wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon-activable protein 205-A (Ifi-205-A) (Interferon-inducible protein p205-A) (Protein D3') (Q8CGE8)
Organism: Mus musculus (Mouse)
Function: May act as a transcriptional regulator in the myeloid lineage. Inhibits cell growth via p53/TP53 and RB1-dependent and independent pathways (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MENEYKRLVLLEGLECINKHQFNLFKSLMVKDLNLEEDNQEKYTTFQIANMMVKKFPADAGLDRLINFCERVPTLKKRAEILKKERSEVTEETSLEINRQEASPATPTSTTSHMLASERGKTSTTQEETSTAQKRKGMSEEKTDVKKIKASGKADQPPCCEGPTATCQSPISQVSSSASSNIPSAKNQKSQPQNQNIPRGAVLHSEPLTVMVLTATDPFEYESPEHEVKNMFHATVATVSQYFHVKVFNIDLKEKFTKNNFITISNYFESKGILEINETSSVLEAAPKQMIEVPNCITRNANASPKICDIQKGTSGTVFYGVFTLHKKKVKTQNTSYEIKDGSGSIEVVGSGQWHNINCKEGDKLHLFCFHLKRERGQPKLVCGDHSFVKVTKAGKKKEASTVQ
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin, subfamily e, member 1) (Smarce1 protein) (Q803S1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1-A
- SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin, subfamily c, member 2.
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- Brahma protein-like protein 1
- AT-rich interactive domain 2
- AT-rich interactive domain 1B
- SWI/SNF complex subunit SMARCC1 isoform X1
- Bromodomain-containing 7
- PHD finger protein 10
Sequence:
MSKRPPYAPAPTPAPTTQMPTTPGFVGYNPYSHLAYNNYRLGGNPSGNNRNSSGITVPKPPKPPDKPLMPYMRYSRKVWDQVKASNPDLKLWEIGKIIGGMWRDLTDEEKQDYLNEYEAEKIEYNDSLKAYHNSPAYLAYVNAKNRAEAALEEESRQRQSRLDKGEPYMSIQPAEDPDDYDDGFSMKHTAAARFQRNHRLISDILSEVVVPDVRSVVTTARMQVLKRQVQSLMVHQRKLEAELLQIEDRHQEKKRRFLESTDSFNNELKRLCGLKVEVDMEKLAAEMAAAEEAARRRAEEREREAAEQVERAAQEEQQPASAQANANTEQTSASETKDGEDKPTPMETESLAETSEGSQEAEQGTPAAGEKAAQPEPAEGATDEGTSDSTAPSESSSGPPAEHQTASDNTPEERLPTQPQ
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit) (Ribophorin II) (RPN-II) (Ribophorin-2) (F1PCT7)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000269|PubMed:29519914}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Tumor suppressor candidate 3.
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Magnesium transporter 1.
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Protein transport protein Sec61 subunit alpha isoform 1
- Malectin.
Sequence:
MASPGASTVFLLALTILAGTQALTPTHYLTKPDVERLRASLDRPFTSLESAFYSIVGLSSLGVQVPDVKKACAFIKSNLDPGNVDSLFYAAQSSQALSGCEISISNETKDLLLAAVSEDSSVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSIVEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAIFSKKNFESLSEAFSVASAAAALSQNRYHVPVVVVPEGTPSDTHEQAILRLQVTNVLSQPLTQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFSVKVEGDNRYIANSVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQLVDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDSKNVYKFELDTSERKIEFDSASGTYTLYLIIGDATLKNPILWNVADVVIKFPEEDAPSTVLSKNLFTPKQEIQHLFREPEKRPPTVVSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTIIFHLGHAAMLGLMYVYWTQLNMFQTLKYLAILGSVTFLAGNRMLAQQAIKRTAH
Protein: Visual system homeobox 2 (Ceh-10 homeodomain-containing homolog) (Homeobox protein CHX10) (Q61412)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional regulator through binding to DNA at the consensus sequence 5'-[TC]TAATT[AG][AG]-3' upstream of gene promoters. Plays a significant role in the specification and morphogenesis of the sensory retina. May play a role in specification of V2a interneurons during spinal cord development. Mediates differentiation of V2a interneurons by repression of motor neuron gene transcription, via competitively binding to response elements that are activated by the ISL1-LHX3 complex, such as VSX1 and MNX1. Acts as a positive transcriptional regulator of NXNL1; regulation is significantly increased in synergy with VSX1. Acts as a negative transcriptional regulator of MITF. Represses SAG transcription by competitive inhibition of ISL1-LHX3 response elements (By similarity). Binds to the photoreceptor conserved element-1 (PCE-1) in the promoter of rod photoreceptor arrestin SAG and acts as a transcriptional repressor. Involved in the development of retinal ganglion cells (RGCs) which leads to release of SHH by RGCs, promoting Hedgehog signaling and subsequent proliferation of retinal progenitor cells. Participates in the development of the cells of the inner nuclear layer, by promoting postnatal differentiation of bipolar cells with a comparable inhibition of rod cell differentiation. May play a role in the maintenance of neural retina identity during development by regulation of canonical Wnt genes and CTNNB1 localization, suggesting a role in the regulation of canonical Wnt signaling (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:8630490}.
