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Reviewed, UniProtKB/Swiss-Prot P49790 (NU153_HUMAN)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nuclear pore complex protein Nup153
Alternative name(s):
    Nucleoporin Nup153
    153 kDa nucleoporin
Gene names
Name: NUP153
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Possible DNA-binding subunit of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane.

Subunit structure

Interacts with SENP2 and XPO5. Ref.4

Subcellular location

Nucleusnuclear pore complex. Note: Located to the terminal ring structure of the nucleoplasmic cage.

Domain

Contains F-X-F-G repeats.

Sequence similarities

Contains 4 RanBP2-type zinc fingers.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 14751474Nuclear pore complex protein Nup153
PRO_0000204842

Regions

Zinc finger657 – 68731RanBP2-type 1
Zinc finger722 – 75130RanBP2-type 2
Zinc finger793 – 82230RanBP2-type 3
Zinc finger851 – 88030RanBP2-type 4
Compositional bias4 – 1411Gly-rich
Compositional bias443 – 4475Poly-Gly

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue2091Phosphoserine Ref.7 Ref.10 Ref.11
Modified residue2401Phosphoserine Ref.11
Modified residue2571Phosphoserine Ref.11 Ref.9
Modified residue2811Phosphothreonine Ref.9
Modified residue3301Phosphoserine Ref.11
Modified residue3341Phosphoserine Ref.11 Ref.9 Ref.6
Modified residue3381Phosphoserine Ref.11 Ref.9 Ref.6
Modified residue3431Phosphoserine Ref.11
Modified residue3691Phosphothreonine Ref.11
Modified residue5161Phosphoserine Ref.11
Modified residue5221Phosphoserine Ref.11
Modified residue5291Phosphoserine Ref.11 Ref.5
Modified residue5881Phosphothreonine Ref.6
Modified residue6141Phosphoserine Ref.11
Modified residue6191Phosphoserine Ref.7 Ref.11
Modified residue6331Phosphoserine Ref.7
Modified residue6871Phosphoserine Ref.11 Ref.8
Modified residue14571Phosphoserine Ref.11
Modified residue14631Phosphoserine Ref.11

Natural variations

Natural variant901D → N: dbSNP rs16879902.
VAR_046554
Natural variant2481I → V: dbSNP rs2228375.
VAR_046555
Natural variant4021N → K: dbSNP rs6906499.
VAR_046556
Natural variant8211P → L: dbSNP rs6905654.
VAR_046557
Natural variant8271A → T: dbSNP rs2274136.
VAR_046558
Natural variant13881T → A: dbSNP rs45475293.
VAR_046559

Experimental info

Sequence conflict454 – 4552TR → HA in CAA80982. Ref.1

Secondary structure

..... 1475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49790-1 [UniParc].

Last modified September 23, 2008. Version 2.
Checksum: D07455A691F7CD1F

FASTA1,475153,938
        10         20         30         40         50         60 
MASGAGGVGG GGGGKIRTRR CHQGPIKPYQ QGRQQHQGIL SRVTESVKNI VPGWLQRYFN 

        70         80         90        100        110        120 
KNEDVCSCST DTSEVPRWPE NKEDHLVYAD EESSNITDGR ITPEPAVSNT EEPSTTSTAS 

       130        140        150        160        170        180 
NYPDVLTRPS LHRSHLNFSM LESPALHCQP STSSAFPIGS SGFSLVKEIK DSTSQHDDDN 

       190        200        210        220        230        240 
ISTTSGFSSR ASDKDITVSK NTSLPPLWSP EAERSHSLSQ HTATSSKKPA FNLSAFGTLS 

       250        260        270        280        290        300 
PSLGNSSILK TSQLGDSPFY PGKTTYGGAA AAVRQSKLRN TPYQAPVRRQ MKAKQLSAQS 

       310        320        330        340        350        360 
YGVTSSTARR ILQSLEKMSS PLADAKRIPS IVSSPLNSPL DRSGIDITDF QAKREKVDSQ 

       370        380        390        400        410        420 
YPPVQRLMTP KPVSIATNRS VYFKPSLTPS GEFRKTNQRI DNKCSTGYEK NMTPGQNREQ 

       430        440        450        460        470        480 
RESGFSYPNF SLPAANGLSS GVGGGGGKMR RERTRFVASK PLEEEEMEVP VLPKISLPIT 

       490        500        510        520        530        540 
SSSLPTFNFS SPEITTSSPS PINSSQALTN KVQMTSPSST GSPMFKFSSP IVKSTEANVL 

       550        560        570        580        590        600 
PPSSIGFTFS VPVAKTAELS GSSSTLEPII SSSAHHVTTV NSTNCKKTPP EDCEGPFRPA 

       610        620        630        640        650        660 
EILKEGSVLD ILKSPGFASP KIDSVAAQPT ATSPVVYTRP AISSFSSSGI GFGESLKAGS 

       670        680        690        700        710        720 
SWQCDTCLLQ NKVTDNKCIA CQAAKLSPRD TAKQTGIETP NKSGKTTLSA SGTGFGDKFK 

       730        740        750        760        770        780 
PVIGTWDCDT CLVQNKPEAI KCVACETPKP GTCVKRALTL TVVSESAETM TASSSSCTVT 

       790        800        810        820        830        840 
TGTLGFGDKF KRPIGSWECS VCCVSNNAED NKCVSCMSEK PGSSVPASSS STVPVSLPSG 

