Q8IYW5 (RN168_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase RNF168
Short name=hRNF168
EC=6.3.2.-

Alternative name(s):
RING finger protein 168

Gene names

Name:

RNF168

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	571 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro; possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively). Ref.6 Ref.7 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Monomer. Interacts with UBE2N/UBC13. Ref.6 Ref.17
Subcellular location	Nucleus. Note: Localizes to double-strand breaks (DSBs) sites of DNA damage. Ref.5 Ref.6 Ref.7 Ref.10 Ref.15
Domain	The MIU motif (motif interacting with ubiquitin) mediates the interaction with both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains (Ref.5). The UMI motif mediates interaction with ubiquitin with a preference for 'Lys-63'-linked ubiquitin (Ref.10). The specificity for different types of ubiquitin is mediated by juxtaposition of ubiquitin-binding motifs (MIU and UMI motifs) with LR motifs (LRMs) (Ref.15).
Post-translational modification	Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks (DSBs). Ref.13 Ubiquitinated. Ref.5 Ref.10
Involvement in disease	Riddle syndrome (RIDDLES) [MIM:611943]: Characterized by increased radiosensitivity, immunodeficiency, mild motor control and learning difficulties, facial dysmorphism, and short stature. Defects are probably due to impaired localization of TP53BP1 and BRCA1 at DNA lesions. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6
Sequence similarities	Belongs to the RNF168 family. Contains 1 RING-type zinc finger.
Caution	According to a well-established model, RNF168 cannot initiate H2A 'Lys-63'-linked ubiquitination and is recruited following RNF8-dependent histone ubiquitination to amplify H2A 'Lys-63'-linked ubiquitination (Ref.5, Ref.6 and Ref.7). However, other data suggest that RNF168 is the priming ubiquitin ligase by mediating monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub respectively) (Ref.16). These data suggest that RNF168 might be recruited to DSBs sites in a RNF8-dependent manner by binding to non-histone proteins ubiquitinated via 'Lys-63'-linked and initiates monoubiquitination of H2A, which is then amplified by RNF8 (Ref.16). Additional evidences are however required to confirm these data.
Sequence caution	The sequence BAC04060.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	double-strand break repair Inferred from direct assay Ref.6Ref.7Ref.16. Source: UniProtKB histone H2A K63-linked ubiquitination Inferred from direct assay Ref.6Ref.7Ref.5. Source: UniProtKB histone H2A monoubiquitination Inferred from direct assay Ref.16. Source: UniProtKB histone H2A-K13 ubiquitination Inferred from direct assay Ref.16. Source: UniProtKB histone H2A-K15 ubiquitination Inferred from direct assay Ref.16. Source: UniProtKB interstrand cross-link repair Traceable author statement Ref.14. Source: UniProtKB isotype switching Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of translational elongation Inferred from mutant phenotype Ref.9. Source: UniProtKB positive regulation of DNA repair Inferred from direct assay Ref.6Ref.7. Source: UniProtKB response to ionizing radiation Inferred from direct assay Ref.6Ref.7. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.12. Source: UniProtKB
Cellular_component	nucleus Inferred from direct assay Ref.6Ref.7. Source: UniProtKB site of double-strand break Inferred from direct assay Ref.5Ref.10. Source: UniProtKB ubiquitin ligase complex Inferred from direct assay Ref.6Ref.7. Source: UniProtKB
Molecular_function	K63-linked polyubiquitin binding Inferred from direct assay Ref.5Ref.10Ref.15. Source: UniProtKB histone binding Inferred from direct assay Ref.6Ref.7. Source: UniProtKB nucleosome binding Inferred from direct assay Ref.15. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.6Ref.7Ref.5Ref.12Ref.16. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
UBE2N	P61088	2	EBI-914207,EBI-1052908

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 571

571

E3 ubiquitin-protein ligase RNF168

PRO_0000245596

Regions

Zinc finger

16 – 55

40

RING-type

Motif

110 – 128

19

LR motif 1

Motif

143 – 151

9

UMI motif

Motif

168 – 191

24

MIU motif 1

Motif

439 – 462

24

MIU motif 2

Motif

466 – 477

12

LR motif 2

Compositional bias

115 – 177

63

Glu-rich

Amino acid modifications

Modified residue

411

1

Phosphoserine Ref.4 Ref.8

Modified residue

414

1

Phosphoserine Ref.4 Ref.8

Modified residue

415

1

Phosphoserine Ref.4 Ref.8

Natural variations

Natural variant

387

1

K → R.
Corresponds to variant rs35774921 [ dbSNP | Ensembl ].

