wanglab/gogpt-training-data huggingface dataset:
Protein: Activin receptor type-1-like (EC 2.7.11.30) (Serine/threonine-protein kinase receptor R3) (SKR3) (TGF-B superfamily receptor type I) (TSR-I) (P80203)
Organism: Rattus norvegicus (Rat)
Function: Type I receptor for TGF-beta family ligands BMP9/GDF2 and BMP10 and important regulator of normal blood vessel development. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. May bind activin as well.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P37023}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Bone morphogenetic protein 10
- Growth/differentiation factor 2
- Bone morphogenetic protein receptor type-2
- Transforming growth factor beta-3 proprotein
- Endoglin.
- Activin receptor type-2A
- TGF-beta receptor type-2
- Activin receptor type-1
- Transforming growth factor beta-1 proprotein
- Bone morphogenetic protein 4
Sequence:
MTLGIFRRVFLMLSVALGLTKGDLVKPSRGQLVNCTCENPHCKRPICQGAWCTVVLVREQGRHPQVYRGCGSLNQELCLGRPTEFVNHHCCYRSFCNHNVSLMLEATQTPSEEPEVDAHLPLILGPVLALLVLVALGTLGLWRVRRRQEKQRGLHSDLGESSLILKASEQGDSMLGDFLVSDCTTGSGSGLPFLVQRTVARQVALVECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSLYDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYLDIGNNPRVGTKRYMAPEVLDEQIRTDCFESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPNDPSFEDMKKVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKLSQNPEKPKVIH
Protein: Interferon alpha/beta receptor 1 (IFN-R-1) (IFN-alpha/beta receptor 1) (Cytokine receptor class-II member 1) (Cytokine receptor family 2 member 1) (CRF2-1) (Type I interferon receptor 1) (P17181)
Organism: Homo sapiens (Human)
Function: Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response. Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another. The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors. STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes. Can also act independently of IFNAR2: form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (By similarity).
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:18056411, ECO:0000269|PubMed:2153461, ECO:0000269|PubMed:35442418, ECO:0000305|PubMed:7665574}; Single-pass type I membrane protein {ECO:0000305}. Late endosome {ECO:0000269|PubMed:18056411, ECO:0000305|PubMed:14532120}. Lysosome {ECO:0000269|PubMed:18056411, ECO:0000305|PubMed:14532120}. Note=Interferon binding triggers internalization of the receptor from the cell membrane into endosomes and then into lysosomes. {ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:18056411}.
Interaction partners:
- Interferon alpha-2
- Non-receptor tyrosine-protein kinase TYK2
- Interferon beta
- Interferon alpha/beta receptor 2
- Tyrosine-protein kinase JAK1
- Signal transducer and activator of transcription 2
