wanglab/gogpt-training-data huggingface dataset:
Protein: Terpene synthase 3 (PnTPS3) (Copaene synthase) (PnCop) (EC 4.2.3.133) (Germacrene D synthase) (PnGDS) (EC 4.2.3.-) (A0A2R4QKX7)
Organism: Piper nigrum (Black pepper)
Function: Sesquiterpene synthase involved in the biosynthesis of volatile compounds that contribute to the characteristic flavors of black pepper. Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into alpha-copaene and germacrene D.
Interaction partners:
Sequence:
MGFSFVTNAAIAAHMPPSKQEIIRRDAKFHPTIWGDHFIQYLDTPIDPPQKVVERMEELKKQVRAMLRDTNLDISLIDWIQRTGIAYHFEEQIAETLKHVYEASTLTTDSSKYLEHFDLRHIALRFRLSRQQGYHASTDVFKRFMDEGDKFKQSIANDIEGMLSLYEASFMSVKGEAILDEALAFTGKNLEATLPNLTGSLAQQVECALEIPLRRCTDLVKARRSISCYENKNGRNEVVLELAKLDFNLLQAVHQRELALLTSWWNELGASTNLPFTRNRVVELYFWVLEVLSKPEHARAREIMVKSIIMASILDDVYDVYGTLEELQLFTSALERWDLQALEQLPNTIKTAYSIVLRVFKEYEDLLKPHEVYRVGFARKALIPYMNAYFLEAKWFYSHHHPSFEEYMDNALVSCGYPFLFLVSLVGLDEIATKDVFEWAIKRPNIVVAASMICRNRDDIVGHKEEQERGDVPSGVECYTKDHGCTEEEACMALQAMVDDAWKDINCELLHDTSMPKAILMRAVGLARIISILYQYRDGYSDSTHETKAHVTQVLVQPIPL
Protein: Nuclear cap-binding protein subunit 2 (20 kDa nuclear cap-binding protein) (NCBP 20 kDa subunit) (CBP20) (Q93594)
Organism: Caenorhabditis elegans
Function: Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA interference and is required for primary microRNAs (miRNAs) processing. In the CBC complex, ncbp-2 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires ncbp-1 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Nuclear cap-binding protein subunit 1
- Probable small nuclear ribonucleoprotein Sm D2
- Probable small nuclear ribonucleoprotein G
- U1 small nuclear ribonucleoprotein 70 kDa
- Probable small nuclear ribonucleoprotein F
- Splicing factor 3B subunit 3
- PSP proline-rich domain-containing protein
- RRM domain-containing protein
- Probable U2 small nuclear ribonucleoprotein A'
- Serrate RNA effector molecule homolog
Sequence:
MVFDPRTLDNPKEISAYRDQRYQGTVRDQETALRTSCTLYVGNLSYYTKEDQVYELFGRAGDVRRVIMGLDRFKKTPCGFCFVEYYTREDAELALQNISNTRMDDRVIRADWDAGFIEGRQYGRGKHGGQVRDEYRKDYDPERGGYNRAIAQKGGDRQ
Protein: Protein SMALL AUXIN UP-REGULATED RNA 16 (Q9T0J3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the acidification of the apoplast and the facilitation of solutes and water uptake to drive cell expansion (By similarity). Triggers plant growth probably by promoting cell elongation. Regulates branch angles and bending.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FJG1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9FJG1}.
Interaction partners:
- Auxin-responsive protein SAUR63
Sequence:
MAVKRSSKLTQTAMLKQILKRCSSLGKKQCYDEEGLPLDVPKGHFPVYVGEKRTRYIVPISFLTHPEFLILLQQAEEEFGFRHDMGGLTIPCEEVVFLSLTSMIR
Protein: Hylin-b2 (Hy-b2) (P84003)
Organism: Boana lundii (Brazilian tree frog) (Hypsiboas lundii)
Function: Has hemolytic activity against human erythrocytes. May have antimicrobial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:15638808}.
