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Protein

E3 ubiquitin-protein ligase TRIM71

Gene

TRIM71

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

Functioni

E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance. Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A. Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity).By similarity

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 fingeri12 – 9584RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri194 – 24148B box-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri273 – 31442B box-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Ligase

Keywords - Biological processi

RNA-mediated gene silencing, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM71 (EC:6.3.2.-)
Alternative name(s):
Protein lin-41 homolog
Tripartite motif-containing protein 71
Gene namesi
Name:TRIM71
Synonyms:LIN41
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:32669. TRIM71.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA144596246.

Polymorphism and mutation databases

BioMutaiTRIM71.
DMDMi121941685.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 868867E3 ubiquitin-protein ligase TRIM71PRO_0000279511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Post-translational modificationi

Autoubiquitinated.By similarity

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

EPDiQ2Q1W2.
MaxQBiQ2Q1W2.
PaxDbiQ2Q1W2.
PRIDEiQ2Q1W2.

PTM databases

iPTMnetiQ2Q1W2.
PhosphoSiteiQ2Q1W2.

Expressioni

Tissue specificityi

Specifically expressed in testis.1 Publication

Inductioni

Negatively regulated by the microRNA (miRNA) let-7 which causes degradation of the mRNA encoding this protein. This requires a let-7 complementary site (LCS) in the 3'-UTR of the mRNA encoding this protein. Down-regulated by retinoic acid in Tera-2 cells.1 Publication

Gene expression databases

BgeeiQ2Q1W2.
CleanExiHS_TRIM71.
GenevisibleiQ2Q1W2. HS.

Organism-specific databases

HPAiHPA038141.
HPA038142.

Interactioni

Subunit structurei

Interacts (via NHL repeats) with AGO2. Interacts with SHCBP1; leading to enhance its stability (By similarity).By similarity

Protein-protein interaction databases

BioGridi126279. 17 interactions.
STRINGi9606.ENSP00000373272.

Structurei

3D structure databases

ProteinModelPortaliQ2Q1W2.
SMRiQ2Q1W2. Positions 489-583, 606-868.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati479 – 580102FilaminAdd
BLAST
Repeati593 – 63644NHL 1Add
BLAST
Repeati640 – 68344NHL 2Add
BLAST
Repeati687 – 73044NHL 3Add
BLAST
Repeati734 – 77744NHL 4Add
BLAST
Repeati781 – 82444NHL 5Add
BLAST
Repeati828 – 86841NHL 6Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili391 – 42737Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi26 – 4217Ser-richAdd
BLAST
Compositional biasi146 – 15712His-richAdd
BLAST

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 2 B box-type zinc fingers.PROSITE-ProRule annotation
Contains 1 filamin repeat.PROSITE-ProRule annotation
Contains 6 NHL repeats.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri12 – 9584RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri194 – 24148B box-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri273 – 31442B box-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITG8. Eukaryota.
ENOG410XSQC. LUCA.
GeneTreeiENSGT00550000074377.
HOGENOMiHOG000006755.
HOVERGENiHBG081916.
InParanoidiQ2Q1W2.
KOiK12035.
OMAiMASFPET.
OrthoDBiEOG7HB58K.
PhylomeDBiQ2Q1W2.
TreeFamiTF331018.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
2.60.40.10. 1 hit.
3.30.40.10. 2 hits.
4.10.45.10. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00630. Filamin. 1 hit.
PF01436. NHL. 6 hits.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 2 hits.
SM00557. IG_FLMN. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
PROSITEiPS50194. FILAMIN_REPEAT. 1 hit.
PS51125. NHL. 6 hits.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2Q1W2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFPETDFQ ICLLCKEMCG SPAPLSSNSS ASSSSSQTST SSGGGGGGPG
60 70 80 90 100
AAARRLHVLP CLHAFCRPCL EAHRLPAAGG GAAGEPLKLR CPVCDQKVVL
110 120 130 140 150
AEAAGMDALP SSAFLLSNLL DAVVATADEP PPKNGRAGAP AGAGGHSNHR
160 170 180 190 200
HHAHHAHPRA SASAPPLPQA PQPPAPSRSA PGGPAASPSA LLLRRPHGCS
210 220 230 240 250
SCDEGNAASS RCLDCQEHLC DNCVRAHQRV RLTKDHYIER GPPGPGAAAA
260 270 280 290 300
AQQLGLGPPF PGPPFSILSV FPERLGFCQH HDDEVLHLYC DTCSVPICRE
310 320 330 340 350
CTMGRHGGHS FIYLQEALQD SRALTIQLLA DAQQGRQAIQ LSIEQAQTVA
360 370 380 390 400
EQVEMKAKVV QSEVKAVTAR HKKALEEREC ELLWKVEKIR QVKAKSLYLQ
410 420 430 440 450
VEKLRQNLNK LESTISAVQQ VLEEGRALDI LLARDRMLAQ VQELKTVRSL
460 470 480 490 500
LQPQEDDRVM FTPPDQALYL AIKSFGFVSS GAFAPLTKAT GDGLKRALQG
510 520 530 540 550
KVASFTVIGY DHDGEPRLSG GDLMSAVVLG PDGNLFGAEV SDQQNGTYVV
560 570 580 590 600
SYRPQLEGEH LVSVTLCNQH IENSPFKVVV KSGRSYVGIG LPGLSFGSEG
610 620 630 640 650
DSDGKLCRPW GVSVDKEGYI IVADRSNNRI QVFKPCGAFH HKFGTLGSRP
660 670 680 690 700
GQFDRPAGVA CDASRRIVVA DKDNHRIQIF TFEGQFLLKF GEKGTKNGQF
710 720 730 740 750
NYPWDVAVNS EGKILVSDTR NHRIQLFGPD GVFLNKYGFE GALWKHFDSP
760 770 780 790 800
RGVAFNHEGH LVVTDFNNHR LLVIHPDCQS ARFLGSEGTG NGQFLRPQGV
810 820 830 840 850
AVDQEGRIIV ADSRNHRVQM FESNGSFLCK FGAQGSGFGQ MDRPSGIAIT
860
PDGMIVVVDF GNNRILVF
Length:868
Mass (Da):93,385
Last modified:January 24, 2006 - v1
Checksum:iA71A1E5CC019F80D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ232881 mRNA. Translation: ABB18374.1.
CCDSiCCDS43060.1.
RefSeqiNP_001034200.1. NM_001039111.2.
UniGeneiHs.113170.
Hs.567678.