- Interferon alpha-1/13
- Signal transducer and activator of transcription 1-alpha/beta
- Interferon epsilon
- Interferon kappa
Sequence:
MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSKIWLIVGICIALFALPFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDSGNYSNEDESESKTSEELQQDFV
Protein: Alcohol dehydrogenase 2 (EC 1.1.1.1) (Alcohol dehydrogenase II) (ADH II) (P54202)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Pyruvate decarboxylase
- Pyruvate decarboxylase
- catechol O-methyltransferase
- catechol O-methyltransferase
- Amine oxidase
- catechol O-methyltransferase
- monoamine oxidase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase ALDH
Sequence:
MAAPEIPKKQKAVIYDNPGTVSTKVVELDVPEPGDNEVLINLTHSGVCHSDFGIMTNTWKILPFPTQPGQVGGHEGVGKVVKLGAGAEASGLKIGDRVGVKWISSACGQCPPCQDGADGLCFNQKVSGYYTPGTFQQYVLGPAQYVTPIPDGLPSAEAAPLLCAGVTVYASLKRSKAQPGQWIVISGAGGGLGHLAVQIAAKGMGLRVIGVDHGSKEELVKASGAEHFVDITKFPTGDKFEAISSHVKSLTTKGLGAHAVIVCTASNIAYAQSLLFLRYNGTMVCVGIPENEPQAIASAYPGLFIQKHVHVTGSAVGNRNEAIETMEFAARGVIKAHFREEKMEALTEIFKEMEEGKLQGRVVLDLS
Protein: Zinc finger protein 34 (E9PNZ6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAALFLSAPPQAEVTFEDVAVYLSREEWGRLGPAQRGLYRDVMLETYGNLVSLALGTRTEYKELTSQETFGEEDPQGSEPVEACDHISKSEGSLEKLVEQRGPRAVTLTNGESSRESGGNLRLLSRPVPDQRPHKCDICEQSFEQRSYLNNHKRVHRSKKTNTVRNSGEIFSANLVVKEDQKIPTGKKLHYCSYCGKTFRYSANLVKHQRLHTEEKPYKCDECGKAFSQSCEFINHRRMHSGEIPYRCDECGKTFTRRPNLMKHQRIHTGEKPYKCGECGKHFSAYSSLIYHQRIHTGEKPYKCNDCGKAFSDGSILIRHRRTHTGEKPFECKECGKGFTQSSNLIQHQRIHTGEKPYKCNECEKAFIQKTKLVEHQRSHTGEKPYECNDCGKVFSQSTHLIQHQRIHTGEKPYKCSECGKAFHNSSRLIHHQRLHHGEKPYRCSDCKKAFSQSTYLIQHRRIHTGEKPYKCSECGKAFRHSSNMCQHQRIHLREDFSM
Protein: DNA replication licensing factor MCM3 (EC 3.6.4.12) (A0A499FHX9)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368061}.
Interaction partners:
Sequence:
MLICSQGPRLFLEVTFGGGKSSEVFAPGWSHPGNLHATLVEVVLWQRAWRVPWCWTMWSCGRLREITWTSWTTRLLNNAFEELVAFQRALKDFVASIDATYAKQYEEFYVGLEGSFGSKHVSPRTLTSCFLSCVVCVEGIVTKCSLVRPKVVRSVHYCPATKKTIERRYSDLTTLVAFPSSSVYPTKDEENNPLETEYGLSVYKDHQTITIQEMPEKAPAGQLPRSVDVILDDDLVDKAKPGDRVQVVGTYRCLPGKKGGYTSGTFRTVLIACNVKQMSKDAQPSFSAEDIAKIKKFSKTRSKDIFDQLAKSLAPSIHGHDYVKKAILCLLLGGVERDLENGSHIRGDINILLIGDPSVAKSQLLRYVLCTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDMDRTAIHEVMEQGRVTIAKAGIHARLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFIMLDQMDPEQDREISDHVLRMHRYRAPGEQDGDAMPLGSAVDILATDDPNFSQEDQQDTQIYEKHDNLLHGTKKKKEKMVSAAFMKKYIHVAKIIKPVLTQESATYIAEEYSRLRSQDSMSSDTARTSPVTARTLETLIRLATAHAKARMSKTVDLQDAEEAVELVQYAYFKKVLEKEKKRKKRSEDESETEDEEEKSQEDQEQKRKRRKTRQPDAKDGDSYDPYDFSDTEEEMPQVHTPKTADSQETKESQKVELSESRLKAFKVALLDVFREAHAQSIGMNRLTESINRDSEEPFSSVEIQAALSKMQDDNQVMVSEGIIFLI
Protein: HEAT repeat-containing protein 5B (O01485)
Organism: Caenorhabditis elegans
Interaction partners:
