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Protein

Histone H3.2

Gene

Hist1h3b

more
Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1266695 Interleukin-7 signaling
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-212300 PRC2 methylates histones and DNA
R-MMU-2299718 Condensation of Prophase Chromosomes
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-3214841 PKMTs methylate histone lysines
R-MMU-3214842 HDMs demethylate histones
R-MMU-3214847 HATs acetylate histones
R-MMU-3214858 RMTs methylate histone arginines
R-MMU-3247509 Chromatin modifying enzymes
R-MMU-427359 SIRT1 negatively regulates rRNA expression
R-MMU-427413 NoRC negatively regulates rRNA expression
R-MMU-5250924 B-WICH complex positively regulates rRNA expression
R-MMU-5578749 Transcriptional regulation by small RNAs
R-MMU-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-MMU-73728 RNA Polymerase I Promoter Opening
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-9018519 Estrogen-dependent gene expression
R-MMU-983231 Factors involved in megakaryocyte development and platelet production

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.2
Gene namesi
Name:Hist1h3b
Synonyms:H3-53, H3.2, H3b
AND
Name:Hist1h3c
Synonyms:H3-143
AND
Name:Hist1h3d
Synonyms:H3-B
AND
Name:Hist1h3e
Synonyms:H3-F
AND
Name:Hist1h3f
Synonyms:H3.2-221, H3f
AND
Name:Hist2h3b
Synonyms:H3.2-616
AND
Name:Hist2h3c1
Synonyms:H3.2-615, Hist2h3ca1
AND
Name:Hist2h3c2
Synonyms:H3.2-614, Hist2h3ca2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 13, Chromosome 3

Organism-specific databases

MGIiMGI:2448319 Hist1h3b
MGI:2448320 Hist1h3c
MGI:2448322 Hist1h3d
MGI:2448326 Hist1h3e
MGI:2448329 Hist1h3f
MGI:2448351 Hist2h3b
MGI:2448355 Hist2h3c1
MGI:2448357 Hist2h3c2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002212502 – 136Histone H3.2Add BLAST135

