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Protein

Tripartite motif-containing protein 54

Gene

TRIM54

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

Functioni

May bind and stabilize microtubules during myotubes formation.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri26 – 8257RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri121 – 16343B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • signal transducer activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • microtubule-based process Source: UniProtKB
  • multicellular organismal development Source: UniProtKB-KW
  • negative regulation of microtubule depolymerization Source: UniProtKB
  • signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:TRIM54
Synonyms:MURF, MURF3, RNF30
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:16008. TRIM54.

Subcellular locationi

GO - Cellular componenti

  • microtubule Source: UniProtKB
  • microtubule associated complex Source: Ensembl
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34434.

Polymorphism and mutation databases

BioMutaiTRIM54.
DMDMi209572715.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Tripartite motif-containing protein 54PRO_0000056282Add
BLAST

Proteomic databases

MaxQBiQ9BYV2.
PaxDbiQ9BYV2.
PRIDEiQ9BYV2.

PTM databases

PhosphoSiteiQ9BYV2.

Expressioni

Tissue specificityi

Specifically expressed in heart and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ9BYV2.
CleanExiHS_TRIM54.
GenevisibleiQ9BYV2. HS.

Organism-specific databases

HPAiHPA019690.

Interactioni

Subunit structurei

Homooligomer and heterooligomer. Interacts with tubulin (By similarity). Interacts with TRIM63 and probably with TRIM55.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A8K2R33EBI-2130429,EBI-9977437
A8KAD63EBI-2130429,EBI-10174974
Q9BRL53EBI-2130429,EBI-10296986
ADCY4Q8NFM43EBI-2130429,EBI-2838710
ALS2CR11Q53TS83EBI-2130429,EBI-739879
ARFIP2P533653EBI-2130429,EBI-638194
ARHGEF5Q127743EBI-2130429,EBI-602199
BYSLQ138954EBI-2130429,EBI-358049
C12orf49Q9H7413EBI-2130429,EBI-2836158
C1orf109Q9NX043EBI-2130429,EBI-8643161
C1orf216Q8TAB53EBI-2130429,EBI-747505
C1QTNF2Q9BXJ53EBI-2130429,EBI-2817707
CARD9Q9H2573EBI-2130429,EBI-751319
CCDC102BA1A4H13EBI-2130429,EBI-10171570
CCDC146Q8IYE0-23EBI-2130429,EBI-10247802
CCDC28AQ7Z6N93EBI-2130429,EBI-10258115
CCDC28AQ8IWP93EBI-2130429,EBI-355471
CCDC67E9PJR53EBI-2130429,EBI-10177066
CCDC67Q05D603EBI-2130429,EBI-748597
CCDC87Q9NVE43EBI-2130429,EBI-749261
CDK18Q070023EBI-2130429,EBI-746238
CDKN1AP389363EBI-2130429,EBI-375077
CEP57L1Q8IYX8-23EBI-2130429,EBI-10181988
CHCHD2Q9Y6H13EBI-2130429,EBI-2321769
CRADDP785603EBI-2130429,EBI-520375
CYTH4Q8WWE83EBI-2130429,EBI-10277443
DCUN1D1Q96GG93EBI-2130429,EBI-740086
