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Protein

Nuclear pore complex protein Nup93

Gene

NUP93

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. May anchor nucleoporins, but not NUP153 and TPR, to the NPC.2 Publications

GO - Molecular functioni

  • structural constituent of nuclear pore Source: UniProtKB

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:
Nuclear pore complex protein Nup93
Alternative name(s):
93 kDa nucleoporin
Nucleoporin Nup93
Gene namesi
Name:NUP93
Synonyms:KIAA0095
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:28958. NUP93.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • nuclear envelope Source: Reactome
  • nuclear membrane Source: UniProtKB
  • nuclear periphery Source: UniProtKB
  • nuclear pore Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134912759.

Polymorphism and mutation databases

BioMutaiNUP93.
DMDMi116242684.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 819819Nuclear pore complex protein Nup93PRO_0000124782Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521Phosphoserine2 Publications
Modified residuei72 – 721Phosphoserine3 Publications
Modified residuei75 – 751Phosphoserine1 Publication
Modified residuei80 – 801Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8N1F7.
PaxDbiQ8N1F7.
PRIDEiQ8N1F7.

PTM databases

PhosphoSiteiQ8N1F7.

Expressioni

Gene expression databases

BgeeiQ8N1F7.
CleanExiHS_NUP93.
ExpressionAtlasiQ8N1F7. baseline and differential.
GenevisibleiQ8N1F7. HS.

Organism-specific databases

HPAiHPA017937.

Interactioni

Subunit structurei

Part of the nuclear pore complex (NPC). Component of the p62 complex, a complex composed of NUP62 and NUP54. Forms a complex with NUP53, NUP155, NUP205 and lamin B; the interaction with NUP53 is direct. Does not interact with TPR.2 Publications

Protein-protein interaction databases

BioGridi115041. 49 interactions.
DIPiDIP-44020N.
IntActiQ8N1F7. 18 interactions.
MINTiMINT-3039167.
STRINGi9606.ENSP00000310668.

Structurei

3D structure databases

ProteinModelPortaliQ8N1F7.
SMRiQ8N1F7. Positions 185-814.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG312233.
GeneTreeiENSGT00390000016353.
HOGENOMiHOG000007350.
HOVERGENiHBG052701.
InParanoidiQ8N1F7.
KOiK14309.
OrthoDBiEOG73JKTW.
PhylomeDBiQ8N1F7.
TreeFamiTF315118.

Family and domain databases

InterProiIPR007231. Nucleoporin_int_Nup93/Nic96.
[Graphical view]
PANTHERiPTHR11225. PTHR11225. 1 hit.
PfamiPF04097. Nic96. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N1F7-1) [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
MDTEGFGELL QQAEQLAAET EGISELPHVE RNLQEIQQAG ERLRSRTLTR
60 70 80 90 100
TSQETADVKA SVLLGSRGLD ISHISQRLES LSAATTFEPL EPVKDTDIQG
110 120 130 140 150
FLKNEKDNAL LSAIEESRKR TFGMAEEYHR ESMLVEWEQV KQRILHTLLA
160 170 180 190 200
SGEDALDFTQ ESEPSYISDV GPPGRSSLDN IEMAYARQIY IYNEKIVNGH
210 220 230 240 250
LQPNLVDLCA SVAELDDKSI SDMWTMVKQM TDVLLTPATD ALKNRSSVEV
260 270 280 290 300
RMEFVRQALA YLEQSYKNYT LVTVFGNLHQ AQLGGVPGTY QLVRSFLNIK
310 320 330 340 350
LPAPLPGLQD GEVEGHPVWA LIYYCMRCGD LLAASQVVNR AQHQLGEFKT
360 370 380 390 400
WFQEYMNSKD RRLSPATENK LRLHYRRALR NNTDPYKRAV YCIIGRCDVT
410 420 430 440 450
DNQSEVADKT EDYLWLKLNQ VCFDDDGTSS PQDRLTLSQF QKQLLEDYGE
460 470 480 490 500
SHFTVNQQPF LYFQVLFLTA QFEAAVAFLF RMERLRCHAV HVALVLFELK
510 520 530 540 550
LLLKSSGQSA QLLSHEPGDP PCLRRLNFVR LLMLYTRKFE STDPREALQY
560 570 580 590 600
FYFLRDEKDS QGENMFLRCV SELVIESREF DMILGKLEND GSRKPGVIDK
610 620 630 640 650
FTSDTKPIIN KVASVAENKG LFEEAAKLYD LAKNADKVLE LMNKLLSPVV
660 670 680 690 700
PQISAPQSNK ERLKNMALSI AERYRAQGIS ANKFVDSTFY LLLDLITFFD
710 720 730 740 750
EYHSGHIDRA FDIIERLKLV PLNQESVEER VAAFRNFSDE IRHNLSEVLL
760 770 780 790 800
ATMNILFTQF KRLKGTSPSS SSRPQRVIED RDSQLRSQAR TLITFAGMIP
810
YRTSGDTNAR LVQMEVLMN
Length:819
Mass (Da):93,488
Last modified:October 17, 2006 - v2
Checksum:i7A611FABE964FE98
GO
Isoform 2 (identifier: Q8N1F7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-123: Missing.

