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Protein

Inhibitor of growth protein 4

Gene

ING4

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

Functioni

Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1). Can enhance apoptosis induced by serum starvation in mammary epithelial cell line HC11 (By similarity).By similarity6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei198Histone H3K4me3By similarity1
Metal bindingi199Zinc 1By similarity1
Metal bindingi201Zinc 1By similarity1
Binding sitei209Histone H3K4me3By similarity1
Metal bindingi212Zinc 2By similarity1
Binding sitei213Histone H3K4me3By similarity1
Metal bindingi217Zinc 2By similarity1
Binding sitei221Histone H3K4me3By similarity1
Metal bindingi223Zinc 1; via pros nitrogenBy similarity1
Metal bindingi226Zinc 1By similarity1
Metal bindingi239Zinc 2By similarity1
Metal bindingi242Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri196 – 245PHD-typePROSITE-ProRule annotationAdd BLAST50

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • cell cycle arrest Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
  • DNA replication Source: UniProtKB
  • histone H3 acetylation Source: UniProtKB
  • histone H4-K12 acetylation Source: UniProtKB
  • histone H4-K5 acetylation Source: UniProtKB
  • histone H4-K8 acetylation Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of growth Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • protein acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000111653-MONOMER.
ReactomeiR-HSA-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of growth protein 4
Alternative name(s):
p29ING4
Gene namesi
Name:ING4
ORF Names:My036
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:19423. ING4.

Subcellular locationi

GO - Cellular componenti

  • histone acetyltransferase complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi51147.
OpenTargetsiENSG00000111653.
PharmGKBiPA134976283.

Polymorphism and mutation databases

BioMutaiING4.
DMDMi57012981.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002126681 – 249Inhibitor of growth protein 4Add BLAST249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei112N6-acetyllysineCombined sources1
Modified residuei127N6-acetyllysineCombined sources1
Modified residuei129N6-acetyllysineBy similarity1
Modified residuei133Citrulline1 Publication1
Modified residuei146N6-acetyllysineCombined sources1
Modified residuei148N6-acetyllysineCombined sources1
Modified residuei156N6-acetyllysineCombined sources1
Modified residuei166Citrulline1 Publication1
Isoform 4 (identifier: Q9UNL4-4)
Modified residuei114N6-acetyllysineCombined sources1
Modified residuei127N6-acetyllysineCombined sources1

Post-translational modificationi

Citrullination by PADI4 within the nuclear localization signal disrupts the interaction with p53 and increases susceptibility to degradation.1 Publication

Keywords - PTMi

Acetylation, Citrullination

Proteomic databases

EPDiQ9UNL4.
PaxDbiQ9UNL4.
PeptideAtlasiQ9UNL4.
PRIDEiQ9UNL4.

PTM databases

iPTMnetiQ9UNL4.
PhosphoSitePlusiQ9UNL4.

Expressioni

Gene expression databases

BgeeiENSG00000111653.
CleanExiHS_ING4.
ExpressionAtlasiQ9UNL4. baseline and differential.
GenevisibleiQ9UNL4. HS.

Organism-specific databases

HPAiHPA057338.

Interactioni

Subunit structurei

Homodimer. Interacts with H3K4me3 and to a lesser extent with H3K4me2, the interaction augments HBO1 acetylation activity on H3 tails. Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Interacts with EP300, RELA and TP53; these interactions may be indirect. Interacts with EGLN1. Interacts with BCL2A1 (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST1H3DP684313EBI-2866661,EBI-79722
HNRNPDQ141039EBI-2866661,EBI-299674
HNRNPDQ14103-42EBI-2866661,EBI-432545
NAV2Q8IVL13EBI-2866661,EBI-741200

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119331. 44 interactors.
DIPiDIP-42222N.
IntActiQ9UNL4. 27 interactors.
MINTiMINT-1202585.
STRINGi9606.ENSP00000380024.

