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P49790 (NU153_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). Ref.9 Ref.10 Ref.28

Cofactor

Binds at least 4 zinc ions per subunit By similarity.

Subunit structure

Interacts with RAN; the interaction occurs in a GTP- and GDP-independent manner By similarity. Part of the nuclear pore complex (NPC). Interacts with TPR (via coiled coil region); the interaction is direct and provides a link between the core structure and the TPR-containing nuclear basket of the nuclear pore complex (NPC). Interacts with HIV-1 integrase; this interaction might play a role in nuclear import of HIV pre-integration complex. Interacts with hepatitis B virus capsid protein; this interaction probably plays a role in nuclear import of HBV genome. Interacts with C11orf73/Hikeshi, SENP2 and XPO5. Ref.7 Ref.9 Ref.10 Ref.17 Ref.21 Ref.22 Ref.27 Ref.28

Subcellular location

Nucleus. Nucleus membrane. Nucleusnuclear pore complex. Note: Tightly associated with the nuclear membrane and lamina By similarity. Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Dissociates from the NPC structure early during prophase of mitosis. Integrated in the newly assembled nuclear envelope of postmitotic cells early in G1. Colocalized with NUP98 and TPR to the nuclear basket at the nucleoplasmic side of the NPC. Detected in diffuse and discrete intranuclear foci. Remained localized to the nuclear membrane after poliovirus (PV) infection. Ref.8 Ref.10 Ref.20 Ref.28

Domain

Contains F-X-F-G repeats.

Post-translational modification

Phosphorylated in interphase, hyperphosphorylated during mitosis. May play a role in the reversible disassembly of the nuclear pore complex during mitosis By similarity.

Proteolytically degraded after poliovirus (PV) infection; degradation is partial and NCP- and TPR-binding domains withstand degradation.

O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status. Ref.23

Sequence similarities

Belongs to the NUP153 family.

Contains 4 RanBP2-type zinc fingers.

Sequence caution

The sequence BAE06106.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processHost-virus interaction
mRNA transport
Protein transport
Translocation
Transport
Viral penetration into host nucleus
Virus entry into host cell
   Cellular componentMembrane
Nuclear pore complex
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

glucose transport

Traceable author statement. Source: Reactome

hexose transport

Traceable author statement. Source: Reactome

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

negative regulation of RNA export from nucleus

Inferred from direct assay Ref.28. Source: UniProtKB

nuclear pore complex assembly

Inferred from mutant phenotype Ref.9Ref.10. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of glucose transport

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

viral penetration into host nucleus

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nuclear inclusion body

Inferred from direct assay Ref.8. Source: UniProtKB

nuclear membrane

Inferred from direct assay Ref.8Ref.9Ref.10Ref.20. Source: UniProtKB

nuclear periphery

Inferred from direct assay Ref.8Ref.10. Source: UniProtKB

nuclear pore

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

nuclear pore nuclear basket

Inferred from direct assay Ref.8. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction PubMed 23238392. Source: IntAct

nucleocytoplasmic transporter activity

Inferred from direct assay Ref.28. Source: UniProtKB

protein anchor

Inferred from mutant phenotype Ref.9Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11896061Ref.9Ref.21. Source: UniProtKB

structural constituent of nuclear pore

Inferred from mutant phenotype Ref.10. Source: UniProtKB

transporter activity

Traceable author statement Ref.1. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49790-1)

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.
Isoform 2 (identifier: P49790-2)

The sequence of this isoform differs from the canonical sequence as follows:
     574-615: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P49790-3)

The sequence of this isoform differs from the canonical sequence as follows:
     465-465: E → ERQGLTVLPKLISSSCAQAIIPSWPLKVLRLQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
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

