O43567 (RNF13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase RNF13
EC=6.3.2.-

Alternative name(s):
RING finger protein 13

Gene names

Name:	RNF13
Synonyms:	RZF

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	381 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	E3 ubiquitin-protein ligase that may play a role in controlling cell proliferation. Ref.9
Pathway	Protein modification; protein ubiquitination.
Subcellular location	Endoplasmic reticulum membrane. Golgi apparatus membrane. Late endosome membrane; Single-pass membrane protein By similarity. Lysosome membrane. Nucleus inner membrane By similarity. Note: Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane By similarity. Ref.8 Ref.9
Tissue specificity	Widely expressed (at protein level). In normal pancreas, expressed in islets, but not in ducts, nor in acini (at protein level). Ref.9
Domain	The RING-type zinc finger domain is required for E3 ligase activity.
Post-translational modification	Auto-ubiquitinated.
Sequence similarities	Contains 1 PA (protease associated) domain. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Endoplasmic reticulum Endosome Golgi apparatus Lysosome Membrane Nucleus
Domain	Signal Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein autoubiquitination Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW late endosome membrane Inferred from sequence or structural similarity. Source: UniProtKB lysosomal membrane Inferred from sequence or structural similarity. Source: UniProtKB nuclear inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Signal peptide	1 – 34	34	Potential
	Chain	35 – 381	347	E3 ubiquitin-protein ligase RNF13		PRO_0000056054
Regions
	Topological domain	35 – 182	148	Lumenal Potential
	Transmembrane	183 – 203	21	Helical; Potential
	Topological domain	204 – 381	178	Cytoplasmic Potential
	Domain	65 – 160	96	PA
	Zinc finger	240 – 282	43	RING-type; atypical
Amino acid modifications
	Modified residue	292	1	Phosphoserine By similarity
	Modified residue	294	1	Phosphoserine By similarity
	Modified residue	296	1	Phosphothreonine By similarity
	Modified residue	298	1	Phosphoserine By similarity
	Modified residue	299	1	Phosphoserine By similarity
	Glycosylation	88	1	N-linked (GlcNAc...) Ref.9
Experimental info
	Mutagenesis	43	1	N → A: No effect on glycosylation. Ref.9
	Mutagenesis	88	1	N → A: Loss of glycosylation. Ref.9
	Mutagenesis	258	1	C → A: Complete loss of E3 ligase activity; when associated with A-260. Ref.9
	Mutagenesis	260	1	H → A: Complete loss of E3 ligase activity; when associated with A-258. Ref.9
	Mutagenesis	270	1	W → A: Drastically reduces E3 ligase activity. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	O43567 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 4600727D0F197653	FASTA	381	42,814
	10 20 30 40 50 60 MLLSIGMLML SATQVYTILT VQLFAFLNLL PVEADILAYN FENASQTFDD LPARFGYRLP 70 80 90 100 110 120 AEGLKGFLIN SKPENACEPI VPPPVKDNSS GTFIVLIRRL DCNFDIKVLN AQRAGYKAAI 130 140 150 160 170 180 VHNVDSDDLI SMGSNDIEVL KKIDIPSVFI GESSANSLKD EFTYEKGGHL ILVPEFSLPL 190 200 210 220 230 240 EYYLIPFLII VGICLILIVI FMITKFVQDR HRARRNRLRK DQLKKLPVHK FKKGDEYDVC 250 260 270 280 290 300 AICLDEYEDG DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ 310 320 330 340 350 360 EENEVTEHTP LLRPLASVSA QSFGALSESR SHQNMTESSD YEEDDNEDTD SSDAENEINE 370 380 HDVVVQLQPN GERDYNIANT V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The gene for a RING zinc finger protein is expressed in the inner chick ear after noise exposure." Lomax M.I., Warner S.J., Bersirli C.G., Gong T.-W.L. Prim. Sens. Neuron 2:305-316(1998) Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Yu W., Gibbs R.A. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"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: Glial tumor and Spleen.
[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].
[5]	"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].
[6]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 and Urinary bladder.
[8]	"Integral and associated lysosomal membrane proteins." Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A. Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Placenta.
[9]	"RNF13: a novel RING-type ubiquitin ligase over-expressed in pancreatic cancer." Zhang Q., Meng Y., Zhang L., Chen J., Zhu D. Cell Res. 19:348-357(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AUTOUBIQUITINATION, GLYCOSYLATION AT ASN-88, MUTAGENESIS OF ASN-43; ASN-88; CYS-258; HIS-260 AND TRP-270.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF037204 mRNA. Translation: AAC03769.1. AF070558 mRNA. Translation: AAC28641.1. AK313304 mRNA. Translation: BAG36109.1. AK090638 mRNA. Translation: BAG52202.1. CR456804 mRNA. Translation: CAG33085.1. AC069216 Genomic DNA. No translation available. AC117395 Genomic DNA. No translation available. CH471052 Genomic DNA. Translation: EAW78859.1. CH471052 Genomic DNA. Translation: EAW78861.1. CH471052 Genomic DNA. Translation: EAW78863.1. BC009803 mRNA. Translation: AAH09803.1. BC009781 mRNA. Translation: AAH09781.1.
IPI	IPI00151036.
RefSeq	NP_009213.1. NM_007282.4. NP_899237.1. NM_183381.2.
UniGene	Hs.12333.
3D structure databases
ProteinModelPortal	O43567.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43567. 7 interactions.
STRING	9606.ENSP00000341361.
PTM databases
PhosphoSite	O43567.
Proteomic databases
PaxDb	O43567.
PRIDE	O43567.
Protocols and materials databases
DNASU	11342.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000344229; ENSP00000341361; ENSG00000082996. ENST00000392894; ENSP00000376628; ENSG00000082996.
GeneID	11342.
KEGG	hsa:11342.
UCSC	uc003exn.4. human.
Organism-specific databases
CTD	11342.
GeneCards	GC03P149531.
HGNC	HGNC:10057. RNF13.
HPA	HPA008709.
MIM	609247. gene.
neXtProt	NX_O43567.
PharmGKB	PA34422.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5540.
HOGENOM	HOG000234362.
HOVERGEN	HBG063762.
InParanoid	O43567.
KO	K15692.
OMA	MGSNDID.
OrthoDB	EOG41NTMB.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	O43567.
Bgee	O43567.
CleanEx	HS_RNF13.
Genevestigator	O43567.
GermOnline	ENSG00000082996. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR003137. Protease-assoc_domain. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF02225. PA. 1 hit. PF13639. zf-RING_2. 1 hit. [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
ChiTaRS	RNF13. human.
GenomeRNAi	11342.
NextBio	43096.
SOURCE	Search...

Entry information

Entry name

RNF13_HUMAN

Accession

Primary (citable) accession number: O43567
Secondary accession number(s): Q6IBJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 98 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.