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Protein

E3 ubiquitin-protein ligase TM129

Gene

TMEM129

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase involved in ER-associated protein degradation, preferentially associates with the E2 enzyme UBE2J2. Exploited by viral US11 proteins to mediate HLA class I proteins degradation.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri285 – 35066RING-type; degenerateAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway, Unfolded protein response

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TM129 (EC:6.3.2.-)
Gene namesi
Name:TMEM129
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:25137. TMEM129.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66LumenalSequence Analysis
Transmembranei7 – 2721HelicalSequence AnalysisAdd
BLAST
Topological domaini28 – 5629CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei57 – 7721HelicalSequence AnalysisAdd
BLAST
Topological domaini78 – 9417LumenalSequence AnalysisAdd
BLAST
Transmembranei95 – 11521HelicalSequence AnalysisAdd
BLAST
Topological domaini116 – 362247CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485649.

Polymorphism and mutation databases

BioMutaiTMEM129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362E3 ubiquitin-protein ligase TM129PRO_0000291041Add
BLAST

Proteomic databases

MaxQBiA0AVI4.
PaxDbiA0AVI4.
PRIDEiA0AVI4.

PTM databases

PhosphoSiteiA0AVI4.

Expressioni

Gene expression databases

BgeeiA0AVI4.
CleanExiHS_TMEM129.
ExpressionAtlasiA0AVI4. baseline and differential.
GenevestigatoriA0AVI4.

Organism-specific databases

HPAiHPA053826.
HPA060920.

Interactioni

Subunit structurei

Integral component of ER-resident dislocation complexes.

Protein-protein interaction databases

BioGridi124932. 1 interaction.
IntActiA0AVI4. 3 interactions.
STRINGi9606.ENSP00000372394.

Structurei

3D structure databases

ProteinModelPortaliA0AVI4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity.

Sequence similaritiesi

Belongs to the TMEM129 family.Curated
Contains 1 RING-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri285 – 35066RING-type; degenerateAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiNOG302378.
GeneTreeiENSGT00390000013284.
HOGENOMiHOG000006582.
HOVERGENiHBG097695.
InParanoidiA0AVI4.
OMAiNVVIHQS.
OrthoDBiEOG7JMGF6.
PhylomeDBiA0AVI4.
TreeFamiTF314487.

Family and domain databases

InterProiIPR018801. Tmpp129.
[Graphical view]
PfamiPF10272. Tmpp129. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: A0AVI4-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDSPEVTFTL AYLVFAVCFV FTPNEFHAAG LTVQNLLSGW LGSEDAAFVP
60 70 80 90 100
FHLRRTAATL LCHSLLPLGY YVGMCLAASE KRLHALSQAP EAWRLFLLLA
110 120 130 140 150
VTLPSIACIL IYYWSRDRWA CHPLARTLAL YALPQSGWQA VASSVNTEFR
160 170 180 190 200
RIDKFATGAP GARVIVTDTW VMKVTTYRVH VAQQQDVHLT VTESRQHELS
210 220 230 240 250
PDSNLPVQLL TIRVASTNPA VQAFDIWLNS TEYGELCEKL RAPIRRAAHV
260 270 280 290 300
VIHQSLGDLF LETFASLVEV NPAYSVPSSQ ELEACIGCMQ TRASVKLVKT
310 320 330 340 350
CQEAATGECQ QCYCRPMWCL TCMGKWFASR QDPLRPDTWL ASRVPCPTCR
360
ARFCILDVCT VR
Length:362
Mass (Da):40,464
Last modified:November 28, 2006 - v1
Checksum:i861C9876B492DC56
GO
Isoform 2 (identifier: A0AVI4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     228-232: LNSTE → SWRPA
     233-362: Missing.

