wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-editing-associated protein 1 (Q38A04)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA editing complex protein MP46
- MP18 RNA editing complex protein
- REH2-associated factor 1
- RNA editing 3' exouridylylase MP99
- RNA editing complex protein MP67
- RNA editing complex protein MP61
- RNA-editing ligase 2, mitochondrial
- REH2-associated factor 2
- RNA-editing ligase 1, mitochondrial
- RNA editing associated helicase 2
Sequence:
MYHYEYDDDHSTNLSQAINAKLITRRGITTDSPDPITPVFSSTAPTRSSTGLTTEWIRHQKLSGRAVPPTLDTLKGTGSGRKYKSVTNSQENNVDPNSINRGTLLVNSSYSAPSPRYNHVSSVVKKLIEGRITPQEARRASSSRRGSSRTTRLVASSRFAPADRPSSAPKRLPMGSGRTGGLLPRLRISSTPHIPVRTQQWIPSNSAKPATAECQKNISPRGPATTQSSGSSRRLNMYQRVPLSRQCDSFPRKPTTVEEKPKPPQPLFSRVPRCAADIPDHRKPSPRHDVQSRRPYVPQSGREVPKAHKTPLSRASSSPKYNSARRRYVQDKQTNETSTISGRQRVPVSAVDVGSREKANVSERQRVPVSAVDVGSREKANVTERQRVPVSAVDVGSREKANVTERQRVPVSAVDVGSREKANVTERQRVPVSAVDVGSREKANVSERQRVPVSAVDVGSREKANVTERQRVPVSAVDVGSKEQEDGRVTAISSDSRGALSQTKAMETQKVVDPLSTKDIISHDAAGRPKHKSLNGGLVIPQVEGIKSLLLFDIKPPKLSETGAVAATVG
Protein: Profilin-5 (ZmPRO5) (Double B-box zinc finger protein 11) (Pollen allergen Zea m 12) (allergen Zea m 12) (Q9FR39)
Organism: Zea mays (Maize)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Has a high affinity for poly-proline.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P35081}.
Interaction partners:
- Actin-1
- Actin-1
- Uncharacterized protein.
- Actin-depolymerizing factor
- Actin-depolymerizing factor
- Actin-depolymerizing factor
- Actin-depolymerizing factor 7
- Ypt homolog3
- Actin-depolymerizing factor 1
- Expansin-B10
Sequence:
MSWQAYVDDHLLCDIEGQHLSAAAIVGHDGSVWAQSENFPELKPEEVAGMIKDFDEPGTLAPTGLFVGGTKYMVIQGEPGVVIRGKKGTGGITIKKTGMSLIIGIYDEPMTPGQCNMVVERLGDYLIEQGF
Protein: Sister chromatid cohesion protein PDS5 homolog B (Precocious dissociation of sisters protein 5-B) (AtPDS5B) (F4I735)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex. Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication (By similarity). Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for proximal-distal cell cycle-driven leaf growth in both lamina and petiole.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
Sequence:
MEKTPTQIVSELCSRLLQLSRPNKDSLVKLLREVANTLSKIDQPSATNKEKGLKLIEAELRPLKKSIIKHALLKNRDNDVSLLVTVCVSELFRILAPHLPFEDEYLRDIFTLFIAEFSELSDTVSPYFSKRAKILETVSRLKFCLLMLDEDCQDLVHEMFNMFFSLVREHHQQSLINQKSMKTQQRKANTQQTQHSLFNNILAIMSDVLEEEANSSFVVVILENLVKEGEDTTSGADKLASSLIERCADRLEPLICSFLTSCFMEKDSIQTNLKDSYHEIIFKISLIAPQMLLAVIPKLTQELLTDQVDVRIKALNLAGRIFAQPKHCLSSYVETYQDLYAEFLRRFSDKSAEVRMAALKCGKQCYFANPSGNKASGVLTAIQERLLDFDDRVRTQALIVACDIMKFNMKYVPLNLISEASERLRDKKISVRKKALQKLTEVYQDYCDKCSEGDMTITDNFEQIPCKILLLCCEKNCEEFRSQNLELVLSDDLFPRLLPVEERMRHWVQCFAIMNHIHLKSLNSILSQKRRLQNELRHCLTLWRKAKVDNIEEAQRKKKSYFVKLSACFPDASEAEDLFEKLDRMRDASIFDVLTLLLEELSSTNAQIIKEKFLKMIGVKHSLFEFLRILSTKCSPSIFSSEHVQCLLNQLCGSTSANTQLKAPSIKLLLVILNMFPSYLRGSEKQFLKLLEENDSAADELIVVLSKAAPYISVNFGDYYPVLEKVCLEGTRSQTKCAVSAISSLAGSSEKSVFSELCEMLMDSLLCGRNIPTTLQSLACVGQYSVLEYDNIYEDITSYIYRVFQAEPSDNQLPCDQSSGCCNSCKLKIYGLKTLVKSFLPRHGQVVRKIDDLLNILKKTLKSQGHDGIKSCEDTGANVRLAAAKAVLLLSRKWDLHISPEVFRLTILMAKDSNAFITKTFLTKLYKLLTEHMIPSRYACAFSFSLSSPCRDLHDDSFRYINGFINKATRESRTCRDLDQGESLTDSPVYMTVFLIHVLAHDPEFPSEDCRDEHIYARFCGPLFSVLQVLLSINNNGFTIKETAPFLFCIFRAIKRAEDAVDSRKTPRLHILADIGYSAVNILNSIVVTSPQAPRSILLPSSLYSLTSITDNQNKAKSRTRNALEQSFIERIVHIFQSQISMHDQRCQKDSLAVGSEDKVLPPLLGNQIETSITGSTEASQNNTRCSRKRTHLGEHISCNSLSLRTVESEIPIKKLERHTTCAKESVKASVSNKITSSKHSGVVSALKDISNHGEAIIGQRIKLLSPTDGCFYPGTVEKFNSKSNSHKIIFDNGDVELVCLDSESWETLSHESMGQQERLGKETESYGSRNCVPEISHTLAKVTAQKQTTTTKQQNKKVPAKLNPPAVPCFMMSAKSKKGNSDSGEGSVSEVTDTSDNIGPRRSRRQRIS
Protein: Hemoglobin subunit beta (Beta-globin) (Hemoglobin beta chain) (P84792)
Organism: Aythya fuligula (Tufted duck) (Anas fuligula)
Function: Involved in oxygen transport from the lung to the various peripheral tissues. The beta chain is a component of adult hemoglobin A and D.
Interaction partners:
Sequence:
MVHWTAEEKQIITGLWGKVNVADCGAEALARLLIVYPWTQRFFSSFGNLSSPTAILGNPMVRAHGKKVLTSFGDAVKNLDNIKNTFAQLSELHCDKLHVDPENFRLLGDILIVVLAAHFSKEFTPECQAAWQKLVRVVAHALARKYH
Protein: Phospho-2-dehydro-3-deoxyheptonate aldolase 1, chloroplastic (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 1) (DAHP synthase 1) (PhDAHP1) (Phospho-2-keto-3-deoxyheptonate aldolase 1) (A0A067XH53)
Organism: Petunia hybrida (Petunia)
Function: Involved in the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26), scent attracting pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:24815009}.
Interaction partners:
Sequence:
MALSTNSTTSSLLPKTPLVQQPLLKNASLPTTTKAIRFIQPISAIHSSDSSKNTPIVSAKPSSPPAATSTAAATAVTKQEWSIDSWKTKKALQLPEYPNQEELKNVLKTIEDFPPIVFAGEARHLEEKLGEAAMGRAFLLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQMPVIKVGRMAGQFAKPRSDNFEEKNGVKLPSYRGDNVNGDAFDLKSRTPDPQRLIRAYCQSAATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELANRVDEALGFMNAAGLTTDHPIMTTTEFWTSHECLLLPYEQSLTRLDSTSGLYYDCSAHFLWVGERTRQLDGAHVEFLRGIANPLGIKVSDKMDPSALVKLIEILNPQNKAGRITIITRMGAENMRVKLPHLIRAVRGAGQIVTWVSDPMHGNTIKAPCGLKTRPFDSIRAEVRAFFDVHEQEGSHPGGVHLEMTGQNVTECIGGSRTVTFDDLSSRYHTHCDPRLNASQSLELAFIIAERLRKRRLGSQSVLGQ
Protein: Homeobox protein Hox-B7 (Homeobox protein HHO.C1) (Homeobox protein Hox-2C) (P09629)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-B6
- X-ray repair cross-complementing protein 6
- Homeobox protein Hox-B5
- Homeobox protein Hox-A5
- DNA-dependent protein kinase catalytic subunit
- X-ray repair cross-complementing protein 5
- Homeobox protein Hox-A7
- Homeobox protein Hox-C6
- Pre-B-cell leukemia transcription factor 1
- Homeobox protein Hox-B4
Sequence:
MSSLYYANTLFSKYPASSSVFATGAFPEQTSCAFASNPQRPGYGAGSGASFAASMQGLYPGGGGMAGQSAAGVYAAGYGLEPSSFNMHCAPFEQNLSGVCPGDSAKAAGAKEQRDSDLAAESNFRIYPWMRSSGTDRKRGRQTYTRYQTLELEKEFHYNRYLTRRRRIEIAHTLCLTERQIKIWFQNRRMKWKKENKTAGPGTTGQDRAEAEEEEEE
Protein: Pentatricopeptide repeat-containing protein 2, mitochondrial (O60142)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial RNA-binding protein that acts as a general translation factor.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:21727087}.
