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Q969Q1

- TRI63_HUMAN

UniProt

Q969Q1 - TRI63_HUMAN

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Protein

E3 ubiquitin-protein ligase TRIM63

Gene

TRIM63

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

Functioni

E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.2 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri23 – 7957RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri117 – 15943B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. signal transducer activity Source: UniProtKB
  3. titin binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: Ensembl
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to dexamethasone stimulus Source: Ensembl
  2. muscle contraction Source: Ensembl
  3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  4. regulation of gene expression Source: Ensembl
  5. response to electrical stimulus involved in regulation of muscle adaptation Source: UniProtKB
  6. response to interleukin-1 Source: Ensembl
  7. signal transduction Source: UniProtKB
  8. skeletal muscle atrophy Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Muscle protein

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM63 (EC:6.3.2.-)
Alternative name(s):
Iris RING finger protein
Muscle-specific RING finger protein 1
Short name:
MuRF-1
Short name:
MuRF1
RING finger protein 28
Striated muscle RING zinc finger protein
Tripartite motif-containing protein 63
Gene namesi
Name:TRIM63
Synonyms:IRF, MURF1, RNF28, SMRZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16007. TRIM63.

Subcellular locationi

Cytoplasm. Nucleus By similarity. CytoplasmmyofibrilsarcomereM line. CytoplasmmyofibrilsarcomereZ line
Note: Colocalizes with TNNI3 in myocytes (By similarity). Localizes to the M- and Z-lines in skeletal muscle.By similarity

GO - Cellular componenti

  1. contractile fiber Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. microtubule Source: UniProtKB
  4. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391C → A: Loss of SUMO2-binding. 1 Publication
Mutagenesisi41 – 411H → A: Loss of SUMO2-binding. 1 Publication
Mutagenesisi44 – 441C → A: Loss of SUMO2-binding. 1 Publication
Mutagenesisi47 – 471C → A: Loss of SUMO2-binding. 1 Publication

Organism-specific databases

PharmGKBiPA34431.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353E3 ubiquitin-protein ligase TRIM63PRO_0000056290Add
BLAST

Proteomic databases

PaxDbiQ969Q1.
PRIDEiQ969Q1.

PTM databases

PhosphoSiteiQ969Q1.

Expressioni

Tissue specificityi

Muscle specific. Selectively expressed in heart and skeletal muscle. Also expressed in the iris.4 Publications

Developmental stagei

Expressed throughout all developmental stages.1 Publication

Gene expression databases

BgeeiQ969Q1.
CleanExiHS_TRIM63.
GenevestigatoriQ969Q1.

Interactioni

Subunit structurei

Homodimer. Homooligomer and heterooligomer. Interacts with SUMO2, titin/TTN and GMEB1. Interacts with TRIM54 and probably with TRIM55 and TNNI3. Forms a ternary complex with GNB2L1 and PRKCE (By similarity). Interacts with CKM.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCAR1Q8IX122EBI-5661333,EBI-356265
EEF1GP266412EBI-5661333,EBI-351467
GFM1Q96RP92EBI-5661333,EBI-2255048
MRPL41Q8IXM32EBI-5661333,EBI-912501
MYOZ1Q9NP982EBI-5661333,EBI-744402
TTNQ8WZ423EBI-5661333,EBI-681210

Protein-protein interaction databases

BioGridi124195. 66 interactions.
IntActiQ969Q1. 37 interactions.
MINTiMINT-6492114.
STRINGi9606.ENSP00000363390.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi123 – 1253
Beta strandi132 – 1343
Turni135 – 1384
Beta strandi139 – 1413
Helixi143 – 1486
Turni150 – 1534
Beta strandi156 – 1583
Helixi214 – 26754

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8UNMR-A119-169[»]
3DDTX-ray1.90A/B/C117-161[»]
4M3LX-ray2.10A/B/C/D214-271[»]
ProteinModelPortaliQ969Q1.
SMRiQ969Q1. Positions 16-78, 117-161, 214-270.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ969Q1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 32559COSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni74 – 218145Interaction with TTNAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili207 – 26963Sequence AnalysisAdd
BLAST

Domaini

The RING-type zinc finger mediates interaction with SUMO2 and localization to the nucleus. Also required for the E3 ubiquitin ligase activity (By similarity).By similarity
The B box-type zinc finger mediates homodimerization.3 Publications

