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Protein

PDZ and LIM domain protein 5

Gene

Pdlim5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play an important role in the heart development by scaffolding PKC to the Z-disk region. Isoform 2 and isoform 3 may negatively modulate the scaffolding activity of isoform 1. May play a role in the regulation of cardiomyocyte expansion. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May restrain postsynaptic growth of excitatory synapses (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
PDZ and LIM domain protein 5
Alternative name(s):
Enigma homolog
Enigma-like PDZ and LIM domains protein
Gene namesi
Name:Pdlim5
Synonyms:Enh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1927489. Pdlim5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 591590PDZ and LIM domain protein 5PRO_0000075878Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei89 – 891N6-acetyllysine; alternateCombined sources
Modified residuei89 – 891N6-succinyllysine; alternateCombined sources
Modified residuei111 – 1111PhosphoserineBy similarity
Modified residuei137 – 1371PhosphoserineBy similarity
Modified residuei228 – 2281PhosphoserineCombined sources
Modified residuei313 – 3131PhosphoserineBy similarity
Modified residuei322 – 3221PhosphoserineBy similarity
Modified residuei350 – 3501N6-acetyllysineCombined sources
Modified residuei359 – 3591PhosphoserineBy similarity
Isoform 3 (identifier: Q8CI51-3)
Modified residuei102 – 1021PhosphoserineCombined sources
Modified residuei105 – 1051PhosphoserineCombined sources
Modified residuei218 – 2181PhosphoserineCombined sources
Isoform 2 (identifier: Q8CI51-2)
Modified residuei316 – 3161PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CI51.
MaxQBiQ8CI51.
PaxDbiQ8CI51.
PRIDEiQ8CI51.

PTM databases

iPTMnetiQ8CI51.
PhosphoSiteiQ8CI51.

Expressioni

Gene expression databases

BgeeiQ8CI51.
CleanExiMM_PDLIM5.
ExpressionAtlasiQ8CI51. baseline and differential.
GenevisibleiQ8CI51. MM.

Interactioni

Subunit structurei

Interacts with various PKC isoforms through the LIM domains. Interacts (via LIM domains) with SIPA1L1. Interacts (via PDZ domain) with actin and ACTN1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi207938. 28 interactions.
IntActiQ8CI51. 25 interactions.
MINTiMINT-1870155.
STRINGi10090.ENSMUSP00000029941.

Structurei

Secondary structure

1
591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Beta strandi18 – 214Combined sources
Turni22 – 254Combined sources
Beta strandi26 – 305Combined sources
Helixi38 – 414Combined sources
Beta strandi49 – 535Combined sources
Helixi63 – 7210Combined sources
Beta strandi74 – 818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WF7NMR-A5-94[»]
ProteinModelPortaliQ8CI51.
SMRiQ8CI51. Positions 11-94, 395-587.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CI51.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8584PDZPROSITE-ProRule annotationAdd
BLAST
Domaini413 – 47260LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini472 – 53160LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini531 – 59161LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 LIM zinc-binding domains.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000220936.
HOVERGENiHBG051478.
InParanoidiQ8CI51.
OMAiTNNIQDP.
OrthoDBiEOG7HXCQB.
TreeFamiTF106408.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
2.30.42.10. 1 hit.
InterProiIPR031847. DUF4749.
IPR001478. PDZ.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF15936. DUF4749. 1 hit.
PF00412. LIM. 3 hits.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CI51-1) [UniParc]FASTAAdd to basket

