Q96BH1 (RNF25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase RNF25
EC=6.3.2.-

Alternative name(s):
RING finger protein 25

Gene names

Name:

RNF25

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

General annotation (Comments)

Function	E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NKD2 By similarity. Stimulates transcription mediated by NF-kappa-B. Ref.6
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with UBE2D2, and may also interact with UBE2E1 and UBE2E3. Interacts with NKD2 By similarity. Interacts with RELA. Ref.6
Domain	The RING-type zinc finger domain interacts with an ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination.
Post-translational modification	Ubiquitinated By similarity.
Sequence similarities	Contains 1 RING-type zinc finger. Contains 1 RWD domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of NF-kappaB transcription factor activity Inferred from direct assay Ref.6. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay Ref.6. Source: UniProtKB nucleus Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	ubiquitin-protein ligase activity Inferred from sequence or structural similarity. 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

Chain

1 – 459

459

E3 ubiquitin-protein ligase RNF25

PRO_0000056066

Regions

Domain

18 – 128

111

RWD

Zinc finger

135 – 202

68

RING-type

Amino acid modifications

Modified residue

450

1

Phosphoserine Ref.7

Experimental info

Mutagenesis

159

1

C → S: Reduced activation of NF-kappa-B. Ref.6

Mutagenesis

161

1

C → S: Strongly reduced activation of NF-kappa-B. Ref.6

Sequence conflict

186

1

H → R in BAD96245. Ref.2

Sequence conflict

346

1

P → S in BAD96245. Ref.2

Secondary structure

1

.

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.

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.

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459

Helix Strand Turn

Details...

Helix

15 – 26

12

Turn

28 – 30

3

Beta strand

31 – 34

4

Turn

38 – 40

3

Beta strand

43 – 49

7

Beta strand

55 – 58

4

Beta strand

63 – 70

8

Beta strand

80 – 89

10

Helix

91 – 107

17

Turn

108 – 110

3

Helix

114 – 125

12

Sequences

	Sequence		Length	Mass (Da)
	Q96BH1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: CE7C66EF2E988917	FASTA	459	51,219
	10 20 30 40 50 60 MAASASAAAG EEDWVLPSEV EVLESIYLDE LQVIKGNGRT SPWEIYITLH PATAEDQDSQ 70 80 90 100 110 120 YVCFTLVLQV PAEYPHEVPQ ISIRNPRGLS DEQIHTILQV LGHVAKAGLG TAMLYELIEK 130 140 150 160 170 180 GKEILTDNNI PHGQCVICLY GFQEKEAFTK TPCYHYFHCH CLARYIQHME QELKAQGQEQ 190 200 210 220 230 240 EQERQHATTK QKAVGVQCPV CREPLVYDLA SLKAAPEPQQ PMELYQPSAE SLRQQEERKR 250 260 270 280 290 300 LYQRQQERGG IIDLEAERNR YFISLQQPPA PAEPESAVDV SKGSQPPSTL AAELSTSPAV 310 320 330 340 350 360 QSTLPPPLPV ATQHICEKIP GTRSNQQRLG ETQKAMLDPP KPSRGPWRQP ERRHPKGGEC 370 380 390 400 410 420 HAPKGTRDTQ ELPPPEGPLK EPMDLKPEPH SQGVEGPPQE KGPGSWQGPP PRRTRDCVRW 430 440 450 ERSKGRTPGS SYPRLPRGQG AYRPGTRRES LGLESKDGS

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]. Tissue: Cerebellum.
[2]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adipose tissue.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]. Tissue: Placenta.
[6]	"RING finger protein AO7 supports NF-kappaB-mediated transcription by interacting with the transactivation domain of the p65 subunit." Asamitsu K., Tetsuka T., Kanazawa S., Okamoto T. J. Biol. Chem. 278:26879-26887(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RELA, MUTAGENESIS OF CYS-159 AND CYS-161.
[7]	"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-450, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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].
[9]	"An extended conformation of the RWD domain of human RING finger protein 25." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 10-134.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK023968 mRNA. Translation: BAB14743.1.
AK289501 mRNA. Translation: BAF82190.1.
AK222525 mRNA. Translation: BAD96245.1.
AC009974 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70645.1.
BC015612 mRNA. Translation: AAH15612.1.

IPI

IPI00059944.

RefSeq

NP_071898.2. NM_022453.2.

UniGene

Hs.471403.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DAY	NMR	-	A	11-125	[»]
2DMF	NMR	-	A	11-134	[»]

ProteinModelPortal

Q96BH1.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29063N.

IntAct

Q96BH1. 10 interactions.

STRING

9606.ENSP00000295704.

PTM databases

PhosphoSite

Q96BH1.

Polymorphism databases

DMDM

21362899.

Proteomic databases

PaxDb

Q96BH1.

PRIDE

Q96BH1.

Protocols and materials databases

DNASU

64320.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295704; ENSP00000295704; ENSG00000163481.

GeneID

64320.

KEGG

hsa:64320.

UCSC

uc002vit.3. human.

Organism-specific databases

CTD

64320.

GeneCards

GC02M219528.

HGNC

HGNC:14662. RNF25.

HPA

HPA036421.

neXtProt

NX_Q96BH1.

PharmGKB

PA34429.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG243985.

HOGENOM

HOG000012992.

HOVERGEN

HBG055249.

InParanoid

Q96BH1.

KO

K10640.

OMA

EDWVLPS.

OrthoDB

EOG4PVNZP.

PhylomeDB

Q96BH1.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q96BH1.

Bgee

Q96BH1.

CleanEx

HS_RNF25.

Genevestigator

Q96BH1.

GermOnline

ENSG00000163481. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.
3.30.40.10. 1 hit.

InterPro

IPR006575. RWD-domain.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Pfam

PF05773. RWD. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]

SMART

SM00184. RING. 1 hit.
SM00591. RWD. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS50908. RWD. 1 hit.
PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q96BH1.

GenomeRNAi

64320.

NextBio

66233.

Entry information

Entry name

RNF25_HUMAN

Accession

Primary (citable) accession number: Q96BH1
Secondary accession number(s): A8K0D6, Q53HQ5, Q9H874

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 106 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.