Sequence similaritiesi

Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 COS domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri23 – 7957RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri117 – 15943B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG310224.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000231156.
HOVERGENiHBG071242.
InParanoidiQ969Q1.
KOiK10655.
OMAiDGNPMEN.
OrthoDBiEOG7VDXPK.
PhylomeDBiQ969Q1.
TreeFamiTF331669.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR017903. COS_domain.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS51262. COS. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q969Q1) [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
MDYKSSLIQD GNPMENLEKQ LICPICLEMF TKPVVILPCQ HNLCRKCAND
60 70 80 90 100
IFQAANPYWT SRGSSVSMSG GRFRCPTCRH EVIMDRHGVY GLQRNLLVEN
110 120 130 140 150
IIDIYKQECS SRPLQKGSHP MCKEHEDEKI NIYCLTCEVP TCSMCKVFGI
160 170 180 190 200
HKACEVAPLQ SVFQGQKTEL NNCISMLVAG NDRVQTIITQ LEDSRRVTKE
210 220 230 240 250
NSHQVKEELS QKFDTLYAIL DEKKSELLQR ITQEQEKKLS FIEALIQQYQ
260 270 280 290 300
EQLDKSTKLV ETAIQSLDEP GGATFLLTAK QLIKSIVEAS KGCQLGKTEQ
310 320 330 340 350
GFENMDFFTL DLEHIADALR AIDFGTDEEE EEFIEEEDQE EEESTEGKEE

GHQ
Length:353
Mass (Da):40,248
Last modified:December 1, 2001 - v1
Checksum:i9BE4B1505039BC86
GO
Isoform 2 (identifier: Q969Q1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-131: Missing.

Note: No experimental confirmation available.

Show »
Length:325
Mass (Da):36,950
Checksum:iB03213D38E2063B0
GO

Sequence cautioni

The sequence AAK52497.1 differs from that shown. Reason: Sequencing errors.
The sequence AAK52497.1 differs from that shown. Reason: Frameshift at several positions.
The sequence CAC33173.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti237 – 2371K → E.2 Publications
Corresponds to variant rs2275950 [ dbSNP | Ensembl ].
VAR_020116

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei104 – 13128Missing in isoform 2. 1 PublicationVSP_055443Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ291713 mRNA. Translation: CAC33173.1. Different initiation.
AF353673 mRNA. Translation: AAK39519.1.
AJ276484 mRNA. Translation: CAC81706.1.
AF361946 mRNA. Translation: AAK52497.1. Sequence problems.
AK056942 mRNA. Translation: BAB71318.1.
AK297820 mRNA. Translation: BAG60157.1.
AL391650 Genomic DNA. Translation: CAI17133.1.
BC080529 mRNA. Translation: AAH80529.1.
CCDSiCCDS273.1. [Q969Q1-1]
RefSeqiNP_115977.2. NM_032588.3. [Q969Q1-1]
UniGeneiHs.279709.

Genome annotation databases

EnsembliENST00000374272; ENSP00000363390; ENSG00000158022. [Q969Q1-1]
GeneIDi84676.
KEGGihsa:84676.
UCSCiuc001bli.2. human. [Q969Q1-1]

Polymorphism databases

DMDMi21362898.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ291713 mRNA. Translation: CAC33173.1 . Different initiation.
AF353673 mRNA. Translation: AAK39519.1 .
AJ276484 mRNA. Translation: CAC81706.1 .
AF361946 mRNA. Translation: AAK52497.1 . Sequence problems.
AK056942 mRNA. Translation: BAB71318.1 .
AK297820 mRNA. Translation: BAG60157.1 .
AL391650 Genomic DNA. Translation: CAI17133.1 .
BC080529 mRNA. Translation: AAH80529.1 .
CCDSi CCDS273.1. [Q969Q1-1 ]
RefSeqi NP_115977.2. NM_032588.3. [Q969Q1-1 ]
UniGenei Hs.279709.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D8U NMR - A 119-169 [» ]
3DDT X-ray 1.90 A/B/C 117-161 [» ]
4M3L X-ray 2.10 A/B/C/D 214-271 [» ]
ProteinModelPortali Q969Q1.
SMRi Q969Q1. Positions 16-78, 117-161, 214-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124195. 66 interactions.
IntActi Q969Q1. 37 interactions.
MINTi MINT-6492114.
STRINGi 9606.ENSP00000363390.

PTM databases

PhosphoSitei Q969Q1.

Polymorphism databases

DMDMi 21362898.

