UniProtKB - Q6NXT2 (H3C_HUMAN)
Protein
Histone H3.3C
Gene
H3-5
Organism
Homo sapiens (Human)
Status
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. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes.1 Publication
GO - Molecular functioni
- nucleosomal DNA binding Source: UniProtKB
- protein heterodimerization activity Source: InterPro
GO - Biological processi
- brain development Source: Ensembl
- cell population proliferation Source: Ensembl
- embryo implantation Source: Ensembl
- male gonad development Source: Ensembl
- multicellular organism growth Source: Ensembl
- muscle cell differentiation Source: Ensembl
- negative regulation of chromosome condensation Source: Ensembl
- nucleus organization Source: Ensembl
- oogenesis Source: Ensembl
- osteoblast differentiation Source: Ensembl
- pericentric heterochromatin assembly Source: Ensembl
- positive regulation of cell growth Source: UniProtKB
- regulation of centromere complex assembly Source: Ensembl
- response to hormone Source: Ensembl
- single fertilization Source: Ensembl
- spermatid development Source: Ensembl
- subtelomeric heterochromatin assembly Source: Ensembl
Keywordsi
Molecular function | DNA-binding |
Enzyme and pathway databases
PathwayCommonsi | Q6NXT2 |
Names & Taxonomyi
Protein namesi | Recommended name: Histone H3.3CAlternative name(s): Histone H3.5Imported |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:33164, H3-5 |
MIMi | 616134, gene |
neXtProti | NX_Q6NXT2 |
VEuPathDBi | HostDB:ENSG00000188375.4 |
Subcellular locationi
Nucleus
Other locations
Nucleus
- Barr body Source: Ensembl
- nuclear euchromatin Source: UniProtKB
- nucleus Source: GO_Central
Other locations
- nucleosome Source: UniProtKB-KW
Keywords - Cellular componenti
Chromosome, Nucleosome core, NucleusPathology & Biotechi
Organism-specific databases
DisGeNETi | 440093 |
OpenTargetsi | ENSG00000188375 |
PharmGKBi | PA165512903 |
Miscellaneous databases
Pharosi | Q6NXT2, Tbio |
Genetic variation databases
BioMutai | H3F3C |
DMDMi | 116248097 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCurated | |||
ChainiPRO_0000253960 | 2 – 135 | Histone H3.3CAdd BLAST | 134 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 3 | Asymmetric dimethylarginine; by PRMT6; alternateBy similarity | 1 | |
Modified residuei | 3 | Citrulline; alternateBy similarity | 1 | |
Modified residuei | 4 | Phosphothreonine; by HASPINBy similarity | 1 | |
Modified residuei | 5 | Allysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 7 | Phosphothreonine; by PKCBy similarity | 1 | |
Modified residuei | 9 | Citrulline; alternateBy similarity | 1 | |
Modified residuei | 9 | Symmetric dimethylarginine; by PRMT5; alternateBy similarity | 1 | |
Modified residuei | 10 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 11 | ADP-ribosylserine; alternateBy similarity | 1 | |
Modified residuei | 11 | Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5By similarity | 1 | |
Modified residuei | 12 | Phosphothreonine; by PKCBy similarity | 1 | |
Modified residuei | 15 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 15 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 15 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 15 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 15 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 18 | Asymmetric dimethylarginine; by CARM1; alternateBy similarity | 1 | |
Modified residuei | 18 | Citrulline; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-butyryllysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-butyryllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 27 | CitrullineBy similarity | 1 | |
Modified residuei | 28 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 29 | ADP-ribosylserine; alternateBy similarity | 1 | |
Modified residuei | 29 | Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5By similarity | 1 | |
Modified residuei | 32 | PhosphoserineBy similarity | 1 | |
Modified residuei | 37 | N6-methyllysineBy similarity | 1 | |
