Reviewed, UniProtKB/Swiss-Prot Q9BYV2 (TRI54_HUMAN)

Names and origin

Protein names

Recommended name:
    Tripartite motif-containing protein 54
Alternative name(s):
    Muscle-specific RING finger protein 3
      Short name=MURF-3
      Short name=MuRF3
    Muscle-specific RING finger protein
      Short name=MuRF
    RING finger protein 30

Gene names

Name:	TRIM54
Synonyms:	MURF, MURF3, RNF30

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cytoplasm › myofibril › sarcomere › Z-disk 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.

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
Gene Ontology (GO)
Biological process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW microtubule-based process Ref.1 Non-traceable author statement. Source: UniProtKB multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of microtubule depolymerization Ref.1 Non-traceable author statement. Source: UniProtKB signal transduction Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	Z disc Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	signal transducer activity Ref.1 Non-traceable author statement. Source: UniProtKB zinc ion binding Ref.1 Non-traceable author statement. 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

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. 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: 11243782] [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: 15815621] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. NP_912730.2.
UniGene	Hs.516036
3D structure databases
SMR	Q9BYV2. Positions 118-173.
ModBase	Search...
Genome annotation databases
Ensembl	ENSG00000138100. Homo sapiens. [Contig view]
GeneID	57159.
KEGG	hsa:57159.
Organism-specific databases
GeneCards	GC02P027418.
H-InvDB	HIX0029859.
HGNC	HGNC:16008. TRIM54.
MIM	606474. gene.
PharmGKB	PA34434.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q9BYV2.
OMA	Q9BYV2. TVSVEHV.
Gene expression databases
Bgee	Q9BYV2.
CleanEx	HS_TRIM54.
GermOnline	ENSG00000138100. Homo sapiens.
Family and domain databases
InterPro	IPR017903. COS_domain. IPR000315. Znf_B-box. IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00643. zf-B_box. 1 hit. PF00097. zf-C3HC4. 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 Resources
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:	June 16, 2009
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)