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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	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. 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. Ref.4 Ref.15 Ref.16
Subcellular location	Nucleus › nuclear pore complex. Note: Located to the terminal ring structure of the nucleoplasmic cage. Tightly associated with the nuclear membrane and lamina By similarity.
Domain	Contains F-X-F-G repeats.
Sequence similarities	Contains 4 RanBP2-type zinc fingers.

Ontologies

Keywords
Biological process	Host-virus interaction Initiation of viral infection Protein transport Translocation Transport Viral penetration into host nucleus mRNA transport
Cellular component	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 glucose transport Traceable author statement. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of glucose transport Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nuclear membrane Inferred from direct assay. Source: HPA nuclear pore Traceable author statement. Source: ProtInc nucleolus Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW transporter activity Traceable author statement. Source: ProtInc
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

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3 Ref.12

Modified residue

209

1

Phosphoserine Ref.7 Ref.10 Ref.11 Ref.12 Ref.13

Modified residue

240

1

Phosphoserine Ref.11

Modified residue

257

1

Phosphoserine Ref.9 Ref.11 Ref.13

Modified residue

260

1

Phosphotyrosine Ref.12 Ref.13

Modified residue

281

1

Phosphothreonine Ref.9

Modified residue

320

1

Phosphoserine Ref.12 Ref.13

Modified residue

330

1

Phosphoserine Ref.11

Modified residue

334

1

Phosphoserine Ref.6 Ref.9 Ref.11 Ref.12 Ref.13

Modified residue

338

1

Phosphoserine Ref.6 Ref.9 Ref.11 Ref.12 Ref.13

Modified residue

343

1

Phosphoserine Ref.11

Modified residue

369

1

Phosphothreonine Ref.11

Modified residue

384

1

N6-acetyllysine Ref.14

Modified residue

516

1

Phosphoserine Ref.11 Ref.12 Ref.13

Modified residue

518

1

Phosphoserine Ref.12

Modified residue

522

1

Phosphoserine Ref.11 Ref.12 Ref.13

Modified residue

529

1

Phosphoserine Ref.5 Ref.11 Ref.12

Modified residue

588

1

Phosphothreonine Ref.6

Modified residue

614

1

Phosphoserine Ref.11

Modified residue

619

1

Phosphoserine Ref.7 Ref.11 Ref.12

Modified residue

633

1

Phosphoserine Ref.7

Modified residue

687

1

Phosphoserine Ref.8 Ref.11

Modified residue

718

1

N6-acetyllysine Ref.14

Modified residue

954

1

N6-acetyllysine Ref.14

Modified residue

1457

1

Phosphoserine Ref.11

Modified residue

1463

1

Phosphoserine Ref.11 Ref.12 Ref.13

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

729 – 731

3

Beta strand

743 – 745

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: 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. , 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: Cervix carcinoma.
[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: Cervix carcinoma.
[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: Cervix carcinoma.
[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: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[12]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; TYR-260; SER-320; SER-334; SER-338; SER-516; SER-518; SER-522; SER-529; SER-619 AND SER-1463, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-257; TYR-260; SER-320; SER-334; SER-338; SER-516; SER-522 AND SER-1463, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384; LYS-718 AND LYS-954, MASS SPECTROMETRY.
[15]	"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: 19369352] [Abstract] Cited for: INTERACTION WITH HIV INTEGRASE.
[16]	"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: 20126445] [Abstract] Cited for: INTERACTION WITH HEPATITIS B VIRUS CAPSID PROTEIN.
[17]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"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

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.

SMR

P49790. Positions 661-686, 722-761, 777-822, 855-890.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38185N.

IntAct

P49790. 13 interactions.

MINT

MINT-121422.

STRING

P49790.

PTM databases

PhosphoSite

P49790.

Polymorphism databases

DMDM

206729891.

Proteomic databases

PRIDE

P49790.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262077; ENSP00000262077; ENSG00000124789.

GeneID

9972.

KEGG

hsa:9972.

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

Search...

Phylogenomic databases

eggNOG

prNOG04837.

HOVERGEN

HBG052679.

InParanoid

P49790.

OrthoDB

EOG4WDDD4.

PhylomeDB

P49790.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_15518. Transmembrane transport of small molecules.
REACT_474. Metabolism of carbohydrates.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpress

P49790.

Bgee

P49790.

CleanEx

HS_NUP153.

Genevestigator

P49790.

GermOnline

ENSG00000124789. Homo sapiens.

Family and domain databases

InterPro

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

KO

K14296.

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

Search...

Other

NextBio

37662.

PMAP-CutDB

P49790.

SOURCE

Search...

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:	January 25, 2012
This is version 109 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.