Modified residuei | 41 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 56 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 56 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 56 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 56 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 56 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 56 | N6-methyllysine; by EHMT2; alternateBy similarity | 1 | |
Modified residuei | 56 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 57 | Phosphoserine1 Publication | 1 | |
Modified residuei | 64 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 64 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 80 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 86 | PhosphoserineBy similarity | 1 | |
Modified residuei | 107 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 115 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 115 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 122 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 122 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 122 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 122 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 122 | N6-succinyllysine; alternateBy similarity | 1 |
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-122 (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 (By similarity).By similarity
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.By similarity
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) is linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. 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) requires 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-56 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication (By similarity).By similarity
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-41 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin (By similarity).By similarity
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
Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.By similarity
Succinylated. Desuccinylation at Lys-122 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair.By similarity
Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).By similarity
Keywords - PTMi
Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | Q6NXT2 |
jPOSTi | Q6NXT2 |
MassIVEi | Q6NXT2 |
MaxQBi | Q6NXT2 |
PaxDbi | Q6NXT2 |
PeptideAtlasi | Q6NXT2 |
PRIDEi | Q6NXT2 |
ProteomicsDBi | 66771 |
TopDownProteomicsi | Q6NXT2 |
PTM databases
iPTMneti | Q6NXT2 |
PhosphoSitePlusi | Q6NXT2 |
SwissPalmi | Q6NXT2 |
Expressioni
Tissue specificityi
Specifically expressed in the seminiferous tubules of testis.1 Publication
Gene expression databases
Bgeei | ENSG00000188375, Expressed in testis and 75 other tissues |
Genevisiblei | Q6NXT2, HS |
Organism-specific databases
HPAi | ENSG00000188375, Group enriched (blood, testis) |
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.
Binary interactionsi
Hide detailsQ6NXT2
GO - Molecular functioni
- protein heterodimerization activity Source: InterPro
Protein-protein interaction databases
BioGRIDi | 136289, 43 interactors |
IntActi | Q6NXT2, 43 interactors |
MINTi | Q6NXT2 |
STRINGi | 9606.ENSP00000339835 |
Miscellaneous databases
RNActi | Q6NXT2, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q6NXT2 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q6NXT2 |
Family & Domainsi
Sequence similaritiesi
Belongs to the histone H3 family.Curated
Phylogenomic databases
eggNOGi | KOG1745, Eukaryota |
GeneTreei | ENSGT01010000222292 |
HOGENOMi | CLU_078295_4_0_1 |
InParanoidi | Q6NXT2 |
OMAi | PKMARTK |
OrthoDBi | 1564596at2759 |
PhylomeDBi | Q6NXT2 |
TreeFami | TF314241 |
Family and domain databases
Gene3Di | 1.10.20.10, 1 hit |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR007125, Histone_H2A/H2B/H3 IPR000164, Histone_H3/CENP-A |
PANTHERi | PTHR11426, PTHR11426, 1 hit |
Pfami | View protein in Pfam PF00125, Histone, 1 hit |
PRINTSi | PR00622, HISTONEH3 |
SMARTi | View protein in SMART SM00428, H3, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00322, HISTONE_H3_1, 1 hit PS00959, HISTONE_H3_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q6NXT2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MARTKQTARK STGGKAPRKQ LATKAARKST PSTCGVKPHR YRPGTVALRE
