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Protein

Sulfotransferase 1C2

Gene

SULT1C2

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

Functioni

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. May be involved in the activation of carcinogenic hyroxylamines. Shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei109 – 1091Proton acceptorBy similarity
Binding sitei131 – 1311PAPS
Binding sitei139 – 1391PAPS
Binding sitei194 – 1941PAPS

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 546PAPS
Nucleotide bindingi228 – 2336PAPS
Nucleotide bindingi256 – 2605PAPS

GO - Molecular functioni

  1. sulfotransferase activity Source: BHF-UCL

GO - Biological processi

  1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
  2. amine metabolic process Source: ProtInc
  3. small molecule metabolic process Source: Reactome
  4. sulfation Source: BHF-UCL
  5. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.8.2.1. 2681.
ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfotransferase 1C2 (EC:2.8.2.-)
Short name:
ST1C2
Alternative name(s):
Sulfotransferase 1C1
Short name:
SULT1C#1
humSULTC2
Gene namesi
Name:SULT1C2
Synonyms:SULT1C1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:11456. SULT1C2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164742557.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Sulfotransferase 1C2PRO_0000085132Add
BLAST

Proteomic databases

MaxQBiO00338.
PaxDbiO00338.
PRIDEiO00338.

Expressioni

Tissue specificityi

Found in adult stomach, kidney and thyroid gland, and in fetal kidney and liver.

Gene expression databases

BgeeiO00338.
CleanExiHS_SULT1C2.
ExpressionAtlasiO00338. baseline and differential.
GenevestigatoriO00338.

Organism-specific databases

HPAiHPA007190.

Interactioni

Protein-protein interaction databases

BioGridi112688. 10 interactions.
IntActiO00338. 2 interactions.
STRINGi9606.ENSP00000319622.

Structurei

Secondary structure

1
296
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163Combined sources
Beta strandi19 – 213Combined sources
Helixi23 – 275Combined sources
Helixi29 – 335Combined sources
Beta strandi42 – 465Combined sources
Helixi52 – 6413Combined sources
Helixi93 – 997Combined sources
Beta strandi105 – 1084Combined sources
Turni112 – 1143Combined sources
Helixi118 – 1214Combined sources
Beta strandi125 – 1306Combined sources
Helixi133 – 14614Combined sources
Helixi156 – 1649Combined sources
Helixi173 – 18311Combined sources
Turni184 – 1863Combined sources
Beta strandi187 – 1937Combined sources
Helixi194 – 1996Combined sources
Helixi201 – 21111Combined sources
Helixi218 – 22710Combined sources
Helixi230 – 2356Combined sources
Helixi265 – 2684Combined sources
Helixi271 – 28515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BFXX-ray1.80A/B3-296[»]
ProteinModelPortaliO00338.
SMRiO00338. Positions 12-296.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00338.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 1093Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

eggNOGiNOG260792.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiO00338.
KOiK01025.
PhylomeDBiO00338.
TreeFamiTF321745.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform Short (identifier: O00338-1) [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
MALTSDLGKQ IKLKEVEGTL LQPATVDNWS QIQSFEAKPD DLLICTYPKA
60 70 80 90 100
GTTWIQEIVD MIEQNGDVEK CQRAIIQHRH PFIEWARPPQ PSGVEKAKAM
110 120 130 140 150
PSPRILKTHL STQLLPPSFW ENNCKFLYVA RNAKDCMVSY YHFQRMNHML
160 170 180 190 200
PDPGTWEEYF ETFINGKVVW GSWFDHVKGW WEMKDRHQIL FLFYEDIKRD
210 220 230 240 250
PKHEIRKVMQ FMGKKVDETV LDKIVQETSF EKMKENPMTN RSTVSKSILD
260 270 280 290
QSISSFMRKG TVGDWKNHFT VAQNERFDEI YRRKMEGTSI NFCMEL
Length:296
Mass (Da):34,880
Last modified:July 1, 1997 - v1
Checksum:i3DC01C8A8ED61EFD
GO
Isoform Long (identifier: O00338-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-113: GVEKAKAMPSPRILKTHLSTQ → ETGFHHVAQAGLKLLSSSNPPASTSQSAKITD

Show »
Length:307
Mass (Da):35,868
Checksum:iDB83191FA88BFAD1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281Y → H.
Corresponds to variant rs17036091 [ dbSNP | Ensembl ].
VAR_021986
Natural varianti255 – 2551S → A.
Corresponds to variant rs17036104 [ dbSNP | Ensembl ].
VAR_021987
Natural varianti282 – 2821R → T.
Corresponds to variant rs45515691 [ dbSNP | Ensembl ].
VAR_061888

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei93 – 11321GVEKA…HLSTQ → ETGFHHVAQAGLKLLSSSNP PASTSQSAKITD in isoform Long. CuratedVSP_006303Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66036 mRNA. Translation: AAC51285.1.
AB008164 mRNA. Translation: BAA28346.1.
AF026303 mRNA. Translation: AAC00409.1.
AF186251 mRNA. Translation: AAF72799.1.
AF186252 mRNA. Translation: AAF72800.1.
AF186253 mRNA. Translation: AAF72801.1.
AF186254 mRNA. Translation: AAF72802.1.
AF186255 mRNA. Translation: AAF72803.1.
AF186256 mRNA. Translation: AAF72804.1.
AF186262
, AF186258, AF186260, AF186261 Genomic DNA. Translation: AAF72805.1.
AF186262
, AF186258, AF186259, AF186260, AF186261 Genomic DNA. Translation: AAF72806.1.
BT006951 mRNA. Translation: AAP35597.1.
AK313193 mRNA. Translation: BAG36010.1.
AC019100 Genomic DNA. Translation: AAY14790.1.
CH471182 Genomic DNA. Translation: EAW53889.1.
CH471182 Genomic DNA. Translation: EAW53890.1.
BC005353 mRNA. Translation: AAH05353.1.
CCDSiCCDS2075.1. [O00338-1]
CCDS2076.1. [O00338-2]
RefSeqiNP_001047.1. NM_001056.3. [O00338-1]
NP_789795.1. NM_176825.2. [O00338-2]
UniGeneiHs.436123.

