wanglab/gogpt-training-data huggingface dataset:
Protein: Sphingosine-1-phosphate lyase 1 (S1PL) (SP-lyase 1) (SPL 1) (mSPL) (EC 4.1.2.27) (Sphingosine-1-phosphate aldolase) (Q8R0X7)
Organism: Mus musculus (Mouse)
Function: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro-inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP. Seems to play a role in establishing neuronal contact sites and axonal maintenance (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15522238, ECO:0000269|PubMed:28165339}; Single-pass type III membrane protein {ECO:0000269|PubMed:15522238}; Cytoplasmic side {ECO:0000269|PubMed:15522238}.
Interaction partners:
- Sphingosine-1-phosphate phosphatase 1
- Sphingosine-1-phosphate phosphatase 2
- Sphingosine kinase 2
- Sphingosine kinase 1
- Phospholipid phosphatase 3
- Phospholipid phosphatase 2
- Serine palmitoyltransferase 1
- Sphingosine 1-phosphate receptor 2
- Serine palmitoyltransferase 2
- Ceramide synthase 4
Sequence:
MPGTDLLKLKDFEPYLEILESYSTKAKNYVNGYCTKYEPWQLIAWSVLCTLLIVWVYELIFQPESLWSRFKKKLFKLIRKMPFIGRKIEQQVSKAKKDLVKNMPFLKVDKDYVKTLPAQGMGTAEVLERLKEYSSMDGSWQEGKASGAVYNGEPKLTELLVQAYGEFTWSNPLHPDIFPGLRKLEAEIVRMTCSLFNGGPDSCGCVTSGGTESILMACKAYRDLALEKGIKTPEIVAPESAHAAFDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISRNTAMLVCSTPQFPHGVMDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYPLEKPFDFRVKGVTSISADTHKYGYAPKGSSVVMYSNEKYRTYQFFVGADWQGGVYASPSIAGSRPGGIIAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKNIFIFGDPQLSVIALGSNDFDIYRLSNMMSAKGWNFNYLQFPRSIHFCITLVHTRKRVAIQFLKDIRESVTQIMKNPKAKTTGMGAIYGMAQATIDRKLVAEISSVFLDCLYTTDPVTQGNQMNGSPKPR
Protein: Heme oxygenase 2 (HO-2) (EC 1.14.14.18) [Cleaved into: Heme oxygenase 2 soluble form] (P23711)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:P30519}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09601}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}.
Interaction partners:
- Biliverdin reductase A
- Ferrochelatase
- Biliverdin reductase B
- Ceruloplasmin
- Hephaestin
- Heme oxygenase 1
- Protoheme IX farnesyltransferase, mitochondrial
- Holocytochrome c-type synthase
- histidine--tRNA ligase
- Myoglobin
Sequence:
MSSEVETSEGVDESENNSTAPEKENHTKMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPTELHRKEALIKDMEYFFGENWEEQVKCSEAAQKYVDRIHYVGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFEHVDNAQQFKQFYRARMNALDLSMKTKERIVEEANKAFEYNMQIFSELDQAGSMLTKETLEDGLPVHDGKGDVRKCPFYAAQPDKGTLGGSNCPFRTAMAVLRKPSLQLILAASVALVAGLLAWYYM
Protein: Cadherin-5 (Vascular endothelial cadherin) (VE-cadherin) (CD antigen CD144) (P55284)
Organism: Mus musculus (Mouse)
Function: Cadherins are calcium-dependent cell adhesion proteins (By similarity). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types (By similarity). This cadherin may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. It associates with alpha-catenin forming a link to the cytoskeleton (By similarity). Acts in concert with KRIT1 and PALS1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B (By similarity). Required for activation of PRKCZ and for localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction (By similarity).
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:24806444, ECO:0000269|PubMed:33972531}. Cell membrane {ECO:0000269|PubMed:19635461}; Single-pass type I membrane protein {ECO:0000269|PubMed:19635461}. Cytoplasm {ECO:0000269|PubMed:24806444}. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries. KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions (By similarity). {ECO:0000250|UniProtKB:P33151}.
