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

Zinc finger protein AEBP2

Gene

AEBP2

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

Functioni

DNA-binding transcriptional repressor. May interact with and stimulate the activity of the PRC2 complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri261 – 28626C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri300 – 32223C2H2-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri328 – 35225C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_264352. PRC2 methylates histones and DNA.
REACT_268728. PKMTs methylate histone lysines.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein AEBP2
Alternative name(s):
Adipocyte enhancer-binding protein 2
Short name:
AE-binding protein 2
Gene namesi
Name:AEBP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24051. AEBP2.

Subcellular locationi

GO - Cellular componenti

  • ESC/E(Z) complex Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134875401.

Polymorphism and mutation databases

BioMutaiAEBP2.
DMDMi190358163.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 517516Zinc finger protein AEBP2PRO_0000341590Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei18 – 181Phosphoserine2 Publications
Modified residuei24 – 241Phosphoserine2 Publications
Modified residuei206 – 2061Phosphoserine3 Publications
Modified residuei210 – 2101Phosphoserine1 Publication
Modified residuei211 – 2111Phosphoserine1 Publication
Modified residuei390 – 3901Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ6ZN18.
PaxDbiQ6ZN18.
PRIDEiQ6ZN18.

PTM databases

PhosphoSiteiQ6ZN18.

Expressioni

Gene expression databases

BgeeiQ6ZN18.
CleanExiHS_AEBP2.
ExpressionAtlasiQ6ZN18. baseline and differential.
GenevisibleiQ6ZN18. HS.

Organism-specific databases

HPAiHPA020893.
HPA022282.

Interactioni

Subunit structurei

Self-associates. Interacts with EED, EZH2, RBBP4 and SUZ12. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2 (By similarity). May also interact with RBBP7.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HMBOX1Q6NT763EBI-10255023,EBI-2549423

Protein-protein interaction databases

BioGridi125736. 20 interactions.
DIPiDIP-58581N.
IntActiQ6ZN18. 4 interactions.
MINTiMINT-1439056.
STRINGi9606.ENSP00000381840.

Structurei

3D structure databases

ProteinModelPortaliQ6ZN18.
SMRiQ6ZN18. Positions 261-388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni209 – 29486Interaction with RBBP4Add
BLAST
Regioni353 – 517165Interaction with SUZ12Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi34 – 12390Glu-richAdd
BLAST
Compositional biasi61 – 205145Gly-richAdd
BLAST
Compositional biasi110 – 256147Ser-richAdd
BLAST

Sequence similaritiesi

Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri261 – 28626C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri300 – 32223C2H2-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri328 – 35225C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG291563.
GeneTreeiENSGT00510000048519.
HOGENOMiHOG000033826.
InParanoidiQ6ZN18.
KOiK17452.
OMAiQTXVIAK.
PhylomeDBiQ6ZN18.
TreeFamiTF328864.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[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: Q6ZN18-1) [UniParc]FASTAAdd to basket

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
MAAAITDMAD LEELSRLSPL PPGSPGSAAR GRAEPPEEEE EEEEEEEEAE
60 70 80 90 100
AEAVAALLLN GGSGGGGGGG GGGVGGGEAE TMSEPSPESA SQAGEDEDEE
110 120 130 140 150
EDDEEEEDES SSSGGGEEES SAESLVGSSG GSSSDETRSL SPGAASSSSG
160 170 180 190 200
DGDGKEGLEE PKGPRGSQGG GGGGSSSSSV VSSGGDEGYG TGGGGSSATS
210 220 230 240 250
GGRRGSLEMS SDGEPLSRMD SEDSISSTIM DVDSTISSGR STPAMMNGQG
260 270 280 290 300
STTSSSKNIA YNCCWDQCQA CFNSSPDLAD HIRSIHVDGQ RGGVFVCLWK
310 320 330 340 350
GCKVYNTPST SQSWLQRHML THSGDKPFKC VVGGCNASFA SQGGLARHVP
360 370 380 390 400
THFSQQNSSK VSSQPKAKEE SPSKAGMNKR RKLKNKRRRS LPRPHDFFDA
410 420 430 440 450
QTLDAIRHRA ICFNLSAHIE SLGKGHSVVF HSTVIAKRKE DSGKIKLLLH
460 470 480 490 500
WMPEDILPDV WVNESERHQL KTKVVHLSKL PKDTALLLDP NIYRTMPQKR
510
LKRTLIRKVF NLYLSKQ
Length:517
Mass (Da):54,467
Last modified:June 10, 2008 - v2
Checksum:i6C59888ACEE4F9AF
GO
Isoform 2 (identifier: Q6ZN18-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     504-517: Missing.

