P49790 (NU153_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear pore complex protein Nup153

Alternative name(s):
153 kDa nucleoporin
Nucleoporin Nup153

Gene names

Name:

NUP153

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.6 Ref.7 Ref.23
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.4 Ref.6 Ref.7 Ref.13 Ref.17 Ref.18 Ref.22 Ref.23
Subcellular location	Nucleus. Nucleus membrane. Nucleus › nuclear 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.5 Ref.7 Ref.16 Ref.23
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.
Sequence similarities	Belongs to the NUP153 family. Contains 4 RanBP2-type zinc fingers.

Ontologies

Keywords
Biological process	Host-virus interaction Protein transport Translocation Transport Viral penetration into host nucleus Virus entry into host cell mRNA transport
Cellular component	Membrane Nuclear pore complex Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome cytokine-mediated signaling pathway Traceable author statement. Source: Reactome glucose transport Traceable author statement. Source: Reactome mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of RNA export from nucleus Inferred from direct assay Ref.23. Source: UniProtKB nuclear pore complex assembly Inferred from mutant phenotype Ref.6Ref.7. 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 reproduction Traceable author statement. Source: Reactome
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nuclear inclusion body Inferred from direct assay Ref.5. Source: UniProtKB nuclear membrane Inferred from direct assay Ref.5Ref.6Ref.7Ref.16. Source: UniProtKB nuclear periphery Inferred from direct assay Ref.5Ref.7. Source: UniProtKB nuclear pore nuclear basket Inferred from direct assay Ref.5. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleocytoplasmic transporter activity Inferred from direct assay Ref.23. Source: UniProtKB protein anchor Inferred from mutant phenotype Ref.6Ref.7. Source: UniProtKB structural constituent of nuclear pore Inferred from mutant phenotype Ref.7. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 1475

1474

Nuclear pore complex protein Nup153

PRO_0000204842

Regions

Zinc finger

657 – 687

31

RanBP2-type 1

Zinc finger

722 – 751

30

RanBP2-type 2

Zinc finger

793 – 822

30

RanBP2-type 3

Zinc finger

851 – 880

30

RanBP2-type 4

Compositional bias

4 – 14

11

Gly-rich

Compositional bias

443 – 447

5

Poly-Gly

Sites

Metal binding

664

1

Zinc 1 By similarity

Metal binding

667

1

Zinc 1 By similarity

Metal binding

678

1

Zinc 1 By similarity

Metal binding

681

1

Zinc 1 By similarity

Metal binding

728

1

Zinc 2

Metal binding

731

1

Zinc 2

Metal binding

742

1

Zinc 2

Metal binding

745

1

Zinc 2

Metal binding

799

1

Zinc 3 By similarity

Metal binding

802

1

Zinc 3 By similarity

Metal binding

813

1

Zinc 3 By similarity

Metal binding

816

1

Zinc 3 By similarity

Metal binding

857

1

Zinc 4 By similarity

Metal binding

860

1

Zinc 4 By similarity

Metal binding

871

1

Zinc 4 By similarity

Metal binding

874

1

Zinc 4 By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3

Modified residue

192

1

Phosphoserine Ref.19 Ref.21

Modified residue

209

1

Phosphoserine Ref.9 Ref.11 Ref.12 Ref.19 Ref.21

Modified residue

240

1

Phosphoserine Ref.12 Ref.19

Modified residue

257

1

Phosphoserine Ref.10 Ref.12

Modified residue

330

1

Phosphoserine Ref.12

Modified residue

334

1

Phosphoserine Ref.12 Ref.14

Modified residue

338

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.19

Modified residue

343

1

Phosphoserine Ref.12

Modified residue

369

1

Phosphothreonine Ref.12

Modified residue

384

1

N6-acetyllysine Ref.15

Modified residue

500

1

Phosphoserine Ref.19

Modified residue

516

1

Phosphoserine Ref.14

Modified residue

522

1

Phosphoserine Ref.12 Ref.14

Modified residue

529

1

Phosphoserine Ref.12

Modified residue

588

1

Phosphothreonine Ref.8

Modified residue

614

1

Phosphoserine Ref.12 Ref.19

Modified residue

619

1

Phosphoserine Ref.12 Ref.19

Modified residue

633

1

Phosphoserine Ref.9 Ref.19

Modified residue

687

1

Phosphoserine Ref.19 Ref.21

Modified residue

718

1

N6-acetyllysine Ref.15

Modified residue

954

1

N6-acetyllysine Ref.15

Modified residue

1457

1

Phosphoserine Ref.12

Modified residue

1463

1

Phosphoserine Ref.12 Ref.14 Ref.19

Natural variations

Natural variant

90

1

D → N.
Corresponds to variant rs16879902 [ dbSNP | Ensembl ].