Interaction partners:
- Catenin delta-1
- Vascular endothelial growth factor receptor 2
- Catenin beta-1
- Platelet endothelial cell adhesion molecule
- Junction plakoglobin
- Receptor-type tyrosine-protein phosphatase beta
- Claudin-5
- Tight junction protein 1
- Cadherin-1
- Occludin
Sequence:
MQRLTELATALGAFLGLLAVAAMAGPNFPQIDTPNMLPAHHRQKRDWIWNQMHIDEEKNESLPHYVGKIKSNVNRQNAKYVLQGEFAGKIFGVDANTGNVLAYERLDREKVSEYFLTALIVDKNTNKNLEQPSSFTVKVHDINDNWPVFSHQVFNASVPEMSAIGTSVIRVTAVDADDPTVAGHATVLYQIVKGNEYFSIDNSGLIFTKIKNLDREKQAEYKIVVETQDALGLRGESGTATVMIRLEDINDNFPVFTQSTYTFSVPEDIRVGKPLGFLTVVDPDEPQNRMTKYSIMQGEYRDTFTIETDPKRNEGIIKPTKSLDYEVIQQYTFYIEATDPTIRYEYLSSTSGKNKAMVTINVLDVDEPPVFQRHFYHFKLPENQKKPLIGTVVAKDPDKAQRSIGYSIRKTSDRGQFFRITKQGNIYNEKELDRETYAWYNLTVEANELDSRGNPVGKESIVQVYIEVLDENDNPPEFAQPYEPKVCENAAQGKLVVQISATDKDVVPVNPKFKFALKNEDSNFTLINNHDNTANITVKYGQFNREHAKFHYLPVLISDNGVPSLTGTSTLTVGVCKCNEQGEFTFCEEMAAQAGVSIQALVAIFLCILTITVITLLIILRRRIRKQAHAHSKSALEIHEQLVTYDEEGGGEMDTTSYDVSVLNSVRGGSTKPLRSTMDARPAVYTQVQKPPRLAPGLHGGPREMATMIDVKKEEADNDGGGPPYDTLHIYGYEGAESIAESLSSLSTNSSDSDIDYDFLNDWGPRFKMLAELYGSDPQEELII
Protein: Phosducin-like protein 3 (HTPHLP) (PhPL3) (Viral IAP-associated factor 1) (VIAF-1) (Q9H2J4)
Organism: Homo sapiens (Human)
Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation. Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding. Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15371430, ECO:0000269|PubMed:26059764}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26059764}. Endoplasmic reticulum {ECO:0000269|PubMed:26059764}.
Interaction partners:
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit epsilon
- Actin, cytoplasmic 2
- Proteolipid protein 2
Sequence:
MQDPNADTEWNDILRKKGILPPKESLKELEEEAEEEQRILQQSVVKTYEDMTLEELEDHEDEFNEEDERAIEMYRRRRLAEWKATKLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSGLARKFPDVKFIKAISTTCIPNYPDRNLPTIFVYLEGDIKAQFIGPLVFGGMNLTRDELEWKLSESGAIMTDLEENPKKPIEDVLLSSVRRSVLMKRDSDSEGD
Protein: Tropomyosin 1 (A0A494C0V8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDQLYQQLEQNRRLTNELKLALNED
Protein: FHA domain-containing protein (Q57US5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
- BRCT domain-containing protein
- non-specific serine/threonine protein kinase
- Histone H2A
- Endo/exonuclease Mre11
- DNA repair protein RAD50
- Recombination initiation protein NBS1, putative
- BRCT domain-containing protein
- DNA repair protein RAD51 homolog
- BRCT domain-containing protein