Interaction partners:
- Pentatricopeptide repeat-containing protein 8
- Uncharacterized protein C106.19
- Pentatricopeptide repeat-containing protein 5
- DNA-directed RNA polymerase, mitochondrial
- Mitochondrial cox1 translation regulator ppr4
- Pentatricopeptide repeat-containing protein 6
- Pentatricopeptide repeat-containing protein 7
- Uncharacterized protein PB1E7.11c
Sequence:
MQFIKRTFPRRAFVDLLLNRFCLREFATTYSVSVSNARKLVRKRLLIADALKFKEQVNNLNEFRNKKTKSSLIRNDGFKLAKNVSSLLQKESLEKALHLLYERSNAKKTVAYNLVLQYHLAKGHYNAAWSLYNDMKKRQQKPSDHTYSILLKGFCDAIEKNKQGNFSKLREYSEKVTASALKESNNVTSNLHHIRIISKCSLKLKSMVLVSMIIPSIKQTLDFYSGSQILRLLNDFSMFNPEQREEVLKMGTNLWNYFVLECQKKGIAVDESLICSFVKLLATSNSPQVRNVGLNILTKVMGLEYQIFEDSNLRYPLPPYCDCTSRSLVTALQVIRQIQNGDLLARYWKYFEESHKFDLNLQVYHEKLRNLVQQGQAAECLNTIKRMSHNGPFPTQQTFLIVLSLCKRPKFYSYTKSFLDLAKKLNVPVEAT
Protein: Protein PafB (Proteasome accessory factor B) (P9WIM1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the pafABC operon, however PafB does not seem to be involved in pupylation or substrate degradation. Appears to play at least a small role in resistance to reactive nitrogen intermediates (RNI) in vitro.
Interaction partners:
- Protein PafC
- Pup--protein ligase
- RNA polymerase-binding protein RbpA
- DNA-directed RNA polymerase subunit omega
- Sec-independent protein translocase protein TatA
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta'
- Sensor-type histidine kinase PrrB
- Methionine aminopeptidase 1
Sequence:
MATSKVERLVNLVIALLSTRGYITAEKIRSSVAGYSDSPSVEAFSRMFERDKNELRDLGIPLEVGRVSALEPTEGYRINRDAYALSPVELTPDEAAAVAVATQLWESPELITATQGALLKLRAAGVDVDPLDTGAPVAIASAAAVSGLRGSEDVLGILLSAIDSGQVVQFSHRSSRAEPYTVRTVEPWGVVTEKGRWYLVGHDRDRDATRVFRLSRIGAQVTPIGPAGATTVPAGVDLRSIVAQKVTEVPTGEQATVWVAEGRATALRRAGRSAGPRQLGGRDGEVIELEIRSSDRLAREITGYGADAIVLQPGSLRDDVLARLRAQAGALA
Protein: Calcium-binding and spermatid-specific protein 1 (Casein-like phosphoprotein) (Protein RSD-6) (Q68FX6)
Organism: Rattus norvegicus (Rat)
Function: Calcium-binding protein. Essential for maintaining the structural integrity of the sperm flagella (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19271754}. Mitochondrion inner membrane {ECO:0000269|PubMed:19271754}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q8C633}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q8C633}. Note=Mostly cytoplasmic, but associated with the mitochondrial inner membrane during the last steps of spermatid differentiation (PubMed:19271754). Localizes to the principal piece of the sperm flagellum (By similarity). {ECO:0000250|UniProtKB:Q8C633, ECO:0000269|PubMed:19271754}.