Genome annotation databases

EnsembliENST00000251481; ENSP00000251481; ENSG00000198203. [O00338-1]
ENST00000326853; ENSP00000319622; ENSG00000198203. [O00338-2]
GeneIDi6819.
KEGGihsa:6819.
UCSCiuc002tdx.3. human. [O00338-2]
uc002tdy.3. human. [O00338-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66036 mRNA. Translation: AAC51285.1.
AB008164 mRNA. Translation: BAA28346.1.
AF026303 mRNA. Translation: AAC00409.1.
AF186251 mRNA. Translation: AAF72799.1.
AF186252 mRNA. Translation: AAF72800.1.
AF186253 mRNA. Translation: AAF72801.1.
AF186254 mRNA. Translation: AAF72802.1.
AF186255 mRNA. Translation: AAF72803.1.
AF186256 mRNA. Translation: AAF72804.1.
AF186262
, AF186258, AF186260, AF186261 Genomic DNA. Translation: AAF72805.1.
AF186262
, AF186258, AF186259, AF186260, AF186261 Genomic DNA. Translation: AAF72806.1.
BT006951 mRNA. Translation: AAP35597.1.
AK313193 mRNA. Translation: BAG36010.1.
AC019100 Genomic DNA. Translation: AAY14790.1.
CH471182 Genomic DNA. Translation: EAW53889.1.
CH471182 Genomic DNA. Translation: EAW53890.1.
BC005353 mRNA. Translation: AAH05353.1.
CCDSiCCDS2075.1. [O00338-1]
CCDS2076.1. [O00338-2]
RefSeqiNP_001047.1. NM_001056.3. [O00338-1]
NP_789795.1. NM_176825.2. [O00338-2]
UniGeneiHs.436123.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BFXX-ray1.80A/B3-296[»]
ProteinModelPortaliO00338.
SMRiO00338. Positions 12-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112688. 10 interactions.
IntActiO00338. 2 interactions.
STRINGi9606.ENSP00000319622.

Chemistry

ChEMBLiCHEMBL1743295.

Proteomic databases

MaxQBiO00338.
PaxDbiO00338.
PRIDEiO00338.

Protocols and materials databases

DNASUi6819.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251481; ENSP00000251481; ENSG00000198203. [O00338-1]
ENST00000326853; ENSP00000319622; ENSG00000198203. [O00338-2]
GeneIDi6819.
KEGGihsa:6819.
UCSCiuc002tdx.3. human. [O00338-2]
uc002tdy.3. human. [O00338-1]

Organism-specific databases

CTDi6819.
GeneCardsiGC02P108905.
HGNCiHGNC:11456. SULT1C2.
HPAiHPA007190.
MIMi602385. gene.
neXtProtiNX_O00338.
PharmGKBiPA164742557.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG260792.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiO00338.
KOiK01025.
PhylomeDBiO00338.
TreeFamiTF321745.

Enzyme and pathway databases

BRENDAi2.8.2.1. 2681.
ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.

Miscellaneous databases

EvolutionaryTraceiO00338.
GeneWikiiSULT1C2.
GenomeRNAii6819.
NextBioi26627.
PROiO00338.
SOURCEiSearch...

Gene expression databases

BgeeiO00338.
CleanExiHS_SULT1C2.
ExpressionAtlasiO00338. baseline and differential.
GenevestigatoriO00338.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human sulfotransferase SULT1C1: cDNA cloning, tissue-specific expression, and chromosomal localization."
    Her C., Kaur G.P., Athwal R.S., Weinshilboum R.M.
    Genomics 41:467-470(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal liver and Fetal spleen.
  2. "Molecular characterization of ST1C1-related human sulfotransferase."
    Yoshinari K., Nagata K., Shimada M., Yamazoe Y.
    Carcinogenesis 19:951-953(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal liver.
  3. "Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene."
    Sakakibara Y., Yanagisawa K., Katafuchi J., Ringer D.P., Takami Y., Nakayama T., Suiko M., Liu M.-C.
    J. Biol. Chem. 273:33929-33935(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Fetal lung.
  4. "Molecular cloning, expression, localisation and functional characterisation of a rabbit SULT1C2 sulfotransferase."
    Hehonah N., Zhu X., Brix L., Bolton-Grob R., Barnett A., Windmill K., McManus M.
    Int. J. Biochem. Cell Biol. 31:869-882(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Stomach.
  5. "Human sulfotransferases SULT1C1 and SULT1C2: cDNA characterization, gene cloning, and chromosomal localization."
    Freimuth R.R., Raftogianis R.B., Wood T.C., Moon E., Kim U.-J., Xu J., Siciliano M.J., Weinshilboum R.M.
    Genomics 65:157-165(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
  7. "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 SHORT).
    Tissue: Kidney.
  8. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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: Kidney.
  11. "Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3'- 5'-diphosphate (PAP)."
    Dombrovski L., Dong A., Bochkarev A., Plotnikov A.N.
    Proteins 64:1091-1094(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-296 IN COMPLEX WITH ADENOSINE-3'- 5'-DIPHOSPHATE.

Entry informationi

Entry nameiST1C2_HUMAN
AccessioniPrimary (citable) accession number: O00338
Secondary accession number(s): B2R813, Q53SG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 1, 1997
Last modified: January 7, 2015
This is version 140 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 2
    Human chromosome 2: 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

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.