- KU80 protein
Sequence:
MKRYFLIDESTGRIMRLLTGENIIRRGAEIAVKGANVVCVGTTCINVSRTHAIIKLCENGEAWLRDCESTNGTFLHSDTGVSVRLEPGFFYQLKRGNHVTFGDLKLRFEWDVIAVCGGRVPVYDSNANLMDSSQGSGMNGASNDLLRLEGTVCSSICASCSLAGTDATPPLPVTLTAASDEKTCAVVSVQLDCGVLCKPLCELENVVPYLSESTGAGRKRSRSVIKNTTDRLSKVKSLPSSATVKSETTARGSRLKPKSKSKGRVKVCFSGMCGEATLAAKFLAKKHCWSIVDNVCMADLLIINHPPVRTPKFIIAVARGIPVVTEEFFACGDMRQVRQFAPSLVHNNCTYDAGRLFQVITSNVGKPALLGRRFSLEKVPPAWRRTARNILTGCGAVVFTKGTKSKSVISLTGATLTALYDDILRGKVPA
Protein: Capicua transcriptional repressor b (F1Q6M9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Ataxin 1b
- Ataxin 1b
Sequence:
MRPPKKQRGRSPLSARGKGTRKRGGKLDGHSQTTPPAPSHQKYTPSKEDSSQDKQIKSSNMTNSEGLKGQIKERTMETSKSEETAGIVNKAKSPKNINTNNLTDNTDSIKIASNAHENSHSNSTDICNTNTQNLTSTNSKSSNQHTNSTASNTQNTNNIGNSLNKSSSLSANHTSTTLSSRKTATFKARVPKKKYMYEHQATSTSPISSKPVTQLTLHINHLGSPQNSISQNTTPVIRNDLFKASTSDLDDSGNSRSRLEIANIASTETSKGDRIMGDMLKSEVPSEVEKVIQMVEADGYGEQAPNSVRSSSTDTASEHSVDLEVLEPSCMQLNSGNHVRASRRFNPLNNSTLSVVLSPNHTQVEQEGSATVAETLAKGLKNQRVLARRRPRRSLKEDEKLVKECIFICGVVRGSNKEQLNVELQINGEGTLLSYPFHTLVSRPHQPIDLILDAPPPGNELVEVGTRVCVPYGGDKEKEWYREGVVAQVDSHSACPYMVLLQEEQKKERCSKEETKQTSSSVWVARQNLRLLVPPWDGVMREKEREEREHREEIEVERELCQLSEGMDLVTAGPPRENCRFPSPDTGAHRYESTLSSSTSPAVVMVANNMFGLASRGENEGTENRERVREREHERKQLQTPEVDMEVLRLNMAPLRDSGGPLVSGGPKTGAPNQHRQILSKPPGYPSPITVVRGISGTTLGSPQPTPSSVVLGSDGGNSHHISPSVPPSPSSRGSLTPLDKTPTPSQTSTPVPGSSASSASSSRSRTPLSAVQQKYKKGDVVCTPNGIRKKFNGKQWRRLCSREGCMKESQRRGYCSRHLSMRTKEMEGAVGERGSGGGGESSSGTVTPSDLRGRASSEFEWDETSRDSSETSSRGTDSRPRLGLPSLLPQDFSRFDFDECEAATMLVSLGSRSVTPSFSPISNQSPFSPTPSPSASPLFGFHPANFSPITASPVLPHRRHKHPSGTNSGLPKHGTGGTEREKDRHLSGIVPSFHPNLTFTVPMSPGKRRTDAPPPPVPLLQEYTKPDQEQSCRDPSLVTNLCIISPQTTTVTHPQRLLSTTASSSPASPLSLESGSQCTISQQPLRDSPVIVRNPEVPLIKFTELPLARVAEVDRTSFTENSQTGVHPETGLQVPVPINAASTNGSVLLQNPTSTLVLVSTTSSIPNPNPAGLPTQPSATLACISVPSPVSGAGLIGAGDGGGQDKSCPATLQQPVPCHPAPTALLPLILPTETLHPVPCKDIIMGRPGTVWTNVEPRSVPVFPWHSLVPFLAPTQSDPSAQPGEGQQTVSHPQTAALKKESQSGSVLKEIIEGAPNPSSRPTPSADELPPEREKDAERERPDSETESDVDDPFFPGVLPDPPISASPGKRRSQSLSALPKDDKNSPGKREKDHIRRPMNAFMIFSKRHRALVHQRHPNQDNRTVSKILGEWWYALGPKEKQKYHDLAFQVKEAHFKAHPDWKWCNKDRKKSSSEGRGVPGGKDIRERSMSETTEPPSVSMGMELKGMGPGMVSVSERVGGEGHGQLTRPRAFSQSAMHSLERSERGNPQALAELAQMCGDGSQVGGRGALSQTQRGVSEDMTSDDERMVICEEEGDDDVIEDSYPGSSIDLKCKERVTDSDSENGSGDEGERKRVFAPVICSSSYGPGHGRSVSLSSYPTSRRFSDTSSKRKRTIEAGDGEQREGEGGASQPSAGQSILVSSGGGVSSMLGAVRVASTVVTNVVRPVVSTPVPIASKSPHDRKLAPSQTQLLIGHGATGNTAAASAGGGGYYSSSSPSPINAPAGQAGLVTNLVLGGTFQAPPAVQLVTPPPPSQNPASPAHSNGPLPLPVLQSHILPSGSLAPSSGQKPITQVQYILPTLSANNPKSPSPQQASQPTSIFTLPTALPTHATLANGKQSGYVSSPVGVVSPGARVQTQSPVLQGKMLVPMATVRAAPAPSPQFPLVAPPLPVQNGAQAGSKIIQIAPMPVVQSQLPSAGPVQPGSPFSVTMGTATVVAPGSTPSQTVLLPPPPTRITYVQSTPGVPSPLPLVPSTTGSSSQTVSAAPGSAYVSSPLATFAAIAHPGQTLVQPLIAGQPSLLAPAQSPNPPHAPAITALYTPTNVTLATGVVSMATVSPSVVYTVSSSSSLSPHILPKHTTATSMTPVTLDRQVNVSVHSERQLHQERSLERQHTDSQVYTLSSERQTEKGCLLQLDKHFQVPSKGSSSSVAPPSATSVPLQPGSPAQPSHSGSAPGTPKLITARPPQKVKATLANIPVGSYDGGGRGKEREKERDRDKEREREKDKDTSSRFSFEVEKVEKIEKSNSPAEEGAPETPTHFGVETSAPSGRCKETNAKEVEKKDSHPSSPLPPPSGSDPSPSQSHGDKDAPPKKVKARPPPLKRPFDSVDKVLSEVYFEERFAELPEFRPEEVLPSPTLQSLATSPRAILGSYRRKRKNSTDLDSSTEDPISPKRKSRRRSSCSSEPNTPKSAAKCEGDIFTFDRPDGEDILGELEFDKVPYSSLRRTLDQRRALVMQLFQDHGFFPSAQATAAFQARYADIFPTKVCLQLKIREVRQKIMQTAAPSESAGISDLSLPGPSGVVTMDPALGADPLEKEVEREGEQHSPEEPRNAGDSQDSSR
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 2 (BLOC-1 subunit 2) (Q9VTE0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- SNAPIN protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Dysbindin protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 3
- KxDL motif-containing protein CG10681
- Uncharacterized protein, isoform A
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- BLOC-2 complex member HPS5 homolog
Sequence:
MDKPTTSAAAAAAQDSNLLPDSPQHGPTLSSASSFEALTRHDPNLSRLATKMFNKTEEYITHELNAPLEDYKLLEEMNKATIAKYKDMRQIAENLNTSTSELSLKFQQLAPMMQQIDEISDTVDKLEAAAYKLDAYSIALENRVKCVLQRKSGGGQVAQ
Protein: Somatostatin receptor type 4 (SS-4-R) (SS4-R) (SS4R) (P49660)
Organism: Mus musculus (Mouse)
Function: Receptor for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. It is functionally coupled not only to inhibition of adenylate cyclase, but also to activation of both arachidonate release and mitogen-activated protein (MAP) kinase cascade.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Somatostatin
- Cortistatin
Sequence:
MNAPATLPPGVEDTTWTPGINASWAPDEEEEDAMGSDGTGTAGMVTIQCIYALVCLVGLVGNALVIFVILRYAKMKTATNIYLLNLAVADELFMLSVPFARSAAALRHWPFGAVLCRAVLSVDGLNMFTSVFCLTVLSVDRYVAVVHPLATATYRRPSVAKLINLGVWLASLLVTLPIAVFADTRPARGGEAVACNLHWPHPAWSAVFVIYTFLLGFLPPVLAIGLCYLLIVGKMRAVALAGGWQQRRRSEKKITRLVLMVVTVFVLCWMPFYVVQLLNLFVTSLDATVNHVSLILSYANSCANPILYGFLSDNFRRSFQRVLCLRCCLLETTGGAEEEPLDYYATALKSRGGAGCICPPLPCQQEPVQAEPGCKQVPFTKTTTF
Protein: Leucine-rich repeat protein kinase family protein (F4KEN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046288}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00046288}.