Interaction partners:
- Testicular spindle-associated protein SHCBP1L
- Tetratricopeptide repeat domain 21A
- HEAT repeat containing 9
Sequence:
MAEDGSPKIYSRPPRDSSKTPTEADIFFGADNTIPKSETTITSEGDHITSVNDCTADGDFSTTVNKLTPTKEKLKLEEDIEASLKSTTLPEKEITTPTETTNSKPKESITENFIPVKIGNISSPVGTVSLIDFSSNMAKEDILLATIDAEDKEVKPTTELSETQEDSSANDEDTSVPPDENTETDVSSSTSSDVPDDGAVQVTDSFSPESDVPPSTEKEVTTIPDNVAEDKVTKIDLIVSEDRPKTVTKLSDSEEEKFITVFELTNSAEKAKDNPEDPLTDEEPADGVNTWVEKDAANEAESHAVLLTAVESRYDFVVTASETNSVVVEEPHVDTKNSPEKDAAESVTNVTEEFPSVTSVVEQSGNKEDLSTNDSGIFKLLKEEPDELMM
Protein: Androgen receptor (bfAR) (Dihydrotestosterone receptor) (Nuclear receptor subfamily 3 group C member 4) (Q7T1K4)
Organism: Aquarana catesbeiana (American bullfrog) (Rana catesbeiana)
Function: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}.
Interaction partners:
Sequence:
MEVHIGLGGVYKQPPGKMIRGAFENLFLSVREALQGERRSAASLDTSSPISACVHPHPTWNEPSTWTEVRGTPWREPQGAQPDPPPCSPRSQAPQFTLSSCTTELKEILGEQGGMPEEGNSESASKEGYPESISDSAKEICKAVSVSLGLSMEALEHLSAAGEWQRGDCMFAGPPHHTMGAQTCQVAEEDKSDTSFSQYREGAFRRAGQSTYSAGKAPEDGSSLPTEDKEQPCTDMALSEPGSLRSRGMEVMPSLTLYKPTAFMEDASAYPGRDYYSFQMALAPHGRIKVESPIEFAGSAWGGPSRYSEFPGFSHCGPSANWHSLFEEGQATASYTDSSLYSYPRSHVPAGPDGEFSAEAWYPATAMLGRVHMAVPMRPRMTHGWTATLGIRRRLGWTGVESTFYPIDYYFPPQKPCLSCEDEASGCHYEALTCGSCKVFFKRAAEGNQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKAQEELEGSPGQSEGREMPPNMSIPQLEGYSCQPIFLNVLEAIEPMVVCSGHDNNQPDSFALLLSSLNELGERQLVHVVKWAKALPGFRNLHVNDQMTVIQYSWMGLMIFAMGWRSFKNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQVTPEEFLCDEGPSALSIIPVEGLKDQKCFDELRMNYIKELDRVISCKRNNPASSSPRFFNLPKLLGSVQPIDVNLVQFTFGLFGKAQMVSVDFPEMMSEIISVQVPKILSGRVKPLYFHSS
Protein: Type-2 angiotensin II receptor (Angiotensin II type-2 receptor) (AT2 receptor) (P35351)
Organism: Rattus norvegicus (Rat)
Function: Receptor for angiotensin II, a vasoconstricting peptide. Signals primarily via a non-canonical G-protein- and beta-arrestin independent pathways. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P35374}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P50052}.
