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Arylsulfatase J (ASJ) (EC 3.1.6.-)

 ARSJ_HUMAN              Reviewed;         599 AA.
Q5FYB0; A2RUG0; B7ZM45; Q1HA39; Q5FWE4; Q6UWT9;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 1.
08-MAY-2019, entry version 121.
RecName: Full=Arylsulfatase J;
Short=ASJ;
EC=3.1.6.-;
Flags: Precursor;
Name=ARSJ; ORFNames=UNQ372/PRO708;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16174644; DOI=10.1093/hmg/ddi351;
Sardiello M., Annunziata I., Roma G., Ballabio A.;
"Sulfatases and sulfatase modifying factors: an exclusive and
promiscuous relationship.";
Hum. Mol. Genet. 14:3203-3217(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16500042; DOI=10.1016/j.gene.2005.12.023;
Obaya A.J.;
"Molecular cloning and initial characterization of three novel human
sulfatases.";
Gene 372:110-117(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Chondrosarcoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- PTM: The conversion to 3-oxoalanine (also known as C-
formylglycine, FGly), of a serine or cysteine residue in
prokaryotes and of a cysteine residue in eukaryotes, is critical
for catalytic activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAQ89010.1; Type=Frameshift; Positions=425; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY875938; AAW66666.1; -; mRNA.
EMBL; AM049401; CAJ18095.1; -; mRNA.
EMBL; AY358647; AAQ89010.1; ALT_FRAME; mRNA.
EMBL; AC104779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC089445; AAH89445.1; -; mRNA.
EMBL; BC132879; AAI32880.1; -; mRNA.
EMBL; BC132881; AAI32882.1; -; mRNA.
EMBL; BC144265; AAI44266.1; -; mRNA.
CCDS; CCDS43264.1; -.
RefSeq; NP_078866.3; NM_024590.3.
RefSeq; XP_005263269.1; XM_005263212.4.
RefSeq; XP_016864081.1; XM_017008592.1.
SMR; Q5FYB0; -.
BioGrid; 122770; 4.
IntAct; Q5FYB0; 1.
MINT; Q5FYB0; -.
STRING; 9606.ENSP00000320219; -.
iPTMnet; Q5FYB0; -.
PhosphoSitePlus; Q5FYB0; -.
BioMuta; ARSJ; -.
DMDM; 74722580; -.
PaxDb; Q5FYB0; -.
PeptideAtlas; Q5FYB0; -.
PRIDE; Q5FYB0; -.
ProteomicsDB; 62820; -.
Ensembl; ENST00000315366; ENSP00000320219; ENSG00000180801.
GeneID; 79642; -.
KEGG; hsa:79642; -.
UCSC; uc003ibq.2; human.
CTD; 79642; -.
DisGeNET; 79642; -.
GeneCards; ARSJ; -.
HGNC; HGNC:26286; ARSJ.
HPA; HPA036481; -.
HPA; HPA036482; -.
MIM; 610010; gene.
neXtProt; NX_Q5FYB0; -.
OpenTargets; ENSG00000180801; -.
PharmGKB; PA143485310; -.
eggNOG; KOG3867; Eukaryota.
eggNOG; COG3119; LUCA.
GeneTree; ENSGT00940000159954; -.
HOGENOM; HOG000135354; -.
InParanoid; Q5FYB0; -.
KO; K12375; -.
OMA; DNGGQPM; -.
OrthoDB; 875384at2759; -.
PhylomeDB; Q5FYB0; -.
TreeFam; TF314186; -.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-1663150; The activation of arylsulfatases.
ChiTaRS; ARSJ; human.
GenomeRNAi; 79642; -.
PRO; PR:Q5FYB0; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000180801; Expressed in 124 organ(s), highest expression level in cartilage tissue.
ExpressionAtlas; Q5FYB0; baseline and differential.
Genevisible; Q5FYB0; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004065; F:arylsulfatase activity; TAS:HGNC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR024607; Sulfatase_CS.
InterPro; IPR000917; Sulfatase_N.
Pfam; PF00884; Sulfatase; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00523; SULFATASE_1; 1.
PROSITE; PS00149; SULFATASE_2; 1.
2: Evidence at transcript level;
Calcium; Complete proteome; Glycoprotein; Hydrolase; Metal-binding;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 49 {ECO:0000255}.
CHAIN 50 599 Arylsulfatase J.
/FTId=PRO_0000042217.
ACT_SITE 122 122 Nucleophile.
{ECO:0000250|UniProtKB:P15289}.
ACT_SITE 178 178 {ECO:0000250|UniProtKB:P15289}.
METAL 84 84 Calcium. {ECO:0000250}.
METAL 85 85 Calcium. {ECO:0000250}.
METAL 122 122 Calcium; via 3-oxoalanine. {ECO:0000250}.
METAL 327 327 Calcium. {ECO:0000250}.
METAL 328 328 Calcium. {ECO:0000250}.
BINDING 176 176 Substrate. {ECO:0000250}.
BINDING 269 269 Substrate. {ECO:0000250}.