Note: No experimental confirmation available.
Show »
Length:696
Mass (Da):79,882
Checksum:i8B232CEE9284D4B1
GO

Sequence cautioni

The sequence BAA07680.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti509 – 5091S → R.1 Publication
Corresponds to variant rs17853288 [ dbSNP | Ensembl ].
VAR_028160

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 123123Missing in isoform 2. 1 PublicationVSP_043117Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D42085 mRNA. Translation: BAA07680.2. Different initiation.
AK294176 mRNA. Translation: BAH11689.1.
BC034346 mRNA. Translation: AAH34346.1.
AC012181 Genomic DNA. No translation available.
AC106779 Genomic DNA. No translation available.
AC127456 Genomic DNA. No translation available.
AK056637 mRNA. Translation: BAG51770.1.
CCDSiCCDS10769.1. [Q8N1F7-1]
CCDS55996.1. [Q8N1F7-2]
RefSeqiNP_001229724.1. NM_001242795.1. [Q8N1F7-2]
NP_001229725.1. NM_001242796.1. [Q8N1F7-2]
NP_055484.3. NM_014669.4. [Q8N1F7-1]
XP_005256320.1. XM_005256263.2. [Q8N1F7-1]
UniGeneiHs.276878.

Genome annotation databases

EnsembliENST00000308159; ENSP00000310668; ENSG00000102900. [Q8N1F7-1]
ENST00000542526; ENSP00000440235; ENSG00000102900. [Q8N1F7-2]
ENST00000564887; ENSP00000458039; ENSG00000102900. [Q8N1F7-2]
GeneIDi9688.
KEGGihsa:9688.
UCSCiuc002eka.3. human. [Q8N1F7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D42085 mRNA. Translation: BAA07680.2. Different initiation.
AK294176 mRNA. Translation: BAH11689.1.
BC034346 mRNA. Translation: AAH34346.1.
AC012181 Genomic DNA. No translation available.
AC106779 Genomic DNA. No translation available.
AC127456 Genomic DNA. No translation available.
AK056637 mRNA. Translation: BAG51770.1.
CCDSiCCDS10769.1. [Q8N1F7-1]
CCDS55996.1. [Q8N1F7-2]
RefSeqiNP_001229724.1. NM_001242795.1. [Q8N1F7-2]
NP_001229725.1. NM_001242796.1. [Q8N1F7-2]
NP_055484.3. NM_014669.4. [Q8N1F7-1]
XP_005256320.1. XM_005256263.2. [Q8N1F7-1]
UniGeneiHs.276878.

3D structure databases

ProteinModelPortaliQ8N1F7.
SMRiQ8N1F7. Positions 185-814.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115041. 49 interactions.
DIPiDIP-44020N.
IntActiQ8N1F7. 18 interactions.
MINTiMINT-3039167.
STRINGi9606.ENSP00000310668.

PTM databases

PhosphoSiteiQ8N1F7.

Polymorphism and mutation databases

BioMutaiNUP93.
DMDMi116242684.

Proteomic databases

MaxQBiQ8N1F7.
PaxDbiQ8N1F7.
PRIDEiQ8N1F7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308159; ENSP00000310668; ENSG00000102900. [Q8N1F7-1]
ENST00000542526; ENSP00000440235; ENSG00000102900. [Q8N1F7-2]
ENST00000564887; ENSP00000458039; ENSG00000102900. [Q8N1F7-2]
GeneIDi9688.
KEGGihsa:9688.
UCSCiuc002eka.3. human. [Q8N1F7-1]

Organism-specific databases

CTDi9688.
GeneCardsiGC16P056764.
HGNCiHGNC:28958. NUP93.
HPAiHPA017937.
MIMi614351. gene.
neXtProtiNX_Q8N1F7.
PharmGKBiPA134912759.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG312233.
GeneTreeiENSGT00390000016353.
HOGENOMiHOG000007350.
HOVERGENiHBG052701.
InParanoidiQ8N1F7.
KOiK14309.
OrthoDBiEOG73JKTW.
PhylomeDBiQ8N1F7.
TreeFamiTF315118.

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

ChiTaRSiNUP93. human.
GeneWikiiNUP93.
GenomeRNAii9688.
NextBioi36387.
PROiQ8N1F7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N1F7.
CleanExiHS_NUP93.
ExpressionAtlasiQ8N1F7. baseline and differential.
GenevisibleiQ8N1F7. HS.

Family and domain databases

InterProiIPR007231. Nucleoporin_int_Nup93/Nic96.
[Graphical view]
PANTHERiPTHR11225. PTHR11225. 1 hit.
PfamiPF04097. Nic96. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  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: Amygdala and Brain.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [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] (ISOFORM 1), VARIANT ARG-509.
    Tissue: Skin.
  5. "Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly."
    Grandi P., Dang T., Pane N., Shevchenko A., Mann M., Forbes D., Hurt E.
    Mol. Biol. Cell 8:2017-2038(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "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.
  7. "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.
  8. "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, INTERACTION WITH NUP53, IDENTIFICATION IN A COMPLEX WITH NUP155; NUP205 AND LAMIN B.
  9. "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.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-52 AND SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-72 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNUP93_HUMAN
AccessioniPrimary (citable) accession number: Q8N1F7
Secondary accession number(s): B3KPQ8, Q14705
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 17, 2006
Last modified: June 24, 2015
This is version 118 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. 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.