Interaction partners:
- Angiotensinogen
- Angiotensin-converting enzyme
- Guanine nucleotide-binding protein G
- Angiotensin-converting enzyme
- Type-1 angiotensin II receptor A
- Type-1 angiotensin II receptor B
- Renin
- Angiotensin-converting enzyme 2
- Kininogen-1
- Endothelin-1
Sequence:
MKDNFSFAATSRNITSSLPFDNLNATGTNESAFNCSHKPADKHLEAIPVLYYMIFVIGFAVNIVVVSLFCCQKGPKKVSSIYIFNLAVADLLLLATLPLWATYYSYRYDWLFGPVMCKVFGSFLTLNMFASIFFITCMSVDRYQSVIYPFLSQRRNPWQASYVVPLVWCMACLSSLPTFYFRDVRTIEYLGVNACIMAFPPEKYAQWSAGIALMKNILGFIIPLIFIATCYFGIRKHLLKTNSYGKNRITRDQVLKMAAAVVLAFIICWLPFHVLTFLDALTWMGIINSCEVIAVIDLALPFAILLGFTNSCVNPFLYCFVGNRFQQKLRSVFRVPITWLQGKRETMSCRKSSSLREMDTFVS
Protein: Mce-family protein Mce2F (O07784)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible Mce-family lipoprotein LprL
- Conserved hypothetical integral membrane protein YrbE2A
- Conserved hypothetical integral membrane protein YrbE2B
- Mce-family protein Mce2A
- Mce-family protein Mce2B
- Mce-family protein Mce2C
- Mce-family protein Mce2D
- Conserved integral membrane protein YrbE4A. Possible ABC transporter
- Conserved integral membrane protein YrbE1A
- Conserved integral membrane protein YrbE4B. Possible ABC transporter
Sequence:
MLTRAIKTQLVLLTVLAVIAVVVLGWYFLRIPSLVGIGRYTLYAELPRSGGLYRTANVTYRGITIGKVTGVEPTERGARATMSIDNGYQIPTDASANVHSVSAVGEQFVDLVSTRTSGPYLRHGQTITTTTVPSQIGPALDAANRGLAVLPKDRVASVLHEASEAVGGLGSSLNRLIEATQAIAHDVRGSLEDIDDIIERSAPIIDSQVNSGNEIARWAANLNTLAAQTAQTDPAVRSILANAAPTADQVNATFSDVRESLPQTLANLEVVIDMLKRYHNGVEQALVFLPQSGAIAQSVTTEFPGQAGLGVGGLALNQPPPCLTGFLPASEWRSPADTSTAPLPKGTYCRIPMDASNVVRGARNNPCVDVPGKRAATPRECRSNEAYVPGGTNPWYGDPNQMLSCPAPAARCDQPVKPGQVIPAPSVNNGINPLPADQLPGTPPPVNDPLQRPGSGTVQCNGQQPNPCVYTPSTFPTTIYDVQSGKVVAPDGVVYSVEASTHAGADGWKVMLAPTG
Protein: Uncharacterized mitochondrial carrier C27B12.09c (O13660)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Riboflavin kinase
- Copper amine oxidase 1
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
Sequence:
MDQAIAGLAAGTASTLIMHPLDLAKIQMQASMNQDSKSLFQVFKSNIGSNGSIRSLYHGLSINVLGSAASWGAYFCIYDFSKRVVMSMTPFNNGEISVLQTLCSSGFAGCIVAALTNPIWVVKSRILSKRVNYTNPFFGFYDLIKNEGLRGCYAGFAPSLLGVSQGALQFMAYEKLKLWKQRRPTSLDYIFMSAASKVFAAVNMYPLLVIRTRLQVMRSPHRSIMNLVLQTWRLQGILGFYKGFLPHLLRVVPQTCITFLVYEQVGMHFKTQSSKSQ
Protein: Scarecrow-like protein 3 (AtSCL3) (GRAS family protein 5) (AtGRAS-5) (Q9LPR8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in plant development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein JACKDAW
- Protein PAT1 homolog
- Zinc finger protein MAGPIE
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Holliday junction resolvase MOC1, chloroplastic
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Phytochrome A
- Gibberellin receptor GID1B
Sequence:
MVAMFQEDNGTSSVASSPLQVFSTMSLNRPTLLASSSPFHCLKDLKPEERGLYLIHLLLTCANHVASGSLQNANAALEQLSHLASPDGDTMQRIAAYFTEALANRILKSWPGLYKALNATQTRTNNVSEEIHVRRLFFEMFPILKVSYLLTNRAILEAMEGEKMVHVIDLDASEPAQWLALLQAFNSRPEGPPHLRITGVHHQKEVLEQMAHRLIEEAEKLDIPFQFNPVVSRLDCLNVEQLRVKTGEALAVSSVLQLHTFLASDDDLMRKNCALRFQNNPSGVDLQRVLMMSHGSAAEARENDMSNNNGYSPSGDSASSLPLPSSGRTDSFLNAIWGLSPKVMVVTEQDSDHNGSTLMERLLESLYTYAALFDCLETKVPRTSQDRIKVEKMLFGEEIKNIISCEGFERRERHEKLEKWSQRIDLAGFGNVPLSYYAMLQARRLLQGCGFDGYRIKEESGCAVICWQDRPLYSVSAWRCRK
Protein: TPR repeat-containing thioredoxin TDX (HSP70-interacting protein 2) (AtHIP2) (Tetratricoredoxin) (AtTDX) (Q8VWG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-disulfide oxidoreductase that possesses insulin disulfide bonds reducing activity, disulfide reductase, foldase chaperone and holdase chaperone activities. Heat shock causes oligomerization and formation of high molecular weiht (HMW) complexes with concomitant functional switching from a disulfide reductase and foldase chaperone to a holdase chaperone. May interact with HSP70 proteins through the TPR repeats.