Interaction partners:
Sequence:
FIGAILPAIAGLVGGLINR
Protein: PHD finger protein 21A isoform X9 (PHD finger protein 21Ab) (A0A2R8QB31)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MMELQTLQEALKVEIQVHQKLVAQMKQDPQNADLKKQLHELQAKITALSEKQKKVVEQLRKELLVKQEPDLKPQTFAATTDGKTVLLTAACPASQPISGPPHNQGAPQKTLTVTPVITAKTLPLVLKAATSTMPASMATQRSAVAMVTAINNPTRPGANSDSQSTPINLQMASKLPNQDTDAGTRIVSKNVIVVRPKPPTPINVPIAPAPPPPMVAAPLIQRPLMLTTKLTSSLPASAGPIHQVRIVNGQQCTTIDKTTTTVTGTTQLAGIVISPAQTLQISNLNSDLKTVKPQGGPEQVVIKTPPSSSPPLPPPPAKVKREESPQKLAFMVSLGLVTHDHLEEIQSRRQERKRRTTANPVYSGAVFEPERKKSAVTYLNTPLHQGTRKRGRPPKYSTTTTTTTSSSTAVPELGCNPLLSPTSSLPASPAPERPDTGGFPLSVHPHSVPQPSPSSGDGDIHEDFCTVCRRSGQLLMCDTCSRVYHLDCLDPPLKNIPKGMWICPKCQDQILKKEEAIPWPGTLAIVHSYIAYKEAKEEEKQKLMKWSAELKLEREQLEQRVKQLSNSITKCMETKNSILARQKDMQASLEKVKHLVRLIQSFNFTQPMETETLKDSKQDCAESGSIKDSKDTTQVCVQESPTEPSVQVPAAVAVPEVKAEPEVGEMAEPAAAVTPEAVSGESGVSVLEVPKTTVDEDMMDTAKTVEPVESPQVRDVKTNGGTDCVCTGLNPEEESTVDAVDSENIPPIDSSCAEDAGKMEVELQEDGSHGMNTNNGKTSEPSQQALPAPLSSVDNPK
Protein: MLLT6 protein (MLLT6, PHD finger containing) (Q6P2C6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKEMVGGCCVCSDERGWAENPLVYCDGHACSVAVHQACYGIVQVPTGPWFCRKCESQERAARVRCELCPHKDGALKRTDNGGWAHVVCALYIPEVQFANVLTMEPIVLQYVPHDRFNKTCYICEEQGRESKAASGACMTCNRHGCRQAFHVTCAQMAGLLCEEEVLEVDNVKYCGYCKYHFSKMKTSRHSSGGGGGGAGGGGGSMGGGGSGFISGRRSRSASPSTQQEKHPTHHERGQKKSRKDKERLKQKHKKRPESPPSILTPPVVPTADKPRRGHQSPTNHGIGSLGCCLPDTPICLCPEGLSPGLLSAESGGRHSGLLSKF
Protein: Rad17 (Q76F78)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGSAAGRQLAPAEQVTDWFAHSFDDFIGSTDISSSVIPQKSLKGNSGRNHQQKKGLSAVPGCSKSKVLSRKRAKLSSVDLPCSKSRQNWDQPQDEPWVDKYKPETQNDLAVQKKKIEEVETWLKMHIFQRQPKQDGCVLLLTGPAGCGKTATVQILAKDLGVQVQEWTNPISLDFTKEDLRNISGHNSNSHTFPSQAQAALFQDFLLRANKYNKLQMLGESSENDKKLILIEDMPNQFYRDPSSLHEILRRFVRTSRCPLIFIISDNFSGDSNQRLLFPKEILEELCISIISFKPVAPTNMMKVLNRIATAEANMNREKNYAPDRASLELLCKGCSGDIRSAINSLQFFSMKDCSLEKDFWSRKKRSSTLKSETAAAMCSLRKKSKSDISEDQAIQAIGGKDASIFLFHALGKIIYCKREPLSESEFPQLPSHLLEHHRDTLLIHPEDIVEKSHMSGSMFNLYLHQNYVEFFTDIDDVVRASEYLSTADVLCGNWNSRLVMEEYSTSVSTRGVIHSNTSRAFAHCQGGMGFRPLHKPQWFFINSKYQENCAAAKSLFSSFCLSPECLQTELLPYLAKLANPMRNEAQIAFIQDIGRLPLKRHVGRFKLDMLTDKDPGVPDLLVGYEEDPAGMHAAEVAVQMEENRTNENDWDGLPLSSSQRSGSELPCSQPQPVATQVAMEEDELNIEEYDSD
