E3 ubiquitin-protein ligase Topors - Homo sapiens (Human)

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Protein names

Recommended name:
    E3 ubiquitin-protein ligase Topors
    EC=6.3.2.-
Alternative name(s):
    SUMO1-protein E3 ligase Topors
    Topoisomerase I-binding RING finger protein
    Topoisomerase I-binding arginine/serine-rich protein
    Tumor suppressor p53-binding protein 3
      Short name=p53-binding protein 3
      Short name=p53BP3

Gene names

Name:	TOPORS
Synonyms:	LUN, TP53BPL

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Sequence length	1045 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

Hide | Top

Function	Functions as an ubiquitin-protein E3 ligase and as an E3 SUMO1-protein ligase. Can both ubiquitinate and sumoylate p53. Ref.8 Ref.12
Subunit structure	Interacts with PARK7/DJ-1 By similarity. Interacts with TOP1. Interacts with p53. Interacts with the SUMO1 conjugating enzyme UBE2I. Interacts with SUMO1. Ref.1 Ref.5 Ref.7
Subcellular location	Nucleus. Note: Localizes to discrete nuclear foci which partly overlap with PML nuclear bodies. Ref.1 Ref.5 Ref.7 Ref.2 Ref.6
Tissue specificity	Expressed at highest levels in testis and at lower levels in adrenal gland, bone marrow, brain, colon, heart, kidney, liver, muscle, ovary, pancreas, placenta, prostate, skeletal muscle, skin, small intestine, spleen, stomach, testis, thymus, thyroid and uterus. Expressed in the alveolar epithelium of the lung. Expression is commonly decreased in colon adenocarcinomas and lung cancers. Ref.5 Ref.2 Ref.10
Induction	By genotoxic agents such as cisplatin and camptothecin. Ref.13
Post-translational modification	Sumoylated. Ref.12 Ref.7
Involvement in disease	Defects in TOPORS are the cause of retinitis pigmentosa type 31 (RP31) [MIM:609923]. RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP31 inheritance is autosomal dominant. Ref.15
Sequence similarities	Contains 1 RING-type zinc finger.
Caution	Was originally (Ref.2) thought to bind to the palindromic consensus sequence 5'-TCCCAGCACTTTGGGA-3' and to regulate the transcription of numerous genes in the lung.

Hide | Top

Keywords
Biological process	Sensory transduction Ubl conjugation pathway Vision
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Retinitis pigmentosa
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	maintenance of protein location in nucleus Ref.7 Inferred from direct assay. Source: UniProtKB modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to DNA damage stimulus Ref.13 Inferred from direct assay. Source: UniProtKB transcription Ref.1 Non-traceable author statement. Source: UniProtKB visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nuclear speck Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Ref.2 Inferred from direct assay. Source: UniProtKB DNA topoisomerase I binding Ref.1 Inferred from physical interaction. Source: UniProtKB antigen binding Ref.5 Inferred from physical interaction. Source: UniProtKB ligase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Hide | Top

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 1045

1045

E3 ubiquitin-protein ligase Topors

PRO_0000232626

Zinc finger

103 – 142

40

RING-type

Region

1 – 195

195

E3 ubiquitin-protein ligase activity

Region

51 – 374

324

Required for DNA-binding

Region

437 – 654

218

Interaction with SUMO1

Region

437 – 574

138

Required for sumoylation and localization to discrete nuclear foci

Region

456 – 882

427

Interaction with TOP1

Region

456 – 731

276

Interaction with p53

Region

854 – 917

64

Interaction with UBE2I

Compositional bias

579 – 788

210

Arg-rich

Compositional bias

854 – 895

42

Lys-rich

Modified residue

98

1

Phosphoserine Ref.11 Ref.17 Ref.18 Ref.19 Ref.20

Modified residue

194

1

Phosphoserine Ref.16

Modified residue

864

1

Phosphoserine Ref.20

Modified residue

866

1

Phosphoserine Ref.20

Modified residue

902

1

Phosphoserine Ref.14

Modified residue

912

1

Phosphoserine Ref.14

Modified residue

914

1

Phosphoserine Ref.14

Cross-link

560

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Alternative sequence

1 – 65

65

Missing in isoform 2.

VSP_017916

Alternative sequence

66

1

E → M in isoform 2.

VSP_017917

Natural variant

154

1

A → T: dbSNP rs17855104. Ref.4

VAR_037629

Natural variant

517

1

E → K: dbSNP rs17855103. Ref.4

VAR_037630

Natural variant

749

1

N → D: dbSNP rs17857515. Ref.4

VAR_037631

Natural variant

812

1

P → R: dbSNP rs36034138.