Interaction partners:
- NADPH-dependent thioredoxin reductase 3
- Heat shock 70 kDa protein 4
- Fes1C
- ARM repeat superfamily protein
- Fes1B
- Fes1A
- Serine/threonine-protein phosphatase 7 inactive homolog
- Heat shock 70 kDa protein BIP3
- Heat shock 70 kDa protein BIP2
- Protein phosphatase EYA
Sequence:
MVDAIQVAELRRFVEQLKLNPSILHDPSLVFFKEYLRSLGAQVPKIEKTERDYEDKAETKPSFSPKHDDDDDDIMESDVELDNSDVVEPDNEPPQPMGDPTAEVTDENRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHVASKLDYDEEIGTMLKKVEPNAKRIEEHRRKYQRLRKEKELQRAERERRKQQEAQEREAQAALNDGEVISIHSTSELEAKTKAAKKASRLLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGADKGSLEQKIAQHSSSK
Protein: Adenosylhomocysteinase 1 (AdoHcyase 1) (EC 3.13.2.1) (Protein EMBRYO DEFECTIVE 1395) (Protein HOMOLOGY-DEPENDENT GENE SILENCING 1) (S-adenosyl-L-homocysteine hydrolase 1) (SAH hydrolase 1) (O23255)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein during embryogenesis. Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. Required for DNA methylation-dependent gene silencing.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 3
- Homocysteine S-methyltransferase 1
- Cystathionine gamma-synthase 1, chloroplastic
- Cystathionine beta-lyase, chloroplastic
- Probable cystathionine gamma-synthase 2
- DNA
Sequence:
MALLVEKTSSGREYKVKDMSQADFGRLELELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGPGGGPDLIVDDGGDATLLIHEGVKAEEIFEKTGQVPDPTSTDNPEFQIVLSIIKEGLQVDPKKYHKMKERLVGVSEETTTGVKRLYQMQQNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMRATDVMIAGKVAVICGYGDVGKGCAAAMKTAGARVIVTEIDPICALQALMEGLQVLTLEDVVSEADIFVTTTGNKDIIMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETYPGVKRITIKPQTDRWVFPETKAGIIVLAEGRLMNLGCATGHPSFVMSCSFTNQVIAQLELWNEKASGKYEKKVYVLPKHLDEKVALLHLGKLGARLTKLSKDQSDYVSIPIEGPYKPPHYRY
Protein: Protein transport protein SEC23 (A0A0B4K5Z8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side {ECO:0000256|RuleBase:RU365030}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side {ECO:0000256|RuleBase:RU365030}.
