TRI44_HUMAN
ID TRI44_HUMAN Reviewed; 344 AA.
AC Q96DX7; D3DR14; Q96QY2; Q9UGK0;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Tripartite motif-containing protein 44;
DE AltName: Full=Protein DIPB;
GN Name=TRIM44; Synonyms=DIPB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Castello A., Chafey P., Lambert M., Collod-Beroud G.;
RT "Identification of a novel brain potential partner of dystrophin and
RT utrophin C-terminal end.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP INTERACTION WITH TRIM17, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19358823; DOI=10.1016/j.bbrc.2009.04.010;
RA Urano T., Usui T., Takeda S., Ikeda K., Okada A., Ishida Y., Iwayanagi T.,
RA Otomo J., Ouchi Y., Inoue S.;
RT "TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase.";
RL Biochem. Biophys. Res. Commun. 383:263-268(2009).
RN [7]
RP FUNCTION, INVOLVEMENT IN AN3, VARIANT TYR-64, CHARACTERIZATION OF VARIANT
RP TYR-64, VARIANT AN3 ARG-155, AND CHARACTERIZATION OF VARIANT AN3 ARG-155.
RX PubMed=26394807; DOI=10.1002/humu.22907;
RA Zhang X., Qin G., Chen G., Li T., Gao L., Huang L., Zhang Y., Ouyang K.,
RA Wang Y., Pang Y., Zeng B., Yu L.;
RT "Variants in TRIM44 cause aniridia by impairing PAX6 expression.";
RL Hum. Mutat. 36:1164-1167(2015).
CC -!- FUNCTION: May play a role in the process of differentiation and
CC maturation of neuronal cells (By similarity). May regulate the activity
CC of TRIM17. Is a negative regulator of PAX6 expression
CC (PubMed:26394807). {ECO:0000250, ECO:0000269|PubMed:19358823,
CC ECO:0000269|PubMed:26394807}.
CC -!- SUBUNIT: Interacts (via coiled coil) with TRIM17 (via coiled coil).
CC {ECO:0000269|PubMed:19358823}.
CC -!- INTERACTION:
CC Q96DX7; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-8787399, EBI-10269566;
CC Q96DX7; Q5JS98: PBX3; NbExp=3; IntAct=EBI-8787399, EBI-10244393;
CC Q96DX7; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-8787399, EBI-79165;
CC Q96DX7; Q9UDY6-2: TRIM10; NbExp=4; IntAct=EBI-8787399, EBI-11981577;
CC Q96DX7; Q86WT6: TRIM69; NbExp=3; IntAct=EBI-8787399, EBI-749955;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:19358823}.
CC -!- DISEASE: Aniridia 3 (AN3) [MIM:617142]: A form of aniridia, a
CC congenital, bilateral, panocular disorder characterized by complete
CC absence of the iris or extreme iris hypoplasia. Aniridia is not just an
CC isolated defect in iris development but it is associated with macular
CC and optic nerve hypoplasia, cataract, corneal changes, nystagmus.
CC Visual acuity is generally low but is unrelated to the degree of iris
CC hypoplasia. Glaucoma is a secondary problem causing additional visual
CC loss over time. {ECO:0000269|PubMed:26394807}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
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DR EMBL; AJ249128; CAB65108.1; -; mRNA.
DR EMBL; AL138812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68133.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68134.1; -; Genomic_DNA.
DR EMBL; BC013166; AAH13166.1; -; mRNA.
DR EMBL; BC024031; AAH24031.1; -; mRNA.
DR CCDS; CCDS31461.1; -.
DR RefSeq; NP_060053.2; NM_017583.5.
DR AlphaFoldDB; Q96DX7; -.
DR SMR; Q96DX7; -.
DR BioGRID; 120140; 70.
DR IntAct; Q96DX7; 52.
DR STRING; 9606.ENSP00000299413; -.
DR iPTMnet; Q96DX7; -.
DR PhosphoSitePlus; Q96DX7; -.
DR BioMuta; TRIM44; -.
DR DMDM; 56404940; -.
DR EPD; Q96DX7; -.
DR jPOST; Q96DX7; -.
DR MassIVE; Q96DX7; -.