Interaction partners:
Sequence:
MGCRWNPIGFQFSCFMFLIITLQSRSSLSLESEGFVLLKFRARVDSDPHGTLANWNVSDHDHFCSWFGVTCVDNKVQMLNLSGCSLGGTLAPELSQLSELRSLILSKNKLSGDIPNEFASFAKLEFLDLRDNNLNGVVPPELNKVLTPENLLLSGNKFAGFMTVKFLRLQSLYKVQMNKNRELSSVSADVLDCVNRKLGYWVRRESHGKNYVVNYHPSENETSIFKRRELLEETSNLAAMPAPDTPSPSPEIITIVFPRSSGSFPALTNAKKRIPPLIPPSSPPPLPTNNTIASDPPRKFEEKSKGFKDVWLYVVIGVAAFVAMLIIVAVIFFFRKRAVKSIGPWKTGLSGQLQKAFVTGVPKLNRSELETACEDFSNIIEAFDGYTVYKGTLSSGVEIAVASTAILETREWTRAMEMTYRRRIDTMSRVNHKNFINLIGYCEEDEPFNRMMVFEYAPNGTLFEHLHDKEMEHLDWNARTRIIMGTAYCLQYMHELNPPISHTKLVSSAIYLTDDYAAKVGEVPFSGQTGSKPRKPMSGDLDQSLLPLPPEPETNVYSFGVLMLEIISGKLSDSEEEGSILKWASKYLENDNLRDMIDPTLTTYKEEELEAICDVARHCLKLDESQRPKMKYVVQQLKEVINISQEQATPRLSPLWWAELEILSSEAT
Protein: Pyridoxal phosphate binding protein (E5RFX7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVIEAYGHGQRTFGENYVQELLEKASNPKILSLCPEIKWHFIGHLQKQNVNKLMAVPNLFMLETVDSVKLADKVNSSWQRKGSPERLKVMVQINTSGEESKHGLPPSETIAIVEHINAKCPNLEFVGLMTIGSFGHD
Protein: Phosphodiesterase (EC 3.1.4.-) (A0A8I6A5M3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDEYVTIRKKHLQRPIFRLRCLVKQLEKGDVNVVDLKKNIEYAASVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRSIVHAVQAGIFVERMYRKNYHMVGLTYPAAVIVTLKEVDKWSFDVFALNEASGEHSLKFMIYELFTRYDLINRFKIPVSCLIAFAEALEVGYSKHKNPYHNLVHAADVTQTVHYIMLHTGIMHWLTELEILAMVFAAAVHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLMQEEEMNILVNLSKDDWRDLRNLVIEMVLATDMSGHFQQIKNIRSSLQQPEGIDRAKTMSLILHAADISHPAKTWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGFIDFIVEPTFSLLTDSTEKIVIPLIEEASKPESSNYGASSSSTMIGFHVADALRRSNTKGCMSDGTYAPDYSLSAVDLKSFKNNLVDIIQQNKERWKELAAQGELDLHKNSEDLEEKHADTHP
Protein: tRNA-splicing ligase RtcB (EC 6.5.1.8) (3'-phosphate/5'-hydroxy nucleic acid ligase) (tRNA ligase RtcB) [Cleaved into: Pho hyp2 intein (EC 3.1.-.-)] (O59245)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Essential for tRNA splicing and maturation (Probable). Acts by directly joining spliced tRNA halves to mature-sized tRNAs. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends.
Interaction partners:
- Protein archease
- RNA 3'-terminal phosphate cyclase
- Probable RNA 2'-phosphotransferase
- Translation initiation factor 1A
- RNA 2',3'-cyclic phosphodiesterase
- Translation initiation factor 2 subunit alpha
- Polyribonucleotide 5'-hydroxyl-kinase PH0197
- DNA ligase
- 455aa long hypothetical phospho-sugar mutase
- Ribonuclease P protein component 4
Sequence:
MVVPLKRIDKIRWEIPKFDKRMRVPGRVYADEVLLEKMKNDRTLEQATNVAMLPGIYKYSIVMPDGHQGYGFPIGGVAAFDVKEGVISPGGIGYDINCLAPGTRVLTEHGYWLKIEEMPEKFKLQRLRVYNIEEGHNDFSKVVFVAEREVGSEEKAIRIVTESGKVIEGSEDHPVLTPEGYVYLRNVKEGDYILVYPFEGVPYEEKKGVILDESAFEGEDPQVVKFLRERNLIPLQWKDPKVGILARILGFALANGYISENDNLTFHGKEEVLREVRKDLEELGIEAIVAEEDKLKVTSREFAFLLEKLGMAHDSIPEWIIEGPLWIKRNFLAGLFGANGSIVEFKGDVPLPITLTHSRELLNDVSRILEGFKVRAKIKMGKNGSYQLVIEDEDSIRNFLGRINYEYDPEKKARGLIAYAYLKFKELMKGNLMTFEEFARDRGYEGGFVAEKVIEVKSVKPEYDKFYDIGVYHSAHNFIANGIVVHNCGVRLIRTNLTEKEVRPRIKQLVDTLFKNVPSGVGSQGRIKLHWTQIDDVLVDGAKWAVDNGYGWERDLERLEEGGRMEGADPEAVSQRAKQRGAPQLGSLGSGNHFLEVQVVDKIFDPEVAKAYGLFEGQVVVMVHTGSRGLGHQVASDYLRIMERAIRKYRIPWPDRELVSVPFQSEEGQRYFSAMKAAANFAWANRQMITHWVRESFQEVFKQDPEGDLGMDIVYDVAHNIGKVEEHEVDGKRVKVIVHRKGATRAFPPGHEAVPRLYRDVGQPVLIPGSMGTASYILAGTEGAMKETFGSTCHGAGRVLSRKAATRQYRGDRIRQELLNRGIYVRAASMRVVAEEAPGAYKNVDNVVKVVSEAGIAKLVARMRPIGVAKG