BINDING 345 345 Substrate. {ECO:0000250}.
MOD_RES 122 122 3-oxoalanine (Cys).
{ECO:0000250|UniProtKB:P15289}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 497 497 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 527 527 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 565 565 S -> R (in dbSNP:rs17046588).
/FTId=VAR_052515.
CONFLICT 182 182 Y -> N (in Ref. 3; AAQ89010).
{ECO:0000305}.
CONFLICT 263 263 I -> T (in Ref. 3; AAQ89010).
{ECO:0000305}.
CONFLICT 495 495 L -> P (in Ref. 5; AAH89445).
{ECO:0000305}.
CONFLICT 576 576 S -> K (in Ref. 5; AAH89445).
{ECO:0000305}.
CONFLICT 590 599 STCHSGVTCG -> KPANLAR (in Ref. 2;
CAJ18095 and 3; AAQ89010). {ECO:0000305}.
SEQUENCE 599 AA; 67235 MW; 1548898E95C43A7A CRC64;
MAPRGCAGHP PPPSPQACVC PGKMLAMGAL AGFWILCLLT YGYLSWGQAL EEEEEGALLA
QAGEKLEPST TSTSQPHLIF ILADDQGFRD VGYHGSEIKT PTLDKLAAEG VKLENYYVQP
ICTPSRSQFI TGKYQIHTGL QHSIIRPTQP NCLPLDNATL PQKLKEVGYS THMVGKWHLG
FYRKECMPTR RGFDTFFGSL LGSGDYYTHY KCDSPGMCGY DLYENDNAAW DYDNGIYSTQ
MYTQRVQQIL ASHNPTKPIF LYIAYQAVHS PLQAPGRYFE HYRSIININR RRYAAMLSCL
DEAINNVTLA LKTYGFYNNS IIIYSSDNGG QPTAGGSNWP LRGSKGTYWE GGIRAVGFVH
SPLLKNKGTV CKELVHITDW YPTLISLAEG QIDEDIQLDG YDIWETISEG LRSPRVDILH
NIDPIYTKAK NGSWAAGYGI WNTAIQSAIR VQHWKLLTGN PGYSDWVPPQ SFSNLGPNRW
HNERITLSTG KSVWLFNITA DPYERVDLSN RYPGIVKKLL RRLSQFNKTA VPVRYPPKDP
RSNPRLNGGV WGPWYKEETK KKKPSKNQAE KKQKKSKKKK KKQQKAVSGS TCHSGVTCG


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Related Genes :
[Arsb As1 As1-s] Arylsulfatase B (ASB) (EC 3.1.6.12) (N-acetylgalactosamine-4-sulfatase) (G4S)
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DP258_02540 EC3234A_36c00010 EC382_21100 ECTO6_01955 EFV06_13085 EFV16_12340 NCTC8500_02249 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[Arsa As2] Arylsulfatase A (ASA) (EC 3.1.6.8) (Cerebroside-sulfatase)
[atsA PA0183] Arylsulfatase (AS) (EC 3.1.6.1) (Aryl-sulfate sulphohydrolase)
[hchA A8M42_01610 AM465_15370 AWF23_018680 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C1I57_21890 C7B02_06890 CCZ14_26645 CCZ17_22700 CRT43_11430 CT143_08220 D3C88_02905 D6X47_12880 D9D33_15385 D9E49_19020 D9I20_10460 D9J46_03345 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 ECTO124_02024 EGT48_04930 EPS76_06485 ERS085406_02591 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 NCTC9775_01269 SY51_11150] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[Sulf1 Kiaa1077] Extracellular sulfatase Sulf-1 (mSulf-1) (EC 3.1.6.-)
[Ogg1] N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]
[ARSA] Arylsulfatase A (ASA) (EC 3.1.6.8) (Cerebroside-sulfatase) [Cleaved into: Arylsulfatase A component B; Arylsulfatase A component C]
[Apex2 Ape2] DNA-(apurinic or apyrimidinic site) lyase 2 (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease 2) (Apurinic-apyrimidinic endonuclease 2) (AP endonuclease 2)
[Sulf2] Extracellular sulfatase Sulf-2 (mSulf-2) (EC 3.1.6.-)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Prdx6 Aop2 Ltw4 Prdx5] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Akr1c21] Aldo-keto reductase family 1 member C21 (EC 1.1.1.-) (17-alpha-hydroxysteroid dehydrogenase) (17-alpha-HSD) (3(or 17)-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.209) (3-alpha-hydroxysteroid dehydrogenase) (Dihydrodiol dehydrogenase type 1) (DD1) (Dihydrodiol dehydrogenase type 3) (DD3)
[Impad1 Impa3] Inositol monophosphatase 3 (IMP 3) (IMPase 3) (EC 3.1.3.25) (EC 3.1.3.7) (Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase) (Golgi-resident PAP phosphatase) (gPAPP) (Inositol monophosphatase domain-containing protein 1) (Inositol-1(or 4)-monophosphatase 3) (Myo-inositol monophosphatase A3)