Also known as: ENH1

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
MSNYSVSLVG PAPWGFRLQG GKDFNMPLTI SSLKDGGKAS QAHVRIGDVV
60 70 80 90 100
LSIDGISAQG MTHLEAQNKI KACTGSLNMT LQRASAAAKS EPVSVQKGEP
110 120 130 140 150
KEVVKPVPIT SPAVSKVTST TNMAYNKAPR PFGSVSSPKV TSIPSPSSAF
160 170 180 190 200
TPAHAATSSH ASPTPVAAAT PLHLSASGLH VSANLSADQC SSPPNTGKPA
210 220 230 240 250
VNVPRQPTVT SVCSESAQEL AEGQRRGSQG DIKQQNGPPR KHIVERNTEF
260 270 280 290 300
YHIPTHSDAS KKRLIEDTED WRPRTGTTQS RSFRILAQIT GTEHLTESEN
310 320 330 340 350
DNTKKANSTQ EPSQQPASSG ASPLSASEGP ESPGSSRPSV AGLRSAAAFK
360 370 380 390 400
PVGSTSVKSP SWQRPNQAAP STGRISNNAR SSGTGASVGP PQPSDQDTLV
410 420 430 440 450
QRAEHIPAGK RTPMCAHCNQ VIRGPFLVAL GKSWHPEEFN CAHCKNTMAY
460 470 480 490 500
IGFVEEKGAL YCELCYEKFF APECGRCQRK ILGEVINALK QTWHVSCFVC
510 520 530 540 550
VACGKPIRNN VFHLEDGEPY CETDYYALFG TICRGCEFPI EAGDMFLEAL
560 570 580 590
GYTWHDTCFV CSVCCESLEG QTFFSKKDKP LCKKHAHSVN F
Length:591
Mass (Da):63,299
Last modified:July 27, 2011 - v4
Checksum:iE12B9EE1A3D97DC1
GO
Isoform 2 (identifier: Q8CI51-2) [UniParc]FASTAAdd to basket

Also known as: ENH2

The sequence of this isoform differs from the canonical sequence as follows:
     307-337: NSTQEPSQQPASSGASPLSASEGPESPGSSR → KEKIPLHVFSPKYTKLRDWHHEVSARALNVQ
     338-591: Missing.

Show »
Length:337
Mass (Da):36,070
Checksum:iDDDBB44EFD25300F
GO
Isoform 3 (identifier: Q8CI51-3) [UniParc]FASTAAdd to basket

Also known as: ENH3

The sequence of this isoform differs from the canonical sequence as follows:
     98-206: Missing.
     237-237: G → GNPGTVKISPKR
     307-337: NSTQEPSQQPASSGASPLSASEGPESPGSSR → KEKIPLHVFSPKYTKLRDWHHEVSARALNVQ
     338-591: Missing.

Show »
Length:239
Mass (Da):26,346
Checksum:i83FF76D9DA4FBFD8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741T → M in AAH37476 (PubMed:15489334).Curated
Sequence conflicti84 – 841A → T in BAA88827 (PubMed:10833443).Curated
Sequence conflicti84 – 841A → T in BAA88829 (PubMed:10833443).Curated
Sequence conflicti215 – 2151E → D in BAA88827 (PubMed:10833443).Curated
Sequence conflicti215 – 2151E → D in BAA88829 (PubMed:10833443).Curated
Sequence conflicti222 – 2221E → K in BAA88827 (PubMed:10833443).Curated
Sequence conflicti222 – 2221E → K in BAA88829 (PubMed:10833443).Curated
Sequence conflicti226 – 2261R → K in BAA88827 (PubMed:10833443).Curated
Sequence conflicti226 – 2261R → K in BAA88829 (PubMed:10833443).Curated
Sequence conflicti329 – 3291G → R in BAA88827 (PubMed:10833443).Curated
Sequence conflicti433 – 4331S → P in BAA88827 (PubMed:10833443).Curated
Sequence conflicti546 – 5461F → Y in BAA88827 (PubMed:10833443).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei98 – 206109Missing in isoform 3. 1 PublicationVSP_010467Add
BLAST
Alternative sequencei237 – 2371G → GNPGTVKISPKR in isoform 3. 1 PublicationVSP_010468
Alternative sequencei307 – 33731NSTQE…PGSSR → KEKIPLHVFSPKYTKLRDWH HEVSARALNVQ in isoform 2 and isoform 3. 1 PublicationVSP_010469Add
BLAST
Alternative sequencei338 – 591254Missing in isoform 2 and isoform 3. 1 PublicationVSP_010470Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016586 mRNA. Translation: BAA88827.1.
AB016587 mRNA. Translation: BAA88828.1.
AB016588 mRNA. Translation: BAA88829.1.
AK147999 mRNA. Translation: BAE28279.1.
BC037476 mRNA. Translation: AAH37476.1.
CCDSiCCDS17875.1. [Q8CI51-1]
CCDS17876.1. [Q8CI51-2]
CCDS38656.1. [Q8CI51-3]
RefSeqiNP_001177781.1. NM_001190852.1.
NP_001177783.1. NM_001190854.1.
NP_001177784.1. NM_001190855.1.
NP_001177785.1. NM_001190856.1.
NP_062782.2. NM_019808.3. [Q8CI51-1]
UniGeneiMm.117709.