Protein: Secondary metabolism regulator laeA (Methyltransferase laeA) (EC 2.1.1.-) (Velvet complex subunit laeA) (Q4WRY5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Methyltransferase that performs automethylation (By similarity). No other methyl-accepting substrate has been identified yet (By similarity). Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression. Positively controls expression of 20% to 40% of major classes of secondary metabolite biosynthesis genes such as nonribosomal peptide synthetases, polyketide synthases, and P450 monooxygenases. Controls the expression of the gliotoxin gene cluster. Controls the expression of the fumitremorgin, fumagillin, and pseurotin gene clusters, where genes for fumagillin and pseurotin are physically intertwined in a single supercluster. Regulates the biosynthetic genes required for endocrocin production. Secondary metabolites under the transcriptional regulation of laeA are necessary for inhibition of angiogenesis during invasive infection in mice. Controls the expression of cell surface rodA, a hydrophobin that acts as an antiphagocytic molecule. Regulates also the expression of genes involved in conidial biosynthesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:C8VQG9}.
Interaction partners:
- Developmental and secondary metabolism regulator veA
- C2H2 type master regulator of conidiophore development brlA
- Velvet complex subunit B
- pH-response transcription factor pacC/RIM101
- Velvet domain-containing protein
- Probable DNA-binding protein creA
- Conidiophore development regulator abaA
- Orotidine 5'-phosphate decarboxylase
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Cell pattern formation-associated protein stuA
Sequence:
MFLNGQGGQRPPMVAFPPLNVRGSISSGFNALGRSRNNSDAMDIYTITDRGPAAERDPAAGRWHANGSPSINSTSSKNPDRYPCYQENGRTYHGYRKGIYMLPCDEQEQDRLDIFHKLFTVARVSDGLIYAPHPTNGRFLDLGCGTGIWAIDVANKYPEAFVVGVDLAPIQPPNHPRNCDFYAPFDFESLWALGEDSWDLIHMQMGSGSVASWPNLYRRIYSHLRPGAWFEQVEIDFEPRCDDRSLEGLAIRQWYQLLKQATEETMRPVAHNSRETIRNLQEAGFTEIDHQMVGLPLNPWHEDEHERRVARWYNLAISESIETMSLAPFSRVFGWPIERIKQIAADVKSEAFNKEIHTYNILHIYQARKPLAN
Protein: DNA damage checkpoint control protein RAD17 (DNA repair exonuclease RAD17) (P48581)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Associates with sites of DNA damage and modulates the MEC1 signaling pathway and the activation of RAD53 in response to DNA damage at phase G1. The complex also physically regulates DNA polymerase zeta-dependent mutagenesis by controlling the access of polymerase zeta to damaged DNA. Contrary to its human counterpart, the 9-1-1 complex, the checkpoint clamp complex shows no detectable exonuclease activity.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA damage checkpoint control protein MEC3