       850        860        870        880        890        900 
GSLGLEKFKK PEGSWDCELC LVQNKADSTK CLACESAKPG TKSGFKGFDT SSSSSNSAAS 

       910        920        930        940        950        960 
SSFKFGVSSS SSGPSQTLTS TGNFKFGDQG GFKIGVSSDS GSINPMSEGF KFSKPIGDFK 

       970        980        990       1000       1010       1020 
FGVSSESKPE EVKKDSKNDN FKFGLSSGLS NPVSLTPFQF GVSNLGQEEK KEELPKSSSA 

      1030       1040       1050       1060       1070       1080 
GFSFGTGVIN STPAPANTIV TSENKSSFNL GTIETKSASV APFTCKTSEA KKEEMPATKG 

      1090       1100       1110       1120       1130       1140 
GFSFGNVEPA SLPSASVFVL GRTEEKQQEP VTSTSLVFGK KADNEEPKCQ PVFSFGNSEQ 

      1150       1160       1170       1180       1190       1200 
TKDENSSKST FSFSMTKPSE KESEQPAKAT FAFGAQTSTT ADQGAAKPVF SFLNNSSSSS 

      1210       1220       1230       1240       1250       1260 
STPATSAGGG IFGSSTSSSN PPVATFVFGQ SSNPVSSSAF GNTAESSTSQ SLLFSQDSKL 

      1270       1280       1290       1300       1310       1320 
ATTSSTGTAV TPFVFGPGAS SNNTTTSGFG FGATTTSSSA GSSFVFGTGP SAPSASPAFG 

      1330       1340       1350       1360       1370       1380 
ANQTPTFGQS QGASQPNPPG FGSISSSTAL FPTGSQPAPP TFGTVSSSSQ PPVFGQQPSQ 

      1390       1400       1410       1420       1430       1440 
SAFGSGTTPN SSSAFQFGSS TTNFNFTNNS PSGVFTFGAN SSTPAASAQP SGSGGFPFNQ 

      1450       1460       1470 
SPAAFTVGSN GKNVFSSSGT SFSGRKIKTA VRRRK 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153."
McMorrow I., Bastos R., Horton H., Burke B.
Biochim. Biophys. Acta 1217:219-223(1994) [PubMed: 8110839] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Bienvenut W.V., Dozynkiewicz M., Norman J.C.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17; 251-263; 295-309; 367-379; 706-718 AND 1046-1056, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[4]"Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins."
Brownawell A.M., Macara I.G.
J. Cell Biol. 156:53-64(2002) [PubMed: 11777942] [Abstract]
Cited for: INTERACTION WITH XPO5.
[5]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-338 AND THR-588, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-619 AND SER-633, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; THR-281; SER-334 AND SER-338, MASS SPECTROMETRY.
[10]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, MASS SPECTROMETRY.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-240; SER-257; SER-330; SER-334; SER-338; SER-343; THR-369; SER-516; SER-522; SER-529; SER-614; SER-619; SER-687; SER-1457 AND SER-1463, MASS SPECTROMETRY.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]"Solution structure of the second and third ZF-RANBP domains from human nuclear pore complex protein NUP153."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 722-822.
+Additional computationally mapped references.

Cross-references

Sequence databases

Z25535 mRNA. Translation: CAA80982.1.
AL138824, AL138724, AL157776 Genomic DNA. Translation: CAI12246.1.
AL157776, AL138724, AL138824 Genomic DNA. Translation: CAI16393.1.
AL138724, AL138824, AL157776 Genomic DNA. Translation: CAI40945.1.
IPIIPI00292059.
PIRS42718.
RefSeqNP_005115.2.
UniGeneHs.601591
Hs.633334

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2EBQNMR-A722-761[»]
2EBRNMR-A851-890[»]
2EBVNMR-A773-822[»]
2GQENMR-A722-750[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP49790. 3 interactions.

PTM databases

PhosphoSiteP49790.

Proteomic databases

PRIDEP49790.

Genome annotation databases

EnsemblENSG00000124789. Homo sapiens. [Contig view]
GeneID9972.
KEGGhsa:9972.

Organism-specific databases

GeneCardsGC06M017723.
H-InvDBHIX0025219.
HGNCHGNC:8062. NUP153.
MIM603948. gene.
PharmGKBPA31848.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP49790.
HOVERGENP49790.
OMAP49790. ILSRVTE.

Enzyme and pathway databases

Pathway_Interaction_DBsmad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
ReactomeREACT_6185. HIV Infection.

Gene expression databases

ArrayExpressP49790.
BgeeP49790.
CleanExHS_NUP153.
GermOnlineENSG00000124789. Homo sapiens.

Family and domain databases

InterProIPR013913. Nucleoporin_Nup153.
IPR018892. Retro-transposon_transport_CS.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamPF08604. Nup153. 1 hit.
PF10599. Nup_retrotrp_bd. 1 hit.
PF00641. zf-RanBP. 4 hits.
[Graphical view]
SMARTSM00547. ZnF_RBZ. 4 hits.
[Graphical view]
PROSITEPS01358. ZF_RANBP2_1. 4 hits.
PS50199. ZF_RANBP2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio37662.
PMAP-CutDBP49790.
SOURCESearch...

Entry information

Entry nameNU153_HUMAN
AccessionPrimary (citable) accession number: P49790
Secondary accession number(s): Q5T9I7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents