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Protein

Sulfotransferase 4A1

Gene

SULT4A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Atypical sulfotransferase family member with very low affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in the metabolism of drugs and neurotransmitters in the CNS.1 Publication

GO - Molecular functioni

  • aryl sulfotransferase activity Source: Reactome
  • sulfotransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

BRENDAi2.8.2.1. 2681.
ReactomeiR-HSA-156584. Cytosolic sulfonation of small molecules.
SIGNORiQ9BR01.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfotransferase 4A1 (EC:2.8.2.-)
Short name:
ST4A1
Alternative name(s):
Brain sulfotransferase-like protein
Short name:
hBR-STL
Short name:
hBR-STL-1
Nervous system sulfotransferase
Short name:
NST
Gene namesi
Name:SULT4A1
Synonyms:SULTX3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:14903. SULT4A1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA412.

Chemistry

ChEMBLiCHEMBL1743298.

Polymorphism and mutation databases

BioMutaiSULT4A1.
DMDMi22096149.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Sulfotransferase 4A1PRO_0000085167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphothreonineBy similarity
Modified residuei11 – 111PhosphothreonineBy similarity
Modified residuei205 – 2051PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9BR01.
PeptideAtlasiQ9BR01.
PRIDEiQ9BR01.

PTM databases

iPTMnetiQ9BR01.
PhosphoSiteiQ9BR01.

Expressioni

Tissue specificityi

Highly expressed in the cerebral cortex and frontal lobe, slightly less in the cerebellum, occipital and temporal lobes, relatively low in the medulla and putamen, and lowest in the spinal cord. No expression detected in the pancreas (PubMed:10698717). Highly expressed in fetal brain and occipital lobe, slightly less in the whole brain, frontal lobe, hippocampus, and lung, very low expression in cerebellum, medulla oblongata, temporal lobe, testis, kidney and appendix (PubMed:12039030).2 Publications

Gene expression databases

BgeeiQ9BR01.
CleanExiHS_SULT4A1.
ExpressionAtlasiQ9BR01. baseline and differential.
GenevisibleiQ9BR01. HS.

Organism-specific databases

HPAiHPA003129.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PIN1Q135264EBI-6690555,EBI-714158
POT1Q9NUX52EBI-6690555,EBI-752420

Protein-protein interaction databases

BioGridi117358. 10 interactions.
IntActiQ9BR01. 3 interactions.
STRINGi9606.ENSP00000332565.

Structurei

Secondary structure

1
284
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 173Combined sources
Beta strandi18 – 225Combined sources
Beta strandi25 – 273Combined sources
Helixi29 – 313Combined sources
Helixi35 – 395Combined sources
Beta strandi48 – 525Combined sources
Helixi59 – 6810Combined sources
Beta strandi91 – 944Combined sources
Helixi96 – 1016Combined sources
Beta strandi107 – 1104Combined sources
Helixi114 – 1163Combined sources
Helixi119 – 1224Combined sources
Beta strandi126 – 1327Combined sources
Helixi135 – 14410Combined sources
Helixi158 – 1669Combined sources
Helixi175 – 1839Combined sources
Turni184 – 1874Combined sources
Beta strandi191 – 1955Combined sources
Helixi198 – 2014Combined sources
Helixi203 – 21311Combined sources
Helixi220 – 23516Combined sources
Beta strandi242 – 2465Combined sources
Helixi252 – 2554Combined sources
Helixi259 – 27315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZD1X-ray2.24A/B1-284[»]
ProteinModelPortaliQ9BR01.
SMRiQ9BR01. Positions 13-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BR01.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

eggNOGiKOG1584. Eukaryota.
ENOG4111H56. LUCA.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG105932.
InParanoidiQ9BR01.
KOiK11823.
OMAiSDIWIVT.
OrthoDBiEOG7V49ZK.
PhylomeDBiQ9BR01.
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 1 (identifier: Q9BR01-1) [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
MAESEAETPS TPGEFESKYF EFHGVRLPPF CRGKMEEIAN FPVRPSDVWI
60 70 80 90 100
VTYPKSGTSL LQEVVYLVSQ GADPDEIGLM NIDEQLPVLE YPQPGLDIIK
110 120 130 140 150
ELTSPRLIKS HLPYRFLPSD LHNGDSKVIY MARNPKDLVV SYYQFHRSLR
160 170 180 190 200
TMSYRGTFQE FCRRFMNDKL GYGSWFEHVQ EFWEHRMDSN VLFLKYEDMH
210 220 230 240 250
RDLVTMVEQL ARFLGVSCDK AQLEALTEHC HQLVDQCCNA EALPVGRGRV
260 270 280
GLWKDIFTVS MNEKFDLVYK QKMGKCDLTF DFYL
Length:284
Mass (Da):33,085
Last modified:August 2, 2002 - v2
Checksum:iA6EA6844B66C400B
GO
Isoform 2 (identifier: Q9BR01-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     248-284: GRVGLWKDIFTVSMNEKFDLVYKQKMGKCDLTFDFYL → AHCVFARKIFLSW

Show »
Length:260
Mass (Da):30,226
Checksum:i7F71F2C8A264D34F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 562KS → P in AAH30665 (PubMed:15489334).Curated
Sequence conflicti239 – 2391N → S in AAH22459 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei248 – 28437GRVGL…FDFYL → AHCVFARKIFLSW in isoform 2. 2 PublicationsVSP_006304Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188698 mRNA. Translation: AAF61197.1.
AF115311 mRNA. Translation: AAF21970.1.
AF176342 mRNA. Translation: AAK64595.1.
AF251263 mRNA. Translation: AAF98152.1.
AL590119 mRNA. Translation: CAC34872.1.
CR456588 mRNA. Translation: CAG30474.1.
AK313048 mRNA. Translation: BAG35880.1.
Z97055 Genomic DNA. Translation: CAB09788.1.
CH471138 Genomic DNA. Translation: EAW73320.1.
BC022459 mRNA. Translation: AAH22459.1.
BC028171 mRNA. Translation: AAH28171.1.
BC030665 mRNA. Translation: AAH30665.1.
CCDSiCCDS14051.1. [Q9BR01-1]
RefSeqiNP_055166.1. NM_014351.3. [Q9BR01-1]
UniGeneiHs.189810.