Interaction partners:
- Secretory 24CD, isoform C
- Secretory 24AB, isoform A
- small monomeric GTPase
- Protein transport protein Sec31A
- Protein SEC13 homolog
- Secretory 16, isoform I
- Secretory 22, isoform B
- FI09914p
- Syntaxin-5
- Ergic53, isoform A
Sequence:
MTTYEEFIQQNEDRDGVRLTWNVWPSSRIEASRLVVPLACLYQPLKERPDLPPIQYEPVLCTRSNCRAILNPLCQVDYRAKLWVCNFCFQRNPFPPQYAAISEQHQPAELIPGFSTIEYTITRAPTMPPVFIFLVDTCMDEEELDALKDSLQMSLSLLPTNALVGLITFGKMIQVHELGAEGCSKSYVFRGTKDLTAKQVQDMLGIGRGAAPGPQQQQHLPGQPAGAAAPVPPAHRFLQPIGQCDAALGDLLSELQRDPWPVPQGKRYLRSTGAALSIAVGLLECTYPNTGGRIMTFVGGPCSQGPGQVVDDELKHPIRSHHDIHKDNVRFMKKAIKHYDALALRAATNGHSVDIYSCALDQTGLLEMKQLCNSTGGHMVMGDSFNSSLFKQTFQRVFARDGRNDLKMAFNATLEVKCSRELKISGGIGSCVSLNVKSPSVSDVEIGMGNTVQWKLCTLNPSSTVAYFFEVVNQHAAPIPQGGRGCIQFITQYQHPSGQRRIRVTTLARNWADATSNVHHISAGFDQEAAAVLMARMVVYRAETDEGPDILRWVDRQLIRLCQKFGEYSKDDPNSFRLSQNFSLFPQFMYHLRRSQFLQVFNNSPDETTFYRHMLMREDLTQSLIMIQPILYSYSFNGPPEPVLLDTASIQADRILLMDTFFQILIYHGETIAQWRALKYQDMPEYENFKQLLQAPVDDAQEILQTRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAYGQAPIGQVTVDGGAPVLTDDVSLQLFMEHLKKLAVSTTT
Protein: TIR domain-containing adapter molecule 2 (TICAM-2) (Putative NF-kappa-B-activating protein 502) (TRIF-related adapter molecule) (Toll-like receptor adaptor protein 3) (Toll/interleukin-1 receptor domain-containing protein) (MyD88-4) (Q86XR7)
Organism: Homo sapiens (Human)
Function: Functions as sorting adapter in different signaling pathways to facilitate downstream signaling leading to type I interferon induction. In TLR4 signaling, physically bridges TLR4 and TICAM1 and functionally transmits signal to TICAM1 in early endosomes after endocytosis of TLR4. In TLR2 signaling, physically bridges TLR2 and MYD88 and is required for the TLR2-dependent movement of MYD88 to endosomes following ligand engagement. Involved in IL-18 signaling and is proposed to function as a sorting adapter for MYD88 in IL-18 signaling during adaptive immune response. Forms a complex with RAB11FIP2 that is recruited to the phagosomes to promote the activation of the actin-regulatory GTPases RAC1 and CDC42 and subsequent phagocytosis of Gram-negative bacteria.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:25825441}. Golgi apparatus. Cell membrane {ECO:0000269|PubMed:25825441}. Endoplasmic reticulum. Early endosome membrane. Late endosome membrane. Cell projection, phagocytic cup {ECO:0000269|PubMed:30883606}. Note=Localized to the plasma membrane as a result of myristoylation. Phosphorylation on Ser-16 leads to its depletion from the membrane. Upon LPS stimulation colcoalizes with isoform 2 in late endosomes.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum. Early endosome membrane. Late endosome membrane. Note=Translocates to late endosomes upon LPS stimulation where it colcoalizes with isoform 1.
Interaction partners:
- Toll-like receptor 4
- Toll-like receptor 2
- TIR domain-containing adapter molecule 1
- TNF receptor-associated factor 6
- Toll/interleukin-1 receptor domain-containing adapter protein
- Toll-like receptor 9
- Receptor-interacting serine/threonine-protein kinase 1
- Interferon regulatory factor 3
- Toll-like receptor 3
- NAD
Sequence:
MGIGKSKINSCPLSLSWGKRHSVDTSPGYHESDSKKSEDLSLCNVAEHSNTTEGPTGKQEGAQSVEEMFEEEAEEEVFLKFVILHAEDDTDEALRVQNLLQDDFGIKPGIIFAEMPCGRQHLQNLDDAVNGSAWTILLLTENFLRDTWCNFQFYTSLMNSVNRQHKYNSVIPMRPLNNPLPRERTPFALQTINALEEESRGFPTQVERIFQESVYKTQQTIWKETRNMVQRQFIA
Protein: ADAM metallopeptidase domain 28, isoform CRA_a (Epididymis secretory sperm binding protein) (A0A384NKT9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MLQGLLPVSLLLSVAVSAIKELPGVKKYEVVYPIRLHPLHKREAKEPEQQEQFETELKYKMTINGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYYQGHILNEKVSDASISTCRGLRGYFSQGDQRYFIEPLSPIHRDGQEHALFKYNPDEKNYDSTCGMDGVLWAHDLQQNIALPATKLVKLKDRKVQEHEKYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATELAGTTVGLAFMSTMCSPYSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYSCKCPSTICVMDKALSFYIPTDFSSCSRLSYDKFFEDKLSNCLFNAPLPTDIISTPICGNQLVEMGEDCDCGTSEECTNICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDDRFQVNGFPCHHGKGHCLMGTCPTLQEQCTELWGPGRRTNPFPCACAKENHFR