Genome annotation databases

EnsembliENST00000383763; ENSP00000373272; ENSG00000206557.
GeneIDi131405.
KEGGihsa:131405.
UCSCiuc003cff.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ232881 mRNA. Translation: ABB18374.1.
CCDSiCCDS43060.1.
RefSeqiNP_001034200.1. NM_001039111.2.
UniGeneiHs.113170.
Hs.567678.

3D structure databases

ProteinModelPortaliQ2Q1W2.
SMRiQ2Q1W2. Positions 489-583, 606-868.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126279. 17 interactions.
STRINGi9606.ENSP00000373272.

PTM databases

iPTMnetiQ2Q1W2.
PhosphoSiteiQ2Q1W2.

Polymorphism and mutation databases

BioMutaiTRIM71.
DMDMi121941685.

Proteomic databases

EPDiQ2Q1W2.
MaxQBiQ2Q1W2.
PaxDbiQ2Q1W2.
PRIDEiQ2Q1W2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000383763; ENSP00000373272; ENSG00000206557.
GeneIDi131405.
KEGGihsa:131405.
UCSCiuc003cff.4. human.

Organism-specific databases

CTDi131405.
GeneCardsiTRIM71.
HGNCiHGNC:32669. TRIM71.
HPAiHPA038141.
HPA038142.
neXtProtiNX_Q2Q1W2.
PharmGKBiPA144596246.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITG8. Eukaryota.
ENOG410XSQC. LUCA.
GeneTreeiENSGT00550000074377.
HOGENOMiHOG000006755.
HOVERGENiHBG081916.
InParanoidiQ2Q1W2.
KOiK12035.
OMAiMASFPET.
OrthoDBiEOG7HB58K.
PhylomeDBiQ2Q1W2.
TreeFamiTF331018.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GenomeRNAii131405.
NextBioi82904.
PROiQ2Q1W2.

Gene expression databases

BgeeiQ2Q1W2.
CleanExiHS_TRIM71.
GenevisibleiQ2Q1W2. HS.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
2.60.40.10. 1 hit.
3.30.40.10. 2 hits.
4.10.45.10. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00630. Filamin. 1 hit.
PF01436. NHL. 6 hits.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 2 hits.
SM00557. IG_FLMN. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
PROSITEiPS50194. FILAMIN_REPEAT. 1 hit.
PS51125. NHL. 6 hits.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The RBCC gene RFP2 (LEU5/TRIM13), frequently deleted in various malignancies, encodes a ring E3 ubiquitin ligase."
    Lerner M., Corcoran M., Nielsen M., Zubarev R., Uhlen M., Hober S., Grander D., Sangfelt O.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Analysis of the regulation of lin-41 during chick and mouse limb development."
    Lancman J.J., Caruccio N.C., Harfe B.D., Pasquinelli A.E., Schageman J.J., Pertsemlidis A., Fallon J.F.
    Dev. Dyn. 234:948-960(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  3. "Reciprocal expression of lin-41 and the microRNAs let-7 and mir-125 during mouse embryogenesis."
    Maller Schulman B.R., Esquela-Kerscher A., Slack F.J.
    Dev. Dyn. 234:1046-1054(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  4. "Depletion of human micro-RNA miR-125b reveals that it is critical for the proliferation of differentiated cells but not for the down-regulation of putative targets during differentiation."
    Lee Y.S., Kim H.K., Chung S., Kim K.-S., Dutta A.
    J. Biol. Chem. 280:16635-16641(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DOWN-REGULATION BY RETINOIC ACID.
  5. "Human TRIM71 and its nematode homologue are targets of let-7 microRNA and its zebrafish orthologue is essential for development."
    Lin Y.C., Hsieh L.C., Kuo M.W., Yu J., Kuo H.H., Lo W.L., Lin R.J., Yu A.L., Li W.H.
    Mol. Biol. Evol. 24:2525-2534(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLIN41_HUMAN
AccessioniPrimary (citable) accession number: Q2Q1W2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: January 24, 2006
Last modified: April 13, 2016
This is version 100 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.