Show »
Length:232
Mass (Da):25,914
Checksum:iBB10F6F61C2DF4B3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti83 – 831L → I.
Corresponds to variant rs798752 [ dbSNP | Ensembl ].
VAR_032803

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei228 – 2325LNSTE → SWRPA in isoform 2. 1 PublicationVSP_036641
Alternative sequencei233 – 362130Missing in isoform 2. 1 PublicationVSP_036642Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC016773 Genomic DNA. No translation available.
CH471131 Genomic DNA. Translation: EAW82569.1.
CH471131 Genomic DNA. Translation: EAW82570.1.
CH471131 Genomic DNA. Translation: EAW82571.1.
BC009331 mRNA. No translation available.
BC126370 mRNA. Translation: AAI26371.1.
CCDSiCCDS3351.1. [A0AVI4-2]
CCDS46998.1. [A0AVI4-1]
RefSeqiNP_001120738.1. NM_001127266.1. [A0AVI4-1]
NP_612394.1. NM_138385.3. [A0AVI4-2]
UniGeneiHs.518562.

Genome annotation databases

EnsembliENST00000303277; ENSP00000305243; ENSG00000168936. [A0AVI4-2]
ENST00000382936; ENSP00000372394; ENSG00000168936. [A0AVI4-1]
ENST00000536901; ENSP00000441812; ENSG00000168936. [A0AVI4-1]
GeneIDi92305.
KEGGihsa:92305.
UCSCiuc003gdm.3. human. [A0AVI4-2]
uc003gdn.3. human. [A0AVI4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC016773 Genomic DNA. No translation available.
CH471131 Genomic DNA. Translation: EAW82569.1.
CH471131 Genomic DNA. Translation: EAW82570.1.
CH471131 Genomic DNA. Translation: EAW82571.1.
BC009331 mRNA. No translation available.
BC126370 mRNA. Translation: AAI26371.1.
CCDSiCCDS3351.1. [A0AVI4-2]
CCDS46998.1. [A0AVI4-1]
RefSeqiNP_001120738.1. NM_001127266.1. [A0AVI4-1]
NP_612394.1. NM_138385.3. [A0AVI4-2]
UniGeneiHs.518562.

3D structure databases

ProteinModelPortaliA0AVI4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124932. 1 interaction.
IntActiA0AVI4. 3 interactions.
STRINGi9606.ENSP00000372394.

PTM databases

PhosphoSiteiA0AVI4.

Polymorphism and mutation databases

BioMutaiTMEM129.

Proteomic databases

MaxQBiA0AVI4.
PaxDbiA0AVI4.
PRIDEiA0AVI4.

Protocols and materials databases

DNASUi92305.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303277; ENSP00000305243; ENSG00000168936. [A0AVI4-2]
ENST00000382936; ENSP00000372394; ENSG00000168936. [A0AVI4-1]
ENST00000536901; ENSP00000441812; ENSG00000168936. [A0AVI4-1]
GeneIDi92305.
KEGGihsa:92305.
UCSCiuc003gdm.3. human. [A0AVI4-2]
uc003gdn.3. human. [A0AVI4-1]

Organism-specific databases

CTDi92305.
GeneCardsiGC04M001717.
HGNCiHGNC:25137. TMEM129.
HPAiHPA053826.
HPA060920.
MIMi615975. gene.
neXtProtiNX_A0AVI4.
PharmGKBiPA143485649.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG302378.
GeneTreeiENSGT00390000013284.
HOGENOMiHOG000006582.
HOVERGENiHBG097695.
InParanoidiA0AVI4.
OMAiNVVIHQS.
OrthoDBiEOG7JMGF6.
PhylomeDBiA0AVI4.
TreeFamiTF314487.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GenomeRNAii92305.
NextBioi77688.
PROiA0AVI4.
SOURCEiSearch...

Gene expression databases

BgeeiA0AVI4.
CleanExiHS_TMEM129.
ExpressionAtlasiA0AVI4. baseline and differential.
GenevestigatoriA0AVI4.

Family and domain databases

InterProiIPR018801. Tmpp129.
[Graphical view]
PfamiPF10272. Tmpp129. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. 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] (ISOFORMS 1 AND 2).
  4. Cited for: FUNCTION, CATALYTIC ACTIVITY, TOPOLOGY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiTM129_HUMAN
AccessioniPrimary (citable) accession number: A0AVI4
Secondary accession number(s): A6NH49, A6NI98, D3DVP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: November 28, 2006
Last modified: May 27, 2015
This is version 73 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.