wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger MYM-type containing 3 (A6NHB5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDPSDFPSPFDPLTLPEKPLAGDLPVDMEFGEDLLESQTAPTRGWAPPGPSPSSGALDLLDTPAGLEKDPGVLDGATELLGLGGLLYKAPSPPEVDHGPEGTLAWDAGDQTLEPGPGGQTPEVVPPDPGAGANSCSPEGLLEPLAPDSPITLQSPHIEEEETTSIATARRGSPGQEEELPQGQPQSPNAPPSPSVGETLGDGINSSQTKPGGSSPPAHPSLPGDGLTAKASEKPPERVQKRSERVRRAEPPKPEVVDSTESIPVSDEDSDAMVDDPNDEDFVPFRPRRSPRMSLRSSVSQRAGRSAVGTKMTCAHCRTPLQKGQTAYQRKGLPQLFCSSSCLTTFSKKPSGKKTCTFCKKEIWNTKDSVVAQTGSGGSFHEFCTSVCLSLYEAQQQRPIPQSGDPADATRCSICQKTGEVLHEVSNGSVVHRLCSDSCFSKFRANKGLKTNCCDQCGAYIYTKTGSPGPELLFHEGQQKRFCNTTCLGAYKKKNTRVYPCVWCKTLCKNFEMLSHVDRNGKTSLFCSLCCTTSYKVKQAGLTGPPRPCSFCRRSLSDPCYYNKVDRTVYQFCSPSCWTKFQRTSPEGGIHLSCHYCHSLFSGKPEVLDWQDQVFQFCCRDCCEDFKRLRGVVSQCEHCRQEKLLHEKLRFSGVEKSFCSEGCVLLYKQDFTKKLGLCCITCTYCSQTCQRGVTEQLDGSTWDFCSEDCKSKYLLWYCKAARCHACKRQGKLLETIHWRGQIRHFCNQQCLLRFYSQQNQPNLDTQSGPESLLNSQSPESKPQTPSQTKVENSNTVRTPEENGNLGKIPVKTRSAPTAPTPPPPPPPATPRKNKAAMCKPLMQNRGVSCKVEMKSKGSQTEEWKPQVIVLPIPVPIFVPVPMHLYCQKVPVPFSMPIPVPVPMFLPTTLESTDKIVETIEELKVKIPSNPLEADILAMAEMIAEAEELDKASSDLCDLVSNQSAEGLLEDCDLFGPARDDVLAMAVKMANVLDEPGQDLEADFPKNPLDINPSVDFLFDCGLVGPEDVSTEQDLPRTMRKGQKRLVLSESCSRDSMSSQPSCTGLNYSYGVNAWKCWVQSKYANGETSKGDELRFGPKPMRIKEDILACSAAELNYGLAQFVREITRPNGERYEPDSIYYLCLGIQQYLLENNRMVNIFTDLYYLTFVQELNKSLSTWQPTLLPNNTVFSRVEEEHLWECKQLGVYSPFVLLNTLMFFNTKFFGLQTAEEHMQLSFTNVVRQSRKCTTPRGTTKVVSIRYYAPVRQRKGRDTGPGKRKREDEAPILEQRENRMNPLRCPVKFYEFYLSKCPESLRTRNDVFYLQPERSCIAESPLWYSVIPMDRSMLESMLNRILAVREIYEELGRPGEEDLD
Protein: Carbohydrate sulfotransferase 4 (EC 2.8.2.-) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3) (GST-3) (High endothelial cells N-acetylglucosamine 6-O-sulfotransferase) (HEC-GlcNAc6ST) (L-selectin ligand sulfotransferase) (LSST) (N-acetylglucosamine 6-O-sulfotransferase 2) (GlcNAc6ST-2) (Gn6st-2) (Q9R1I1)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase involved in SELL/L-selectin ligand biosynthesis pathway. Catalyzes the transfer of the sulfate group from 3'-phospho-5'-adenylyl sulfate (PAPS) onto the hydroxyl group at C-6 position of the non-reducing N-acetylglucosamine (GlcNAc) residue within O-linked mucin-type glycans. Contributes to generate sialyl 6-sulfo Lewis X determinant (also known as MECA-79 epitope) for SELL recognition, a prerequisite for continuous lymphocyte homing into peripheral lymph nodes and antigen immune surveillance. Transfers the sulfate group primarily on core 2 GlcNAcbeta1-6(Galbeta1-3)GalNAcalphaSer/Thr and extended core 1 GlcNAcbeta1-3Galbeta1-3GalNAcalphaSer/Thr based O-linked glycans on CD34 and GLYCAM1 peripheral node addressins (PNAds) expressed on the lumenal side of high endothelial venules (HEVs). The recognition of PNAds by SELL initiates a multistep process comprising tethering and rolling of blood lymphocytes on HEVs against the blood flow, followed by chemokine signaling, integrin-mediated lymphocyte adhesion onto endothelial cells and lymphocyte transendothelial migration. Modulates rolling velocity and differential T and B lymphocyte recruitment into peripheral lymph nodes, with a major role in B lymphocyte homing. Might be redundant in sulfation of MADCAM1 and lymphocyte trafficking to mesenteric lymph nodes. Can also sulfonate core 3 GlcNAcbeta1-3GalNAc-R based glycans as well as GlcNAcbeta1-3Galbeta1-Glc, GlcNAcbeta1-6ManOMe and GlcNAcbeta1-2Man oligosaccharides, which might be ectopically expressed during tumorigenesis (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15111310}; Single-pass type II membrane protein {ECO:0000269|PubMed:15111310}.
