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P0DMM9

- ST1A3_HUMAN

UniProt

P0DMM9 - ST1A3_HUMAN

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Protein

Sulfotransferase 1A3

Gene
SULT1A3, STM
Organism
Homo sapiens (Human)
Status
Reviewed - 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 phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs.

Catalytic activityi

3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei86 – 861Substrate
Active sitei108 – 1081Proton acceptor By similarity
Binding sitei130 – 1301PAPS
Binding sitei138 – 1381PAPS
Binding sitei146 – 1461Substrate
Binding sitei193 – 1931PAPS

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 536PAPS
Nucleotide bindingi227 – 2326PAPS
Nucleotide bindingi257 – 2593PAPS

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Catecholamine metabolism, Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS05608-MONOMER.
BRENDAi2.8.2.1. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfotransferase 1A3 (EC:2.8.2.1)
Short name:
ST1A3
Alternative name(s):
Aryl sulfotransferase 1A3/1A4
Catecholamine-sulfating phenol sulfotransferase
HAST3
M-PST
Monoamine-sulfating phenol sulfotransferase
Placental estrogen sulfotransferase
Sulfotransferase 1A3/1A4
Sulfotransferase, monoamine-preferring
Thermolabile phenol sulfotransferase
Short name:
TL-PST
Gene namesi
Name:SULT1A3
Synonyms:STM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:11455. SULT1A3.

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA344.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Sulfotransferase 1A3PRO_0000085159Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Expressioni

Tissue specificityi

Liver, colon, kidney, lung, brain, spleen, small intestine, placenta and leukocyte.

Gene expression databases

CleanExiHS_SULT1A3.
HS_SULT1A4.

Organism-specific databases

HPAiHPA049500.
HPA051051.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9606.ENSP00000339221.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 154
Beta strandi18 – 214
Helixi22 – 276
Helixi30 – 334
Beta strandi41 – 455
Helixi51 – 6212
Turni63 – 653
Helixi67 – 704
Helixi75 – 784
Turni95 – 984
Beta strandi104 – 1074
Helixi111 – 1133
Helixi116 – 1205
Beta strandi124 – 1296
Helixi132 – 14514
Helixi155 – 1639
Helixi172 – 18211
Turni183 – 1853
Beta strandi188 – 1925
Helixi193 – 1986
Helixi200 – 21112
Helixi217 – 22610
Helixi229 – 2346
Turni236 – 2383
Turni245 – 2473
Turni250 – 2523
Helixi264 – 2663
Helixi270 – 28314

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CJMX-ray2.40A1-295[»]
2A3RX-ray2.60A/B1-295[»]
DisProtiDP00011.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 1083Substrate binding

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000037209.
HOVERGENiHBG001195.
OMAiPPRLIKS.
TreeFamiTF321745.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P0DMM9-1) [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

MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLINTYPKSG    50
TTWVSQILDM IYQGGDLEKC NRAPIYVRVP FLEVNDPGEP SGLETLKDTP 100
PPRLIKSHLP LALLPQTLLD QKVKVVYVAR NPKDVAVSYY HFHRMEKAHP 150
EPGTWDSFLE KFMAGEVSYG SWYQHVQEWW ELSRTHPVLY LFYEDMKENP 200
KREIQKILEF VGRSLPEETM DFMVQHTSFK EMKKNPMTNY TTVPQELMDH 250
SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL 295
Length:295
Mass (Da):34,196
Last modified:September 3, 2014 - v1
Checksum:iECDDEC03DBE30D46
GO
Isoform 2 (identifier: P0DMM9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     167-295: VSYGSWYQHV...GCSLSFRSEL → GGLDWRKEGVKPRGGGYNVQQPCVGAPCPLL

Note: No experimental confirmation available.

