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Protein

Tripartite motif-containing protein 72

Gene

TRIM72

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

Functioni

Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca2+-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri14 – 5744RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri81 – 12242B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Exocytosis, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-445355. Smooth Muscle Contraction.

Protein family/group databases

TCDBi1.F.1.2.1. the synaptosomal vesicle fusion pore (svf-pore) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Tripartite motif-containing protein 72
Alternative name(s):
Mitsugumin-53
Short name:
Mg53
Gene namesi
Name:TRIM72Imported
Synonyms:MG53
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:32671. TRIM72.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi144 – 1441C → S: No decrease in level upon treatment with hydrogen peroxide. 1 Publication

Organism-specific databases

PharmGKBiPA144596247.

Polymorphism and mutation databases

BioMutaiTRIM72.
DMDMi126253816.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477Tripartite motif-containing protein 72PRO_0000278130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei144 – 1441S-nitrosocysteine1 Publication
Disulfide bondi242 – 242InterchainBy similarity
Modified residuei255 – 2551PhosphoserineBy similarity

Post-translational modificationi

Disulfide bond formation at Cys-242 occurs in case of membrane damage that cause the entry of the oxidized milieu of the extracellular space, resulting in homooligomerization.By similarity
S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiQ6ZMU5.
MaxQBiQ6ZMU5.
PaxDbiQ6ZMU5.
PRIDEiQ6ZMU5.

PTM databases

iPTMnetiQ6ZMU5.
PhosphoSiteiQ6ZMU5.

Expressioni

Gene expression databases

BgeeiQ6ZMU5.
CleanExiHS_TRIM72.
GenevisibleiQ6ZMU5. HS.

Organism-specific databases

HPAiHPA023122.

Interactioni

Subunit structurei

Homooligomer; disulfide-linked. Interacts with DYSF and CAV3 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
TCF12Q990813EBI-2341648,EBI-722877

Protein-protein interaction databases

BioGridi138920. 7 interactions.
IntActiQ6ZMU5. 3 interactions.
STRINGi9606.ENSP00000312675.

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi279 – 2846Combined sources
Turni295 – 2973Combined sources
Beta strandi302 – 3054Combined sources
Turni306 – 3094Combined sources
Beta strandi310 – 3134Combined sources
Beta strandi329 – 3313Combined sources
Beta strandi333 – 3375Combined sources
Beta strandi342 – 3509Combined sources
Beta strandi355 – 3639Combined sources
Beta strandi369 – 3713Combined sources
Helixi376 – 3783Combined sources
Beta strandi380 – 3867Combined sources
Turni387 – 3893Combined sources
Beta strandi390 – 3934Combined sources
Beta strandi396 – 3994Combined sources
Beta strandi411 – 4188Combined sources
Turni419 – 4224Combined sources
Beta strandi423 – 4286Combined sources
Beta strandi436 – 4416Combined sources
Beta strandi449 – 4546Combined sources
Turni459 – 4635Combined sources
Beta strandi467 – 4693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KB5X-ray1.50A278-470[»]
ProteinModelPortaliQ6ZMU5.
SMRiQ6ZMU5. Positions 8-56, 85-150, 278-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6ZMU5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini271 – 475205B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili135 – 16935Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Sequence analysis
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri14 – 5744RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri81 – 12242B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00760000118838.
HOGENOMiHOG000234133.
HOVERGENiHBG098570.
InParanoidiQ6ZMU5.
KOiK12036.
OMAiPCPCCQA.
OrthoDBiEOG7VTDMR.
PhylomeDBiQ6ZMU5.
TreeFamiTF342569.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 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 11 Publication (identifier: Q6ZMU5-1) [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
MSAAPGLLHQ ELSCPLCLQL FDAPVTAECG HSFCRACLGR VAGEPAADGT
60 70 80 90 100
VLCPCCQAPT RPQALSTNLQ LARLVEGLAQ VPQGHCEEHL DPLSIYCEQD
110 120 130 140 150
RALVCGVCAS LGSHRGHRLL PAAEAHARLK TQLPQQKLQL QEACMRKEKS
160 170 180 190 200
VAVLEHQLVE VEETVRQFRG AVGEQLGKMR VFLAALEGSL DREAERVRGE
210 220 230 240 250
AGVALRRELG SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK YCLVTSRLQK
260 270 280 290 300
ILAESPPPAR LDIQLPIISD DFKFQVWRKM FRALMPALEE LTFDPSSAHP
310 320 330 340 350
SLVVSSSGRR VECSEQKAPP AGEDPRQFDK AVAVVAHQQL SEGEHYWEVD
360 370 380 390 400
VGDKPRWALG VIAAEAPRRG RLHAVPSQGL WLLGLREGKI LEAHVEAKEP
410 420 430 440 450
RALRSPERRP TRIGLYLSFG DGVLSFYDAS DADALVPLFA FHERLPRPVY
460 470
PFFDVCWHDK GKNAQPLLLV GPEGAEA
Length:477
Mass (Da):52,731
Last modified:February 20, 2007 - v2
Checksum:i2B4EE9A00318151F
GO
Isoform 21 Publication (identifier: Q6ZMU5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     270-477: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:269
Mass (Da):29,501
Checksum:iB1F5883B42D913F6
GO