VAR_034466

Natural variant

401

1

P → Q. Ref.1
Corresponds to variant rs3796129 [ dbSNP | Ensembl ].

VAR_026997

Natural variant

413

1

E → K.
Corresponds to variant rs6790173 [ dbSNP | Ensembl ].

VAR_052110

Experimental info

Mutagenesis

16

1

C → S: Does not affect ability to bind ubiquitin and localization to DSBs sites, while it abolishes E3 ligase activity; when associated with S-19. Ref.5 Ref.15

Mutagenesis

18

1

I → A: Abolishes ability to ubiquitinate KDM4A. Ref.12 Ref.15

Mutagenesis

19

1

C → S: Does not affect ability to bind ubiquitin and localization to DSBs sites, while it abolishes E3 ligase activity; when associated with S-16. Ref.5 Ref.15

Mutagenesis

57

1

R → D: Does not affect the monomeric structure but abolishes ability to monoubiquitinate H2A in nucleosomes. Ref.15 Ref.16

Mutagenesis

149 – 150

2

LL → AA: Impaired ability to bind ubiquitin. Ref.15

Mutagenesis

179

1

A → G: Impairs ability to form foci following ionizing radiation and impaired binding to 'Lys-63'-linked ubiquitin. Ref.5 Ref.6 Ref.10 Ref.15

Mutagenesis

450

1

A → G: Still able to bind 'Lys-63'-linked ubiquitin. Ref.5 Ref.6 Ref.10 Ref.15

Mutagenesis

476 – 477

2

LR → AA: Does not affect ubiquitin-binding but impairs recruitment to DSBs. Ref.15

Sequence conflict

9

1

P → L in BAB70801. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

571

Helix Strand Turn

Details...