- GOST seven transmembrane domain-containing protein
- Uncharacterized Golgi apparatus membrane protein-like protein C34D4.4
- AP-1 complex subunit gamma
- Uncharacterized protein T28D9.1
Sequence:
MDETHSLLLNEEALEACPEQKRPVFIYEWLRYLDRILPITQREDLKNVQKELQQQLESRLHTVVGPPTRKLIARCIGRVYALTGDIVSLNTLLNSCNDTLKVKDESPKAVQSKLAALACLSAVYDSMGRMAGRSIEDTLAIVKNWMSTAVAHSQAHIMNTLTSMVKALGSGDYVTHKKIHSIAKNSLQDRTLCKTPNVKIASLECLTALVQFHTPIYTTELEASCTMCIKILEGSTYELRCAVAKFTAQLLATSMKPPPGAVIKAKSNQTVPVRPASVTDTLNLLASGFLRGGIGGFLKGSSSTFSTMGRSDIRIGVSICYVEMVREMGSAWLEKHLIAVCCHMVDLASKCGHLAYTQNASHVSEALTIRRCISFILRQTIGSLLGENAQTLACKHLGVLLSQYVDLVSIGTGDNLDSSVDSSDYGSGYAIIVILQEISVLVRQIGTSVMSLFTEATGIMEHIFKCLTHPLASARYAAAWCLRCIATAVPNLMTPLIDRCLPRLDQLSSSSRAISGFSMALSALLAASTDSSKLGIPYAKPLKVLDLAEEMLRTSTQQPKLTIAKLESGWNLIYALIHLGPSVMKEHLPRVIKLWKAAFARSAKEAESENSRGDAFSWQCAMIAQAGALSVMEAVASQPELSSTNNALDAMKVPIECSLVMMSQVGNLIKSYGNEMRQANSVVRIRLYRLLLLLPHKSFEGSYAALLRELVADITLSDNSQSTLTTSLPISQFTGVEKILISPVYDATDYSMVEDLLQTPISSVSLGNIEEDLSNLIRASASQIGDTWPENDSEPLTCLNTALLTYGKVFPLVNNKHKVQITEHFWDTIQKSKNAGRKQAILVNALTAKLLSYKTLCEQRGHKLDNETLQRASFDLISSSLSNSCPMTRLVGAEALARLSQAVNSPPFVASIAQYCFDKLNSCKDEINRSGHVLALGCLHRHVGSLGSGQHLNTGVSVVLALAEESKMPKVQTCALVAMALIAETGSGMFRVFVETTLSSCLKLLISTPTFVVDVVQGISKCLTALITCVGPELSCPGVIDGVRTSLLAACAIQLSHSDPFVQAEAISGLQQMHLFAPRYVHMAQLVVDISSLLSSTHLVIRRQSVSCLRQLVQRESKEVRNHAQVLVPQGIVDTNKKKFALPESGLEGALFGMLDTEVNKELRCHLQETLISLVQGTSGELLNNWLMLSKEILATSNDHGLVRKKEEKKDRGEDDADDDDDEDGDDDTNLAGISSLMEEDKGKVQPRWPTKVFTMEIVNRLMSVCDTERAHLDMALAKELQITSAGKNDYLVLHLSDLVRMSFMAATSDNSLLRIAGLKSLEEVIIRFSSCPEPEFPGHMILEQFQAQVGAALRPAFTDDTPSNVTSVACQVCSTWIGSGVARDLSDLKRVHQLLVSSLNKLKHGSINVQLYSESAATLEKLSILKAWAEVYVTAIEQDRMKNENVEARDHYDYNGSGSLLSLVEPEANSLIAYWLAMLNDSALLALPAHYSDQFLNRGGAFFNAHSAEACREYYQICWPPILLACSTWLSKNNFELPSGIELSSETAAVWRDEGNVSRFYLLIGIAVESLSNKTRQIEDETIQMSVKSLTRLLSCEWCQLHLMSDVPAVIEILYVLHRSVLTRDCLSTQLQCIECVGSIIDAAQLAIRICASRDISNGNLESEDTLRKIPNVLFAGEEGGKDGNINKDGVKTISYAILELAVCAIFKQMPQINSAQLKTNSLAALHLRKVGRLPAEGTHLVIKSMQILVQIPSLCSPHSRVTVLPVIMYLLLGFVRESARLDEGSIQTDRAGHLSAIAAAAIQSIRSIVSQQPDDDTAVSWKTIMRNAFYSVLNMSEDNERIQLDKCIIMVTAVVFTTSAPVDVVLGHQESFNKLIVLLKRHLQSDNVSVVMKTLQSLASIFGRKGFGGIFVKHLGKEIMPVVKRYLSKVDCENEKITESDLVILQECVKVIEVLAMSAKDGKRIQVISLLVQLLVRLLRATSHTEWRKVGPIEKKLHEMAIGRLNAAASMWPAEFKKVIEWNNELKTRLESALLLQSTRHAHQISMAKTQEAKTTPVVQQPRIRLTMFGAESN
Protein: Nuclear receptor coactivator 1 (NCoA-1) (EC 2.3.1.48) (Nuclear receptor coactivator protein 1) (mNRC-1) (Steroid receptor coactivator 1) (SRC-1) (P70365)
Organism: Mus musculus (Mouse)
Function: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:8855229}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- Estrogen receptor
- Peroxisome proliferator-activated receptor gamma
- Estrogen receptor beta
- Nuclear receptor coactivator 2
- Retinoic acid receptor RXR-alpha
