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Protein

E3 ubiquitin-protein ligase RNF103

Gene

RNF103

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway.2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri621 – 66343RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • central nervous system development Source: ProtInc
  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF103 (EC:6.3.2.-)
Alternative name(s):
KF-1
Short name:
hKF-1
RING finger protein 103
Zinc finger protein 103 homolog
Short name:
Zfp-103
Gene namesi
Name:RNF103
Synonyms:ZFP103
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12859. RNF103.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei6 – 2621HelicalSequence analysisAdd
BLAST
Transmembranei326 – 34621HelicalSequence analysisAdd
BLAST
Transmembranei366 – 38621HelicalSequence analysisAdd
BLAST
Transmembranei411 – 43121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi621 – 6211C → S: Loss of E2-dependent ubiquitination. 1 Publication

Organism-specific databases

PharmGKBiPA37448.

Polymorphism and mutation databases

BioMutaiRNF103.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 685685E3 ubiquitin-protein ligase RNF103PRO_0000056084Add
BLAST

Proteomic databases

PaxDbiO00237.
PRIDEiO00237.

PTM databases

iPTMnetiO00237.
PhosphoSiteiO00237.

Expressioni

Tissue specificityi

Highly expressed in the normal cerebellum but not in the cerebral cortex.1 Publication

Gene expression databases

BgeeiO00237.
CleanExiHS_RNF103.
GenevisibleiO00237. HS.

Organism-specific databases

HPAiHPA057922.

Interactioni

Subunit structurei

Interacts with DERL1 and VCP.1 Publication

Protein-protein interaction databases

BioGridi113601. 13 interactions.
IntActiO00237. 9 interactions.
STRINGi9606.ENSP00000237455.

Structurei

3D structure databases

ProteinModelPortaliO00237.
SMRiO00237. Positions 619-663.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri621 – 66343RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00390000006413.
HOGENOMiHOG000006578.
HOVERGENiHBG054144.
InParanoidiO00237.
KOiK15695.
OMAiGKVHWEK.
OrthoDBiEOG7QG44T.
PhylomeDBiO00237.
TreeFamiTF329229.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00237-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLKLFFLLL YFLVLFVLAR FFEAIVWYET GIFATQLVDP VALSFKKLKT
60 70 80 90 100
ILECRGLGYS GLPEKKDVRE LVEKSGDLME GELYSALKEE EASESVSSTN
110 120 130 140 150
FSGEMHFYEL VEDTKDGIWL VQVIANDRSP LVGKIHWEKM VKKVSRFGIR
160 170 180 190 200
TGTFNCSSDP RYCRRRGWVR STLIMSVPQT STSKGKVMLK EYSGRKIEVE
210 220 230 240 250
HIFKWITAHA ASRIKTIYNA EHLKEEWNKS DQYWLKIYLF ANLDQPPAFF
260 270 280 290 300
SALSIKFTGR VEFIFVNVEN WDNKSYMTDI GIYNMPSYIL RTPEGIYRYG
310 320 330 340 350
NHTGEFISLQ AMDSFLRSLQ PEVNDLFVLS LVLVNLMAWM DLFITQGATI
360 370 380 390 400
KRFVVLISTL GTYNSLLIIS WLPVLGFLQL PYLDSFYEYS LKLLRYSNTT
410 420 430 440 450
TLASWVRADW MFYSSHPALF LSTYLGHGLL IDYFEKKRRR NNNNDEVNAN
460 470 480 490 500
NLEWLSSLWD WYTSYLFHPI ASFQNFPVES DWDEDPDLFL ERLAFPDLWL
510 520 530 540 550
HPLIPTDYIK NLPMWRFKCL GVQSEEEMSE GSQDTENDSE SENTDTLSSE
560 570 580 590 600
KEVFEDKQSV LHNSPGTASH CDAEACSCAN KYCQTSPCER KGRSYGSYNT
610 620 630 640 650
NEDMEPDWLT WPADMLHCTE CVVCLENFEN GCLLMGLPCG HVFHQNCIVM
660 670 680
WLAGGRHCCP VCRWPSYKKK QPYAQHQPLS NDVPS
Length:685
Mass (Da):79,405
Last modified:July 1, 1997 - v1
Checksum:i5AE7283EB38F533F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221F → L in BAG36861 (PubMed:14702039).Curated
Sequence conflicti251 – 2511S → P in AAH35053 (PubMed:15489334).Curated
Sequence conflicti287 – 2871S → P in BAG36861 (PubMed:14702039).Curated
Sequence conflicti502 – 5021P → H in AAH35053 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D76444 mRNA. Translation: BAA19739.1.
AB052743 Genomic DNA. Translation: BAB20900.1.
AK314180 mRNA. Translation: BAG36861.1.
AC015971 Genomic DNA. Translation: AAX93079.1.
BC035053 mRNA. Translation: AAH35053.1.
BC110333 mRNA. Translation: AAI10334.1.
CCDSiCCDS33237.1.
PIRiJC5392.
RefSeqiNP_001185880.1. NM_001198951.1.
NP_001185881.1. NM_001198952.1.
NP_005658.1. NM_005667.3.
UniGeneiHs.469199.
Hs.731426.