Genome annotation databases

EnsembliENST00000330884; ENSP00000332565; ENSG00000130540. [Q9BR01-1]
ENST00000422525; ENSP00000388285; ENSG00000130540. [Q9BR01-2]
GeneIDi25830.
KEGGihsa:25830.
UCSCiuc003bee.2. human. [Q9BR01-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188698 mRNA. Translation: AAF61197.1.
AF115311 mRNA. Translation: AAF21970.1.
AF176342 mRNA. Translation: AAK64595.1.
AF251263 mRNA. Translation: AAF98152.1.
AL590119 mRNA. Translation: CAC34872.1.
CR456588 mRNA. Translation: CAG30474.1.
AK313048 mRNA. Translation: BAG35880.1.
Z97055 Genomic DNA. Translation: CAB09788.1.
CH471138 Genomic DNA. Translation: EAW73320.1.
BC022459 mRNA. Translation: AAH22459.1.
BC028171 mRNA. Translation: AAH28171.1.
BC030665 mRNA. Translation: AAH30665.1.
CCDSiCCDS14051.1. [Q9BR01-1]
RefSeqiNP_055166.1. NM_014351.3. [Q9BR01-1]
UniGeneiHs.189810.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZD1X-ray2.24A/B1-284[»]
ProteinModelPortaliQ9BR01.
SMRiQ9BR01. Positions 13-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117358. 10 interactions.
IntActiQ9BR01. 3 interactions.
STRINGi9606.ENSP00000332565.

Chemistry

ChEMBLiCHEMBL1743298.

PTM databases

iPTMnetiQ9BR01.
PhosphoSiteiQ9BR01.

Polymorphism and mutation databases

BioMutaiSULT4A1.
DMDMi22096149.

Proteomic databases

PaxDbiQ9BR01.
PeptideAtlasiQ9BR01.
PRIDEiQ9BR01.

Protocols and materials databases

DNASUi25830.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330884; ENSP00000332565; ENSG00000130540. [Q9BR01-1]
ENST00000422525; ENSP00000388285; ENSG00000130540. [Q9BR01-2]
GeneIDi25830.
KEGGihsa:25830.
UCSCiuc003bee.2. human. [Q9BR01-1]

Organism-specific databases

CTDi25830.
GeneCardsiSULT4A1.
HGNCiHGNC:14903. SULT4A1.
HPAiHPA003129.
MIMi608359. gene.
neXtProtiNX_Q9BR01.
PharmGKBiPA412.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1584. Eukaryota.
ENOG4111H56. LUCA.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG105932.
InParanoidiQ9BR01.
KOiK11823.
OMAiSDIWIVT.
OrthoDBiEOG7V49ZK.
PhylomeDBiQ9BR01.
TreeFamiTF321745.

Enzyme and pathway databases

BRENDAi2.8.2.1. 2681.
ReactomeiR-HSA-156584. Cytosolic sulfonation of small molecules.
SIGNORiQ9BR01.

Miscellaneous databases

EvolutionaryTraceiQ9BR01.
GeneWikiiSULT4A1.
GenomeRNAii25830.
PROiQ9BR01.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BR01.
CleanExiHS_SULT4A1.
ExpressionAtlasiQ9BR01. baseline and differential.
GenevisibleiQ9BR01. HS.

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. "Molecular cloning and expression of novel sulphotransferase-like cDNAs from human and rat brain."
    Falany C.N., Xie X., Wang J., Ferrer J., Falany J.L.
    Biochem. J. 346:857-864(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Brain.
  2. "Highly conserved mouse and human brain sulfotransferases: molecular cloning, expression, and functional characterization."
    Sakakibara Y., Suiko M., Pai T.G., Nakayama T., Takami Y., Katafuchi J., Liu M.-C.
    Gene 285:39-47(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Brain.
  3. "Molecular identification of a human nervous system cytoplasmic sulfotransferase, NST."
    Martin S.C., Farb D.H.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    Tissue: Brain.
  4. "Molecular and physical characterization of human SULT4A1, representing a novel cytosolic sulfotransferase 1 family."
    Walther S.E., Raftogianis R.B.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    Tissue: Brain.
  5. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
    Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
    Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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 1).
    Tissue: Brain.
  8. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [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] (ISOFORMS 1 AND 2).
    Tissue: Fetal brain, Hippocampus and Hypothalamus.
  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 THR-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS), FUNCTION, CHARACTERIZATION.

Entry informationi

Entry nameiST4A1_HUMAN
AccessioniPrimary (citable) accession number: Q9BR01
Secondary accession number(s): B2R7N3, O43728
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: July 6, 2016
This is version 133 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 22
    Human chromosome 22: 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.