Show »
Length:197
Mass (Da):22,069
Checksum:i44C5F13EDA71BC1D
GO
Isoform 3 (identifier: P0DMM9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     198-198: E → EEPSAAQ

Show »
Length:301
Mass (Da):34,780
Checksum:i7018229AD3F67542
GO

Sequence cautioni

Isoform 2 : The sequence BAC85507.1 differs from that shown. Reason: Frameshift at position 101.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011P → H Decreases levels of sulfotransferase activity.
VAR_071108
Natural varianti101 – 1011P → L Decreases levels of sulfotransferase activity.
VAR_071109
Natural varianti144 – 1441R → C No effect on sulfotransferase activity.
VAR_071110
Natural varianti234 – 2341K → N Decreases levels of sulfotransferase activity; accelerates proteasome-dependent degradation.
VAR_071111

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei167 – 295129VSYGS…FRSEL → GGLDWRKEGVKPRGGGYNVQ QPCVGAPCPLL in isoform 2. VSP_012326Add
BLAST
Alternative sequencei198 – 1981E → EEPSAAQ in isoform 3. VSP_047771

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 2256MDFMVQ → VDLMVE in AAC99987. 1 Publication
Sequence conflicti235 – 2351N → T in AAC99987. 1 Publication
Sequence conflicti244 – 2452PQ → RR in AAC99987. 1 Publication
Sequence conflicti290 – 2901S → T in AAC99987. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L19956 mRNA. Translation: AAA02943.1.
L25275 mRNA. Translation: AAA36523.1.
L19956 mRNA. Translation: AAA17723.1.
U20499 Genomic DNA. Translation: AAA64490.1.
X84653 mRNA. Translation: CAA59146.1.
L34160 Genomic DNA. No translation available.
U37686 Genomic DNA. Translation: AAA86536.1.
U34199 mRNA. Translation: AAC99987.1.
AK122733 mRNA. Translation: BAC85507.1. Frameshift.
AK298073 mRNA. Translation: BAG60362.1.
AC106782 Genomic DNA. No translation available.
AC133555 Genomic DNA. No translation available.
AB111094 mRNA. Translation: BAE94928.1.
BC014471 mRNA. Translation: AAH14471.1.
BC078144 mRNA. Translation: AAH78144.1.
U08099 Genomic DNA. Translation: AAA82126.1.
PIRiA55451.
UniGeneiHs.460558.

Polymorphism databases

DMDMi1711609.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L19956 mRNA. Translation: AAA02943.1 .
L25275 mRNA. Translation: AAA36523.1 .
L19956 mRNA. Translation: AAA17723.1 .
U20499 Genomic DNA. Translation: AAA64490.1 .
X84653 mRNA. Translation: CAA59146.1 .
L34160 Genomic DNA. No translation available.
U37686 Genomic DNA. Translation: AAA86536.1 .
U34199 mRNA. Translation: AAC99987.1 .
AK122733 mRNA. Translation: BAC85507.1 . Frameshift.
AK298073 mRNA. Translation: BAG60362.1 .
AC106782 Genomic DNA. No translation available.
AC133555 Genomic DNA. No translation available.
AB111094 mRNA. Translation: BAE94928.1 .
BC014471 mRNA. Translation: AAH14471.1 .
BC078144 mRNA. Translation: AAH78144.1 .
U08099 Genomic DNA. Translation: AAA82126.1 .
PIRi A55451.
UniGenei Hs.460558.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CJM X-ray 2.40 A 1-295 [» ]
2A3R X-ray 2.60 A/B 1-295 [» ]
DisProti DP00011.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000339221.

Chemistry

ChEMBLi CHEMBL1743293.

Polymorphism databases

DMDMi 1711609.

Protocols and materials databases

DNASUi 445329.
6818.
Structural Biology Knowledgebase Search...

Organism-specific databases

GeneCardsi GC16P030213.
HGNCi HGNC:11455. SULT1A3.
HPAi HPA049500.
HPA051051.
MIMi 600641. gene.
PharmGKBi PA344.
GenAtlasi Search...