VAR_037632

Mutagenesis

76

1

K → R: No effect on sumoylation. Ref.7

Mutagenesis

131

1

W → A: Abrogates E3 ubiquitin-protein ligase activity. Ref.8

Mutagenesis

301

1

K → R: No effect on sumoylation. Ref.7

Mutagenesis

485

1

K → R: No effect on sumoylation. Ref.7

Mutagenesis

560

1

K → R: Strongly reduces sumoylation. Ref.7

Mutagenesis

921

1

K → R: No effect on sumoylation. Ref.7

Sequence conflict

124 – 125

2

CF → K Ref.5

Sequence conflict

257

1

N → S in AAD23379. Ref.1

Sequence conflict

308

1

F → S in AAD23379. Ref.1

Sequence conflict

922

1

E → G in AAD23379. Ref.1

Sequence conflict

1040

1

R → K in AAD23379. Ref.1

Hide | Top

Sequence		Length	Mass (Da)
Isoform 1 (LUN-1) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 3DA635FDB5C83B77 Show »	FASTA	1,045	119,198
10 20 30 40 50 60 MGSQPPLGSP LSREEGEAPP PAPASEGRRR SRRVRLRGSC RHRPSFLGCR ELAASAPARP 70 80 90 100 110 120 APASSEIMAS AAKEFKMDNF SPKAGTSKLQ QTVPADASPD SKCPICLDRF DNVSYLDRCL 130 140 150 160 170 180 HKFCFRCVQE WSKNKAECPL CKQPFDSIFH SVRAEDDFKE YVLRPSYNGS FVTPDRRFRY 190 200 210 220 230 240 RTTLTRERNA SVYSPSGPVN RRTTTPPDSG VLFEGLGIST RPRDVEIPQF MRQIAVRRPT 250 260 270 280 290 300 TADERSLRKI QEQDIINFRR TLYRAGARVR NIEDGGRYRD ISAEFFRRNP ACLHRLVPWL 310 320 330 340 350 360 KRELTVLFGA HGSLVNIVQH IIMSNVTRYD LESQAFVSDL RPFLLNRTEH FIHEFISFAR 370 380 390 400 410 420 SPFNMAAFDQ HANYDCPAPS YEEGSHSDSS VITISPDEAE TQELDINVAT VSQAPWDDET 430 440 450 460 470 480 PGPSYSSSEQ VHVTMSSLLN TSDSSDEELV TGGATSQIQG VQTNDDLNND SDDSSDNCVI 490 500 510 520 530 540 VGFVKPLAER TPELVELSSD SEDLGSYEKM ETVKTQEQEQ SYSSGDSDVS RCSSPHSVLG 550 560 570 580 590 600 KDEQINKGHC DSSTRIKSKK EEKRSTSLSS PRNLNSSVRG DRVYSPYNHR HRKRGRSRSS 610 620 630 640 650 660 DSRSQSRSGH DQKNHRKHHG KKRMKSKRSR SRESSRPRGR RDKKRSRTRD SSWSRRSQTL 670 680 690 700 710 720 SLSSESTSRS RSRSSDHGKR RSRSRNRDRY YLRNNYGSRY KWEYTYYSRN KDRDGYESSY 730 740 750 760 770 780 RRRTLSRAHY SRQSSSPEFR VQSFSERTNA RKKNNHSERK YYYYERHRSR SLSSNRSRTA 790 800 810 820 830 840 STGTDRVRNE KPGGKRKYKT RHLEGTNEVA QPSREFASKA KDSHYQKSSS KLDGNYKNES 850 860 870 880 890 900 DTFSDSRSSD RETKHKRRKR KTRSLSVEIV YEGKATDTTK HHKKKKKKHK KKHKKHHGDN 910 920 930 940 950 960 ASRSPVVITI DSDSDKDSEV KEDTECDNSG PQDPLQNEFL APSLEPFETK DVVTIEAEFG 970 980 990 1000 1010 1020 VLDKECDIAT LSNNLNNANK TVDNIPPLAA SVEQTLDVRE ESTFVSDLEN QPSNIVSLQT 1030 1040 EPSRQLPSPR TSLMSVCLGR DCDMS « Hide
Isoform 2 (LUN-2). Checksum: 85E2A39A2978B20E Show »	FASTA	980	112,344
10 20 30 40 50 60 MIMASAAKEF KMDNFSPKAG TSKLQQTVPA DASPDSKCPI CLDRFDNVSY LDRCLHKFCF 70 80 90 100 110 120 RCVQEWSKNK AECPLCKQPF DSIFHSVRAE DDFKEYVLRP SYNGSFVTPD RRFRYRTTLT 130 140 150 160 170 180 RERNASVYSP SGPVNRRTTT PPDSGVLFEG LGISTRPRDV EIPQFMRQIA VRRPTTADER 190 200 210 220 230 240 SLRKIQEQDI INFRRTLYRA GARVRNIEDG GRYRDISAEF FRRNPACLHR LVPWLKRELT 250 260 270 280 290 300 VLFGAHGSLV NIVQHIIMSN VTRYDLESQA FVSDLRPFLL NRTEHFIHEF ISFARSPFNM 310 320 330 340 350 360 AAFDQHANYD CPAPSYEEGS HSDSSVITIS PDEAETQELD INVATVSQAP WDDETPGPSY 370 380 390 400 410 420 SSSEQVHVTM SSLLNTSDSS DEELVTGGAT SQIQGVQTND DLNNDSDDSS DNCVIVGFVK 430 440 450 460 470 480 PLAERTPELV ELSSDSEDLG SYEKMETVKT QEQEQSYSSG DSDVSRCSSP HSVLGKDEQI 490 500 510 520 530 540 NKGHCDSSTR IKSKKEEKRS TSLSSPRNLN SSVRGDRVYS PYNHRHRKRG RSRSSDSRSQ 550 560 570 580 590 600 SRSGHDQKNH RKHHGKKRMK SKRSRSRESS RPRGRRDKKR SRTRDSSWSR RSQTLSLSSE 610 620 630 640 650 660 STSRSRSRSS DHGKRRSRSR NRDRYYLRNN YGSRYKWEYT YYSRNKDRDG YESSYRRRTL 670 680 690 700 710 720 SRAHYSRQSS SPEFRVQSFS ERTNARKKNN HSERKYYYYE RHRSRSLSSN RSRTASTGTD 730 740 750 760 770 780 RVRNEKPGGK RKYKTRHLEG TNEVAQPSRE FASKAKDSHY QKSSSKLDGN YKNESDTFSD 790 800 810 820 830 840 SRSSDRETKH KRRKRKTRSL SVEIVYEGKA TDTTKHHKKK KKKHKKKHKK HHGDNASRSP 850 860 870 880 890 900 VVITIDSDSD KDSEVKEDTE CDNSGPQDPL QNEFLAPSLE PFETKDVVTI EAEFGVLDKE 910 920 930 940 950 960 CDIATLSNNL NNANKTVDNI PPLAASVEQT LDVREESTFV SDLENQPSNI VSLQTEPSRQ 970 980 LPSPRTSLMS VCLGRDCDMS « Hide