- Nuclear receptor coactivator 3
- Progesterone receptor
- Nuclear receptor ROR-beta
- Histone acetyltransferase KAT2B
Sequence:
MSGLGDSSSDPANPDSHKRKGSPCDTLASSTEKRRREQENKYLEELAELLSANISDIDSLSVKPDKCKILKKTVDQIQLMKRMEQEKSTTDDDVQKSDISSSSQGVIEKESLGPLLLEALDGFFFVVNCEGRIVFVSENVTSYLGYNQEELMNTSVYSILHVGDHAEFVKNLLPKSLVNGVPWPQEATRRNSHTFNCRMLIHPPEDPGTENQEACQRYEVMQCFTVSQPKSIQEDGEDFQSCLICIARRLPRPPAITGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFFQPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTKCKLCYPQSPDMQPFIMGIHIIDREHSGLSPQDDSNSGMSIPRINPSVNPGISPAHGVTRSSTLPPSNNNMVSARVNRQQSSDLNSSSSHTNSSNNQGNFGCSPGNQIVANVALNQGQAGSQSSNPSLNLNNSPMEGTGIALSQFMSPRRQANSGLATRARMSNNSFPPNIPTLSSPVGITSGACNNNNRSYSNIPVTSLQGMNEGPNNSVGFSAGSPVLRQMSSQNSPSRLSMQPAKAESKDSKEIASILNEMIQSDNSDNSANEGKPLDSGLLHNNDRLSEGDSKYSQTSHKLVQLLTTTAEQQLRHADIDTSCKDVLSCTGTSSSASSNPSGGTCPSSHSSLTERHKILHRLLQEGSPSDITTLSVEPEKKDSVPASTAVSVSGQSQGSASIKLELDAAKKKESKDHQLLRYLLDKDEKDLRSTPNLCLDDVKVKVEKKEQMDPCNTNPTPMTKPAPEEVKLESQSQFTADLDQFDQLLPTLEKAAQLPSLCETDRMDGAVTGVSIKAEVLPASLQPTTARAAPRLSRLPELELEAIDNQFGQPGAGDQIPWANNTLTTINQNKPEDQCISSQLDELLCPPTTVEGRNDEKALLEQLVSFLSGKDETELAELDRALGIDKLVQGGGLDVLSERFPPQQATPPLMMEDRPTLYSQPYSSPSPTAGLSGPFQGMVRQKPSLGAMPVQVTPPRGTFSPNMGMQPRQTLNRPPAAPNQLRLQLQQRLQGQQQLMHQNRQAILNQFAANAPVGMNMRSGMQQQITPQPPLNAQMLAQRQRELYSQQHRQRQIIQQQRAMLMRHQSFGNNIPPSSGLPVQMGTPRLPQGAPQQFPYPPNYGTNPGTPPASTSPFSQLAANPEASLATRSSMVNRGMAGNMGGQFGAGISPQMQQNVFQYPGPGLVPQGEATFAPSLSPGSSMVPMPVPPPQSSLLQQTPPTSGYQSPDMKAWQQGTMGNNNVFSQAVQSQPAPAQPGVYNNMSITVSMAGGNANIQNMNPMMGQMQMSSLQMPGMNTVCSEQMNDPALRHTGLYCNQLSSTDLLKTDADGNQQVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLTE
Protein: RAB11B GTPase (Q9GQM2)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MTNGNSVKVILLGDSAVGKSKLVERFLMQRYVPVQMSTYALTLFHYDFVTEDDEAIDVDIWDTAGQERFSTMHPAYYHEAHACILVFDVTRKATYKNLEKWLGELRNYREHIPCIVACNKIDTDPSVVNKAFAFVEKHNLSLFYVSAADGTNVVQLLESAISEAVKYKKSPKKDDLMSQVLGFIKE
Protein: TRPA1(A) isoform (G9L8C4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MITAPATATERNQSSKSTRMPKLYNGVYSGQCGALSPPDLMEAQPKLLPKPRSNSSGSTGRNSKYWIFSMIIERSAGPKRIEIDGDDADTPLEAILPAEPPAEVCLLRDSPFRILRAAESGNLDDFKRLFMADNSRIALKDAKGRTAAHQAAARNRVNILRYIRDQNGDFNAKDNAGNTPLHIAVESDAYDALDYLLSIPVDTGVLNEKKQAPVHLATELNKVKSLRVMGQYRNVIDIQQGGEHGRTALHLAAIYDHEECARILITEFDACPRKPCNNGYYPIHEAAKNASSKTMEVFFQWGEQRGCTREEMISFYDSEGNVPLHSAVHGGDIKAVELCLKSGAKISTQQHDLSTPVHLACAQGAIDIVKLMFEMQPMEKRLCLSCTDVQKMTPLHCASMFDHPDIVSYLVAEGADINALDKEHRSPLLLAASRSGWKTVHLLIRLGACISVKDAAARNVLHFVIMNGGRLTDFAEQVANCQTQAQLKLLLNEKDSMGCSPLHYASRDGHIRSLENLIRLGACINLKNNNNESPLHFAARYGRYNTVRQLLDSEKGSFIINESDGAGMTPLHISSQQGHTRVVQLLLNRGALLHRDHTGRNPLQLAAMSGYTETIELLHSVHSHLLDQVDKDGNTALHLATMENKPHAISVLMSMGCKLVYNVLDMSAIDYAIYYKYPEAALAMVTHEERANEVMALRSDKHPCVTLALIASMPKVFEAVQDKCITKANCKKDSKSFYIKYSFAFLQCPFMFAKIDEKTGESITTASPIPLPALNTMVTHGRVELLAHPLSQKYLQMKWNSYGKYFHLANLLIYSIFLVFVTIYSSLMMNNIELKAGDNKTMSQYCNMGWEQLTMNLSQNPSVASQIRLDSCEERINRTTAILFCAVVIVVYILLNSMRELIQIYQQKLHYILETVNLISWVLYISALVMVTPAFQPDGGINTIHYSAASIAVFLSWFRLLLFLQRFDQVGIYVVMFLEILQTLIKVLMVFSILIIAFGLAFYILLSKIIDPQPNHLSFSNIPMSLLRTFSMMLGELDFVGTYVNTYYRDQLKVPMTSFLILSVFMILMPILLMNLLIGLAVGDIESVRRNAQLKRLAMQVVLHTELERKLPHVWLQRVDKMELIEYPNETKCKLGFCDFILRKWFSNPFTEDSSMDVISFDNNDDYINAELERQRRKLRDISRMLEQQHHLVRLIVQKMEIKTEADDVDEGISPNELRSVVGLRSAGGNRWNSPRVRNKLRAALSFNKSM
Protein: Sporozoite threonine and asparagine-rich protein (Q8IC44)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Gametocyte-specific protein
Sequence:
MIHIFYRTAIFTLSIWTTLLYSNKNLKCNFYYNNNNLSTYVIKHNRFLSEYQSNFLGGGYSAALKLVNSKKSGTNVNTKYNSENTNTNNNIPESSSTYTNTRLAANNSTTTSTTKVTDNNKTNIKLTGNNSTTINTNSTENTSATKKVTENVITNQILTGNNNTTTNTSTTEHNNNINTNTNSTENTSATKKVTENVITNQILTGNNNTTTNTSTTEHNNNINTNTNSTDNSNTNTNLTDNTSTTKKLTDNINTTQNLTTSTNTTTVSTDNNNINTKPIDNNNTDIKSTDNYNTGTKETDNKNTDIKATDNNNITTTTDNTNTNVISTDNSKTNVISTDNSKTNTISTDNDNADTILTDNDNNTDIILTDNNNTDTISTDNDNADTKATDNNNNTNTKATDNNNTKIISPDNNNTKTTSTDNNNNTNTKATDNNNTKTISNDNNNTKTISTDNNNTKTISNDNNNTNTISTDNNNNNTNQYVFANNYNETTSDDELNKDSCDYSEEKENIKSMINAYLDKLDLETVRKIHSDISTCIEKKNNPRNQITHLNNLKNMYNIIKFIVVIYIAFNWSEVIYKYVGKLILAFALYMLIN
Protein: PRL-1 phosphatase (EC 3.1.3.48) (Phosphatase of regenerating liver-1) (O61722)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable phosphatase (Probable). Inhibits growth possibly by negatively regulating Src64B-induced growth. Regulates central nervous system circuit formation and stabilization of synapse-dense terminal arbors. In dorsocentral neurons, regulates synaptogenesis in terminal arbors via modulation of the insulin receptor pathway, likely upstream of Akt1, and via reduction of PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) levels. In the nervous system, plays a protective role together with uex in response to olfactory carbon dioxide stimulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23577193}. Cell membrane {ECO:0000269|PubMed:23577193, ECO:0000269|PubMed:31404830}; Lipid-anchor {ECO:0000250|UniProtKB:Q93096}. Apicolateral cell membrane {ECO:0000269|PubMed:23577193}. Cell projection, axon {ECO:0000269|PubMed:31048465}. Note=During embryogenesis localizes to cytoplasmic compartments from 1 to 14 hours after egg laying, thereafter becomes associated with the plasma membrane (PubMed:23577193). Localizes to contralateral axon collaterals of dorsocentral neurons (PubMed:31048465). {ECO:0000269|PubMed:23577193, ECO:0000269|PubMed:31048465}.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta
- Unextended protein
Sequence:
MSITMRQKDLRPAPALIEYKGMKFLITDRPSDITINHYIMELKKNNVNTVVRVCEPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEWFEVLKDKYQQNPEACVAVHCVAGLGRAPVLVALALIELGLKYEAAVEMIRDKRRGAINAKQLSFLEKYKPKARLKHKNGHKNSCSVQ