Protein: Protein kinase superfamily protein (F4JFM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAALLASQSCCYGGETARVTKAIGFSSSLENHFTGEATQCYGSKSKRFRIEMRQSELPSKVGINGRSVKMVPASEVVKRKDGVNGSAGKGVNGASLVSSRNINGAASTLVKAPKKTTESYLPPPVEGVRVLPSDEGFSWADENYSSLQRSIDVWSFVISLRIRILFDNSKWAYVGGFTEEKQKSRRRETASWLRESVLQLGPTFIKLGQLSSTRSDLFPREFVDELSKLQDRVPAFSPEKAKRFIEAELGAPISVMYKEFEEQPIAAASLGQVHRAVLHNGEKVVVKVQRPGLKKLFDIDLRNLKLIAEYFQKSESFGTNDWVGIYEECALILYQEIDYINEAKNADRFRRDFRNINWVRVPLVYWDYSAMKVLTLEYVPGVKINNLDALAARGFNRSRIASRAIEAYLIQILKTGFFHADPHPGNLAIDVDESIIYYDFGMMGEIKTFTRKRLLDLFYSVYEKDAKKVMQNLIDLEALQPTGDLSSVRRSVQFFLDNLLSQSPDQQQTLAAIGEVPIKTVPEKEAELYLYVVLTLKNSSFLWQDLFAISQDQPFRFPSTFTFVIRAFSTLEGIGYILDPEFSFVKVAAPYAQELLDLKQRQRSGTQLVQEIRKQADDARSSTLSMPYRVQRIEEFVKELDSGDLKLRVRVLESERAARKATILQMATMYTVLGGTLLNIGVTFSNQGSQLVANGSFIGAGIFMLLVLRSMQRVNKLDKFEKMI
Protein: Small ribosomal subunit protein uS2 (37 kDa laminin receptor precursor) (37LRP) (37 kDa oncofetal antigen) (37/67 kDa laminin receptor) (LRP/LR) (40S ribosomal protein SA) (67 kDa laminin receptor) (67LR) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40) (OFA/iLRP) (P14206)
Organism: Mus musculus (Mouse)
Function: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA (By similarity). Enables malignant tumor cells to penetrate laminin tissue and vessel barriers. Activates precursor thymic anti-OFA/iLRP specific cytotoxic T-cell. May induce CD8 T-suppressor cells secreting IL-10.
Subcellular location: Cell membrane. Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus. Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus. Colocalizes with PPP1R16B in the cell membrane (By similarity). 37LRP shuttles to the nucleus upon midkine (MDK) binding. {ECO:0000255|HAMAP-Rule:MF_03016}.
Interaction partners:
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein eS10
- Small ribosomal subunit protein uS7
- Elongation factor 2
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL14
Sequence:
MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTAAQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTEWS
Protein: Spermidine hydroxycinnamoyl transferase (AtSHT) (EC 2.3.1.-) (BAHD-like hydroxycinnamoyl transferase) (O64470)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydroxycinnamoyl transferase involved in the conjugation of feruloyl CoA to spermidine. Catalyzes the three conjugating steps required for the biosynthesis of N(1),N(4),N(8)-triferuloyl-spermidine. Spermidine is the only acceptor substrate while feruloyl CoA > caffeoyl CoA > coumaroyl CoA > cinnamoyl CoA >> sinapoyl CoA are efficient acyl donors. No activity with hydroxyferuloyl CoA. Required for the biosynthesis of these conjugated spermidine derivatives, specifically in anther tapetum.