Sites

Metal binding6641Zinc 1 By similarity
Metal binding6671Zinc 1 By similarity
Metal binding6781Zinc 1 By similarity
Metal binding6811Zinc 1 By similarity
Metal binding7281Zinc 2
Metal binding7311Zinc 2
Metal binding7421Zinc 2
Metal binding7451Zinc 2
Metal binding7991Zinc 3 By similarity
Metal binding8021Zinc 3 By similarity
Metal binding8131Zinc 3 By similarity
Metal binding8161Zinc 3 By similarity
Metal binding8571Zinc 4 By similarity
Metal binding8601Zinc 4 By similarity
Metal binding8711Zinc 4 By similarity
Metal binding8741Zinc 4 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.16 Ref.29
Modified residue1921Phosphoserine Ref.24 Ref.26
Modified residue2091Phosphoserine Ref.12 Ref.14 Ref.15 Ref.24 Ref.26
Modified residue2401Phosphoserine Ref.15 Ref.24
Modified residue2571Phosphoserine Ref.13 Ref.15
Modified residue3301Phosphoserine Ref.15
Modified residue3341Phosphoserine Ref.15 Ref.18
Modified residue3381Phosphoserine Ref.11 Ref.12 Ref.13 Ref.15 Ref.18 Ref.24
Modified residue3431Phosphoserine Ref.15
Modified residue3691Phosphothreonine Ref.15
Modified residue3841N6-acetyllysine Ref.19
Modified residue5001Phosphoserine Ref.24
Modified residue5161Phosphoserine Ref.18
Modified residue5221Phosphoserine Ref.15 Ref.18
Modified residue5291Phosphoserine Ref.15
Modified residue5881Phosphothreonine Ref.11
Modified residue6141Phosphoserine Ref.15 Ref.24
Modified residue6191Phosphoserine Ref.15 Ref.24
Modified residue6331Phosphoserine Ref.12 Ref.24
Modified residue6871Phosphoserine Ref.24 Ref.26
Modified residue7181N6-acetyllysine Ref.19
Modified residue9541N6-acetyllysine Ref.19
Modified residue14571Phosphoserine Ref.15
Modified residue14631Phosphoserine Ref.15 Ref.18 Ref.24
Glycosylation5341O-linked (GlcNAc) Ref.23
Glycosylation5441O-linked (GlcNAc) Ref.23
Glycosylation9081O-linked (GlcNAc) Ref.23
Glycosylation9091O-linked (GlcNAc) Ref.23
Glycosylation11131O-linked (GlcNAc) Ref.23
Glycosylation11561O-linked (GlcNAc) Ref.23

Natural variations

Alternative sequence4651E → ERQGLTVLPKLISSSCAQAI IPSWPLKVLRLQ in isoform 3.
VSP_055134
Alternative sequence574 – 61542Missing in isoform 2.
VSP_054265
Natural variant901D → N. Ref.5
Corresponds to variant rs16879902 [ dbSNP | Ensembl ].
VAR_046554
Natural variant2481I → V.
Corresponds to variant rs2228375 [ dbSNP | Ensembl ].
VAR_046555
Natural variant3811V → F. Ref.5
Corresponds to variant rs17857419 [ dbSNP | Ensembl ].
VAR_070841
Natural variant4021N → K.
Corresponds to variant rs6906499 [ dbSNP | Ensembl ].
VAR_046556
Natural variant8211P → L.
Corresponds to variant rs6905654 [ dbSNP | Ensembl ].
VAR_046557
Natural variant8271A → T. Ref.2
Corresponds to variant rs2274136 [ dbSNP | Ensembl ].
VAR_046558
Natural variant13881T → A.
Corresponds to variant rs45475293 [ dbSNP | Ensembl ].
VAR_046559

Experimental info

Sequence conflict1111E → G in BAG58514. Ref.2
Sequence conflict454 – 4552TR → HA in CAA80982. Ref.1
Sequence conflict8131C → S in BAG58514. Ref.2
Sequence conflict8361S → C in BAG58514. Ref.2

Secondary structure

................... 1475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 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

Isoform 2 [UniParc].

Checksum: 109D4036D0912D37
Show »

FASTA1,433149,396
Isoform 3 [UniParc].

Checksum: 9D997D081B22CCD3
Show »

