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Protein

RNA polymerase II elongation factor ELL2

Gene

ELL2

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

Functioni

Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). Plays a role in immunoglobulin secretion in plasma cells: directs efficient alternative mRNA processing, influencing both proximal poly(A) site choice and exon skipping, as well as immunoglobulin heavy chain (IgH) alternative processing. Probably acts by regulating histone modifications accompanying transition from membrane-specific to secretory IgH mRNA expression.4 Publications

GO - Biological processi

  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • snRNA transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription elongation from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-6807505. RNA polymerase II transcribes snRNA genes.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase II elongation factor ELL2
Gene namesi
Name:ELL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:17064. ELL2.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: HPA
  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • transcription elongation factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134935340.

Polymorphism and mutation databases

BioMutaiELL2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 640640RNA polymerase II elongation factor ELL2PRO_0000146735Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei503 – 5031PhosphoserineCombined sources
Modified residuei580 – 5801PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated by SIAH1, leading to its degradation by the proteaseome. Interaction with AFF4 stabilizeS ELL2 and prevent ELL2 ubiquitination.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO00472.
MaxQBiO00472.
PaxDbiO00472.
PRIDEiO00472.

PTM databases

iPTMnetiO00472.
PhosphoSiteiO00472.

Expressioni

Gene expression databases

BgeeiO00472.
CleanExiHS_ELL2.
ExpressionAtlasiO00472. baseline and differential.
GenevisibleiO00472. HS.

Organism-specific databases

HPAiHPA035758.
HPA035759.

Interactioni

Subunit structurei

Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Component of the little elongation complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts with AFF4; the interaction is direct and leads to stabilize ELL2 and prevent ELL2 ubiquitination. Interacts with EAF1 and EAF2.5 Publications

Protein-protein interaction databases

BioGridi116595. 28 interactions.
IntActiO00472. 27 interactions.
STRINGi9606.ENSP00000237853.

Structurei

Secondary structure

1
640
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi206 – 21611Combined sources
Helixi221 – 23111Combined sources
Helixi235 – 24814Combined sources
Beta strandi249 – 2524Combined sources
Turni253 – 2564Combined sources
Beta strandi257 – 2604Combined sources
Helixi264 – 2674Combined sources
Helixi279 – 29012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5NNMR-A200-292[»]
ProteinModelPortaliO00472.
SMRiO00472. Positions 200-292, 528-635.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00472.

Family & Domainsi

Sequence similaritiesi

Belongs to the ELL/occludin family.Curated

Phylogenomic databases

eggNOGiKOG4796. Eukaryota.
ENOG410ZNGU. LUCA.
GeneTreeiENSGT00550000074378.
HOGENOMiHOG000112356.
HOVERGENiHBG005578.
InParanoidiO00472.
KOiK15183.
OMAiTIRKTHS.
OrthoDBiEOG7P02HN.
PhylomeDBiO00472.
TreeFamiTF326161.

Family and domain databases

InterProiIPR031176. ELL/occludin.
IPR031179. ELL2.
IPR019464. ELL_N.
IPR010844. Occludin_ELL.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR23288. PTHR23288. 1 hit.
PTHR23288:SF8. PTHR23288:SF8. 1 hit.
PfamiPF10390. ELL. 1 hit.
PF07303. Occludin_ELL. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00472-1) [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
MAAGGTGGLR EEQRYGLSCG RLGQDNITVL HVKLTETAIR ALETYQSHKN
60 70 80 90 100
LIPFRPSIQF QGLHGLVKIP KNDPLNEVHN FNFYLSNVGK DNPQGSFDCI
110 120 130 140 150
QQTFSSSGAS QLNCLGFIQD KITVCATNDS YQMTRERMTQ AEEESRNRST
160 170 180 190 200
KVIKPGGPYV GKRVQIRKAP QAVSDTVPER KRSTPMNPAN TIRKTHSSST
210 220 230 240 250
ISQRPYRDRV IHLLALKAYK KPELLARLQK DGVNQKDKNS LGAILQQVAN
260 270 280 290 300
LNSKDLSYTL KDYVFKELQR DWPGYSEIDR RSLESVLSRK LNPSQNAAGT
310 320 330 340 350
SRSESPVCSS RDAVSSPQKR LLDSEFIDPL MNKKARISHL TNRVPPTLNG
360 370 380 390 400
HLNPTSEKSA AGLPLPPAAA AIPTPPPLPS TYLPISHPPQ IVNSNSNSPS
410 420 430 440 450
TPEGRGTQDL PVDSFSQNDS IYEDQQDKYT SRTSLETLPP GSVLLKCPKP
460 470 480 490 500
MEENHSMSHK KSKKKSKKHK EKDQIKKHDI ETIEEKEEDL KREEEIAKLN
510 520 530 540 550
NSSPNSSGGV KEDCTASMEP SAIELPDYLI KYIAIVSYEQ RQNYKDDFNA
560 570 580 590 600
EYDEYRALHA RMETVARRFI KLDAQRKRLS PGSKEYQNVH EEVLQEYQKI
610 620 630 640
KQSSPNYHEE KYRCEYLHNK LAHIKRLIGE FDQQQAESWS
Length:640
Mass (Da):72,324
Last modified:July 28, 2009 - v2
Checksum:i96D6228AF868E6C9
GO
Isoform 2 (identifier: O00472-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     140-389: Missing.