Interaction partners:
- Cinnamoyl-CoA reductase 2
- Cinnamoyl-CoA reductase 1
- Caffeoyl-CoA O-methyltransferase 1
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Putative caffeoyl-CoA O-methyltransferase At1g67980
- Probable caffeoyl-CoA O-methyltransferase At4g26220
- Cytochrome P450 98A3
- Trans-cinnamate 4-monooxygenase
- Chalcone synthase
- 4-coumarate--CoA ligase-like 1
Sequence:
MAPITFRKSYTIVPAEPTWSGRFPLAEWDQVGTITHIPTLYFYDKPSESFQGNVVEILKTSLSRVLVHFYPMAGRLRWLPRGRFELNCNAEGVEFIEAESEGKLSDFKDFSPTPEFENLMPQVNYKNPIETIPLFLAQVTKFKCGGISLSVNVSHAIVDGQSALHLISEWGRLARGEPLETVPFLDRKILWAGEPLPPFVSPPKFDHKEFDQPPFLIGETDNVEERKKKTIVVMLPLSTSQLQKLRSKANGSKHSDPAKGFTRYETVTGHVWRCACKARGHSPEQPTALGICIDTRSRMEPPLPRGYFGNATLDVVAASTSGELISNELGFAASLISKAIKNVTNEYVMIGIEYLKNQKDLKKFQDLHALGSTEGPFYGNPNLGVVSWLTLPMYGLDFGWGKEFYTGPGTHDFDGDSLILPDQNEDGSVILATCLQVAHMEAFKKHFYEDI
Protein: Troponin C, slow skeletal and cardiac muscles (A0A060XPN3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Troponin I, slow skeletal muscle
- Troponin I type 1a
- Troponin C, slow skeletal and cardiac muscles
- Troponin T2d, cardiac
- Uncharacterized protein
- Troponin T type 2b
- Troponin T type 3a
- Troponin T2e, cardiac
- Troponin T2e, cardiac
- Troponin I, fast skeletal muscle
Sequence:
MNDIYKAAVEQLTDEQKNEFKAAFDIFVQDAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKTEEELADLFRMFDKNADGYIDLEELKGMLEATGEAITEDDIEELMKDGDKNNDGKIDYDEFLEFMKGVE
Protein: P-loop containing nucleoside triphosphate hydrolases superfamily protein (F4HQ47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLSLSLSNHVPPLTLLSHERRILKLQSRSSILFHQLFHTKFLLLSNSSSLSSSHGVVAISASPSSVAVPELEDEDHFDDELRRLLALVPEEIRQTLKEHPEISELIEIVLDLGRKPLARFPSGDFVISDDAVRVKDLEFAVSQVGEFTNDNRAGISRTLHRISAIRNRKGEIIGLTCRVGRSVRGSANLLRDLVQDGNSLLLIGPPGVGKTTMIREVARMLGNDYEKRVMIVDTSNEIGGDGDIPHPGIGNARRMQVPNSDIQHKVLIEAVENHMPQVIVIDEIGTKLEAIAASTIAERGIQLVATAHGATIENLIKNPSLDLLVGGVQSVTLGDEEATRRGGQKTVLERKGPSTFNCGAEIVSKTEVRVHRSLEATVDAILAGRLPNVEIRKIKSHGVEVIMEKEPFIDEKTVDKKHEEETLDVSKLTKEETVSEVLQTKEITEAESSEKDTLMYLYVYGIAESTVLQAIKQLEMETAVELTDDISEAEALLALQAKIRKNPRIKSFATSHGIPVYVTKTNSGIQVAKAIRALLTDYEDGLGEFGSEDRLKLSEKMDALEEARLAIERIVIPKKETTDLLPRPPRIVSLQGKLVRKYNLRSERKWRGDEMYLRILPYSTEEDRDDREDEGEFGEANGEELDELGFATGESNDSPSGIDRLPLLPD
Protein: Lysine-specific demethylase (EC 1.14.11.65) (A0A8I5ZXX2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU369087}.