Protein: Beta-1,3-galactosyltransferase 6 (Beta-1,3-GalTase 6) (Beta3Gal-T6) (Beta3GalT6) (EC 2.4.1.134) (GAG GalTII) (Galactosyltransferase II) (Galactosylxylosylprotein 3-beta-galactosyltransferase) (UDP-Gal:betaGal beta 1,3-galactosyltransferase polypeptide 6) (Q96L58)
Organism: Homo sapiens (Human)
Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-linked galactose residue. Has a preference for galactose-beta-1,4-xylose that is found in the linker region of glycosaminoglycans, such as heparan sulfate and chondroitin sulfate. Has no activity towards substrates with terminal glucosamine or galactosamine residues.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11551958, ECO:0000269|PubMed:29443383}; Single-pass type II membrane protein {ECO:0000269|PubMed:11551958}.
Interaction partners:
- Beta-1,4-galactosyltransferase 7
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- Xylosyltransferase 1
- Xylosyltransferase 2
- Ubiquitin-conjugating enzyme E2 J2
- Carbohydrate sulfotransferase 14
- Glycosaminoglycan xylosylkinase
Sequence:
MKLLRRAWRRRAALGLGTLALCGAALLYLARCAAEPGDPRAMSGRSPPPPAPARAAAFLAVLVASAPRAAERRSVIRSTWLARRGAPGDVWARFAVGTAGLGAEERRALEREQARHGDLLLLPALRDAYENLTAKVLAMLAWLDEHVAFEFVLKADDDSFARLDALLAELRAREPARRRRLYWGFFSGRGRVKPGGRWREAAWQLCDYYLPYALGGGYVLSADLVHYLRLSRDYLRAWHSEDVSLGAWLAPVDVQREHDPRFDTEYRSRGCSNQYLVTHKQSLEDMLEKHATLAREGRLCKREVQLRLSYVYDWSAPPSQCCQRREGIP
Protein: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I) (3-beta-HSD I) (3-beta-hydroxy-5-ene steroid dehydrogenase) (3-beta-hydroxy-Delta(5)-steroid dehydrogenase) (EC 1.1.1.145) (3-beta-hydroxysteroid 3-dehydrogenase) (EC 1.1.1.270) (Delta-5-3-ketosteroid isomerase) (Dihydrotestosterone oxidoreductase) (EC 1.1.1.210) (Steroid Delta-isomerase) (EC 5.3.3.1) (P22071)
Organism: Rattus norvegicus (Rat)
Function: A bifunctional enzyme responsible for the oxidation and isomerization of 3beta-hydroxy-Delta(5)-steroid precursors to 3-oxo-Delta(4)-steroids, an essential step in steroid hormone biosynthesis. Specifically catalyzes the conversion of pregnenolone to progesterone, dehydroepiandrosterone (DHEA) to 4-androstenedione, and androstenediol to testosterone. Additionally, catalyzes the interconversion between 3beta-hydroxy and 3-oxo-5alpha-androstane steroids controlling the bioavalability of the active forms. Specifically converts dihydrotestosterone to its inactive form 5alpha-androstanediol, that does not bind androgen receptor/AR. Also converts androstanedione, a precursor of testosterone and estrone, to epiandrosterone. Expected to use NAD(+) as preferred electron donor for the 3beta-hydroxy-steroid dehydrogenase activity and NADPH for the 3-ketosteroid reductase activity (Probable).