Proteomic databases

PaxDbi Q969Q1.
PRIDEi Q969Q1.

Protocols and materials databases

DNASUi 84676.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374272 ; ENSP00000363390 ; ENSG00000158022 . [Q969Q1-1 ]
GeneIDi 84676.
KEGGi hsa:84676.
UCSCi uc001bli.2. human. [Q969Q1-1 ]

Organism-specific databases

CTDi 84676.
GeneCardsi GC01M026377.
HGNCi HGNC:16007. TRIM63.
MIMi 606131. gene.
neXtProti NX_Q969Q1.
PharmGKBi PA34431.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG310224.
GeneTreei ENSGT00760000118878.
HOGENOMi HOG000231156.
HOVERGENi HBG071242.
InParanoidi Q969Q1.
KOi K10655.
OMAi DGNPMEN.
OrthoDBi EOG7VDXPK.
PhylomeDBi Q969Q1.
TreeFami TF331669.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSi TRIM63. human.
EvolutionaryTracei Q969Q1.
GeneWikii TRIM63.
GenomeRNAii 84676.
NextBioi 35473548.
PROi Q969Q1.
SOURCEi Search...

Gene expression databases

Bgeei Q969Q1.
CleanExi HS_TRIM63.
Genevestigatori Q969Q1.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProi IPR017903. COS_domain.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF00643. zf-B_box. 1 hit.
[Graphical view ]
SMARTi SM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS51262. COS. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain."
    Centner T., Yano J., Kimura E., McElhinny A.S., Pelin K., Witt C.C., Bang M.-L., Trombitas K., Granzier H., Gregorio C.C., Sorimachi H., Labeit S.
    J. Mol. Biol. 306:717-726(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-237, INTERACTION WITH TTN; TRIM54 AND TRIM55, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
  2. "Expressed sequence tag analysis of adult human iris for the NEIBank project: steroid-response factors and similarities with retinal pigment epithelium."
    Wistow G., Bernstein S.L., Ray S., Wyatt M.K., Behal A., Touchman J.W., Bouffard G., Smith D., Peterson K.
    Mol. Vis. 8:185-195(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Iris.
  3. "Characterisation of MURF2, a new muscle-specific RING finger protein of the RBCC family that associates with microtubules."
    Stanchi F.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  4. "A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain."
    Dai K.-S., Liew C.-C.
    J. Biol. Chem. 276:23992-23999(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SUMO2, MUTAGENESIS OF CYS-39; HIS-41; CYS-44 AND CYS-47, DOMAIN.
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Heart and Skeletal muscle.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1), VARIANT GLU-237.
    Tissue: Skin.
  8. Cited for: TISSUE SPECIFICITY.
  9. "Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1."
    McElhinny A.S., Kakinuma K., Sorimachi H., Labeit S., Gregorio C.C.
    J. Cell Biol. 157:125-136(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAIN, FUNCTION, INTERACTION WITH GMEB1.
  10. "MuRF1-dependent regulation of systemic carbohydrate metabolism as revealed from transgenic mouse studies."
    Hirner S., Krohne C., Schuster A., Hoffmann S., Witt S., Erber R., Sticht C., Gasch A., Labeit S., Labeit D.
    J. Mol. Biol. 379:666-677(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis."
    Koyama S., Hata S., Witt C.C., Ono Y., Lerche S., Ojima K., Chiba T., Doi N., Kitamura F., Tanaka K., Abe K., Witt S.H., Rybin V., Gasch A., Franz T., Labeit S., Sorimachi H.
    J. Mol. Biol. 376:1224-1236(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CKM, FUNCTION.
  12. "Solution structure of the B-box domain of the human tripartite motif-containing 63 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 119-169.
  13. "Structural analysis of B-Box 2 from MuRF1: identification of a novel self-association pattern in a RING-like fold."
    Mrosek M., Meier S., Ucurum-Fotiadis Z., von Castelmur E., Hedbom E., Lustig A., Grzesiek S., Labeit D., Labeit S., Mayans O.
    Biochemistry 47:10722-10730(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 117-161 IN COMPLEX WITH ZINC IONS, DOMAIN, SUBUNIT.

Entry informationi

Entry nameiTRI63_HUMAN
AccessioniPrimary (citable) accession number: Q969Q1
Secondary accession number(s): B4DN95
, Q5T2I1, Q96BD3, Q96KD9, Q9BYV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 130 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3