Interaction partners:
- Transcription factor Atoh7
- Homeobox protein SIX6
- POU domain, class 4, transcription factor 2
- Recoverin
- Homeobox protein SIX3
- POU domain, class 4, transcription factor 1
- Rhodopsin
- Insulin gene enhancer protein ISL-1
- Forkhead box protein N4
- Neurogenic differentiation factor 4
Sequence:
MTGKAGEALSKPKSETVAKSTSGGAPARCTGFGIQEILGLNKEPPSSHPRAALDGLAPGHLLAARSVLSPAGVGSMGLLGPGGLPGFYTQPTFLEVLSDPQSVHLQPLGRASGPLDTSQTASSDSEDVSSSDRKMSKSALNQTKKRKKRRHRTIFTSYQLEELEKAFNEAHYPDVYAREMLAMKTELPEDRIQVWFQNRRAKWRKREKCWGRSSVMAEYGLYGAMVRHSIPLPESILKSAKDGIMDSCAPWLLGMHKKSLEAAAESGRKPEVERQALPKLDKMEQEERAPEAQAAISQEELRENSIAALRAKAQEHSTKVLGTVSGPDSLARNAEKPEEEDATEEDRPAEKLSPPQLEDMA
Protein: Vasotab (P84843)
Organism: Hybomitra bimaculata (Horse fly)
Function: Vasodilator protein that inhibits vasoconstriction of isolated rat femoral artery induced by phenylephrine. Since platelet aggregation and vasoconstriction are key hemostatic responses, particularly in small wounds, this protein likely participates in the antihemostatic responses during blood feeding. Blocks L-type calcium channels (Cav1/CACNA1) in left ventricular myocytes isolated from rat hearts.
Subcellular location: Secreted {ECO:0000269|PubMed:16391356}.
Interaction partners:
Sequence:
MKFALFSVLVVLLIATFVAADECPRICTADYRPVCGTPSGGRRSANRTFGNQCSLNAHNCLNKGDTYDKLHDGECK
Protein: Elongation of very long chain fatty acids protein 2 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL2) (ELOVL fatty acid elongase 2) (ELOVL FA elongase 2) (Very long chain 3-ketoacyl-CoA synthase 2) (Very long chain 3-oxoacyl-CoA synthase 2) (A0A097I5U8)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03202}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03202}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNHLQSLDERLNALFYFLFEDRDSRVRGWLLMDSYLPTLSLTILYLLTVYLGSKYMRNRPAYSLKGVLQVYNFSVTMLSLYMLVELVSATLSAGYRLQCQGLHEAGEADLRVAKVLWWYYFSKVIEFLDTIFFVLRKKNSQITFVHVYHHASMFNIWWCVLNWIPCGQSFFGPTLNSFIHVCMYSYYGLSTIPSMQKYLWWKRYLTQAQLIQFILTITHTLSAIVVPCGFPVGCLLFQFSYMATLVILFVNFYVQTYRKRRPEESIKSSRPNGHTVSTNGTSFKKRK
Protein: Cilia and flagella associated protein 68 (E9PLN1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
Sequence:
MSKFFQYGWRCTTNENTYSNRTLMGNWNQERYDLRNIVQPKPLPSQFGHYFETTYDTSYNNKMPLSTHRFKREPHWFPGHQPELDPPRYKCTEKSTYMNSYSKP
Protein: At2g34585 (Expressed protein) (Transmembrane protein) (Q8S8R9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAAITSAVIAIAGIILGWITIELACKPCLESGREAIDRSLNPDYDPDDQDVDSSSDVRAPLIPNHPPDNSDPDPTTAIKSV
Protein: Small nuclear ribonucleoprotein G (snRNP-G) (Sm protein G) (Sm-G) (SmG) (P40204)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O74966}. Cytoplasm {ECO:0000250|UniProtKB:O74966}.