Interaction partners:
Sequence:
MADAAASPVGKRLLLLFADPTASASASAPTAAAAVSGDPGPALRTRAWRAGTVRAMSGAVPQDLAIFVEFDGCNWKQHAWVKVHAEEVLALLLEGSLVWAPRKDPVLLQGTRVPVAQWPALTFTPLVDKLGLGSVVPVEYLVDRELRFMSDANGLHLFQMGTDVQNQILLEHAALRETVNALVSDQKLQEIFSRGPYSVQGHRVKVYQPEGEEAWLCGVVSRQDSISRLMEVSISETGEIKSVDPRLIHVMLMDNSTPQSEGGTIKAVKSSKGKKKRESIEGRDGRRRKSASDSGCDPATKKLKGDRGEVDSNGSDGGEASRGPWKGGNASGEPGLEQRAKQPPSTFAPQINRSIRFATYTKENGRTLVVQDEPVGGDRPVPFTPYASATGQTPLAPEVGGAENKEAGKTLEQVSQGMVASAAVVTTTSSTPTTVRISDTGLASGTGPEKQKGSWSQASGESSRSSSLASSGFGVSLSSLSQPLTFGSGRSQSNGVLATENKPLGFSLSRSSASESQKDSDLSKNLFFQCMSQNLPSSNYFTSGSEGVADDSSSRDSFRQSLESLSSGLGKGRPVLGADTKPGPKAGSSVDRKVPAESMPTLTPAFPRSLLNTRTPENHENLFLQPPKLSREEPSNPFLAFVEKVEHSPFSSFASQASGSSSSATTVTSKATPSWPESHSSADSASLAKKKPLFITTDSSKLVSGVLGSALSTGGPSLSAMGNGRSSSPTSSLTQPIEMPTLSSSPTEERPTVGPGQQDNPLLKTFSTVFGRHAGSFLSSPAEFAQENKAPFEAVKRFSLDERSLACRQDSDSSTNSDLSDLSDSEEQLQAKSGLKGPPEHLMGKLGPDGGRSAELLLGKGKGKQAPKGRPRTAPLKVGQSVLKDVSKVRKLKQSGEPFLQDGSCINVAPHLHKCRECRLERYRKFKEQEQDDSTVACRFFHFRRLVFTRKGVLRVEGFLSPQQSDPDAMNLWIPSSSLAEGIDLETSKYILANVGDQFCQLVMSEKEAMMMVEPHQKVAWKRAVRGVREMCDVCETTLFNIHWVCRKCGFGVCLDCYRLRKSRPRSETEEMGDEEVFSWLKCAKGQSHEPENLMPTQIIPGTALYNIGDMVHAARGKWGIKANCPCISRQSKSVLRPAVTNGISQLPSITPSASSGNETTFSSGGGTVATTNPEPEQAPKGAGADSRAEEPLKAEGSASNSNSELKAIRPPCPDTAPPSSALHWLADLATQKAKEETKDAGSLRSVLSKESHSPFGLDSLNSTAKGSPLTPKLFNSLLLGPTASNSKTEGSSLRDLLHSGPGKLPQTPLDTGIPFPPVFSSSSAGAKSKASLPNFLDHIIASVVENKKTSDSSKRSCNLTDTQKEVKEMVMGLNVLDPHTSHSWLCDGRLLCLHDPSNKNNWKIFRECWKQGQPVLVSGVHKKLKSELWKPEAFSQEFGDQDVDLVNCRNCAIISDVKVRDFWDGFEIICKRLRSEDGQPMVLKLKDWPPGEDFRDMMPTRFEDLMENLPLPEYTKRDGRLNLASRLPSYFVRPDLGPKMYNAYGLITAEDRRVGTTNLHLDVSDAVNVMVYVGIPIGEGAHDEEVLRTIDEGDADEVTKQRIHDGKEKPGALWHIYAAKDAEKIRELLRKVGEEQGQENPPDHDPIHDQSWYLDQILRKRLFEEYGVQGWAIVQFLGDAVFIPAGAPHQVHNLYSCIKVAEDFVSPEHVKHCFRLTQEFRHLSNTHTNHEDKLQVKNIIYHAVKDAVGTLKAHESKLARS
Protein: NXPE family member 3 (Protein FAM55C) (Q969Y0)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MWTNFFKLRLFCCLLAVLMVVVLVINVTQVEYLDHETVSATFIDSSGQFVSSQVTGISRNPYCGYDQQTLSSQERMEEDSLLAALHRQVPDVGPVPFVKSTDPSSSYFVILNSAAFFKVGSQLEVLVHVQDFQRKPKKYGGDYLQARIHSLKLQAGAVGRVVDYQNGFYKVFFTLLWPGKVKVSVSLVHPSEGIRVLQRLQEDKPDRVYFKSLFRSGRISETTECNVCLPGNLPLCNFTDLYTGEPWFCFKPKKLPCSSRITHFKGGYLKGLLTAAESAFFQSGVNIKMPVNSSGPDWVTVIPRRIKETNSLELSQGSGTFPSGYYYKDQWRPRKFKMRQFNDPDNITECLQRKVVHLFGDSTIRQWFEYLTTFVPDLVEFNLGSPKNVGPFLAVDQKHNILLKYRCHGPPIRFTTVFSNELHYVANELNGIVGGKNTVVAIAVWSHFSTFPLEVYIRRLRNIRRAVVRLLDRSPKTVVVIRTANAQELGPEVSLFNSDWYNFQLDTILRRMFSGVGVYLVDAWEMTLAHYLPHKLHPDEVIVKNQLDMFLSFVCPLET
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q585A7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Heat shock protein 83
- Heat shock protein, mitochondrial, putative
Sequence:
MSTTKLEGVRHSRRKKGDSRLQRPENDEDSATLQSRYDDVEERRLKEWENYQRSHRMKEEQNSCRAFLDMSIDDVLSGRLVFELFDDVVPRTVENFRALITGSCGIDTNTGVKLDYLGTQVHHVDHNNNIIVLGELDSFNLSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGRAIDDLSLLEKLEAVPLDDVGRPVLPVTVSFCGALTGEKPPGRQQVPAAADDSASSEHVSCAGEE
Protein: High affinity immunoglobulin epsilon receptor subunit gamma (Fc receptor gamma-chain) (FcRgamma) (Fc-epsilon RI-gamma) (IgE Fc receptor subunit gamma) (FceRI gamma) (P20411)
Organism: Rattus norvegicus (Rat)
