Q9BYV2 (TRI54_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tripartite motif-containing protein 54

Alternative name(s):
Muscle-specific RING finger protein
Short name=MuRF
Muscle-specific RING finger protein 3
Short name=MuRF-3
Short name=MuRF3
RING finger protein 30

Gene names

Name:	TRIM54
Synonyms:	MURF, MURF3, RNF30

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May bind and stabilize microtubules during myotubes formation By similarity.
Subunit structure	Homooligomer and heterooligomer. Interacts with tubulin By similarity. Interacts with TRIM63 and probably with TRIM55. Ref.1
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cytoplasm › myofibril › sarcomere › Z line By similarity. Note: Associates with microtubules. Localizes to the Z-lines in skeletal muscles By similarity.
Tissue specificity	Specifically expressed in heart and skeletal muscle. Ref.1
Sequence similarities	Contains 1 B box-type zinc finger. Contains 1 COS domain. Contains 1 RING-type zinc finger.
Sequence caution	The sequence AAY24296.1 differs from that shown. Reason: Erroneous initiation. The sequence CAC32841.1 differs from that shown. Reason: Erroneous initiation. The sequence CAC32842.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Differentiation
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Developmental protein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW microtubule-based process Non-traceable author statement Ref.1. Source: UniProtKB multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of microtubule depolymerization Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	Z disc Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Non-traceable author statement Ref.1. Source: UniProtKB microtubule associated complex Inferred from electronic annotation. Source: Compara
Molecular_function	signal transducer activity Non-traceable author statement Ref.1. Source: UniProtKB zinc ion binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BYV2-1)

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.

Isoform 2 (identifier: Q9BYV2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     171-171: K → KKQDLTLLPRLECSGTNTTYCSLDLPSSSDPPILASQNTKIID

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 358

358

Tripartite motif-containing protein 54

PRO_0000056282

Regions

Domain

271 – 329

59

COS

Zinc finger

26 – 82

57

RING-type

Zinc finger

121 – 163

43

B box-type

Region

168 – 211

44

Mediates microtubule-binding and homooligomerization By similarity

Coiled coil

220 – 258

39

Potential

Natural variations

Alternative sequence

171

1

K → KKQDLTLLPRLECSGTNTTY CSLDLPSSSDPPILASQNTK IID in isoform 2.

VSP_016061

Experimental info

Sequence conflict

172

1

S → N in CAC32841. Ref.1

Sequence conflict

214

1

N → T in CAC32841. Ref.1

Sequence conflict

214

1

N → T in CAC32842. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

358

Helix Strand Turn

Details...

Beta strand

127 – 129

3

Beta strand

132 – 138

7

Turn

139 – 142

4

Beta strand

143 – 146

4

Helix

147 – 151

5

Turn

154 – 157

4

Beta strand

160 – 162

3

Helix

164 – 166

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 14, 2008. Version 3. Checksum: C44B08A9871323F6	FASTA	358	40,301
	10 20 30 40 50 60 MNFTVGFKPL LGDAHSMDNL EKQLICPICL EMFSKPVVIL PCQHNLCRKC ANDVFQASNP 70 80 90 100 110 120 LWQSRGSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESSRPLHSKA 130 140 150 160 170 180 EQHLMCEEHE EEKINIYCLS CEVPTCSLCK VFGAHKDCEV APLPTIYKRQ KSELSDGIAM 190 200 210 220 230 240 LVAGNDRVQA VITQMEEVCQ TIEDNSRRQK QLLNQRFESL CAVLEERKGE LLQALAREQE 250 260 270 280 290 300 EKLQRVRGLI RQYGDHLEAS SKLVESAIQS MEEPQMALYL QQAKELINKV GAMSKVELAG 310 320 330 340 350 RPEPGYESME QFTVRVEHVA EMLRTIDFQP GASGEEEEVA PDGEEGSAGP EEERPDGP
	Isoform 2 [UniParc]. Checksum: D4D12B4FA81A841F	FASTA	400	44,833
	10 20 30 40 50 60 MNFTVGFKPL LGDAHSMDNL EKQLICPICL EMFSKPVVIL PCQHNLCRKC ANDVFQASNP 70 80 90 100 110 120 LWQSRGSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESSRPLHSKA 130 140 150 160 170 180 EQHLMCEEHE EEKINIYCLS CEVPTCSLCK VFGAHKDCEV APLPTIYKRQ KKQDLTLLPR 190 200 210 220 230 240 LECSGTNTTY CSLDLPSSSD PPILASQNTK IIDSELSDGI AMLVAGNDRV QAVITQMEEV 250 260 270 280 290 300 CQTIEDNSRR QKQLLNQRFE SLCAVLEERK GELLQALARE QEEKLQRVRG LIRQYGDHLE 310 320 330 340 350 360 ASSKLVESAI QSMEEPQMAL YLQQAKELIN KVGAMSKVEL AGRPEPGYES MEQFTVRVEH 370 380 390 400 VAEMLRTIDF QPGASGEEEE VAPDGEEGSA GPEEERPDGP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, OLIGOMERIZATION, INTERACTION WITH TRIM63 AND TRIM55.
[2]	"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].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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].
[5]	"The B-box domain of TRIM54." Structural genomics consortium (SGC) Submitted (FEB-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 122-168 IN COMPLEX WITH ZINC IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ291714 mRNA. Translation: CAC32841.1. Different initiation.
AJ291714 mRNA. Translation: CAC32842.1. Different initiation.
AC013413 Genomic DNA. Translation: AAY24296.1. Different initiation.
CH471053 Genomic DNA. Translation: EAX00606.1.
BC141807 mRNA. Translation: AAI41808.1.

IPI

IPI00000182.
IPI00376605.

RefSeq

NP_115935.3. NM_032546.3.
NP_912730.2. NM_187841.2.

UniGene

Hs.516036.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3Q1D	X-ray	2.15	A	122-168	[»]

ProteinModelPortal

Q9BYV2.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BYV2. 4 interactions.

STRING

9606.ENSP00000296098.

PTM databases

PhosphoSite

Q9BYV2.

Polymorphism databases

DMDM

209572715.

Proteomic databases

PaxDb

Q9BYV2.

PRIDE

Q9BYV2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296098; ENSP00000296098; ENSG00000138100.
ENST00000380075; ENSP00000369415; ENSG00000138100.

GeneID

57159.

KEGG

hsa:57159.

UCSC

uc002rjn.3. human.
uc002rjo.3. human.

Organism-specific databases

CTD

57159.

GeneCards

GC02P027506.

HGNC

HGNC:16008. TRIM54.

HPA

HPA019690.

MIM

606474. gene.

neXtProt

NX_Q9BYV2.

PharmGKB

PA34434.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG310224.

HOGENOM

HOG000231156.

HOVERGEN

HBG071242.

KO

K10653.

OMA

GYESMDQ.

Gene expression databases

Bgee

Q9BYV2.

CleanEx

HS_TRIM54.

Genevestigator

Q9BYV2.

GermOnline

ENSG00000138100. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.
4.10.45.10. 1 hit.

InterPro

IPR017903. COS_domain.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF00643. zf-B_box. 1 hit.
[Graphical view]

SMART

SM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS51262. COS. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TRIM54. human.

EvolutionaryTrace

Q9BYV2.

GenomeRNAi

57159.

NextBio

63157.

SOURCE

Search...

Entry information

Entry name

TRI54_HUMAN

Accession

Primary (citable) accession number: Q9BYV2
Secondary accession number(s): A5D8T7, Q53SY4, Q9BYV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	October 14, 2008
Last modified:	May 29, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.