Phylogenomic databases

HOGENOMi HOG000037209.
HOVERGENi HBG001195.
OMAi PPRLIKS.
TreeFami TF321745.

Enzyme and pathway databases

BioCyci MetaCyc:HS05608-MONOMER.
BRENDAi 2.8.2.1. 2681.

Miscellaneous databases

SOURCEi Search...

Gene expression databases

CleanExi HS_SULT1A3.
HS_SULT1A4.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Cloning and expression of cDNA encoding human placental estrogen sulfotransferase."
    Bernier F., Lopez-Solache I., Labrie F., Luu-The V.
    Mol. Cell. Endocrinol. 99:R11-R15(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  3. "Genomic organization and DNA sequence of the human catecholamine-sulfating phenol sulfotransferase gene (STM)."
    Dooley T.P., Probst P., Munroe P.B., Mole S.E., Liu Z., Doggett N.A.
    Biochem. Biophys. Res. Commun. 205:1325-1332(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  4. "Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization."
    Wood T.C., Aksoy I.A., Aksoy S., Weinshilboum R.M.
    Biochem. Biophys. Res. Commun. 198:1119-1127(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 84-101.
    Tissue: Liver.
  5. "Human thermolabile phenol sulfotransferase gene (STM): molecular cloning and structural characterization."
    Aksoy I.A., Weinshilboum R.M.
    Biochem. Biophys. Res. Commun. 208:786-795(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Tissue: Platelet.
  6. "Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form."
    Jones A.L., Hagen M., Coughtrie M.W.H., Roberts R.C., Glatt H.
    Biochem. Biophys. Res. Commun. 208:855-862(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Blood.
  7. "Structure of human estrogen and aryl sulfotransferase gene. Two mRNA species issued from a single gene."
    Bernier F., Leblanc G., Labrie F., Luu-The V.
    J. Biol. Chem. 269:28200-28205(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Tissue: Leukocyte.
  8. Gaedigk A., Grant D.M.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  9. "Isolation of seven variants of catecholamine sulfotransferase cDNAs from human kidney."
    Terazawa R., Shimada M., Nagata K., Yamazoe Y.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Kidney.
  10. "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).
    Tissue: Lung.
  11. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "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).
    Tissue: Lung and Pancreas.
  13. "Thermolabile phenol sulfotransferase gene (STM): localization to human chromosome 16p11.2."
    Aksoy I.A., Callen D.F., Apostolou S., Her C., Weinshilboum R.M.
    Genomics 23:275-277(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-198.
    Tissue: Lymphocyte.
  14. "Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies."
    Veronese M.E., Burgess W., Zhu X., McManus M.E.
    Biochem. J. 302:497-502(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    Tissue: Brain.
  17. "Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3'-phosphoadenosine 5'-phosphate."
    Lu J.H., Li H.T., Liu M.C., Zhang J.P., Li M., An X.M., Chang W.R.
    Biochem. Biophys. Res. Commun. 335:417-423(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE AND L-DOPAMINE.
  18. "Human catecholamine sulfotransferase (SULT1A3) pharmacogenetics: functional genetic polymorphism."
    Thomae B.A., Rifki O.F., Theobald M.A., Eckloff B.W., Wieben E.D., Weinshilboum R.M.
    J. Neurochem. 87:809-819(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASN-234, CHARACTERIZATION OF VARIANT ASN-234.
  19. Cited for: VARIANTS LEU-101; HIS-101 AND CYS-144, CHARACTERIZATION OF VARIANTS LEU-101; HIS-101 AND CYS-144.

Entry informationi

Entry nameiST1A3_HUMAN
AccessioniPrimary (citable) accession number: P0DMM9
Secondary accession number(s): B4DNV0
, O95603, P50224, Q1ET66, Q6ZWJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 3, 2014
Last sequence update: September 3, 2014
Last modified: September 3, 2014
This is version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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

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