Interaction partners:
- Pre-mRNA-splicing factor PRP11
- Pre-mRNA-splicing factor 6
- U4/U6 small nuclear ribonucleoprotein PRP3
- Pre-mRNA-splicing factor CEF1
- Small nuclear ribonucleoprotein Sm D1
- Pre-mRNA-splicing factor PRP21
- LSM complex subunit LSM5
- Pre-mRNA-splicing factor 8
- U2 snRNP component HSH155
- U1 small nuclear ribonucleoprotein C
Sequence:
MVSTPELKKYMDKKILLNINGSRKVAGILRGYDIFLNVVLDDAMEINGEDPANNHQLGLQTVIRGNSIISLEALDAI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8IGS1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSWTEKVDPELIFTKQERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIDDIQQEIMVLSQCDSPYVTKYYGSFLKGTKLWIIMEYLGGGSALDLMKAGSFEEMHIGIILREVLKGLDYLHSERKLHRDIKAANVLLSEQGDVKLADFGVAGQLTNTTSKRNTFVGTPFWMAPEVIKQSQYDAKADIWSLGITAIELAKGEPPNSELHPMRVLFLIPKNNPPQLTGSYTKSFKDFVEACLNKDPENRPTAKELLKYPFIKKAKKNAYLIDLIDRFKKWKVSKGDESETESENSDSDSDAKQGGSSQDEPWIMTVKGLHINSAPRAGVNSFQLQEHELTMQKLMQTTHSPAGGGGVQASPAANALSSSVSAVAASASSVSVITANEGVSSASALPPQNSHVHNHNHNNINNNNIRNLSNKHATTTMLNAAPPPSSVTSSSSASELQQKRSSSKPELRQSRSAAPLDQVEDRRASLGLPLQSSVPTPSTAEQQQQRRSSQRESFHANNAALVASCSSSSNNHSHEEHVATNHASHVKHSGAGQRLVQTNSACLNNFLFPVLSDIQREYSGGGSAGSGGSGGRNIGVGSDIGDLKSVFELAERSSPGVSDLFMKELIHMLVPGYSETRINTIMDRAIRNRK
Protein: Kinase (EC 2.7.-.-) (Q55AP4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Inositol-tetrakisphosphate 1-kinase
- Multiple inositol polyphosphate phosphatase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Inositol-pentakisphosphate 2-kinase
- Kinase
- 2,3-bisphosphoglycerate 3-phosphatase
Sequence:
MNEQNKFQVVAEQEGKVFKECTIKEKQFYESLSPDNELSKLIPKYYGTVIQDGKEWIVLEDLTYGYSKPNIMDIKLGLSHHDVDLETIYSPPSSNDPNVNFETLKRQANMSLHKELYESWLLSKYITTPKLGFCVCGSQKYNCCTNQLEKIQKEQGRTFTAVTVKDKLYDFFHNGIKFRPEIIESMINRLSLFKDFFENNPDYRFRSTSILFLYEGDCEFSNRCDIRLIDFTHTKLYPSHMKPHSSKLSHYKSIDVNNIDSKTTSITSGFDHETYFPIDGGYLFGITNLLKILNSLKNKQQPQQPQK
Protein: BHLH domain-containing protein (Q9ASJ3)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAQASSKRGMLLPREAVLYDDEPSMPLEILGYHGNGVGGGGCVDADYYYSWSGSSSSSSSSVLSFDQAAVGGSGGGCARQLAFHPGGDDDDCAMWMDAAAGAMVENTSVVAGGGNNYCHRLQFHGGAAGFGLASPGSSVVDNGLEIHESNVSKPPPPAAKKRACPSGEARAAGKKQCRKGSKPNKAASASSPSPSPSPSPSPNKEQPQSAAAKVRRERISERLKVLQDLVPNGTKVDLVTMLEKAINYVKFLQLQVKVLATDEFWPAQGGKAPELSQVKDALDAILSSQHPNK
Protein: tyrosinase (EC 1.14.18.1) (Q2UP46)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Tyrosinase copper-binding domain-containing protein
- Tyrosinase
- Tyrosinase copper-binding domain-containing protein