Function: Adapter protein containing an immunoreceptor tyrosine-based activation motif (ITAM) that transduces activation signals from various immunoreceptors. As a component of the high-affinity immunoglobulin E (IgE) receptor, mediates allergic inflammatory signaling in mast cells. As a constitutive component of interleukin-3 receptor complex, selectively mediates interleukin 4/IL4 production by basophils priming T-cells toward effector T-helper 2 subset. Associates with pattern recognition receptors CLEC4D and CLEC4E to form a functional signaling complex in myeloid cells. Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of ITAM, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes. May function cooperatively with other activating receptors. Functionally linked to integrin beta-2/ITGB2-mediated neutrophil activation. Also involved in integrin alpha-2/ITGA2-mediated platelet activation.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- C-type lectin domain family 4 member E
- Glycoprotein VI
- Natural cytotoxicity triggering receptor 1
- High affinity immunoglobulin epsilon receptor subunit alpha
- TYRO protein tyrosine kinase-binding protein
- Tyrosine-protein kinase
- Triggering receptor expressed on myeloid cells 2
- Natural cytotoxicity triggering receptor 3
- Tyrosine-protein kinase Lyn
- Fc of IgG, low affinity IIIa, receptor.
Sequence:
MIPAVILFLLLLVEEAAALGEPQLCYILDAILFLYGIVLTLLYCRLKIQVRKADIASREKSDAVYTGLNTRNQETYETLKHEKPPQ
Protein: Kinase suppressor of ras 1 (A0A8I6AR82)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKTETPLPALFFLGTVHWGPGLLRSGPLTMHCLWSWVTTKASRDPETPPPTLPREAQGSSRPASDENCEEIPQELTLDALLEMDEAKAKEMLRRWGASAEECSRLQQALTCLRKVTGLGGEHKEDSGWSSAEARESSSGPSVDMLSSLGRAGASTQGPRSISVSALPASDSPVPGLSEGLSDTCIPLHTSGRLTPRALHSFITPPTTPQLRRHAKLKPPRTPPPPSRKVFQLLPSFPTLTRSKSHESQLGNRIDEVAPMRFELPHGSPQLVRRDIGLPVTHRFSTKSWLSQVCNVCQKSMMFGVKCKHCRLKCHNKCTKEAPACRISFLPLARLRRTESVPSDINNPVDRAAEPHFGTLPKALTKKEHPPAMNLDSSSNPSSTTSSTPSSPAPFLTSSNPSSATTPPNPSPGQRDSRFNFPDISACPQAAPLSSTADSTRLDDQPKTDVLGVPEAEAEEPEAGKSEAEDDEDEIDDLPSSRRHWRGPISRKASQTSVYLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKLSHDWLCYLAPEIVREMIPGRDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVKRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLEKLPKLNRRLSHPGHFWKSAEL
Protein: Carbohydrate sulfotransferase 5 (EC 2.8.2.-) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4-alpha) (GST4-alpha) (Intestinal N-acetylglucosamine-6-O-sulfotransferase) (I-GlcNAc6ST) (Intestinal GlcNAc-6-sulfotransferase) (hIGn6ST) (N-acetylglucosamine 6-O-sulfotransferase 3) (GlcNAc6ST-3) (Gn6st-3) (Q9GZS9)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues and O-linked sugars of mucin-type acceptors. Acts on the non-reducing terminal GlcNAc of short carbohydrate substrates. However, it does not transfer sulfate to longer carbohydrate substrates that have poly-N-acetyllactosamine structures. Has no activity toward keratan. Not involved in generating HEV-expressed ligands for SELL. Its substrate specificity may be influenced by its subcellular location.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:12855678}; Single-pass type II membrane protein {ECO:0000305|PubMed:12855678}. Note=Golgi membrane, early secretory pathway.