Hide | Top

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein." Haluska P. Jr., Saleem A., Rasheed Z., Ahmed F., Su E.W., Liu L.F., Rubin E.H. Nucleic Acids Res. 27:2538-2544(1999) [PubMed: 10352183] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TOP1, SUBCELLULAR LOCATION.
[2]	"Cloning and characterization of LUN, a novel RING-finger protein that is highly expressed in lung and specifically binds to a palindromic sequence." Chu D., Kakazu N., Gorrin-Rivas M.J., Lu H.P., Kawata M., Abe T., Ueda K., Adachi Y. J. Biol. Chem. 276:14004-14013(2001) [PubMed: 11278651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PUTATIVE DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Lung.
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS THR-154; LYS-517 AND ASP-749. Tissue: Placenta.
[5]	"Identification of a novel gene encoding a p53-associated protein." Zhou R., Wen H., Ao S.-Z. Gene 235:93-101(1999) [PubMed: 10415337] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-1045 (ISOFORM 1), INTERACTION WITH TP53, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]	"The topoisomerase I-binding RING protein, topors, is associated with promyelocytic leukemia nuclear bodies." Rasheed Z.A., Saleem A., Ravee Y., Pandolfi P.P., Rubin E.H. Exp. Cell Res. 277:152-160(2002) [PubMed: 12083797] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"The DNA topoisomerase I binding protein topors as a novel cellular target for SUMO-1 modification: characterization of domains necessary for subcellular localization and sumolation." Weger S., Hammer E., Engstler M. Exp. Cell Res. 290:13-27(2003) [PubMed: 14516784] [Abstract] Cited for: INTERACTION WITH SUMO1 AND UBE2I, SUBCELLULAR LOCATION, SUMOYLATION, MUTAGENESIS OF LYS-76; LYS-301; LYS-485; LYS-560 AND LYS-921.
[8]	"Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53." Rajendra R., Malegaonkar D., Pungaliya P., Marshall H., Rasheed Z., Brownell J., Liu L.F., Lutzker S., Saleem A., Rubin E.H. J. Biol. Chem. 279:36440-36444(2004) [PubMed: 15247280] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TRP-131.
[9]	"Expression of LUN gene that encodes a novel RING finger protein is correlated with development and progression of non-small cell lung cancer." Oyanagi H., Takenaka K., Ishikawa S., Kawano Y., Adachi Y., Ueda K., Wada H., Tanaka F. Lung Cancer 46:21-28(2004) [PubMed: 15364129] [Abstract] Cited for: REDUCED EXPRESSION IN LUNG CANCERS.
[10]	"The topoisomerase I- and p53-binding protein topors is differentially expressed in normal and malignant human tissues and may function as a tumor suppressor." Saleem A., Dutta J., Malegaonkar D., Rasheed F., Rasheed Z., Rajendra R., Marshall H., Luo M., Li H., Rubin E.H. Oncogene 23:5293-5300(2004) [PubMed: 15107820] [Abstract] Cited for: TISSUE SPECIFICITY, REDUCED EXPRESSION IN COLON CANCERS.
[11]	"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-98, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo." Weger S., Hammer E., Heilbronn R. FEBS Lett. 579:5007-5012(2005) [PubMed: 16122737] [Abstract] Cited for: FUNCTION, SUMOYLATION.
[13]	"Topors, a p53 and topoisomerase I-binding RING finger protein, is a coactivator of p53 in growth suppression induced by DNA damage." Lin L., Ozaki T., Takada Y., Kageyama H., Nakamura Y., Hata A., Zhang J.H., Simonds W.F., Nakagawara A., Koseki H. Oncogene 24:3385-3396(2005) [PubMed: 15735665] [Abstract] Cited for: INDUCTION.
[14]	"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-902; SER-912 AND SER-914, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"Mutations in TOPORS cause autosomal dominant retinitis pigmentosa with perivascular retinal pigment epithelium atrophy." Chakarova C.F., Papaioannou M.G., Khanna H., Lopez I., Waseem N., Shah A., Theis T., Friedman J., Maubaret C., Bujakowska K., Veraitch B., El-Aziz M.M.A., Prescott de Q., Parapuram S.K., Bickmore W.A., Munro P.M.G., Gal A., Hamel C.P. Bhattacharya S.S. Am. J. Hum. Genet. 81:1098-1103(2007) [PubMed: 17924349] [Abstract] Cited for: INVOLVEMENT IN RP31.
[16]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, MASS SPECTROMETRY.
[17]	"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-98, MASS SPECTROMETRY.
[18]	"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-98, MASS SPECTROMETRY.
[19]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, MASS SPECTROMETRY.
[20]	"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-98; SER-864 AND SER-866, MASS SPECTROMETRY. Tissue: T-cell.
+	Additional computationally mapped references.