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
Interaction partners:
Sequence:
MPGWSCLVTGAGGFVGQRIIRMLVQEKELQEVRALDKVFRPETKEEFSKLQTKAKVTMLEGDILDAQYLRRACQGISVVIHTAAVIDVSHVLPRQTILDVNLKGTQNILEACVEASVPAFIYCSTVDVAGPNSYKKIILNGHEEEHHESTWSDAYPYSKRMAEKAVLAANGSILKNGGTLHTCALRPMYIYGERSPFLSVMILAALKNKGILNVTGKFSIANPVYVGNVAWAHILAARGLRDPKKSQNVQGQFYYISDDTPHQSYDDLNCTLSKEWGLRLDSSWSLPLPLLYWLAFLLETVSFLLRPFYNYRPPFNCHLVTLSNSKFTFSYKKAQRDLGYVPLVSWEEAKQKTSEWIGTLVEQHRETLDTKSQ
Protein: Rab guanine nucleotide exchange factor sec2 (GDP-GTP exchange factor sec2) (O13930)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Guanyl-nucleotide exchange factor for ypt2. Catalyzing the dissociation of GDP from ypt2 and promotes the binding of GTP (By similarity).
Interaction partners:
- GTP-binding protein ypt3
- GTP-binding protein ypt2
- Exocyst complex component sec15
- Nuclear control of ATPase protein 2
- Guanine nucleotide exchange factor MSS4 homolog
- UBA domain-containing protein 7
- Serine/threonine-protein kinase ppk35
- Uncharacterized Rab geranylgeranyltransferase C15C4.03
- Sporulation-specific protein 13
- Sporulation-specific protein 2
Sequence:
MPDVSNVRVKPNQHPYEKEVNGKLMSQEEILSQKLVAAIERQAALDDKYATEVHRNEALSERIRELEAKLSAKKSFDEELVKFHNLEEKLQLTETKCRNAESEKSRVENELEDLTSSLFEEANRMVANARKETVASEKRVNQLKKQLVDAETLLSSTQHQLTELKDVMHSMSDSHEQNNALHPPLSRTTSFVADNVSVGSFASSTSGLDILTGTSARESLDAKEISSDKHLNISGERPATFPNPTFIEGSDERRSASSLGHRTNNNQNQLIRFSTQIRSSSTSPPRSPLIISDSPSSSIIHNPHPTHPSASAMNYMNPCFLEFHAFFNYPMKFARSRSAYSTSANYSNTPPRNTVTPSTARSSTLSQNPSSSSNSIPLISRNLRDFSFFKRCLEEDIEPTLRLDHASGLSWLTRRSVFTAILESSLIINPLHSTSLLSSQPCSLCGFNRTQPLRQFEFRSRPDSTSHASCTYCVARLRSVCNFVAFLHQICKGVWSSCSLEKAWDECLKKREAMFLSRVGLAKELEG
Protein: Tail completion protein gp17 (Gene product 17) (gp17) (Head-tail joining protein gp17) (Tail-to-head joining protein) (O48448)
Organism: Bacillus phage SPP1 (Bacteriophage SPP1)
Function: Tail completion protein that caps the tail and interacts with the connector gp16, thereby attaching the tail to the capsid.
Subcellular location: Virion {ECO:0000269|PubMed:25991862}. Note=Forms a thin ring-like structure at the proximal tip of the tail. {ECO:0000269|PubMed:25991862}.
Interaction partners:
Sequence:
MTWKLASRALQKATVENLESYQPLMEMVNQVTESPGKDDPYPYVVIGDQSSTPFETKSSFGENITMDFHVWGGTTRAEAQDISSRVLEALTYKPLMFEGFTFVAKKLVLAQVITDTDGVTKHGIIKVRFTINNN