Structurei

Secondary structure

1249
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 12Combined sources8
Helixi14 – 16Combined sources3
Helixi17 – 50Combined sources34
Helixi58 – 103Combined sources46
Turni199 – 202Combined sources4
Beta strandi207 – 211Combined sources5
Beta strandi221 – 223Combined sources3
Helixi225 – 227Combined sources3
Helixi240 – 243Combined sources4
Helixi244 – 246Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K1JNMR-A188-249[»]
2M1RNMR-A188-249[»]
2PNXX-ray1.80A/C194-246[»]
2VNFX-ray1.76A/C188-246[»]
4AFLX-ray2.28A/B/C/D/E/F2-105[»]
ProteinModelPortaliQ9UNL4.
SMRiQ9UNL4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UNL4.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili25 – 1181 PublicationAdd BLAST94

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi127 – 148Bipartite nuclear localization signalAdd BLAST22

Domaini

The PHD-type zinc finger mediates the binding to H3K4me3.
The N-terminal coiled-coil domain mediates homodimerization.

Sequence similaritiesi

Belongs to the ING family.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri196 – 245PHD-typePROSITE-ProRule annotationAdd BLAST50

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ9UNL4.
KOiK11346.
OMAiDNCKSAR.
OrthoDBiEOG091G0J8Y.
PhylomeDBiQ9UNL4.
TreeFamiTF352014.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028647. ING4.
IPR028651. ING_fam.
IPR024610. ING_N_histone_binding.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10333. PTHR10333. 1 hit.
PTHR10333:SF40. PTHR10333:SF40. 1 hit.
PfamiPF12998. ING. 1 hit.
[Graphical view]
SMARTiSM01408. ING. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UNL4-1) [UniParc]FASTAAdd to basket
Also known as: ING4_v1

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
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKGKK KGRTQKEKKA ARARSKGKNS
160 170 180 190 200
DEEAPKTAQK KLKLVRTSPE YGMPSVTFGS VHPSDVLDMP VDPNEPTYCL
210 220 230 240
CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP RCSQERKKK
Length:249
Mass (Da):28,530
Last modified:May 1, 2000 - v1
Checksum:iCE3FD9CC9F0CE949
GO
Isoform 2 (identifier: Q9UNL4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: K → S
     132-132: Missing.

Note: May be due to a competing donor splice site.
Show »
Length:248
Mass (Da):28,432
Checksum:i76907CB2119B07E8
GO
Isoform 3 (identifier: Q9UNL4-3) [UniParc]FASTAAdd to basket
Also known as: deltaEx2

The sequence of this isoform differs from the canonical sequence as follows:
     13-37: SIENLPFELQRNFQLMRDLDQRTED → N

Show »
Length:225
Mass (Da):25,554
Checksum:i56E4C5F4AB305918
GO
Isoform 4 (identifier: Q9UNL4-4) [UniParc]FASTAAdd to basket
Also known as: ING4_v4

The sequence of this isoform differs from the canonical sequence as follows:
     129-132: Missing.

Note: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization.Combined sources
Show »
Length:245
Mass (Da):28,089
Checksum:iD6D1003F066112AC
GO
Isoform 5 (identifier: Q9UNL4-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     128-131: GKKK → E

Show »
Length:246
Mass (Da):28,218
Checksum:iAE5F98B0081B189B
GO
Isoform 6 (identifier: Q9UNL4-6) [UniParc]FASTAAdd to basket
Also known as: ING4_v2

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: Missing.

Note: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization.
Show »
Length:248
Mass (Da):28,402
Checksum:i86907CA611946A45
GO
Isoform 7 (identifier: Q9UNL4-7) [UniParc]FASTAAdd to basket
Also known as: ING4_v3

The sequence of this isoform differs from the canonical sequence as follows:
     128-130: Missing.