Genome annotation databases

EnsembliENST00000237455; ENSP00000237455; ENSG00000239305.
GeneIDi7844.
KEGGihsa:7844.
UCSCiuc002srn.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D76444 mRNA. Translation: BAA19739.1.
AB052743 Genomic DNA. Translation: BAB20900.1.
AK314180 mRNA. Translation: BAG36861.1.
AC015971 Genomic DNA. Translation: AAX93079.1.
BC035053 mRNA. Translation: AAH35053.1.
BC110333 mRNA. Translation: AAI10334.1.
CCDSiCCDS33237.1.
PIRiJC5392.
RefSeqiNP_001185880.1. NM_001198951.1.
NP_001185881.1. NM_001198952.1.
NP_005658.1. NM_005667.3.
UniGeneiHs.469199.
Hs.731426.

3D structure databases

ProteinModelPortaliO00237.
SMRiO00237. Positions 619-663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113601. 13 interactions.
IntActiO00237. 9 interactions.
STRINGi9606.ENSP00000237455.

PTM databases

iPTMnetiO00237.
PhosphoSiteiO00237.

Polymorphism and mutation databases

BioMutaiRNF103.

Proteomic databases

PaxDbiO00237.
PRIDEiO00237.

Protocols and materials databases

DNASUi7844.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000237455; ENSP00000237455; ENSG00000239305.
GeneIDi7844.
KEGGihsa:7844.
UCSCiuc002srn.4. human.

Organism-specific databases

CTDi7844.
GeneCardsiRNF103.
HGNCiHGNC:12859. RNF103.
HPAiHPA057922.
MIMi602507. gene.
neXtProtiNX_O00237.
PharmGKBiPA37448.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00390000006413.
HOGENOMiHOG000006578.
HOVERGENiHBG054144.
InParanoidiO00237.
KOiK15695.
OMAiGKVHWEK.
OrthoDBiEOG7QG44T.
PhylomeDBiO00237.
TreeFamiTF329229.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GenomeRNAii7844.
NextBioi30254.
PROiO00237.
SOURCEiSearch...

Gene expression databases

BgeeiO00237.
CleanExiHS_RNF103.
GenevisibleiO00237. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Structure of human kf-1 genomic DNA."
    Tsujimura A., Hashimoto-Gotoh T.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Peripheral blood.
  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: Brain.
  4. "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].
  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: Brain.
  6. "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination."
    Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.
    Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-621.
  7. "Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-associated degradation pathway."
    Maruyama Y., Yamada M., Takahashi K., Yamada M.
    Biochem. Biophys. Res. Commun. 374:737-741(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DERL1 AND VCP.

Entry informationi

Entry nameiRN103_HUMAN
AccessioniPrimary (citable) accession number: O00237
Secondary accession number(s): A6NFV6
, B2RAG4, Q53SU6, Q8IVB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 1, 1997
Last modified: March 16, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.