Note: No experimental confirmation available.
Show »
Length:390
Mass (Da):44,696
Checksum:iC06A6FE25C02C6F5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti298 – 2981A → T.2 Publications
Corresponds to variant rs3815768 [ dbSNP | Ensembl ].
VAR_058406

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei140 – 389250Missing in isoform 2. 1 PublicationVSP_055476Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88629 Genomic DNA. Translation: AAC51232.1.
AK297956 mRNA. Translation: BAG60269.1.
AC008592 Genomic DNA. No translation available.
BC028412 mRNA. Translation: AAH28412.1.
CCDSiCCDS4080.1. [O00472-1]
RefSeqiNP_036213.2. NM_012081.5. [O00472-1]
UniGeneiHs.192221.
Hs.708710.

Genome annotation databases

EnsembliENST00000237853; ENSP00000237853; ENSG00000118985. [O00472-1]
GeneIDi22936.
KEGGihsa:22936.
UCSCiuc003klr.4. human. [O00472-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88629 Genomic DNA. Translation: AAC51232.1.
AK297956 mRNA. Translation: BAG60269.1.
AC008592 Genomic DNA. No translation available.
BC028412 mRNA. Translation: AAH28412.1.
CCDSiCCDS4080.1. [O00472-1]
RefSeqiNP_036213.2. NM_012081.5. [O00472-1]
UniGeneiHs.192221.
Hs.708710.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5NNMR-A200-292[»]
ProteinModelPortaliO00472.
SMRiO00472. Positions 200-292, 528-635.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116595. 28 interactions.
IntActiO00472. 27 interactions.
STRINGi9606.ENSP00000237853.

PTM databases

iPTMnetiO00472.
PhosphoSiteiO00472.

Polymorphism and mutation databases

BioMutaiELL2.

Proteomic databases

EPDiO00472.
MaxQBiO00472.
PaxDbiO00472.
PRIDEiO00472.

Protocols and materials databases

DNASUi22936.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000237853; ENSP00000237853; ENSG00000118985. [O00472-1]
GeneIDi22936.
KEGGihsa:22936.
UCSCiuc003klr.4. human. [O00472-1]

Organism-specific databases

CTDi22936.
GeneCardsiELL2.
H-InvDBHIX0005049.
HGNCiHGNC:17064. ELL2.
HPAiHPA035758.
HPA035759.
MIMi601874. gene.
neXtProtiNX_O00472.
PharmGKBiPA134935340.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4796. Eukaryota.
ENOG410ZNGU. LUCA.
GeneTreeiENSGT00550000074378.
HOGENOMiHOG000112356.
HOVERGENiHBG005578.
InParanoidiO00472.
KOiK15183.
OMAiTIRKTHS.
OrthoDBiEOG7P02HN.
PhylomeDBiO00472.
TreeFamiTF326161.

Enzyme and pathway databases

ReactomeiR-HSA-6807505. RNA polymerase II transcribes snRNA genes.

Miscellaneous databases

ChiTaRSiELL2. human.
EvolutionaryTraceiO00472.
GenomeRNAii22936.
PROiO00472.
SOURCEiSearch...

Gene expression databases

BgeeiO00472.
CleanExiHS_ELL2.
ExpressionAtlasiO00472. baseline and differential.
GenevisibleiO00472. HS.

Family and domain databases

InterProiIPR031176. ELL/occludin.
IPR031179. ELL2.
IPR019464. ELL_N.
IPR010844. Occludin_ELL.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR23288. PTHR23288. 1 hit.
PTHR23288:SF8. PTHR23288:SF8. 1 hit.
PfamiPF10390. ELL. 1 hit.
PF07303. Occludin_ELL. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-298.
  2. "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] (ISOFORM 2).
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 1), VARIANT THR-298.
    Tissue: Testis.
  5. "EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein."
    Simone F., Polak P.E., Kaberlein J.J., Luo R.T., Levitan D.A., Thirman M.J.
    Blood 98:201-209(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EAF1.
  6. "ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with alternative ELL binding properties."
    Simone F., Luo R.T., Polak P.E., Kaberlein J.J., Thirman M.J.
    Blood 101:2355-2362(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EAF2.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription."
    He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J., Alber T., Zhou Q.
    Mol. Cell 38:428-438(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX.
  10. "AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia."
    Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L., Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.
    Mol. Cell 37:429-437(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX, IDENTIFICATION IN THE LEC COMPLEX.
  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-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The ubiquitin ligase Siah1 controls ELL2 stability and formation of super elongation complexes to modulate gene transcription."
    Liu M., Hsu J., Chan C., Li Z., Zhou Q.
    Mol. Cell 46:325-334(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  15. "The super elongation complex (SEC) family in transcriptional control."
    Luo Z., Lin C., Shilatifard A.
    Nat. Rev. Mol. Cell Biol. 13:543-547(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON THE SUPER ELONGATION COMPLEX.
  16. "HIV-1 Tat recruits transcription elongation factors dispersed along a flexible AFF4 scaffold."
    Chou S., Upton H., Bao K., Schulze-Gahmen U., Samelson A.J., He N., Nowak A., Lu H., Krogan N.J., Zhou Q., Alber T.
    Proc. Natl. Acad. Sci. U.S.A. 110:E123-E131(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Solution structure of the ELL_N2 domain of target of RNA polymerase II elongation factor ELL2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 197-292.

Entry informationi

Entry nameiELL2_HUMAN
AccessioniPrimary (citable) accession number: O00472
Secondary accession number(s): B4DNK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 28, 2009
Last modified: June 8, 2016
This is version 130 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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.