60 70 80 90 100
IRRYQKSTEL LIRKLPFQRL VREIAQDFNT DLRFQSAAVG ALQEASEAYL
110 120 130
VGLLEDTNLC AIHAKRVTIM PKDIQLARRI RGERA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 88 | A → V in ADW85800 (PubMed:21274551).Curated | 1 | |
Sequence conflicti | 88 | A → V in AAH66906 (PubMed:15489334).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_068164 | 39 | H → R. Corresponds to variant dbSNP:rs3759295Ensembl. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | HQ873957 mRNA Translation: ADW85800.1 AC023050 Genomic DNA No translation available. BC066906 mRNA Translation: AAH66906.1 |
CCDSi | CCDS31769.1 |
RefSeqi | NP_001013721.2, NM_001013699.2 |
Genome annotation databases
Ensembli | ENST00000340398; ENSP00000339835; ENSG00000188375 |
GeneIDi | 440093 |
KEGGi | hsa:440093 |
UCSCi | uc001rkr.3, human |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | HQ873957 mRNA Translation: ADW85800.1 AC023050 Genomic DNA No translation available. BC066906 mRNA Translation: AAH66906.1 |
CCDSi | CCDS31769.1 |
RefSeqi | NP_001013721.2, NM_001013699.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2PUY | X-ray | 1.43 | E | 2-11 | [»] | |
3KV4 | X-ray | 2.19 | B | 2-25 | [»] | |
4Z5T | X-ray | 2.80 | A/E | 1-135 | [»] | |
5BWN | X-ray | 1.94 | B | 6-14 | [»] | |
5BWO | X-ray | 2.38 | B | 6-14 | [»] | |
5F6K | X-ray | 2.41 | M | 2-10 | [»] | |
5I3L | X-ray | 1.85 | C | 2-21 | [»] | |
6OI3 | X-ray | 1.66 | B | 2-22 | [»] | |
SMRi | Q6NXT2 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 136289, 43 interactors |
IntActi | Q6NXT2, 43 interactors |
MINTi | Q6NXT2 |
STRINGi | 9606.ENSP00000339835 |
PTM databases
iPTMneti | Q6NXT2 |
PhosphoSitePlusi | Q6NXT2 |
SwissPalmi | Q6NXT2 |
Genetic variation databases
BioMutai | H3F3C |
DMDMi | 116248097 |
Proteomic databases
EPDi | Q6NXT2 |
jPOSTi | Q6NXT2 |
MassIVEi | Q6NXT2 |
MaxQBi | Q6NXT2 |
PaxDbi | Q6NXT2 |
PeptideAtlasi | Q6NXT2 |
PRIDEi | Q6NXT2 |
ProteomicsDBi | 66771 |
TopDownProteomicsi | Q6NXT2 |
Protocols and materials databases
Antibodypediai | 55173, 30 antibodies |
Genome annotation databases
Ensembli | ENST00000340398; ENSP00000339835; ENSG00000188375 |
GeneIDi | 440093 |
KEGGi | hsa:440093 |
UCSCi | uc001rkr.3, human |
Organism-specific databases
CTDi | 440093 |
DisGeNETi | 440093 |
GeneCardsi | H3-5 |
HGNCi | HGNC:33164, H3-5 |
HPAi | ENSG00000188375, Group enriched (blood, testis) |
MIMi | 616134, gene |
neXtProti | NX_Q6NXT2 |
OpenTargetsi | ENSG00000188375 |
PharmGKBi | PA165512903 |
VEuPathDBi | HostDB:ENSG00000188375.4 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1745, Eukaryota |
GeneTreei | ENSGT01010000222292 |
HOGENOMi | CLU_078295_4_0_1 |
InParanoidi | Q6NXT2 |
OMAi | PKMARTK |
OrthoDBi | 1564596at2759 |
PhylomeDBi | Q6NXT2 |
TreeFami | TF314241 |
Enzyme and pathway databases
PathwayCommonsi | Q6NXT2 |
Miscellaneous databases
BioGRID-ORCSi | 440093, 43 hits in 853 CRISPR screens |
ChiTaRSi | H3F3C, human |
EvolutionaryTracei | Q6NXT2 |
GenomeRNAii | 440093 |
Pharosi | Q6NXT2, Tbio |
PROi | PR:Q6NXT2 |
RNActi | Q6NXT2, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000188375, Expressed in testis and 75 other tissues |
Genevisiblei | Q6NXT2, HS |
Family and domain databases
Gene3Di | 1.10.20.10, 1 hit |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR007125, Histone_H2A/H2B/H3 IPR000164, Histone_H3/CENP-A |
PANTHERi | PTHR11426, PTHR11426, 1 hit |
Pfami | View protein in Pfam PF00125, Histone, 1 hit |
PRINTSi | PR00622, HISTONEH3 |
SMARTi | View protein in SMART SM00428, H3, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00322, HISTONE_H3_1, 1 hit PS00959, HISTONE_H3_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | H3C_HUMAN | |
Accessioni | Q6NXT2Primary (citable) accession number: Q6NXT2 Secondary accession number(s): E9P281 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 17, 2006 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 10, 2021 | |
This is version 152 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families