Interaction partners:
- Lumican
- Sulfotransferase 1B1
- Sulfotransferase 1C3
- Sulfotransferase 1C4
- Galactose-3-O-sulfotransferase 2
Sequence:
MGMRARVPKVAHSTRRPPAARMWLPRFSSKTVTVLLLAQTTCLLLFIISRPGPSSPAGGEDRVHVLVLSSWRSGSSFLGQLFSQHPDVFYLMEPAWHVWTTLSQGSAATLHMAVRDLMRSIFLCDMDVFDAYMPQSRNLSAFFNWATSRALCSPPACSAFPRGTISKQDVCKTLCTRQPFSLAREACRSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREAAGPILARDNGIVLGTNGKWVEADPHLRLIREVCRSHVRIAEAATLKPPPFLRGRYRLVRFEDLAREPLAEIRALYAFTGLTLTPQLEAWIHNITHGSGIGKPIEAFHTSSRNARNVSQAWRHALPFTKILRVQEVCAGALQLLGYRPVYSADQQRDLTLDLVLPRGPDHFSWASPD
Protein: UL144 protein (Q8V2D1)
Organism: Human cytomegalovirus (HHV-5) (Human herpesvirus 5)
Interaction partners:
Sequence:
MKPLIMLICFAVILLQLGVTKVCQHNEVQLGNECCPPCGSGQRVTKVCTDYTSVTCTPCPNGTYVSGLYNCTDCTQCNVTQVMIRNCTSTNNTVCAPKNHTYFPTPGVHHKQRQQNHTAHITVKQGKSGRHTLAWLSLFIFLVGIILLILYLIAAYRSERCQQCCSIGKIFYRTL
Protein: Abnormal pharyngeal pumping eat-20 (Q9NL29)
Organism: Caenorhabditis elegans
Function: Regulates pharyngeal pumping during feeding.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- MAGUK p55 subfamily member 5
- Syndecan
- Protein Scribble homolog let-413
- Rab GTPase-activating protein eat-17
- PDZ domain-containing protein
Sequence:
MTTFCRVLLIFGIYVAVCCAQSVEDDVFHFTNPSQGNAVWILDESSLPWTGGYQFLRSISGMPTTLLSVVDSSTGVTLGQCVAPQDATGNFSKRWERFSWELTASGLDCTFEHGAAIRVEFDRTQNPRTFSIRIQSITGPACLRDVVVQTEQATGCPPHLSRNSFTANALNCSCPFLDAANEDSEIENEDVDMLANTPQFPLFKGIDPSVLGSANPPTLPPSPCANHECHNNGTCLVSQEGAATCLCRNGFTGDRCELDVCSSVPCQNGGVCRSNNGIAYCECPPAFTGLLCESAHTDESVAPICRPECSNGQCVFKDGQAQCECRQGFTGANCNVLDVCLGDAACSMFGPLAKCVLDDNMDKMSSLTLINGTYDCLCPHPIHGQFVDCMQLHAPSATSVQPTEQVVINNVTPSFPVLEISKLPTGAPVTFTATSTTLMVTQPTVTVSPTHQVPSEPFVGFTVTRAPLRPLDIGSTTLPPPFNQHIITAGEPTWSSQQPHQPSEVPTQTTFIFPQTPETTTFAPTTGTQQPVHKFVSPSVPDENEEEEEEETTEETEETFPTPSTMQVATNGQFTTETAFVTSTIPSTTTDMEETDEDEDMTEEVTDSSTQPSTTVFVQPTTTFTTEAPTTTMEEEEEMTTDQVEDIESEEIATTTTQTSLPFWMTTTNKQVVPDSPTPMVIMPHPQPDEKMETSTEGVVDEESDEERTTVPESNEEVVTKNAEATTPSDITHHHTSSGKQSSAAASWIIAIIALIVLGLLLLATSLFILRYIRQSRKLHGKYNPAREEHNLSAAYAMPMSHIAKEERLI
Protein: Zinc finger protein 2 (Q381U0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Polyubiquitin, putative
Sequence:
MAFNQRFDRGAQPSYAAVQLPPGWQMAYSVEGEVYYIDHNTRTTHWKIPQEVLNEMYHQGQTYRPSRSRRGIDRSKMKTKMCMNIQNGGKCTWGNACAFAHSSEELAAVPHNGGGQRMRMDPGAHQGNDNGLDNNHLQQ
Protein: (-)-kolavenyl diphosphate synthase TPS10, chloroplastic (EC 5.5.1.28) (Terpene synthase 10) (TwTPS10) (A0A1C7AAN2)
Organism: Tripterygium wilfordii (Thunder God vine)
Function: Diterpene synthase that catalyzes the formation of (-)-kolavenyl diphosphate from geranylgeranyl diphosphate (GGPP).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MFMSSSSSSHARRPQLSSFSYLHPPLPFPGLSFSSTRDKRVNFDSTRIISIAKSKPARTTPEYSDVLQTGLPLIVEDDIQEQEEPLEVSLENQIRQGVDIVKSMLGSIEDGEISISAYDTAWVALVENIHHPGSPQFPSTLQWIANNQLPDSSWGDPDMFLTHDRLINTLACVIALKKWNIHPRKCKRGLSFVKENISKLAKEDEEHMLIGFEIAFPSLLEMAKKLGIEIPDDCPAMQDIYTKKDLKLTRIPRDIMHNVPTTLLYSLEGLPSLDWEKLVKLQCQDGSFLFSPSSTACALMHTKDGNCFSYLNNLVHKFNGGVPNVYPVDLFEHIWSVDRLLRLGISRFFRPEIKECLEYVHRYWTKDGICWARNSNVQDIDDTSMGFRLLRLHGYEVSPDVFKQFKKGNEFVCVVGQSDQAITGIYNLYRASQLMFPKETILHGAKEFAGNFLRKKRTANELLDKWIITKDLPGEVGFALDVPWYACLPRVETRLYIEQYGGQDDVWIGKTLYRMPYVNNNVYLELAKLDYNNCQSLHRIEWDNIQKWYEEYNVGGFGVSKRGLLKTYFVATASIFEPERSVERLAWAKTAILVETIRSYFGNSREERIAFPNEFQKAKTRGYINGRRLDGKQATKGLIEMVFATLNHLSQDALVVHGQDITPHLYQSWEKWVLTWQEGGDRGEGEAELLVQTINLMAGHTHSQEEELLYERLFKLTNTVCHQLGHYHHLNKDKQPQQVQDNGGYNNSNPESISKLQIESDMRELVQLVLNSSDGMDSNIKQTFLTVTKSFYYTAFTHPGTVNYHIAKVLFERVV
Protein: Cysteine synthase (CSase) (EC 2.5.1.47) (O-acetylserine (thiol)-lyase) (OAS-TL) (Superoxide-inducible protein 11) (SOI11) (P37887)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.
Interaction partners:
- Serine acetyltransferase
- Cystathionine gamma-lyase
- Sulfite reductase hemoprotein beta-component
- Cystathionine gamma-synthase/O-acetylhomoserine
- Cystathionine beta-lyase MetC
- Sulfite reductase flavoprotein alpha-component
- Phosphoserine aminotransferase
- Cystathionine beta-lyase PatB
- Uncharacterized methyltransferase YrrT
- S-ribosylhomocysteine lyase
Sequence:
MVRVANSITELIGNTPIVKLNRLADENSADVYLKLEYMNPGSSVKDRIGLAMIEAAEKEGKLKAGNTIIEPTSGNTGIGLAMVAAAKGLKAILVMPDTMSMERRNLLRAYGAELVLTPGAEGMKGAIKKAEELAEKHGYFVPQQFNNPSNPEIHRQTTGKEIVEQFGDDQLDAFVAGIGTGGTITGAGEVLKEAYPSIKIYAVEPSDSPVLSGGKPGPHKIQGIGAGFVPDILNTEVYDEIFPVKNEEAFEYARRAAREEGILGGISSGAAIYAALQVAKKLGKGKKVLAIIPSNGERYLSTPLYQFD