DNAL4O960153EBI-2130429,EBI-742362
DTX2Q4ZH493EBI-2130429,EBI-10192429
DTX2Q86UW93EBI-2130429,EBI-740376
EHHADHQ084263EBI-2130429,EBI-2339219
EIF4E2O605733EBI-2130429,EBI-398610
ELMO1Q925563EBI-2130429,EBI-346417
ENKD1Q9H0I23EBI-2130429,EBI-744099
EPM2AIP1Q7L7753EBI-2130429,EBI-6255981
EXOSC5Q9NQT43EBI-2130429,EBI-371876
FAM110AQ9BQ893EBI-2130429,EBI-1752811
FAM124AQ86V423EBI-2130429,EBI-744506
FAM124BQ9H5Z63EBI-2130429,EBI-741626
FAM161AQ3B8203EBI-2130429,EBI-719941
FARS2O953633EBI-2130429,EBI-2513774
FBF1Q8TES7-63EBI-2130429,EBI-10244131
FLJ13057Q53SE73EBI-2130429,EBI-10172181
GEMP550403EBI-2130429,EBI-744104
GTF2IRD2Q86UP83EBI-2130429,EBI-6425928
HAUS1Q96CS23EBI-2130429,EBI-2514791
ING3A0A0C4DG383EBI-2130429,EBI-10263367
INPP5JQ157353EBI-2130429,EBI-10236940
IQUBQ8NA543EBI-2130429,EBI-10220600
KIFC3Q9BVG83EBI-2130429,EBI-2125614
KLHL38Q2WGJ63EBI-2130429,EBI-6426443
KPNA2Q6NVW73EBI-2130429,EBI-9377406
KRT6AP025383EBI-2130429,EBI-702198
KRT6BP042593EBI-2130429,EBI-740907
KRT6CP486683EBI-2130429,EBI-2564105
LENG1Q96BZ83EBI-2130429,EBI-726510
LIN37Q96GY33EBI-2130429,EBI-748884
LMO2P257913EBI-2130429,EBI-739696
LNX1Q8TBB13EBI-2130429,EBI-739832
LSM2Q9Y3333EBI-2130429,EBI-347416
MBD3O959833EBI-2130429,EBI-1783068
MCM7P339933EBI-2130429,EBI-355924
MEAF6Q9HAF13EBI-2130429,EBI-399266
MFAP1P550813EBI-2130429,EBI-1048159
MID2Q9UJV3-23EBI-2130429,EBI-10172526
MYO5BQ9ULV03EBI-2130429,EBI-311356
NGLY1Q96IV03EBI-2130429,EBI-6165879
OSTF1Q928823EBI-2130429,EBI-1051152
OTUB2Q96DC93EBI-2130429,EBI-746259
PIK3R3Q8N3813EBI-2130429,EBI-749096
PPP1R18Q6NYC83EBI-2130429,EBI-2557469
RABGEF1Q9UJ413EBI-2130429,EBI-913954
RAD23AP547253EBI-2130429,EBI-746453
RBM41Q96IZ53EBI-2130429,EBI-740773
RCOR3Q9P2K33EBI-2130429,EBI-743428
RSRC2Q7L4I2-23EBI-2130429,EBI-10256202
SCNM1Q9BWG63EBI-2130429,EBI-748391
SDCBPO005603EBI-2130429,EBI-727004
SH2D1BO147963EBI-2130429,EBI-3923013
SMARCE1Q969G33EBI-2130429,EBI-455078
SNF8Q96H203EBI-2130429,EBI-747719
SPG21Q9NZD83EBI-2130429,EBI-742688
SSX2IPQ9Y2D83EBI-2130429,EBI-2212028
STRA13A8MT693EBI-2130429,EBI-5529694
TBC1D22BQ9NU193EBI-2130429,EBI-8787464
TCEA2Q155603EBI-2130429,EBI-710310
TCEB3Q142413EBI-2130429,EBI-742350
THOC1Q96FV93EBI-2130429,EBI-1765605
TSHZ3A1L0U73EBI-2130429,EBI-10171826
TTC23Q5W5X93EBI-2130429,EBI-6447954
USHBP1Q8N6Y03EBI-2130429,EBI-739895
UTP14CQ08E773EBI-2130429,EBI-10225961
VPS28Q548N13EBI-2130429,EBI-10243107
WDR34Q96EX33EBI-2130429,EBI-2556091
WDYHV1Q96HA83EBI-2130429,EBI-741158
ZBTB16Q055163EBI-2130429,EBI-711925
ZGPATQ8N5A53EBI-2130429,EBI-3439227
ZNF250P15622-33EBI-2130429,EBI-10177272
ZNF417Q8TAU33EBI-2130429,EBI-740727
ZNF572A1L4E93EBI-2130429,EBI-10172590
ZNF572Q7Z3I73EBI-2130429,EBI-10257016
ZNF587Q96SQ53EBI-2130429,EBI-6427977