Hide | Top

Sequence databases
EMBL GenBank DDBJ	AF098300 mRNA. Translation: AAD23379.1. AB045732 mRNA. Translation: BAB03714.1. AB045733 mRNA. Translation: BAB03715.1. AL353671 Genomic DNA. Translation: CAH71253.1. AL353671 Genomic DNA. Translation: CAH71254.1. BC060884 mRNA. Translation: AAH60884.1. U82939 mRNA. Translation: AAC98530.1. Different initiation.
IPI	IPI00396077. IPI00643426.
RefSeq	NP_005793.2.
UniGene	Hs.589962
3D structure databases
SMR	Q9NS56. Positions 99-163.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9NS56.
PTM databases
PhosphoSite	Q9NS56.
Proteomic databases
PRIDE	Q9NS56.
Genome annotation databases
Ensembl	ENST00000360538; ENSP00000353735; ENSG00000197579; Homo sapiens. [Genome view]
GeneID	10210.
KEGG	hsa:10210.
UCSC	uc003zrb.1. human. uc003zrc.1. human.
Organism-specific databases
CTD	10210.
GeneCards	GC09M032530.
H-InvDB	HIX0034742.
HGNC	HGNC:21653. TOPORS.
MIM	609507. gene. 609923. phenotype.
Orphanet	791. Retinitis pigmentosa.
PharmGKB	PA134979531.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18391.
HOGENOM	HBG283067.
HOVERGEN	Q9NS56.
InParanoid	Q9NS56.
OMA	DIINFRR.
OrthoDB	EOG9QNQGF.
PhylomeDB	Q9NS56.
Gene expression databases
ArrayExpress	Q9NS56.
Bgee	Q9NS56.
CleanEx	HS_TOPORS.
Genevestigator	Q9NS56.
GermOnline	ENSG00000197579. Homo sapiens.
Family and domain databases
InterPro	IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	38656.
SOURCE	Search...

Hide | Top

Entry name

TOPRS_HUMAN

Accession

Primary (citable) accession number: Q9NS56
Secondary accession number(s): O43273

Q9UNR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	October 1, 2000
Last modified:	January 19, 2010
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

Hide | Top

Human chromosome 9

Human chromosome 9: 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

SIMILARITY comments

Index of protein domains and families

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NS56-1)

Also known as: LUN-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: Q9NS56-2)

Also known as: LUN-2;

The sequence of this isoform differs from the canonical sequence as follows:
1-65: Missing.
66-66: E → M