Sequence cautioni

The sequence BAC03506.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921R → C in BAD18630 (PubMed:14702039).Curated
Sequence conflicti315 – 3151E → G in BAC03506 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei270 – 477208Missing in isoform 2. 1 PublicationVSP_052318Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK090695 mRNA. Translation: BAC03506.1. Different initiation.
AK131485 mRNA. Translation: BAD18630.1.
AC009088 Genomic DNA. No translation available.
BC033211 mRNA. Translation: AAH33211.1.
CCDSiCCDS32437.1. [Q6ZMU5-1]
RefSeqiNP_001008275.2. NM_001008274.3. [Q6ZMU5-1]
UniGeneiHs.661859.

Genome annotation databases

EnsembliENST00000322122; ENSP00000312675; ENSG00000177238. [Q6ZMU5-1]
ENST00000613872; ENSP00000481813; ENSG00000177238. [Q6ZMU5-2]
GeneIDi493829.
KEGGihsa:493829.
UCSCiuc002ebn.3. human. [Q6ZMU5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK090695 mRNA. Translation: BAC03506.1. Different initiation.
AK131485 mRNA. Translation: BAD18630.1.
AC009088 Genomic DNA. No translation available.
BC033211 mRNA. Translation: AAH33211.1.
CCDSiCCDS32437.1. [Q6ZMU5-1]
RefSeqiNP_001008275.2. NM_001008274.3. [Q6ZMU5-1]
UniGeneiHs.661859.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KB5X-ray1.50A278-470[»]
ProteinModelPortaliQ6ZMU5.
SMRiQ6ZMU5. Positions 8-56, 85-150, 278-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi138920. 7 interactions.
IntActiQ6ZMU5. 3 interactions.
STRINGi9606.ENSP00000312675.

Protein family/group databases

TCDBi1.F.1.2.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

iPTMnetiQ6ZMU5.
PhosphoSiteiQ6ZMU5.

Polymorphism and mutation databases

BioMutaiTRIM72.
DMDMi126253816.

Proteomic databases

EPDiQ6ZMU5.
MaxQBiQ6ZMU5.
PaxDbiQ6ZMU5.
PRIDEiQ6ZMU5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322122; ENSP00000312675; ENSG00000177238. [Q6ZMU5-1]
ENST00000613872; ENSP00000481813; ENSG00000177238. [Q6ZMU5-2]
GeneIDi493829.
KEGGihsa:493829.
UCSCiuc002ebn.3. human. [Q6ZMU5-1]

Organism-specific databases

CTDi493829.
GeneCardsiTRIM72.
H-InvDBHIX0202276.
HGNCiHGNC:32671. TRIM72.
HPAiHPA023122.
MIMi613288. gene.
neXtProtiNX_Q6ZMU5.
PharmGKBiPA144596247.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00760000118838.
HOGENOMiHOG000234133.
HOVERGENiHBG098570.
InParanoidiQ6ZMU5.
KOiK12036.
OMAiPCPCCQA.
OrthoDBiEOG7VTDMR.
PhylomeDBiQ6ZMU5.
TreeFamiTF342569.

Enzyme and pathway databases

ReactomeiR-HSA-445355. Smooth Muscle Contraction.

Miscellaneous databases

ChiTaRSiTRIM72. human.
EvolutionaryTraceiQ6ZMU5.
GenomeRNAii493829.
NextBioi111770.
PROiQ6ZMU5.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZMU5.
CleanExiHS_TRIM72.
GenevisibleiQ6ZMU5. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 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. "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] (ISOFORM 1).
    Tissue: CerebellumImported and ThymusImported.
  2. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 2).
    Tissue: MuscleImported.
  4. "S-nitrosylation of TRIM72 at cysteine 144 is critical for protection against oxidation-induced protein degradation and cell death."
    Kohr M.J., Evangelista A.M., Ferlito M., Steenbergen C., Murphy E.
    J. Mol. Cell. Cardiol. 69:67-74(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION AT CYS-144, MUTAGENESIS OF CYS-144.
  5. "Crystal structure of PRY-SPRY domain of human TRIM72."
    Park E.Y., Kwon O.B., Jeong B.C., Yi J.S., Lee C.S., Ko Y.G., Song H.K.
    Proteins 78:790-795(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 278-470.

Entry informationi

Entry nameiTRI72_HUMAN
AccessioniPrimary (citable) accession number: Q6ZMU5
Secondary accession number(s): Q8N4X6, Q8NBD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: May 11, 2016
This is version 112 of the entry and version 2 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 16
    Human chromosome 16: 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

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 one 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.