Genome annotation databases

EnsembliENSMUST00000029941; ENSMUSP00000029941; ENSMUSG00000028273. [Q8CI51-1]
ENSMUST00000196908; ENSMUSP00000143098; ENSMUSG00000028273. [Q8CI51-2]
GeneIDi56376.
KEGGimmu:56376.
UCSCiuc008rol.2. mouse. [Q8CI51-1]
uc008ron.2. mouse. [Q8CI51-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016586 mRNA. Translation: BAA88827.1.
AB016587 mRNA. Translation: BAA88828.1.
AB016588 mRNA. Translation: BAA88829.1.
AK147999 mRNA. Translation: BAE28279.1.
BC037476 mRNA. Translation: AAH37476.1.
CCDSiCCDS17875.1. [Q8CI51-1]
CCDS17876.1. [Q8CI51-2]
CCDS38656.1. [Q8CI51-3]
RefSeqiNP_001177781.1. NM_001190852.1.
NP_001177783.1. NM_001190854.1.
NP_001177784.1. NM_001190855.1.
NP_001177785.1. NM_001190856.1.
NP_062782.2. NM_019808.3. [Q8CI51-1]
UniGeneiMm.117709.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WF7NMR-A5-94[»]
ProteinModelPortaliQ8CI51.
SMRiQ8CI51. Positions 11-94, 395-587.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207938. 28 interactions.
IntActiQ8CI51. 25 interactions.
MINTiMINT-1870155.
STRINGi10090.ENSMUSP00000029941.

PTM databases

iPTMnetiQ8CI51.
PhosphoSiteiQ8CI51.

Proteomic databases

EPDiQ8CI51.
MaxQBiQ8CI51.
PaxDbiQ8CI51.
PRIDEiQ8CI51.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029941; ENSMUSP00000029941; ENSMUSG00000028273. [Q8CI51-1]
ENSMUST00000196908; ENSMUSP00000143098; ENSMUSG00000028273. [Q8CI51-2]
GeneIDi56376.
KEGGimmu:56376.
UCSCiuc008rol.2. mouse. [Q8CI51-1]
uc008ron.2. mouse. [Q8CI51-2]

Organism-specific databases

CTDi10611.
MGIiMGI:1927489. Pdlim5.

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000220936.
HOVERGENiHBG051478.
InParanoidiQ8CI51.
OMAiTNNIQDP.
OrthoDBiEOG7HXCQB.
TreeFamiTF106408.

Miscellaneous databases

EvolutionaryTraceiQ8CI51.
NextBioi312444.
PROiQ8CI51.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CI51.
CleanExiMM_PDLIM5.
ExpressionAtlasiQ8CI51. baseline and differential.
GenevisibleiQ8CI51. MM.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
2.30.42.10. 1 hit.
InterProiIPR031847. DUF4749.
IPR001478. PDZ.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF15936. DUF4749. 1 hit.
PF00412. LIM. 3 hits.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ENH, containing PDZ and LIM domains, heart/skeletal muscle-specific protein, associates with cytoskeletal proteins through the PDZ domain."
    Nakagawa N., Hoshijima M., Oyasu M., Saito N., Tanizawa K., Kuroda S.
    Biochem. Biophys. Res. Commun. 272:505-512(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    Strain: 129/SvJ.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  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 1).
    Strain: FVB/N.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-105 AND SER-218 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89 AND LYS-350, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. "Solution structure of the PDZ domain of enigma homologue protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 5-94.

Entry informationi

Entry nameiPDLI5_MOUSE
AccessioniPrimary (citable) accession number: Q8CI51
Secondary accession number(s): Q3UGD0
, Q9QYN0, Q9QYN1, Q9QYN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: July 27, 2011
Last modified: April 13, 2016
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.