Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone H3.3C

Gene

H3F3C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. 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

GO - Biological processi

  • positive regulation of cell growth Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.3C
Alternative name(s):
Histone H3.5
Gene namesi
Name:H3F3C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:33164. H3F3C.

Subcellular locationi

GO - Cellular componenti

  • nuclear euchromatin Source: UniProtKB
  • nucleosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165512903.

Polymorphism and mutation databases

BioMutaiH3F3C.
DMDMi116248097.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 135134Histone H3.3CPRO_0000253960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Asymmetric dimethylarginine; by PRMT6; alternateBy similarity
Modified residuei3 – 31Citrulline; alternateBy similarity
Modified residuei4 – 41Phosphothreonine; by GSG2By similarity
Modified residuei5 – 51Allysine; alternateBy similarity
Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei5 – 51N6,N6-dimethyllysine; alternateBy similarity
Modified residuei5 – 51N6-acetyllysine; alternateBy similarity
Modified residuei5 – 51N6-methyllysine; alternateBy similarity
Modified residuei7 – 71Phosphothreonine; by PKCBy similarity
Modified residuei9 – 91Citrulline; alternateBy similarity
Modified residuei9 – 91Symmetric dimethylarginine; by PRMT5; alternateBy similarity
Modified residuei10 – 101N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei10 – 101N6,N6-dimethyllysine; alternateBy similarity
Modified residuei10 – 101N6-acetyllysine; alternateBy similarity
Modified residuei10 – 101N6-methyllysine; alternateBy similarity
Modified residuei11 – 111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5By similarity
Modified residuei12 – 121Phosphothreonine; by PKCBy similarity
Modified residuei15 – 151N6-acetyllysineBy similarity
Modified residuei18 – 181Asymmetric dimethylarginine; by CARM1; alternateBy similarity
Modified residuei18 – 181Citrulline; alternateBy similarity
Modified residuei19 – 191N6-acetyllysine; alternateBy similarity
Modified residuei19 – 191N6-methyllysine; alternateBy similarity
Modified residuei24 – 241N6-acetyllysine; alternateBy similarity
Modified residuei24 – 241N6-methyllysine; alternateBy similarity
Modified residuei27 – 271CitrullineBy similarity
Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei28 – 281N6,N6-dimethyllysine; alternateBy similarity
Modified residuei28 – 281N6-acetyllysine; alternateBy similarity
Modified residuei28 – 281N6-methyllysine; alternateBy similarity
Modified residuei29 – 291Phosphoserine; by AURKB, AURKC and RPS6KA5By similarity
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei37 – 371N6-methyllysineBy similarity
Modified residuei41 – 411PhosphotyrosineBy similarity
Modified residuei56 – 561N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei56 – 561N6-acetyllysine; alternateBy similarity
Modified residuei56 – 561N6-methyllysine; by EHMT2; alternateBy similarity
Modified residuei57 – 571Phosphoserine1 Publication
Modified residuei64 – 641N6-methyllysineBy similarity
Modified residuei80 – 801Phosphothreonine1 Publication
Modified residuei86 – 861PhosphoserineBy similarity
Modified residuei107 – 1071PhosphothreonineBy similarity
Modified residuei115 – 1151N6-acetyllysineBy similarity
Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
Modified residuei122 – 1221N6-methyllysine; alternateBy similarity

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 GSG2/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 MLTK 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

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6NXT2.
PaxDbiQ6NXT2.
PRIDEiQ6NXT2.
TopDownProteomicsiQ6NXT2.

PTM databases

iPTMnetiQ6NXT2.
SwissPalmiQ6NXT2.

Expressioni

Tissue specificityi

Specifically expressed in the seminiferous tubules of testis.1 Publication

Gene expression databases

BgeeiQ6NXT2.
GenevisibleiQ6NXT2. HS.

Organism-specific databases

HPAiHPA042570.