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3Asymmetric dimethylarginine; by PRMT6; alternateBy similarity1
Modified residuei3Citrulline; alternate1 Publication1
Modified residuei4Phosphothreonine; by HASPIN1 Publication1
Modified residuei5Allysine; alternateBy similarity1
Modified residuei5N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei5N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei5N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei5N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei5N6-acetyllysine; alternate1 Publication1
Modified residuei5N6-crotonyllysine; alternate1 Publication1
Modified residuei5N6-methyllysine; alternate1 Publication1
Modified residuei7Phosphothreonine; by PKCBy similarity1
Modified residuei9Citrulline; alternate1 Publication1
Modified residuei9Symmetric dimethylarginine; by PRMT5; alternate1 Publication1
Modified residuei10N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei10N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei10N6-acetyllysine; alternate2 Publications1
Modified residuei10N6-crotonyllysine; alternate1 Publication1
Modified residuei10N6-methyllysine; alternate2 Publications1
Modified residuei11ADP-ribosylserine; alternateBy similarity1
Modified residuei11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA55 Publications1
Modified residuei12Phosphothreonine; by PKCBy similarity1
Modified residuei15N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei15N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei15N6-acetyllysine; alternate3 Publications1
Modified residuei15N6-succinyllysine; alternateBy similarity1
Modified residuei18Asymmetric dimethylarginine; by CARM1; alternate3 Publications1
Modified residuei18Citrulline; alternate1 Publication1
Modified residuei19N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei19N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei19N6-acetyllysine; alternate3 Publications1
Modified residuei19N6-butyryllysine; alternate1 Publication1
Modified residuei19N6-crotonyllysine; alternate1 Publication1
Modified residuei19N6-methyllysine; alternate1 Publication1
Modified residuei24N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei24N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei24N6-acetyllysine; alternate3 Publications1
Modified residuei24N6-butyryllysine; alternate1 Publication1
Modified residuei24N6-crotonyllysine; alternate1 Publication1
Modified residuei24N6-methyllysine; alternate1 Publication1
Modified residuei27Citrulline1 Publication1
Modified residuei28N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei28N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei28N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei28N6-acetyllysine; alternate1 Publication1
Modified residuei28N6-butyryllysine; alternate1 Publication1
Modified residuei28N6-crotonyllysine; alternate1 Publication1
Modified residuei28N6-methyllysine; alternate2 Publications1
Modified residuei29ADP-ribosylserine; alternateBy similarity1
Modified residuei29Phosphoserine; alternate; by AURKB, AURKC and RPS6KA56 Publications1
Modified residuei37N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei37N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei37N6-acetyllysine; alternate1 Publication1
Modified residuei37N6-butyryllysine; alternate1 Publication1
Modified residuei37N6-methyllysine; alternate2 Publications1
Modified residuei38N6-butyryllysine; alternate1 Publication1
Modified residuei38N6-methyllysine; alternateBy similarity1
Modified residuei42PhosphotyrosineBy similarity1
Modified residuei57N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei57N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei57N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei57N6-acetyllysine; alternateBy similarity1
Modified residuei57N6-crotonyllysine; alternate1 Publication1
Modified residuei57N6-methyllysine; by EHMT2; alternateBy similarity1
Modified residuei57N6-succinyllysine; alternate1 Publication1
Modified residuei58PhosphoserineBy similarity1
Modified residuei65N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei65N6-methyllysine; alternateBy similarity1
Modified residuei80N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei80N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei80N6-acetyllysine; alternateBy similarity1
Modified residuei80N6-butyryllysine; alternate1 Publication1
Modified residuei80N6-methyllysine; alternate2 Publications1
Modified residuei80N6-succinyllysine; alternate1 Publication1
Modified residuei81PhosphothreonineBy similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei116N6-acetyllysineBy similarity1
Modified residuei123N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei123N6-acetyllysine; alternateBy similarity1
Modified residuei123N6-butyryllysine; alternate1 Publication1
Modified residuei123N6-methyllysine; alternate1 Publication1
Modified residuei123N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.6 Publications
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.5 Publications
Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity).By similarity
Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.9 Publications
Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.10 Publications
Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins (By similarity). Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination.By similarity1 Publication
Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (By similarity).By similarity
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication
Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.1 Publication
Hydroxybutyrylation of histones is induced by starvation. It is linked to gene activation and may replace histone acetylation on the promoter of specific genes in response to fasting.1 Publication
Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP84228
MaxQBiP84228
PaxDbiP84228
PRIDEiP84228
TopDownProteomicsiP84228

PTM databases

iPTMnetiP84228

Expressioni

Developmental stagei

Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.

Gene expression databases

BgeeiENSMUSG00000069267
CleanExiMM_HIST1H3B
MM_HIST1H3C
MM_HIST1H3D
MM_HIST1H3E
MM_HIST1H3F
MM_HIST2H3C1
MM_HIST2H3C2
ExpressionAtlasiP84228 baseline and differential
GenevisibleiP84228 MM

Interactioni

Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. During nucleosome assembly the chaperone ASF1A interacts with the histone H3-H4 heterodimer (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
HASPINQ8TF76-13EBI-2658213,EBI-15815652From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi234451, 5 interactors
235068, 1 interactor
235070, 1 interactor
DIPiDIP-49015N
IntActiP84228, 29 interactors
MINTiP84228
STRINGi10090.ENSMUSP00000135215

Structurei

Secondary structure

1136
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V86X-ray2.05D/E2-9[»]
2V87X-ray1.80D/E2-14[»]
2V88X-ray2.00D/F2-8[»]
4QWNX-ray2.10E/F30-44[»]
4QX7X-ray2.34E/F30-44[»]
4QX8X-ray1.65E/F30-44[»]
4QXBX-ray1.60E/F30-44[»]
4QXCX-ray1.75E/F30-44[»]
4QXHX-ray2.20E/F30-44[»]
ProteinModelPortaliP84228
SMRiP84228
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiKOG1745 Eukaryota
COG2036 LUCA
GeneTreeiENSGT00760000118967
HOVERGENiHBG001172
InParanoidiP84228
KOiK11253
OMAiANLCTIH
OrthoDBiEOG091G0XGD
PhylomeDBiP84228
TreeFamiTF314241

Family and domain databases

Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR007125 Histone_H2A/H2B/H3
IPR000164 Histone_H3/CENP-A
PANTHERiPTHR11426 PTHR11426, 1 hit
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PRINTSiPR00622 HISTONEH3
SMARTiView protein in SMART
SM00428 H3, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00322 HISTONE_H3_1, 1 hit
PS00959 HISTONE_H3_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P84228-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,388
Last modified:January 23, 2007 - v2
Checksum:i6FD8508EA50A0EEC
GO