DR MaxQB; Q96DX7; -.
DR PaxDb; Q96DX7; -.
DR PeptideAtlas; Q96DX7; -.
DR PRIDE; Q96DX7; -.
DR ProteomicsDB; 76337; -.
DR Antibodypedia; 25982; 289 antibodies from 24 providers.
DR DNASU; 54765; -.
DR Ensembl; ENST00000299413.7; ENSP00000299413.5; ENSG00000166326.7.
DR GeneID; 54765; -.
DR KEGG; hsa:54765; -.
DR MANE-Select; ENST00000299413.7; ENSP00000299413.5; NM_017583.6; NP_060053.2.
DR UCSC; uc001mwi.3; human.
DR CTD; 54765; -.
DR DisGeNET; 54765; -.
DR GeneCards; TRIM44; -.
DR HGNC; HGNC:19016; TRIM44.
DR HPA; ENSG00000166326; Low tissue specificity.
DR MalaCards; TRIM44; -.
DR MIM; 612298; gene.
DR MIM; 617142; phenotype.
DR neXtProt; NX_Q96DX7; -.
DR OpenTargets; ENSG00000166326; -.
DR Orphanet; 250923; Isolated aniridia.
DR PharmGKB; PA134906584; -.
DR VEuPathDB; HostDB:ENSG00000166326; -.
DR eggNOG; ENOG502RHR7; Eukaryota.
DR GeneTree; ENSGT00440000034605; -.
DR HOGENOM; CLU_070347_0_0_1; -.
DR InParanoid; Q96DX7; -.
DR OMA; LREAYMW; -.
DR OrthoDB; 869824at2759; -.
DR PhylomeDB; Q96DX7; -.
DR TreeFam; TF333911; -.
DR PathwayCommons; Q96DX7; -.
DR SignaLink; Q96DX7; -.
DR BioGRID-ORCS; 54765; 13 hits in 1113 CRISPR screens.
DR ChiTaRS; TRIM44; human.
DR GenomeRNAi; 54765; -.
DR Pharos; Q96DX7; Tbio.
DR PRO; PR:Q96DX7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96DX7; protein.
DR Bgee; ENSG00000166326; Expressed in pons and 211 other tissues.
DR Genevisible; Q96DX7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061944; P:negative regulation of protein K48-linked ubiquitination; IDA:BHF-UCL.
DR GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:BHF-UCL.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Disease variant; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..344
FT /note="Tripartite motif-containing protein 44"
FT /id="PRO_0000220372"
FT ZN_FING 174..215
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 290..325
FT /evidence="ECO:0000255"
FT COMPBIAS 75..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXA7"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXA7"
FT VARIANT 64
FT /note="S -> Y (does not affect function in negative
FT regulation of PAX6 expression; dbSNP:rs377117775)"
FT /evidence="ECO:0000269|PubMed:26394807"
FT /id="VAR_077852"
FT VARIANT 155
FT /note="G -> R (in AN3; affects function and results in
FT increased negative regulation of PAX6 expression compared
FT to wild-type; dbSNP:rs886039241)"
FT /evidence="ECO:0000269|PubMed:26394807"
FT /id="VAR_077853"
FT CONFLICT 41
FT /note="C -> S (in Ref. 1; CAB65108)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="A -> G (in Ref. 1; CAB65108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38472 MW; 5DC26DD73C347AF1 CRC64;
MASGVGAAFE ELPHDGTCDE CEPDEAPGAE EVCRECGFCY CRRHAEAHRQ KFLSHHLAEY
VHGSQAWTPP ADGEGAGKEE AEVKVEQERE IESEAGEESE SEEESESEEE SETEEESEDE
SDEESEEDSE EEMEDEQESE AEEDNQEEGE SEAEGETEAE SEFDPEIEME AERVAKRKCP
DHGLDLSTYC QEDRQLICVL CPVIGAHQGH QLSTLDEAFE ELRSKDSGGL KAAMIELVER
LKFKSSDPKV TRDQMKMFIQ QEFKKVQKVI ADEEQKALHL VDIQEAMATA HVTEILADIQ
SHMDRLMTQM AQAKEQLDTS NESAEPKAEG DEEGPSGASE EEDT