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

WithEntry#Exp.IntActNotes
NASPP49321-23EBI-2868501,EBI-7038920

GO - Molecular functioni

  • nucleosomal DNA binding Source: UniProtKB

Protein-protein interaction databases

BioGridi136289. 24 interactions.
IntActiQ6NXT2. 14 interactions.
MINTiMINT-8417671.
STRINGi9606.ENSP00000339835.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 128Combined sources
Helixi45 – 5612Combined sources
Helixi64 – 7815Combined sources
Helixi86 – 11328Combined sources
Beta strandi117 – 1193Combined sources
Helixi121 – 13010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KV4X-ray2.19B2-25[»]
4Z5TX-ray2.80A/E1-135[»]
5F6KX-ray2.41M2-10[»]
5I3LX-ray1.85C2-21[»]
ProteinModelPortaliQ6NXT2.
SMRiQ6NXT2. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6NXT2.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiKOG1745. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000118967.
HOGENOMiHOG000155290.
HOVERGENiHBG001172.
InParanoidiQ6NXT2.
KOiK11253.
OMAiTPSTCGV.
OrthoDBiEOG7HB5C2.
PhylomeDBiQ6NXT2.
TreeFamiTF314241.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6NXT2-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:135
Mass (Da):15,214
Last modified:January 23, 2007 - v3
Checksum:iF2941F8A9BC61BB5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881A → V in ADW85800 (PubMed:21274551).Curated
Sequence conflicti88 – 881A → V in AAH66906 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391H → R.
Corresponds to variant rs3759295 [ dbSNP | Ensembl ].
VAR_068164

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.
CCDSiCCDS31769.1.
RefSeqiNP_001013721.2. NM_001013699.2.
UniGeneiHs.448697.

Genome annotation databases

EnsembliENST00000340398; ENSP00000339835; ENSG00000188375.
GeneIDi440093.
KEGGihsa:440093.
UCSCiuc001rkr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

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.
CCDSiCCDS31769.1.
RefSeqiNP_001013721.2. NM_001013699.2.
UniGeneiHs.448697.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KV4X-ray2.19B2-25[»]
4Z5TX-ray2.80A/E1-135[»]
5F6KX-ray2.41M2-10[»]
5I3LX-ray1.85C2-21[»]
ProteinModelPortaliQ6NXT2.
SMRiQ6NXT2. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi136289. 24 interactions.
IntActiQ6NXT2. 14 interactions.
MINTiMINT-8417671.
STRINGi9606.ENSP00000339835.

PTM databases

iPTMnetiQ6NXT2.
SwissPalmiQ6NXT2.

Polymorphism and mutation databases

BioMutaiH3F3C.
DMDMi116248097.

Proteomic databases

EPDiQ6NXT2.
PaxDbiQ6NXT2.
PRIDEiQ6NXT2.
TopDownProteomicsiQ6NXT2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340398; ENSP00000339835; ENSG00000188375.
GeneIDi440093.
KEGGihsa:440093.
UCSCiuc001rkr.3. human.

Organism-specific databases

CTDi440093.
GeneCardsiH3F3C.
HGNCiHGNC:33164. H3F3C.
HPAiHPA042570.
MIMi616134. gene.
neXtProtiNX_Q6NXT2.
PharmGKBiPA165512903.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1745. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000118967.
HOGENOMiHOG000155290.
HOVERGENiHBG001172.
InParanoidiQ6NXT2.
KOiK11253.
OMAiTPSTCGV.
OrthoDBiEOG7HB5C2.
PhylomeDBiQ6NXT2.
TreeFamiTF314241.

Miscellaneous databases

EvolutionaryTraceiQ6NXT2.
GenomeRNAii440093.
PROiQ6NXT2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6NXT2.
GenevisibleiQ6NXT2. HS.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "H3.5 is a novel hominid-specific histone H3 variant that is specifically expressed in the seminiferous tubules of human testes."
    Schenk R., Jenke A., Zilbauer M., Wirth S., Postberg J.
    Chromosoma 120:275-285(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Seminiferous tubule.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [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].
    Tissue: Testis.
  4. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
    Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
    Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-57 AND THR-80.

Entry informationi

Entry nameiH3C_HUMAN
AccessioniPrimary (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: June 8, 2016
This is version 114 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.