- Aromatic-L-amino-acid/L-histidine decarboxylase
- histidinol-phosphate transaminase
- aromatic-amino-acid transaminase
- Tyrosinase copper-binding domain-containing protein
- Tyrosinase copper-binding domain-containing protein
- aromatic-amino-acid transaminase
- Tyrosinase copper-binding domain-containing protein
Sequence:
MPYLITGIPKDPKHPLPIRKDIDDWYLEQTSAGSNRIQLTLFVEALTVIQNRPLNDQLSYFRLAGIHGAPWTEWDGVPGGQKDSKGNPTGFCVHNNYTFPTWHRVYVTLYEQVIYEAMLDFIKQNVPQNGKADWENEAKQWRLPYWDFARFARHGHDNTQGDELRLPILVTMPMVKVLVPGQPGKQLSKPNPLYRFQMQTLMGTLERPYAITSQKTEEHGWSFDLPFDKCQSTTKYGLLENYNADVWADGGQNWLRANLALNEHPWYQNLDGWASVPTLQDMTFRLLTTGGLNWGEFSSTRYDDKKEEAQPKNNEQAPKNWMNLEAIHNNVHNWVGGFMFSRPGRHDLKLWGAGHMSSVPVAAFDPIFWLHHWLTAIWQTVNSGSWFNDDKSKVSKDDDLRPFHRFCEKTRKVVFFRSDDVKDWRSLNYDYAITKDASRIRKEISDLYGQRTKEVYKDFGEEDYILSIRYSRYALGGKPFQINIFFGDVDGKDFYDARSQNFVGSVFNFSGSLEDSNCDKCAQQEQEGVLSVSQLPARLAVHYYKKQNKGEVPTPRYVVVNSQGKAEAEVKVEVALHKTEVFHSVDSESWDLRMEHTHCFSTHGMGGHYHYDTTAEVVEYEAWLNTAKVIYRIDQPGQ
Protein: NAD(+) hydrolase TcpC (EC 3.2.2.6) (NADP(+) hydrolase TcpC) (EC 3.2.2.-) (TIR domain-containing protein in E.coli) (tcpC) (A0A0H2V8B5)
Organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Function: Virulence factor that suppresses host Toll-like receptor (TLR)-mediated cytokine production upon infection, thereby increasing bacterial burden in the urinary tract and promoting renal tissue damage. Acts as a NAD(+) hydrolase (NADase) by catalyzing cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide. Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules.
Subcellular location: Secreted {ECO:0000269|PubMed:18327267}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- MobA/MobL protein domain-containing protein
Sequence:
MIAYENIEFFICLVNVLGNNMYNILFFIFLSIAIPFLLFLAWKQHLKTKEIRSYLLKEGYNIIFNGEGNSYLAFNISNATFRAGNLTSNDYFQASISYIHDYRWEWKEVEAKKINNIFIIYISNIDFPSQKLFYRNNKSLAEIDWAKLQAIFHQPYEIQNDVMQDNNNTHYDFFISHAKEDKDTFVRPLVDELNRLGVIIWYDEQTLEVGDSLRRNIDLGLRKANYGIVILSHNFLNKKWTQYELDSLINRAVYDDNKIILPIWHNINAQEVSKYSHYLADKMALQTSLYSVKEIARELAEIAYRRR
Protein: GDP-fucose protein O-fucosyltransferase 2 (EC 2.4.1.221) (Peptide-O-fucosyltransferase 2) (O-FucT-2) (Q9W589)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of several protein families including the ADAMTS, the thrombospondin (TSP) and spondin families.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16464857}. Golgi apparatus {ECO:0000269|PubMed:16464857}. Note=Mainly located in the endoplasmic reticulum. {ECO:0000269|PubMed:16464857}.