Sequence cautioni

The sequence AAH94041 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAO06264 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01685 Genomic DNA Translation: CAA25840.1
M32459 Genomic DNA Translation: AAA37810.1
M32461 Genomic DNA Translation: AAA37812.1
X16148 Genomic DNA Translation: CAA34274.1
M33989 Genomic DNA Translation: AAA37764.1
X80328 Genomic DNA Translation: CAA56577.1
U62669 Genomic DNA Translation: AAB04760.1
U62671 Genomic DNA Translation: AAB04764.1
U62674 Genomic DNA Translation: AAB04771.1
U62675 Genomic DNA Translation: AAB04772.1
AY158941 Genomic DNA Translation: AAO06251.1
AY158947 Genomic DNA Translation: AAO06257.1
AY158948 Genomic DNA Translation: AAO06258.1
AY158949 Genomic DNA Translation: AAO06259.1
AY158950 Genomic DNA Translation: AAO06260.1
AY158951 Genomic DNA Translation: AAO06261.1
AY158954 Genomic DNA Translation: AAO06264.1 Different initiation.
AY158955 Genomic DNA Translation: AAO06265.1
AK010121 mRNA Translation: BAB26714.1
AK020421 mRNA Translation: BAB32097.1
AL590388 Genomic DNA Translation: CAI25840.1
AL590388 Genomic DNA Translation: CAI25844.1
BC015270 mRNA Translation: AAH15270.1
BC094041 mRNA Translation: AAH94041.1 Different initiation.
BC101954 mRNA Translation: AAI01955.1
BC101955 mRNA Translation: AAI01956.1
BC101956 mRNA Translation: AAI01957.1
BC103549 mRNA Translation: AAI03550.1
BC120800 mRNA Translation: AAI20801.1
BC120802 mRNA Translation: AAI20803.1
BC132488 mRNA Translation: AAI32489.1
BC132490 mRNA Translation: AAI32491.1
Z30939 mRNA Translation: CAA83209.1
CCDSiCCDS17638.1
CCDS26344.1
CCDS26347.1
CCDS26352.1
CCDS26362.1
CCDS26365.1
CCDS38554.2
CCDS57240.1
PIRiA39525
JH0304
S06743
S48060 S45111
RefSeqiNP_038576.1, NM_013548.4
NP_473386.1, NM_054045.4
NP_783584.1, NM_175653.2
NP_835510.1, NM_178203.2
NP_835511.1, NM_178204.2
NP_835512.1, NM_178205.2
NP_835587.1, NM_178215.2
NP_835734.2, NM_178216.3
UniGeneiMm.221389
Mm.261658
Mm.262517
Mm.347699
Mm.358797
Mm.383293
Mm.422680

Genome annotation databases

EnsembliENSMUST00000075558; ENSMUSP00000074994; ENSMUSG00000100210
ENSMUST00000091703; ENSMUSP00000089295; ENSMUSG00000069267
ENSMUST00000091752; ENSMUSP00000089346; ENSMUSG00000069310
ENSMUST00000098843; ENSMUSP00000096442; ENSMUSG00000074403
ENSMUST00000105105; ENSMUSP00000100737; ENSMUSG00000099583
ENSMUST00000105107; ENSMUSP00000100739; ENSMUSG00000069273
ENSMUST00000167403; ENSMUSP00000135215; ENSMUSG00000081058
ENSMUST00000176059; ENSMUSP00000134751; ENSMUSG00000093769
GeneIDi15077
260423
319148
319149
319150
319151
319154
97114
KEGGimmu:15077
mmu:260423
mmu:319148
mmu:319149
mmu:319150
mmu:319151
mmu:319154
mmu:97114
UCSCiuc007ptz.3 mouse

Similar proteinsi

Entry informationi

Entry nameiH32_MOUSE
AccessioniPrimary (citable) accession number: P84228
Secondary accession number(s): A3KMN6
, P02295, P02297, P16105, P17269, P17320, Q60582, Q78E59, Q8CGN9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 146 of the entry and version 2 of the sequence. See 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
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Main funding by: National Institutes of Health