Helix

11 – 14

4

Turn

17 – 19

3

Helix

37 – 43

7

Turn

44 – 48

5

Turn

52 – 54

3

Helix

59 – 67

9

Helix

74 – 83

10

Helix

85 – 93

9

Sequences

	Sequence		Length	Mass (Da)
	Q8IYW5 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 51E16DA92BA654C1	FASTA	571	65,020
	10 20 30 40 50 60 MALPKDAIPS LSECQCGICM EILVEPVTLP CNHTLCKPCF QSTVEKASLC CPFCRRRVSS 70 80 90 100 110 120 WTRYHTRRNS LVNVELWTII QKHYPRECKL RASGQESEEV ADDYQPVRLL SKPGELRREY 130 140 150 160 170 180 EEEISKVAAE RRASEEEENK ASEEYIQRLL AEEEEEEKRQ AEKRRRAMEE QLKSDEELAR 190 200 210 220 230 240 KLSIDINNFC EGSISASPLN SRKSDPVTPK SEKKSKNKQR NTGDIQKYLT PKSQFGSASH 250 260 270 280 290 300 SEAVQEVRKD SVSKDIDSSD RKSPTGQDTE IEDMPTLSPQ ISLGVGEQGA DSSIESPMPW 310 320 330 340 350 360 LCACGAEWYH EGNVKTRPSN HGKELCVLSH ERPKTRVPYS KETAVMPCGR TESGCAPTSG 370 380 390 400 410 420 VTQTNGNNTG ETENEESCLL ISKEISKRKN QESSFEAVKD PCFSAKRRKV SPESSPDQEE 430 440 450 460 470 480 TEINFTQKLI DLEHLLFERH KQEEQDRLLA LQLQKEVDKE QMVPNRQKGS PDEYHLRATS 490 500 510 520 530 540 SPPDKVLNGQ RKNPKDGNFK RQTHTKHPTP ERGSRDKNRQ VSLKMQLKQS VNRRKMPNST 550 560 570 RDHCKVSKSA HSLQPSISQK SVFQMFQRCT K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , 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], VARIANT GLN-401. Tissue: Cerebellum and Testis.
[2]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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]. Tissue: Brain.
[4]	"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-411; SER-414 AND SER-415, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX." Pinato S., Scandiuzzi C., Arnaudo N., Citterio E., Gaudino G., Penengo L. BMC Mol. Biol. 10:55-55(2009) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITIN-BINDING, MIU MOTIF, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF CYS-16; CYS-19; ALA-179 AND ALA-450.
[6]	"The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage." Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K., Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M., Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L., Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R., Durocher D. Cell 136:420-434(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN RIDDLES, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH UBE2N, MUTAGENESIS OF ALA-179 AND ALA-450.
[7]	"RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins." Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H., Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J., Lukas J., Lukas C. Cell 136:435-446(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
[8]	"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-411; SER-414 AND SER-415, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"ATM-dependent chromatin changes silence transcription in cis to DNA double-strand breaks." Shanbhag N.M., Rafalska-Metcalf I.U., Balane-Bolivar C., Janicki S.M., Greenberg R.A. Cell 141:970-981(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"UMI, a novel RNF168 ubiquitin binding domain involved in the DNA damage signaling pathway." Pinato S., Gatti M., Scandiuzzi C., Confalonieri S., Penengo L. Mol. Cell. Biol. 31:118-126(2011) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITIN-BINDING, UMI MOTIF, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF 149-LEU-LEU-150; ALA-179 AND ALA-450.
[11]	"A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase." Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L. Cell Cycle 11:2538-2544(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites." Mallette F.A., Mattiroli F., Cui G., Young L.C., Hendzel M.J., Mer G., Sixma T.K., Richard S. EMBO J. 31:1865-1878(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN UBIQUITINATION OF KDM4A, MUTAGENESIS OF ILE-18.
[13]	"DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger." Danielsen J.R., Povlsen L.K., Villumsen B.H., Streicher W., Nilsson J., Wikstrom M., Bekker-Jensen S., Mailand N. J. Cell Biol. 197:179-187(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION.
[14]	"A ubiquitin-binding protein, FAAP20, links RNF8-mediated ubiquitination to the Fanconi anemia DNA repair network." Yan Z., Guo R., Paramasivam M., Shen W., Ling C., Fox D. III, Wang Y., Oostra A.B., Kuehl J., Lee D.Y., Takata M., Hoatlin M.E., Schindler D., Joenje H., de Winter J.P., Li L., Seidman M.M., Wang W. Mol. Cell 47:61-75(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks." Panier S., Ichijima Y., Fradet-Turcotte A., Leung C.C., Kaustov L., Arrowsmith C.H., Durocher D. Mol. Cell 47:383-395(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, UBIQUITIN-BINDING, LR MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF 476-LEU-ARG-477.
[16]	"RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage signaling." Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E., Vermeulen W., Marteijn J.A., Sixma T.K. Cell 150:1182-1195(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-57.
[17]	"Molecular insights into the function of RING Finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation." Campbell S.J., Edwards R.A., Leung C.C., Neculai D., Hodge C.D., Dhe-Paganon S., Glover J.N. J. Biol. Chem. 287:23900-23910(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 1-113, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK054732 mRNA. Translation: BAB70801.1.
AK093113 mRNA. Translation: BAC04060.1. Different initiation.
AC092933 Genomic DNA. No translation available.
AC117490 Genomic DNA. No translation available.
BC033791 mRNA. Translation: AAH33791.1.

IPI

IPI00217899.

RefSeq

NP_689830.2. NM_152617.3.

UniGene

Hs.250648.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3L11	X-ray	2.12	A	1-113	[»]

ProteinModelPortal

Q8IYW5.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37451N.

IntAct

Q8IYW5. 8 interactions.

MINT

MINT-1180501.

STRING

9606.ENSP00000320898.

PTM databases

PhosphoSite

Q8IYW5.

Polymorphism databases

DMDM

74762499.

Proteomic databases

PaxDb

Q8IYW5.

PRIDE

Q8IYW5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000318037; ENSP00000320898; ENSG00000163961.

GeneID

165918.

KEGG

hsa:165918.

UCSC

uc003fwq.3. human.

Organism-specific databases

CTD

165918.

GeneCards

GC03M196195.

HGNC

HGNC:26661. RNF168.

MIM

611943. phenotype.
612688. gene.

neXtProt

NX_Q8IYW5.

PharmGKB

PA134945219.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG292819.

HOGENOM

HOG000154156.

HOVERGEN

HBG067220.

InParanoid

Q8IYW5.

OMA

KSIFQMF.

OrthoDB

EOG4THVT2.

PhylomeDB

Q8IYW5.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q8IYW5.

Bgee

Q8IYW5.

CleanEx

HS_RNF168.

Genevestigator

Q8IYW5.

GermOnline

ENSG00000163961. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

SMART

SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q8IYW5.

GenomeRNAi

165918.

NextBio

88572.

SOURCE

Search...

Entry information

Entry name

RN168_HUMAN

Accession

Primary (citable) accession number: Q8IYW5
Secondary accession number(s): Q8NA67, Q96NS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 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.