Protein-protein interaction databases

BioGridi121415. 126 interactions.
IntActiQ9BYV2. 107 interactions.

Structurei

Secondary structure

1
358
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi127 – 1293Combined sources
Beta strandi132 – 1387Combined sources
Turni139 – 1424Combined sources
Beta strandi143 – 1464Combined sources
Helixi147 – 1515Combined sources
Turni154 – 1574Combined sources
Beta strandi160 – 1623Combined sources
Helixi164 – 1663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q1DX-ray2.15A122-168[»]
ProteinModelPortaliQ9BYV2.
SMRiQ9BYV2. Positions 17-85, 122-168, 218-274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BYV2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini271 – 32959COSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni168 – 21144Mediates microtubule-binding and homooligomerizationBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili220 – 25839Sequence AnalysisAdd
BLAST

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 fingeri26 – 8257RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri121 – 16343B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG310224.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000231156.
HOVERGENiHBG071242.
InParanoidiQ9BYV2.
KOiK10653.
OMAiGYESMDQ.
OrthoDBiEOG7VDXPK.
PhylomeDBiQ9BYV2.
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. AlignAdd to basket

Isoform 1 (identifier: Q9BYV2-1) [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
MNFTVGFKPL LGDAHSMDNL EKQLICPICL EMFSKPVVIL PCQHNLCRKC
60 70 80 90 100
ANDVFQASNP LWQSRGSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL
110 120 130 140 150
VENIIDIYKQ ESSRPLHSKA EQHLMCEEHE EEKINIYCLS CEVPTCSLCK
160 170 180 190 200
VFGAHKDCEV APLPTIYKRQ KSELSDGIAM LVAGNDRVQA VITQMEEVCQ
210 220 230 240 250
TIEDNSRRQK QLLNQRFESL CAVLEERKGE LLQALAREQE EKLQRVRGLI
260 270 280 290 300
RQYGDHLEAS SKLVESAIQS MEEPQMALYL QQAKELINKV GAMSKVELAG
310 320 330 340 350
RPEPGYESME QFTVRVEHVA EMLRTIDFQP GASGEEEEVA PDGEEGSAGP

EEERPDGP
Length:358
Mass (Da):40,301
Last modified:October 14, 2008 - v3
Checksum:iC44B08A9871323F6
GO
Isoform 2 (identifier: Q9BYV2-2) [UniParc]FASTAAdd to basket

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

Show »
Length:400
Mass (Da):44,833
Checksum:iD4D12B4FA81A841F
GO

Sequence cautioni

The sequence AAY24296.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC32841.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC32842.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721S → N in CAC32841 (PubMed:11243782).Curated
Sequence conflicti214 – 2141N → T in CAC32841 (PubMed:11243782).Curated
Sequence conflicti214 – 2141N → T in CAC32842 (PubMed:11243782).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei171 – 1711K → KKQDLTLLPRLECSGTNTTY CSLDLPSSSDPPILASQNTK IID in isoform 2. 1 PublicationVSP_016061

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1745.2. [Q9BYV2-2]
CCDS1746.2. [Q9BYV2-1]
RefSeqiNP_115935.3. NM_032546.3. [Q9BYV2-2]
NP_912730.2. NM_187841.2. [Q9BYV2-1]
UniGeneiHs.516036.

Genome annotation databases

EnsembliENST00000296098; ENSP00000296098; ENSG00000138100. [Q9BYV2-2]
ENST00000380075; ENSP00000369415; ENSG00000138100.
GeneIDi57159.
KEGGihsa:57159.
UCSCiuc002rjn.3. human. [Q9BYV2-2]
uc002rjo.3. human. [Q9BYV2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1745.2. [Q9BYV2-2]
CCDS1746.2. [Q9BYV2-1]
RefSeqiNP_115935.3. NM_032546.3. [Q9BYV2-2]
NP_912730.2. NM_187841.2. [Q9BYV2-1]
UniGeneiHs.516036.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q1DX-ray2.15A122-168[»]
ProteinModelPortaliQ9BYV2.
SMRiQ9BYV2. Positions 17-85, 122-168, 218-274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121415. 126 interactions.
IntActiQ9BYV2. 107 interactions.

PTM databases

PhosphoSiteiQ9BYV2.

Polymorphism and mutation databases

BioMutaiTRIM54.
DMDMi209572715.

Proteomic databases

MaxQBiQ9BYV2.
PaxDbiQ9BYV2.
PRIDEiQ9BYV2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296098; ENSP00000296098; ENSG00000138100. [Q9BYV2-2]
ENST00000380075; ENSP00000369415; ENSG00000138100.
GeneIDi57159.
KEGGihsa:57159.
UCSCiuc002rjn.3. human. [Q9BYV2-2]
uc002rjo.3. human. [Q9BYV2-1]

Organism-specific databases

CTDi57159.
GeneCardsiGC02P027506.
HGNCiHGNC:16008. TRIM54.
HPAiHPA019690.
MIMi606474. gene.
neXtProtiNX_Q9BYV2.
PharmGKBiPA34434.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG310224.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000231156.
HOVERGENiHBG071242.
InParanoidiQ9BYV2.
KOiK10653.
OMAiGYESMDQ.
OrthoDBiEOG7VDXPK.
PhylomeDBiQ9BYV2.
TreeFamiTF331669.

Miscellaneous databases

ChiTaRSiTRIM54. human.
EvolutionaryTraceiQ9BYV2.
GenomeRNAii57159.
NextBioi63157.
PROiQ9BYV2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BYV2.
CleanExiHS_TRIM54.
GenevisibleiQ9BYV2. HS.

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]
ProtoNetiSearch...

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] (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. 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.

Entry informationi

Entry nameiTRI54_HUMAN
AccessioniPrimary (citable) accession number: Q9BYV2
Secondary accession number(s): A5D8T7, Q53SY4, Q9BYV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 14, 2008
Last modified: July 22, 2015
This is version 125 of the entry and version 3 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.