Note: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization.
Show »
Length:246
Mass (Da):28,217
Checksum:i405F98B0061B1C31
GO
Isoform 8 (identifier: Q9UNL4-8) [UniParc]FASTAAdd to basket
Also known as: deltaEx6A

The sequence of this isoform differs from the canonical sequence as follows:
     168-249: SPEYGMPSVT...PRCSQERKKK → VPLSGSILPVWG

Show »
Length:179
Mass (Da):20,482
Checksum:iCE8BCDAD65CECE67
GO

Sequence cautioni

The sequence AAG43153 differs from that shown. Reason: Frameshift at positions 240 and 243.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04128813 – 37SIENL…QRTED → N in isoform 3. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_041289128 – 131GKKK → E in isoform 5. 1 Publication4
Alternative sequenceiVSP_041290128 – 130Missing in isoform 7. 1 Publication3
Alternative sequenceiVSP_041291129 – 132Missing in isoform 4. 1 Publication4
Alternative sequenceiVSP_012518131K → S in isoform 2. 3 Publications1
Alternative sequenceiVSP_041292131Missing in isoform 6. 1 Publication1
Alternative sequenceiVSP_012519132Missing in isoform 2. 3 Publications1
Alternative sequenceiVSP_041293168 – 249SPEYG…ERKKK → VPLSGSILPVWG in isoform 8. 1 PublicationAdd BLAST82

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156552 mRNA. Translation: AAL79773.1.
AB197695 mRNA. Translation: BAF30477.1.
AB197696 mRNA. Translation: BAF30478.1.
AB197697 mRNA. Translation: BAF30479.1.
EF152349 mRNA. Translation: ABO61139.1.
EF152351 mRNA. Translation: ABO61141.1.
AF063594 mRNA. Translation: AAG43153.1. Frameshift.
AF110645 mRNA. Translation: AAD48585.1.
CH471116 Genomic DNA. Translation: EAW88763.1.
CH471116 Genomic DNA. Translation: EAW88768.1.
CH471116 Genomic DNA. Translation: EAW88770.1.
CH471116 Genomic DNA. Translation: EAW88772.1.
BC007781 mRNA. Translation: AAH07781.1.
BC013038 mRNA. Translation: AAH13038.2.
BC095434 mRNA. Translation: AAH95434.1.
CCDSiCCDS44812.1. [Q9UNL4-3]
CCDS44813.1. [Q9UNL4-1]
CCDS44814.1. [Q9UNL4-5]
CCDS44815.1. [Q9UNL4-4]
CCDS44816.1. [Q9UNL4-8]
CCDS8555.1. [Q9UNL4-2]
RefSeqiNP_001121054.1. NM_001127582.1. [Q9UNL4-1]
NP_001121055.1. NM_001127583.1. [Q9UNL4-5]
NP_001121056.1. NM_001127584.1. [Q9UNL4-4]
NP_001121057.1. NM_001127585.1. [Q9UNL4-3]
NP_001121058.1. NM_001127586.1. [Q9UNL4-8]
NP_057246.2. NM_016162.3. [Q9UNL4-2]
UniGeneiHs.524210.

Genome annotation databases

EnsembliENST00000341550; ENSP00000343396; ENSG00000111653. [Q9UNL4-2]
ENST00000396807; ENSP00000380024; ENSG00000111653. [Q9UNL4-1]
ENST00000412586; ENSP00000412705; ENSG00000111653. [Q9UNL4-5]
ENST00000423703; ENSP00000414008; ENSG00000111653. [Q9UNL4-8]
ENST00000444704; ENSP00000397343; ENSG00000111653. [Q9UNL4-3]
ENST00000446105; ENSP00000415903; ENSG00000111653. [Q9UNL4-4]
GeneIDi51147.
KEGGihsa:51147.
UCSCiuc001qpv.5. human. [Q9UNL4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156552 mRNA. Translation: AAL79773.1.
AB197695 mRNA. Translation: BAF30477.1.
AB197696 mRNA. Translation: BAF30478.1.
AB197697 mRNA. Translation: BAF30479.1.
EF152349 mRNA. Translation: ABO61139.1.
EF152351 mRNA. Translation: ABO61141.1.
AF063594 mRNA. Translation: AAG43153.1. Frameshift.
AF110645 mRNA. Translation: AAD48585.1.
CH471116 Genomic DNA. Translation: EAW88763.1.
CH471116 Genomic DNA. Translation: EAW88768.1.
CH471116 Genomic DNA. Translation: EAW88770.1.
CH471116 Genomic DNA. Translation: EAW88772.1.
BC007781 mRNA. Translation: AAH07781.1.
BC013038 mRNA. Translation: AAH13038.2.
BC095434 mRNA. Translation: AAH95434.1.
CCDSiCCDS44812.1. [Q9UNL4-3]
CCDS44813.1. [Q9UNL4-1]
CCDS44814.1. [Q9UNL4-5]
CCDS44815.1. [Q9UNL4-4]
CCDS44816.1. [Q9UNL4-8]
CCDS8555.1. [Q9UNL4-2]
RefSeqiNP_001121054.1. NM_001127582.1. [Q9UNL4-1]
NP_001121055.1. NM_001127583.1. [Q9UNL4-5]
NP_001121056.1. NM_001127584.1. [Q9UNL4-4]
NP_001121057.1. NM_001127585.1. [Q9UNL4-3]
NP_001121058.1. NM_001127586.1. [Q9UNL4-8]
NP_057246.2. NM_016162.3. [Q9UNL4-2]
UniGeneiHs.524210.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K1JNMR-A188-249[»]
2M1RNMR-A188-249[»]
2PNXX-ray1.80A/C194-246[»]
2VNFX-ray1.76A/C188-246[»]
4AFLX-ray2.28A/B/C/D/E/F2-105[»]
ProteinModelPortaliQ9UNL4.
SMRiQ9UNL4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119331. 44 interactors.
DIPiDIP-42222N.
IntActiQ9UNL4. 27 interactors.
MINTiMINT-1202585.
STRINGi9606.ENSP00000380024.