- DNA damage checkpoint protein 1
- Checkpoint protein RAD24
- Serine/threonine-protein kinase MEC1
- DNA repair protein RAD9
- Replication factor C subunit 2
- Replication factor C subunit 4
- Replication factor C subunit 3
- DNA repair protein RAD51
- Replication factor C subunit 5
Sequence:
MRINSELANKFSASTVHLEHITTALSCLTPFGSKDDVLIFIDADGLSFVRENNHVIKIQLLLSRELFMSYSYRNETEDHMKLCVKINHILDSVSVMNRNSDDIVECTLSYDGHGSPFVLIFEDSFISERVEYSTYLIKDFDTNGLELDRERISFEAIIKGEALHSALKDLKEIGCKECYVYAKTEANDENVFALISKSQLGFSKIKLPSNRSILEKLQVFDGDSTTVIDGFAVIGFFDFTSFDKIRKSTKIASKVLFRMDVHGVLSVNILSQTDDVIITDTTRPSNNRPGSIRQLQLPKDYPGIVIEVCMLEKESIDEAAQTEIELLMETNELGNRNSFKKSTIRKRYGTDKGNETSNDNLLQLNGKKIKLPSEEENNKNRESEDEENHCKYPTKDIPIFF
Protein: Interferon alpha 2 (Q1A3D7)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MYTMQSWTCIFLIICSMQSVYHCCDWIRHHYGHLSSEYLSLLDQMGGDITKQDAPVFFPTSLYRHIDDGEVEDKVRFLKETIYQITKLFDGNMKSVTWDKKNLDDFLNILERQLENLNSCLSPAMKPERRLKRYFKKLNKNVLRKMNYSAQAWELIRKETKRHLQRLDILAAQMY
Protein: Ciliary microtubule inner protein 2B (A8MTA8)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A2AIP0}.
Interaction partners:
- Cilia- and flagella-associated protein 161
- EF-hand domain-containing family member C2
- Piercer of microtubule wall 1 protein
- Meiosis-specific nuclear structural protein 1
- Piercer of microtubule wall 2 protein
- EF-hand domain-containing protein 1
- Tektin-3
- Cilia- and flagella-associated protein 53
- Cilia- and flagella-associated protein 52
- Tektin-1
Sequence:
MAVASTFIPGLNPQNPHYIPGYTGHCPLLRFSVGQTYGQVTGQLLRGPPGLAWPPVHRTLLPPIRPPRSPEVPRESLPVRRGQERLSSSMIPGYTGFVPRAQFIFAKNCSQVWAEALSDFTHLHEKQGSEELPKEAKGRKDTEKDQVPEPEGQLEEPTLEVVEQASPYSMDDRDPRKFFMSGFTGYVPCARFLFGSSFPVLTNQALQEFGQKHSPGSAQDPKHLPPLPRTYPQNLGLLPNYGGYVPGYKFQFGHTFGHLTHDALGLSTFQKQLLA
Protein: Oskyddad, isoform A (Oskyddad, isoform C) (RE14039p) (Q86P18)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- RH01747p
Sequence:
MDAAADGVPPTAPAATATTANSDLDLAARRRLFISQPSTLATRRQQAVCVRRAHKMYGSSKNPNVVLDGLNMTVPKGSIYGLLGASGCGKTTLLSCIVGRRRLNSGEIWVLGGRPGSRGSGVPGPRIGYMPQEIALYGEFTMRETLIYFGIISAMSKGDIEDRTEFLLKLLNLPNASKFVKNLSGGQQRRVSLAVALLHEPELLILDEPTVGVDPVLRQSIWDHLVDITKNGHTTVIITTHYIDECAQAHMIGLLRGGKMLAEESPDYLRQQYNADSLEDVFLKLSVLQNMGKRRRSSIAQEIVEQVTVPAISNPALDMSDEQHAAEISGEFGDNISMSSAARDPISTTAPAAPPLPPPQEIPTSFWYNLHVMQSHHLHALIWKNFLWMMRNVGVMLFIVGLPVVQILLFCYAIGHDPTGLKLAVANHEMSGEMIMEQFCPVHTGCNQTMLSCRYLDMLVKNKSMVVQYVTDDEMAYEEVRKGRAWAALVIQPNYTASLMERVEDGRYAEDGTIESSDLAVRMDWSNQQISQLLYRDLQYTFFNFVGDMLSDCDVNPKLGRVPVDFQHPVYGYRNPNFTDFAAPGVILTIIFFLAVAVTSGAMLIDRNEGMLERCLVAGITGPEILLSQVVTQFTVMLSQTTFVLIVSFYFFELTLVGNIWLVVALCILNGLCGMSFGFVISCAVDTERTATYVAMGSFLPIVMLCGIIWPIEGMFPLLQFFTAFLPLTKPTESMRSILQRGWGIDNPVVYNGFISISSWVLVFLVLTILLLKFKKG