mRNA. Translation: AAH61698.1.
CCDSiCCDS2290.1. [Q8NFH5-1]
CCDS74614.1. [Q8NFH5-2]
RefSeqiNP_001274513.1. NM_001287584.1. [Q8NFH5-2]
NP_001274514.1. NM_001287585.1.
NP_612142.2. NM_138285.4. [Q8NFH5-1]
XP_006712317.1. XM_006712254.1. [Q8NFH5-2]
XP_011508878.1. XM_011510576.1. [Q8NFH5-2]
XP_011508879.1. XM_011510577.1. [Q8NFH5-2]
XP_011508880.1. XM_011510578.1. [Q8NFH5-2]
UniGeneiHs.180591.

Genome annotation databases

EnsembliENST00000295119; ENSP00000295119; ENSG00000163002.
ENST00000409798; ENSP00000387305; ENSG00000163002. [Q8NFH5-2]
GeneIDi129401.
KEGGihsa:129401.
UCSCiuc002upf.3. human. [Q8NFH5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF514993 mRNA. Translation: AAM76704.1.
AF411516 mRNA. Translation: AAL86379.1.
AK298199 mRNA. Translation: BAG60469.1.
AK302350 mRNA. Translation: BAG63676.1.
AC064871 Genomic DNA. Translation: AAY24198.1.
AC079249 Genomic DNA. Translation: AAX88896.1.
BC047029 mRNA. Translation: AAH47029.1.
BC061698 mRNA. Translation: AAH61698.1.
CCDSiCCDS2290.1. [Q8NFH5-1]
CCDS74614.1. [Q8NFH5-2]
RefSeqiNP_001274513.1. NM_001287584.1. [Q8NFH5-2]
NP_001274514.1. NM_001287585.1.
NP_612142.2. NM_138285.4. [Q8NFH5-1]
XP_006712317.1. XM_006712254.1. [Q8NFH5-2]
XP_011508878.1. XM_011510576.1. [Q8NFH5-2]
XP_011508879.1. XM_011510577.1. [Q8NFH5-2]
XP_011508880.1. XM_011510578.1. [Q8NFH5-2]
UniGeneiHs.180591.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LIRX-ray2.46A/B151-266[»]
ProteinModelPortaliQ8NFH5.
SMRiQ8NFH5. Positions 169-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126190. 14 interactions.
DIPiDIP-47308N.
IntActiQ8NFH5. 4 interactions.
MINTiMINT-4301788.
STRINGi9606.ENSP00000295119.

PTM databases

PhosphoSiteiQ8NFH5.

Polymorphism and mutation databases

DMDMi74730292.

Proteomic databases

MaxQBiQ8NFH5.
PaxDbiQ8NFH5.
PeptideAtlasiQ8NFH5.
PRIDEiQ8NFH5.

Protocols and materials databases

DNASUi129401.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295119; ENSP00000295119; ENSG00000163002.
ENST00000409798; ENSP00000387305; ENSG00000163002. [Q8NFH5-2]
GeneIDi129401.
KEGGihsa:129401.
UCSCiuc002upf.3. human. [Q8NFH5-1]

Organism-specific databases

CTDi129401.
GeneCardsiGC02P183982.
HGNCiHGNC:29797. NUP35.
HPAiHPA018401.
HPA018410.
HPA018441.
MIMi608140. gene.
neXtProtiNX_Q8NFH5.
PharmGKBiPA134861481.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG253574.
GeneTreeiENSGT00390000005923.
HOGENOMiHOG000231921.
HOVERGENiHBG060396.
InParanoidiQ8NFH5.
KOiK14313.
OMAiSGAQFLP.
PhylomeDBiQ8NFH5.
TreeFamiTF325369.

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_264487. Regulation of HSF1-mediated heat shock response.
REACT_268530. Transcriptional regulation by small RNAs.
REACT_355174. SUMOylation of DNA damage response and repair proteins.
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

GeneWikiiNUP35.
GenomeRNAii129401.
NextBioi35473792.
PROiQ8NFH5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NFH5.
CleanExiHS_NUP35.
ExpressionAtlasiQ8NFH5. baseline and differential.
GenevisibleiQ8NFH5. HS.

Family and domain databases

InterProiIPR017389. Nucleoporin_NUP53.
IPR007846. RRM_NUP35_dom.
[Graphical view]
PfamiPF05172. Nup35_RRM. 1 hit.
[Graphical view]
PIRSFiPIRSF038119. Nucleoporin_NUP53. 1 hit.
PROSITEiPS51472. RRM_NUP35. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Proteomic analysis of the mammalian nuclear pore complex."
    Cronshaw J.M., Krutchinsky A.N., Zhang W., Chait B.T., Matunis M.J.
    J. Cell Biol. 158:915-927(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "Molecular cloning and expression analysis of human mitotic phosphoprotein 44 gene."
    Guo J.H., Yu L.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] (ISOFORMS 2 AND 3).
    Tissue: Testis.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Bone marrow and Skin.
  6. "Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex."
    Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W.
    Mol. Biol. Cell 16:2382-2394(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NUP93, IDENTIFICATION IN A COMPLEX WITH LAMIN B; NUP155 AND NUP205.
  7. "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-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "The conserved transmembrane nucleoporin NDC1 is required for nuclear pore complex assembly in vertebrate cells."
    Mansfeld J., Guettinger S., Hawryluk-Gara L.A., Pante N., Mall M., Galy V., Haselmann U., Muehlhaeusser P., Wozniak R.W., Mattaj I.W., Kutay U., Antonin W.
    Mol. Cell 22:93-103(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM48.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-100; THR-106; THR-129; SER-138; THR-265; THR-273; SER-279; THR-280 AND THR-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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-66; SER-73; SER-100; THR-106; SER-121; THR-273; SER-279 AND THR-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273 AND THR-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNUP53_HUMAN
AccessioniPrimary (citable) accession number: Q8NFH5
Secondary accession number(s): B4DP57
, B4DYB4, Q4ZFZ9, Q53S95, Q8TDJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 1, 2002
Last modified: July 22, 2015
This is version 106 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 2
    Human chromosome 2: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.