Reviewed, UniProtKB/Swiss-Prot Q8WVD3 (RN138_HUMAN)

Names and origin

Protein names

Recommended name:
    E3 ubiquitin-protein ligase RNF138
    EC=6.3.2.-
Alternative name(s):
    RING finger protein 138
    Nemo-like kinase-associated RING finger protein
      Short name=NLK-associated RING finger protein
      Short name=hNARF

Gene names

Name:	RNF138
Synonyms:	NARF
ORF Names:	HSD4, HSD-4

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	245 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	E3 ubiquitin-protein ligase. Together with NLK, involved in the ubiquitination and degradation of TCF/LEF. Also exhibits auto-ubiquitination activity in combination with UBE2K. May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway. Ref.7
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with NLK. Ref.7
Domain	The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme By similarity.
Post-translational modification	Auto-ubiquitinated. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8
Sequence similarities	Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway Wnt signaling pathway
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW protein kinase binding Ref.7 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q8WVD3-1)

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: Q8WVD3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     38-131: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 245	245	E3 ubiquitin-protein ligase RNF138		PRO_0000261607
Regions
	Zinc finger	18 – 58	41	RING-type
Amino acid modifications
	Modified residue	124	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	38 – 131	94	Missing in isoform 2.		VSP_021732
	Natural variant	81	1	K → R: dbSNP rs7229690.		VAR_052109
Experimental info
	Sequence conflict	118	1	I → V in AAD46623. Ref.1
	Sequence conflict	215	1	H → R in AAD46623. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 807EE4500BE0919C	FASTA	245	28,193
	10 20 30 40 50 60 MAEDLSAATS YTEDDFYCPV CQEVLKTPVR TTACQHVFCR KCFLTAMRES GAHCPLCRGN 70 80 90 100 110 120 VTRRERACPE RALDLENIMR KFSGSCRCCA KQIKFYRMRH HYKSCKKYQD EYGVSSIIPN 130 140 150 160 170 180 FQISQDSVGN SNRSETSTSD NTETYQENTS SSGHPTFKCP LCQESNFTRQ RLLDHCNSNH 190 200 210 220 230 240 LFQIVPVTCP ICVSLPWGDP SQITRNFVSH LNQRHQFDYG EFVNLQLDEE TQYQTAVEES FQVNI
	Isoform 2. Checksum: 4FDCD6069E17B2BB	FASTA	151	17,262
	10 20 30 40 50 60 MAEDLSAATS YTEDDFYCPV CQEVLKTPVR TTACQHVNRS ETSTSDNTET YQENTSSSGH 70 80 90 100 110 120 PTFKCPLCQE SNFTRQRLLD HCNSNHLFQI VPVTCPICVS LPWGDPSQIT RNFVSHLNQR 130 140 150 HQFDYGEFVN LQLDEETQYQ TAVEESFQVN I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new spermatogenesis-related gene." Wang L., Miao S., Yang J., Zhang X., Li M. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Placenta.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-245 (ISOFORM 1). Tissue: Testis.
[7]	"NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF)." Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K., Hyodo-Miura J., Kawachi K., Natsume T., Shibuya H. J. Biol. Chem. 281:20749-20760(2006) [PubMed: 16714285] [Abstract] Cited for: FUNCTION, INTERACTION WITH NLK.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF162680 mRNA. Translation: AAD46623.2. AK023579 mRNA. Translation: BAB14614.1. BT006878 mRNA. Translation: AAP35524.1. CR457150 mRNA. Translation: CAG33431.1. BC018107 mRNA. Translation: AAH18107.1. AL133557 mRNA. Translation: CAB63712.1.
IPI	IPI00012239. IPI00328938.
PIR	T43439.
RefSeq	NP_057355.2. NP_937761.1.
UniGene	Hs.302408
3D structure databases
HSSP	HSSP built from PDB template 1JM7 based on UniProtKB P38398.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8WVD3. 4 interactions.
PTM databases
PhosphoSite	Q8WVD3.
Proteomic databases
PRIDE	Q8WVD3.
Genome annotation databases
Ensembl	ENSG00000134758. Homo sapiens. [Contig view]
GeneID	51444.
KEGG	hsa:51444.
Organism-specific databases
GeneCards	GC18P027925.
HGNC	HGNC:17765. RNF138.
PharmGKB	PA134952071.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q8WVD3.
OMA	Q8WVD3. IETYQEN.
Gene expression databases
ArrayExpress	Q8WVD3.
Bgee	Q8WVD3.
CleanEx	HS_NARF. HS_RNF138.
Family and domain databases
InterPro	IPR015880. Znf_C2H2-like. 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. 2 hits. SM00355. ZnF_C2H2. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	55035.

Entry information

Entry name

RN138_HUMAN

Accession

Primary (citable) accession number: Q8WVD3
Secondary accession number(s): Q9H8K2, Q9UF87, Q9UKI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	March 1, 2002
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)