Show »
Length:503
Mass (Da):52,761
Checksum:i032090A790243D07
GO
Isoform 3 (identifier: Q6ZN18-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-216: Missing.
     217-223: SRMDSED → MYTRRYS

Show »
Length:301
Mass (Da):33,981
Checksum:iDD766CAAB61DADB3
GO

Sequence cautioni

The sequence AAH15624.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH22220.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD18513.1 differs from that shown. Reason: Erroneous termination at position 269. Translated as Gln.Curated
The sequence EAW96400.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 216216Missing in isoform 3. 1 PublicationVSP_034357Add
BLAST
Alternative sequencei217 – 2237SRMDSED → MYTRRYS in isoform 3. 1 PublicationVSP_034358
Alternative sequencei504 – 51714Missing in isoform 2. 1 PublicationVSP_034359Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK131361 mRNA. Translation: BAD18513.1. Sequence problems.
AK131410 mRNA. Translation: BAD18557.1.
CH471094 Genomic DNA. Translation: EAW96400.1. Different initiation.
BC015624 mRNA. Translation: AAH15624.1. Different initiation.
BC022220 mRNA. Translation: AAH22220.1. Different initiation.
AB209384 mRNA. Translation: BAD92621.1.
CCDSiCCDS44841.1. [Q6ZN18-1]
CCDS44842.1. [Q6ZN18-2]
CCDS58215.1. [Q6ZN18-3]
RefSeqiNP_001107648.1. NM_001114176.1. [Q6ZN18-1]
NP_001253972.1. NM_001267043.1. [Q6ZN18-3]
NP_694939.2. NM_153207.4. [Q6ZN18-2]
UniGeneiHs.126497.

Genome annotation databases

EnsembliENST00000266508; ENSP00000266508; ENSG00000139154. [Q6ZN18-2]
ENST00000360995; ENSP00000354267; ENSG00000139154. [Q6ZN18-3]
ENST00000398864; ENSP00000381840; ENSG00000139154. [Q6ZN18-1]
GeneIDi121536.
KEGGihsa:121536.
UCSCiuc001ree.2. human. [Q6ZN18-1]
uc001reg.2. human. [Q6ZN18-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK131361 mRNA. Translation: BAD18513.1. Sequence problems.
AK131410 mRNA. Translation: BAD18557.1.
CH471094 Genomic DNA. Translation: EAW96400.1. Different initiation.
BC015624 mRNA. Translation: AAH15624.1. Different initiation.
BC022220 mRNA. Translation: AAH22220.1. Different initiation.
AB209384 mRNA. Translation: BAD92621.1.
CCDSiCCDS44841.1. [Q6ZN18-1]
CCDS44842.1. [Q6ZN18-2]
CCDS58215.1. [Q6ZN18-3]
RefSeqiNP_001107648.1. NM_001114176.1. [Q6ZN18-1]
NP_001253972.1. NM_001267043.1. [Q6ZN18-3]
NP_694939.2. NM_153207.4. [Q6ZN18-2]
UniGeneiHs.126497.

3D structure databases

ProteinModelPortaliQ6ZN18.
SMRiQ6ZN18. Positions 261-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125736. 20 interactions.
DIPiDIP-58581N.
IntActiQ6ZN18. 4 interactions.
MINTiMINT-1439056.
STRINGi9606.ENSP00000381840.

Chemistry

ChEMBLiCHEMBL3137287.

PTM databases

PhosphoSiteiQ6ZN18.

Polymorphism and mutation databases

BioMutaiAEBP2.
DMDMi190358163.

Proteomic databases

MaxQBiQ6ZN18.
PaxDbiQ6ZN18.
PRIDEiQ6ZN18.

Protocols and materials databases

DNASUi121536.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266508; ENSP00000266508; ENSG00000139154. [Q6ZN18-2]
ENST00000360995; ENSP00000354267; ENSG00000139154. [Q6ZN18-3]
ENST00000398864; ENSP00000381840; ENSG00000139154. [Q6ZN18-1]
GeneIDi121536.
KEGGihsa:121536.
UCSCiuc001ree.2. human. [Q6ZN18-1]
uc001reg.2. human. [Q6ZN18-3]

Organism-specific databases

CTDi121536.
GeneCardsiGC12P019556.
HGNCiHGNC:24051. AEBP2.
HPAiHPA020893.
HPA022282.
neXtProtiNX_Q6ZN18.
PharmGKBiPA134875401.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG291563.
GeneTreeiENSGT00510000048519.
HOGENOMiHOG000033826.
InParanoidiQ6ZN18.
KOiK17452.
OMAiQTXVIAK.
PhylomeDBiQ6ZN18.
TreeFamiTF328864.

Enzyme and pathway databases

ReactomeiREACT_264352. PRC2 methylates histones and DNA.
REACT_268728. PKMTs methylate histone lysines.

Miscellaneous databases

ChiTaRSiAEBP2. human.
GenomeRNAii121536.
NextBioi80766.
PROiQ6ZN18.

Gene expression databases

BgeeiQ6ZN18.
CleanExiHS_AEBP2.
ExpressionAtlasiQ6ZN18. baseline and differential.
GenevisibleiQ6ZN18. HS.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Teratocarcinoma and Uterus.
  2. 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] (ISOFORM 2).
    Tissue: Eye and Uterus.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-517 (ISOFORM 1).
    Tissue: Brain.
  5. "Role of histone H3 lysine 27 methylation in Polycomb-group silencing."
    Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y.
    Science 298:1039-1043(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EED; EZH2; RBBP4; RBBP7 AND SUZ12.
  6. "SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex."
    Cao R., Zhang Y.
    Mol. Cell 15:57-67(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH EED; EZH2; RBBP4 AND SUZ12.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-210 AND SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-24 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAEBP2_HUMAN
AccessioniPrimary (citable) accession number: Q6ZN18
Secondary accession number(s): Q59FS5, Q6ZN62, Q96BG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: June 24, 2015
This is version 99 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.