FASTA1,506157,338

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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. expand/collapse author list , 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 3), VARIANT THR-827.
Tissue: Hippocampus.
[3]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Myeloma.
[4]"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] [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), VARIANTS ASN-90 AND PHE-381.
Tissue: Testis.
[6]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[7]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XPO5.
[8]"Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"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: FUNCTION IN ANCHORING TPR, INTERACTION WITH TPR.
[10]"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.
[11]"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-338 AND THR-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-338 AND SER-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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] [Europe PMC] [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-522; SER-529; SER-614; SER-619; SER-1457 AND SER-1463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1."
Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A.
J. Virol. 83:6522-6533(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV INTEGRASE.
[18]"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-334; SER-338; SER-516; SER-522 AND SER-1463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384; LYS-718 AND LYS-954, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion."
Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H., Thyberg J., Cordes V.C.
EMBO J. 29:1659-1673(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
[21]"Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis."
Nakano H., Funasaka T., Hashizume C., Wong R.W.
J. Biol. Chem. 285:10841-10849(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TPR.
[22]"Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket."
Schmitz A., Schwarz A., Foss M., Zhou L., Rabe B., Hoellenriegel J., Stoeber M., Pante N., Kann M.
PLoS Pathog. 6:E1000741-E1000741(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HEPATITIS B VIRUS CAPSID PROTEIN.
[23]"Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis."
Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.
Sci. Signal. 3:RA2-RA2(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-534; SER-544; SER-908; SER-909; SER-1113 AND THR-1156.
[24]"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-192; SER-209; SER-240; SER-338; SER-500; SER-614; SER-619; SER-633; SER-687 AND SER-1463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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-192; SER-209 AND SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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.
[28]"Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA."
Rajanala K., Nandicoori V.K.
PLoS ONE 7:E29921-E29921(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RNA EXPORT, INTERACTION WITH MAPK1, SUBCELLULAR LOCATION.
[29]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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.
[31]"Solution structure of the second ZF-ranbp domain from human nuclear pore complex protein nup153."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 722-761.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z25535 mRNA. Translation: CAA80982.1.
AK295644 mRNA. Translation: BAG58514.1.
AB210024 mRNA. Translation: BAE06106.1. Different initiation.
AL138824, AL138724, AL157776 Genomic DNA. Translation: CAI12246.1.
AL157776, AL138724, AL138824 Genomic DNA. Translation: CAI16393.1.
AL138724, AL138824, AL157776 Genomic DNA. Translation: CAI40945.1.
BC052965 mRNA. Translation: AAH52965.1.
CCDSCCDS4541.1.
PIRS42718.
RefSeqNP_001265138.1. NM_001278209.1.
NP_001265139.1. NM_001278210.1. [P49790-2]
NP_005115.2. NM_005124.3. [P49790-1]
UniGeneHs.601591.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBQNMR-A722-761[»]
2EBRNMR-A851-890[»]
2EBVNMR-A773-822[»]
2GQENMR-A722-750[»]
ProteinModelPortalP49790.
SMRP49790. Positions 661-686, 722-761, 777-822, 855-890.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115297. 46 interactions.
DIPDIP-38185N.
IntActP49790. 22 interactions.
MINTMINT-121422.
STRING9606.ENSP00000262077.

PTM databases

PhosphoSiteP49790.

Polymorphism databases

DMDM206729891.

Proteomic databases

MaxQBP49790.
PaxDbP49790.
PRIDEP49790.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262077; ENSP00000262077; ENSG00000124789.
ENST00000537253; ENSP00000444029; ENSG00000124789.
GeneID9972.
KEGGhsa:9972.
UCSCuc003ncd.2. human. [P49790-1]

Organism-specific databases

CTD9972.
GeneCardsGC06M017559.
H-InvDBHIX0032892.
HIX0200901.
HGNCHGNC:8062. NUP153.
HPAHPA027896.
HPA027897.
HPA027898.
MIM603948. gene.
neXtProtNX_P49790.
PharmGKBPA31848.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000088610.
HOVERGENHBG052679.
InParanoidP49790.
KOK14296.
OrthoDBEOG73JKTK.
PhylomeDBP49790.
TreeFamTF323517.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6900. Immune System.
SignaLinkP49790.

Gene expression databases

ArrayExpressP49790.
BgeeP49790.
CleanExHS_NUP153.
GenevestigatorP49790.

Family and domain databases

InterProIPR013913. Nucleoporin_Nup153.
IPR018892. Retro-transposon_transp_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

EvolutionaryTraceP49790.
GeneWikiNUP153.
GenomeRNAi9972.
NextBio37662.
PMAP-CutDBP49790.
PROP49790.
SOURCESearch...

Entry information

Entry nameNU153_HUMAN
AccessionPrimary (citable) accession number: P49790
Secondary accession number(s): B4DIK2 expand/collapse secondary AC list , E7EPX5, F6QR24, Q4LE47, Q5T9I7, Q7Z743
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

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