PTM databases

iPTMnetiQ9UNL4.
PhosphoSitePlusiQ9UNL4.

Polymorphism and mutation databases

BioMutaiING4.
DMDMi57012981.

Proteomic databases

EPDiQ9UNL4.
PaxDbiQ9UNL4.
PeptideAtlasiQ9UNL4.
PRIDEiQ9UNL4.

Protocols and materials databases

DNASUi51147.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341550; ENSP00000343396; ENSG00000111653. [Q9UNL4-2]
ENST00000396807; ENSP00000380024; ENSG00000111653. [Q9UNL4-1]
ENST00000412586; ENSP00000412705; ENSG00000111653. [Q9UNL4-5]
ENST00000423703; ENSP00000414008; ENSG00000111653. [Q9UNL4-8]
ENST00000444704; ENSP00000397343; ENSG00000111653. [Q9UNL4-3]
ENST00000446105; ENSP00000415903; ENSG00000111653. [Q9UNL4-4]
GeneIDi51147.
KEGGihsa:51147.
UCSCiuc001qpv.5. human. [Q9UNL4-1]

Organism-specific databases

CTDi51147.
DisGeNETi51147.
GeneCardsiING4.
HGNCiHGNC:19423. ING4.
HPAiHPA057338.
MIMi608524. gene.
neXtProtiNX_Q9UNL4.
OpenTargetsiENSG00000111653.
PharmGKBiPA134976283.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ9UNL4.
KOiK11346.
OMAiDNCKSAR.
OrthoDBiEOG091G0J8Y.
PhylomeDBiQ9UNL4.
TreeFamiTF352014.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000111653-MONOMER.
ReactomeiR-HSA-3214847. HATs acetylate histones.

Miscellaneous databases

ChiTaRSiING4. human.
EvolutionaryTraceiQ9UNL4.
GeneWikiiING4.
GenomeRNAii51147.
PROiQ9UNL4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111653.
CleanExiHS_ING4.
ExpressionAtlasiQ9UNL4. baseline and differential.
GenevisibleiQ9UNL4. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028647. ING4.
IPR028651. ING_fam.
IPR024610. ING_N_histone_binding.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10333. PTHR10333. 1 hit.
PTHR10333:SF40. PTHR10333:SF40. 1 hit.
PfamiPF12998. ING. 1 hit.
[Graphical view]
SMARTiSM01408. ING. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiING4_HUMAN
AccessioniPrimary (citable) accession number: Q9UNL4
Secondary accession number(s): A4KYM4
, A4KYM6, D3DUR8, Q0EF62, Q0EF63, Q4VBQ6, Q96E15, Q9H3J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 153 of the entry and version 1 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. 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.