Interaction partners:
- GDP-fucose protein O-fucosyltransferase 1
- Polypeptide N-acetylgalactosaminyltransferase 35A
- Polypeptide N-acetylgalactosaminyltransferase 5
- Transmembrane protein 11 homolog, mitochondrial
- Protein O-mannosyl-transferase 2
- Mannose-P-dolichol utilization defect 1 protein homolog
- Putative alpha-L-fucosidase
Sequence:
MRGSWPRLGFPALLLLLHLLTGSDAAVRNGTAKREIGDSRGSSGTCVKGFLQEILPLPATCPPEVLGMRGAVYILYDVNISEGFNLRRDVYIRMAVFVRRLQRRRRFRHVRLVLPPWPRLYHWHSQGLQQSGLPWSHFFDLASLRRYAPVLDYEEFLAEQRLFGNPGAPLVHVGHAFRLQHYEVMLEQGIFRDKFERVTDKPCSEGSLSGGPLLQQAELRVGRFHCVRFQGSAGLLEKLLREAIDEDTAGPEDVDDMRTYALLSAETVLHDHWGDEHFWQARRSMRFARRLEQVAADFRRQALDTTDASAGVQRPAMWELERPKRNAKGGDYLCAHLRRGDFVRSRDATTPTLKAAAQQVKQLLRGFNMTTVFLATDATPYELMELKELFYRFRLVHFAPESNVQRRELKDGGVAVVDQLVCAYARYFVGTYESTFTYRIYEEREILGFTQASTFNTFCKALGGSCSRNAVWPIVWADGDSDSEEDSDPY
Protein: High mobility group protein B2 (High mobility group protein 2) (HMG-2) (P40673)
Organism: Bos taurus (Bovine)
Function: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes (By similarity). Binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. In the extracellular compartment acts as a chemokine. Promotes proliferation and migration of endothelial cells implicating AGER/RAGE. Has antimicrobial activity in gastrointestinal epithelial tissues. Involved in inflammatory response to antigenic stimulus coupled with pro-inflammatory activity. May play a role in germ cell differentiation. Involved in modulation of neurogenesis probably by regulation of neural stem proliferation. Involved in articular cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin pathway (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P26583, ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000250|UniProtKB:P26583}. Cytoplasm {ECO:0000250|UniProtKB:P26583, ECO:0000250|UniProtKB:P30681}. Secreted {ECO:0000250|UniProtKB:P26583}.
Interaction partners:
- High mobility group protein B1
Sequence:
MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSEHRPKIKSEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEDEDEEEEDEDEE
Protein: Adenylosuccinate lyase (ASL) (EC 4.3.2.2) (Adenylosuccinase) (A0A0A6YY92)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTSLILSRGVIKAYCNLRLPGSDSSPVSVSQLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKAELCL
Protein: Peroxisomal membrane associated protein 20 (Peroxiredoxin homolog pmp20) (Prx) (O14313)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May act as a chaperone rather than a peroxidase. Has no thioredoxin-dependent peroxidase activity. Shows weak chaperone activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Peroxiredoxin tpx1
- E3 ubiquitin-protein ligase dbl4
- Glutathione reductase
- Glutathione peroxidase-like peroxiredoxin gpx1
- Putative glutamine amidotransferase PB2B2.05
- Thioredoxin-1
- Thioredoxin-2, mitochondrial
- Catalase
- Dihydrolipoyl dehydrogenase, mitochondrial
- Putative aldehyde dehydrogenase-like protein C9E9.09c
Sequence:
MVAVGSTLPKVTLWENKPEEVVEFPSQGKFIIVGVPGAFTPPCSSQVPGYIANEKQFAAKGISGIYVVAVNDVFVTKAWKKSFDGGEQSGVHFVADWNGEFTKAFDAGFDASGLLGPLRSKRYAAVVENGKVVKVFIENEVTDVDISSADKVLSSL
Protein: Thioredoxin reductase gliT (EC 1.8.1.-) (Gliotoxin biosynthesis protein T) (E9RAH5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. GliT is required for self-protection against gliotoxin. GliT plays a role in preventing dysregulation of the methyl/methionine cycle to control intracellular S-adenosylmethionine (SAM) depletion and S-adenosylhomocysteine (SAH) homeostasis during gliotoxin biosynthesis and exposure.