VAR_046554

Natural variant

248

1

I → V.
Corresponds to variant rs2228375 [ dbSNP | Ensembl ].

VAR_046555

Natural variant

402

1

N → K.
Corresponds to variant rs6906499 [ dbSNP | Ensembl ].

VAR_046556

Natural variant

821

1

P → L.
Corresponds to variant rs6905654 [ dbSNP | Ensembl ].

VAR_046557

Natural variant

827

1

A → T.
Corresponds to variant rs2274136 [ dbSNP | Ensembl ].

VAR_046558

Natural variant

1388

1

T → A.
Corresponds to variant rs45475293 [ dbSNP | Ensembl ].

VAR_046559

Experimental info

Sequence conflict

454 – 455

2

TR → HA in CAA80982. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1475

Helix Strand Turn

Details...

Beta strand

723 – 727

5

Beta strand

729 – 731

3

Beta strand

743 – 745

3

Helix

755 – 757

3

Beta strand

794 – 796

3

Beta strand

800 – 802

3

Beta strand

814 – 816

3

Beta strand

858 – 860

3

Beta strand

872 – 874

3

Sequences

	Sequence		Length	Mass (Da)
	P49790 [UniParc]. Last modified September 23, 2008. Version 2. Checksum: D07455A691F7CD1F	FASTA	1,475	153,938
	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

References

	« Hide 'large scale' referencesShow '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].
[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. , 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].
[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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH XPO5.
[5]	"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.
[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: FUNCTION IN ANCHORING TPR, INTERACTION WITH TPR.
[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]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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.
[14]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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, MASS SPECTROMETRY.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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].
[21]	"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, MASS SPECTROMETRY.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
AL138824, AL138724, AL157776 Genomic DNA. Translation: CAI12246.1.
AL157776, AL138724, AL138824 Genomic DNA. Translation: CAI16393.1.
AL138724, AL138824, AL157776 Genomic DNA. Translation: CAI40945.1.

IPI

IPI00292059.

PIR

S42718.

RefSeq

NP_005115.2. NM_005124.2.

UniGene

Hs.601591.
Hs.718703.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EBQ	NMR	-	A	722-761	[»]
2EBR	NMR	-	A	851-890	[»]
2EBV	NMR	-	A	773-822	[»]
2GQE	NMR	-	A	722-750	[»]

ProteinModelPortal

P49790.

ModBase

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Protein-protein interaction databases

DIP

DIP-38185N.

IntAct

P49790. 15 interactions.

MINT

MINT-121422.

STRING

9606.ENSP00000262077.

PTM databases

PhosphoSite

P49790.

Polymorphism databases

DMDM

206729891.

Proteomic databases

PaxDb

P49790.

PRIDE

P49790.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000262077; ENSP00000262077; ENSG00000124789.

GeneID

9972.

KEGG

hsa:9972.

UCSC

uc003ncd.1. human.

Organism-specific databases

CTD

9972.

GeneCards

GC06M017559.

H-InvDB

HIX0032892.
HIX0200901.

HGNC

HGNC:8062. NUP153.

HPA

HPA027896.
HPA027897.
HPA027898.

MIM

603948. gene.

neXtProt

NX_P49790.

PharmGKB

PA31848.

GenAtlas

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Phylogenomic databases

eggNOG

NOG12793.

HOGENOM

HOG000088610.

HOVERGEN

HBG052679.

InParanoid

P49790.

KO

K14296.

OrthoDB

EOG4WDDD4.

PhylomeDB

P49790.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P49790.

Bgee

P49790.

CleanEx

HS_NUP153.

Genevestigator

P49790.

GermOnline

ENSG00000124789. Homo sapiens.

Family and domain databases

InterPro

IPR026054. Nucleoporin.
IPR013913. Nucleoporin_Nup153.
IPR018892. Retro-transposon_transp_CS.
IPR001876. Znf_RanBP2.
[Graphical view]

PANTHER

PTHR23193. PTHR23193. 1 hit.

Pfam

PF08604. Nup153. 1 hit.
PF10599. Nup_retrotrp_bd. 1 hit.
PF00641. zf-RanBP. 4 hits.
[Graphical view]

SMART

SM00547. ZnF_RBZ. 4 hits.
[Graphical view]

PROSITE

PS01358. ZF_RANBP2_1. 4 hits.
PS50199. ZF_RANBP2_2. 4 hits.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

P49790.

GenomeRNAi

9972.

NextBio

37662.

PMAP-CutDB

P49790.

SOURCE

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Entry information

Entry name

NU153_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.