[hmpA hmp A8C65_03855 A9R57_17040 ACN002_2592 ACN77_09545 ACN81_26320 ACU57_10360 ACU90_01485 AM270_07210 AM464_04560 AML07_10430 APZ14_05505 AUQ13_13215 AUS26_21665 AW106_11070 AWF80_015090 BANRA_01097 BANRA_03418 BANRA_04525 BB545_05760 BHS81_15570 BHS87_14445 BJJ90_06510 BK292_20760 BMT53_22940 BMT91_09730 BN17_18391 BUE81_08005 BVL39_14050 BW690_11150 BZL31_13550 C2U48_21325 C4J69_10505 C5N07_10115 C5P01_05560 C5P43_25010 C6986_16510 C7235_06805 C9E25_16695 CG691_06165 CG705_05290 CG706_03875 COD30_01045 COD46_11500 CRM83_27495 CWS33_10010 D2184_18725 D2185_06690 D3821_11445 D3O91_03570 D3Y67_23905 D9E22_02790 D9F57_20505 D9H68_00985 D9I18_09865 D9I97_07905 D9J11_04290 D9J44_00060 DIV22_11300 DL545_07245 DL800_19195 DMZ31_01715 DNQ41_17925 DP277_03620 DTL43_01910 E2855_03303 E2863_03210 EAI42_06330 EAI44_09410 EC1094V2_1116 EC3234A_44c01590 EC95NR1_01777 ECTO6_01279 ED600_07770 EEP23_02350 EFV01_13935 EFV02_11870 EFV04_05815 EFV08_03440 EFV11_08940 EFV12_11800 EFV15_03135 ERS085365_01518 ERS085374_00038 ERS085416_03760 ERS139211_00868 ERS150873_01392 ERS150876_00857 FORC28_1400 HW43_17160 NCTC11022_02631 NCTC11181_03552 NCTC13148_02382 NCTC8500_01411 NCTC8960_04037 NCTC8985_06124 NCTC9036_01390 NCTC9037_01459 NCTC9058_00631 NCTC9062_01812 NCTC9073_04581 NCTC9706_04593 NCTC9962_00729 PU06_05410 RG28_09110 RK56_022045 SAMEA3446340_03873 SAMEA3472043_01058 SAMEA3472044_03009 SAMEA3472070_00042 SAMEA3472080_01630 SAMEA3484427_00463 SAMEA3484429_00572 SAMEA3752553_02327 SAMEA3752557_00946 SAMEA3753097_02775 SK85_02808 WQ89_05840] Flavohemoprotein (Flavohemoglobin) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (EC 1.14.12.17)
[Cyb5r4 Ncb5or] Cytochrome b5 reductase 4 (EC 1.6.2.2) (Flavohemoprotein b5/b5R) (b5+b5R) (N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein) (cb5/cb5R)
[Ptpn6 Hcp Hcph Ptp1C] Tyrosine-protein phosphatase non-receptor type 6 (EC 3.1.3.48) (70Z-SHP) (Hematopoietic cell protein-tyrosine phosphatase) (PTPTY-42) (Protein-tyrosine phosphatase 1C) (PTP-1C) (SH-PTP1) (SHP-1)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[Wrnip1 Whip] ATPase WRNIP1 (EC 3.6.1.3) (Werner helicase-interacting protein 1)
[Nthl1 Nth1] Endonuclease III-like protein 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[Arsg Kiaa1001] Arylsulfatase G (ASG) (EC 3.1.6.1)
[Tas1r3 Sac T1r3 Tr3] Taste receptor type 1 member 3 (Saccharin preference protein) (Sweet taste receptor T1R3)
[ARSB] Arylsulfatase B (ASB) (EC 3.1.6.12) (N-acetylgalactosamine-4-sulfatase) (G4S)
[Kmt2c Mll3] Histone-lysine N-methyltransferase 2C (Lysine N-methyltransferase 2C) (EC 2.1.1.43) (Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog)
[nnrD nnrE BHS81_24940 BUE81_24185 BW690_00535 C4J69_05655 C5P01_11605 C5P43_09775 CG692_00180 COD46_22200 CWS33_03515 D2185_07770 D3821_07085 D3O91_01535 D3Y67_00680 D9D20_08295 D9E22_11680 D9H68_15720 D9H94_06330 D9I18_04405 D9J11_13510 EAI42_08035 EAI42_19730 EAI46_08330 EEP23_07485 EFV08_07420 EFV15_06635 EFV17_14450 EL75_3998 EL79_4176 EL80_4091 RK56_012375] Multifunctional fusion protein [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase)]
[Kmt2a All1 Hrx Mll Mll1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[Oprm1 Mor Oprm] Mu-type opioid receptor (M-OR-1) (MOR-1)
[Got1] Aspartate aminotransferase, cytoplasmic (cAspAT) (EC 2.6.1.1) (EC 2.6.1.3) (Cysteine aminotransferase, cytoplasmic) (Cysteine transaminase, cytoplasmic) (cCAT) (Glutamate oxaloacetate transaminase 1) (Transaminase A)

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