Interaction partners:
- Nonribosomal peptide synthetase gliP
- Glutathione S-transferase gliG
- C6 finger domain transcription factor gliZ
- O-methyltransferase gliM
- Cytochrome P450 monooxygenase gliF
- Gamma-glutamyl cyclotransferase gliK
- Cytochrome P450 monooxygenase gliC
- N-methyltransferase gliN
Sequence:
MSIGKLLSNGALLVDVLIIGAGPAGLSTATGLARQLHTAVVFDSGVYRNAKTQHMHNVLGWDHRNPAELRAAGRADLTTRYSTIQFQNSTIEAIRQVETNQLFEARDNEGHSWYGRKVVLATGVRDIPLDIEGYSECWANGIYHCLFCDGYEERGQETVGVLALGPIANPARALHLARMALRLSESVTIYTNGNEQLAKEIQQAAEESPVGASGLKFEARPIRRFEKGDVAKTVIVHLGESESKTEGFLVYNPQTEVNGPFAKQLALNMTEGGDILTTPPFYETSVPGVFAVGDCATPLKAVTPAVSMGSLAAGGLVAQLQAQALPEFRLDQEL
Protein: Low-density lipoprotein receptor-related protein (B5L5I6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGAVLQTLLLCTLCLQIRGLPLLLYANRRDLRLVDAAHGRANATLVMGGLEDAAAVDYIYAQGLIYWSDVSEESIKRTLFNGSAPSGVQTTVISGLASPDGLACDWMGNKLYWTDSETNRIEVAELDGTHRKVLFWQDLDQPRAIALDPGRGFMYWTDWGEIPKIERAGMDGSLRSVIVETEIYWPNGLTLDYQQQQLYWADAKFNCIHRSNLDGSSREVVVKGSLPHPFALTLYEDTLFWTDWNTHSIHSCHKHTGENSREVHSNIFSPMDIHVYSQQRQPMDVASPCSVRNGGCSHLCLLSPAKPYYQCACPTGVQLLEDHKSCRDGGPSQLLLLARRTDLRRISLDTPDFTDIVLQAEDIRHAIAIDYDPVEGHIYWTDDEVRAIRRSLLDGSDAQLVVTSQVNHPDGIAVDWIARNLYWTDTGTDRIEVTRLNGTMRKILISEDLDEPRAIVLDPVAGYMYWTDWGEVPKIERAALDGSQRMVMVNTSLGWPNGLALDYSERKIYWGDAKTDVIEVMEMDGSGRRVLLEDNLPHVFGFTLLGDYIYWTDWQRRSIERVHKRSTEREVIIDQLPDLMGIKATFVHQTFGVNPCAWANGGCSHLCLYRPQGVSCACPIGLELMADLSTCIVPEAFLLFSRHTDIRRISLETNNNNVAIPLTGVKEASALDFDITDNRIYWTDITLKTISRAFMNGSSLEHVVEFGLDYPEGMAVDWLGKNLYWADTGTNRIEVAKLDGQHRQVLVWKDLDSPRALALDPAEGFMYWTEWGGRPKIDRAAMDGSGRITLVPNVGRANGLTIDYAERRLYWTDLDTTLIESSNMLGLEREVIADDLPHPFGLTQYQDYIYWTDWSQRSIERANKTSGQNRTVIQGHLDYVMDILVFHSSRQSGWNACAATNGHCSHLCLAVPVCSFTCGCPAHYSLNTDNKTCSAPTSFLLFSQKTAINRMVMDELQSPDIILPIHSLRNVRAIDYDPLDRHLYWIDAKQNVIRRAQEDGNQSVTVVSGAVGGSNLGLQPYDLSIDIYSRFIYWTSELTNVINVTRTDGSRVGVVLRGEHDKPRAIAVNPERGYMYFSNLQERSPKIERCALDGTEREVLFFSNLGRPVALAVDNELGKLFWVDMDLRRIESSDLSGANRIVIEDSNILQPVGLTVFGNFLYWIDRQQQMIERIHKVTREGRTKIQARIASLSDIHAVHQLDMQEYSKHPCTSDNGGCTHICIVKGDGTTRCSCPIHLVLLQDELSCGEPPTCSPEQFSCVSGEVDCIPQAWRCDGFAECDDSSDERDCPVCSSREFQCDSRQCVDAALRCNGEINCQDRSDENKCEVLCPADQFTCSNGQCIGRHKKCDNNMDCTDNSDEIGCYATEEPSFAPTNTIGSIVGVVMVLFVVGAVYFVCQRVLCPQMKDDADTMTNDFVVHGPPPVPLGYVPHPASLSGSLPGMSRGKSVMGSLSIMGGSSGPPYDRAHVTGASSSSSSSTKGAYFPPILNPPPSPATVRSQYTMEFGYSSNSPSTHRSYSYRPYSYRHFAPPTTPCSTDVCDSDYTPGRRAPHASSATAAKGYASDLNYDSEPLPPPPTPRSQYLSAEENCESCPPSPYTERSYSHQLYPPPPSPCTDSS