Interaction partners:
- Carbohydrate sulfotransferase 2
- Protein N-terminal asparagine amidohydrolase
- Glycosylation-dependent cell adhesion molecule 1
Sequence:
MMLLKKGRLLMFLGSQVIVVALFIHMSVHRHLSQREESRRPVHVLVLSSWRSGSSFVGQLFGQHPDVFYLMEPAWHVWMTFTSSTAWKLHMAVRDLLRSVFLCDMSVFDAYMNPGPRKQSSLFQWEQSRALCSAPVCDFFPAHEISSPKHCKLLCGQQPFDMVEKACRSHGFVVLKEVRFLSLQALYPLLTDPSLNLHVVHLVRDPRAVFRSREHTTIELVVDSHIVLGQHLETIKEEDQPYYAMKIICKSQVDIVKAIQTLPEALQQRYLFLRYEDLVRAPLAQTTRLYKFVGLDFLPHLQTWVHNVTRGKGMGQHAFHTNARNALNVSQAWRWSLPYEKVSQLQDACGEAMDLLGYLQVRSQQEQGNLSLDLLSSSHILGQVFREG
Protein: Secretoglobin family 1C member 2 (P0DMR2)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000250|UniProtKB:P11684}.
Interaction partners:
Sequence:
MKGSRALLLVALTLFCICRMATGEDNDEFFMDFLQTLLVGTPEELYEGTLGKYNVNEDAKAAMTELKSCRDGLQPMHKAELVKLLVQVLGSQDGA
Protein: RNA polymerase sigma factor (Q92N11)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
Sequence:
MSSENQEFKREMLAALPSLRAFAMSLIGRHDRADDLVQDTIMKAWAKQDHFEIGTNMKAWLFTILRNELYSQMRKRGREVQDSDGHLTETLAHHPEQYGSLDLQDFRRALEQLPPDQREAIILVGASGFSYEEAATICGCALGTIKSRVNRARQRLQEILQVRGENDYGPDETSAPITSRAFVS
Protein: Acetyl-CoA carboxylase (Q39478)
Organism: Cyclotella cryptica
Interaction partners:
Sequence:
MALRRGLYAAAATAILVTASVTAFAPQHSTFTPQSLSAAPTRNVFGQIKSAFFNHDVATSRTILHAATLDETVLSASDSVAKSVEDYVKSRGGNRVIRKVLIANNGMAATKSILSMRQWAYMEFGDERAIQFVAMATPEDLKANAEFIRLADSFVEVPGGKNLNNYANVDVITRIAKEQGVDAVWPGWGHASENPKLPNALDKLGIKFIGPTGPVMSVLGDKIAANILAQTAKVPSIPWSGSFGGPDDGPLQADLTEEGTIPMEIFNKGLVTSADEAVIVANKIGWENGIMIKASEGGGGKGIRFVDNEADLRNAFVQVSNEVIGSPIFLMQLCKNARHIEVQIVGDQHGNAVALNGRDCSTQRRFQKIFEEGPPSIVPKETFHEMELAAQRLTQNIGYQGAGTVEYLYNAADNKFFFLELNPRLQVEHPVTEGITGANLPATQLQVAMGIPLFNIPDIRRLYGREDAYGTDPIDFLQERYRELDSHVIAARITAENPDEGFKPTSGSIERIKFQSTPNVWGYFSVGANGGIHEFADSQFGHLFAKGPNREQARKALVLALKEMEVRGDIRNSVEYLVKLLETEAFKKNTIDTSWLDGIIKEKSVKVEMPSHLVVVGAAVFKAFEHVKVATEEVKESFRKGQVSTAGIPGINSFNIEVAYLDTKYPFHVERISPDVYRFTLDGNTIDVEVTQTAEGALLATFGGETHRIFGMDEPLGLRLSLDGATVLMPTIFDPSELRTDVTGKVVRYLQDNGATVEAGQPYVEVEAMKMIMPIKATESGKITHNLSAGSVISAGDLLASLELKDPSRVKKIETFSGKLDIMESKVDLEPQKAVMNVLSGFNLDPEAVAQQAIDSATDSSAAADLLVQVLDEFYRVESQFDGVIADDVVRTLTKANTETLDVVISENLAHQQLKRRSQLLLAMIRQLDTFQDRFGREVPDAVIEALSRLSTLKDKSYGEIILAAEERVREAKVPSFEVRRADLRAKLADPETDLIDLSKSSTLSAGVDLLTNLFDDEDESVRAAAMEVYTRRVYRTYNIPELTVGVENGRLSCSFSFQFADVPAKDRVTRQGFFSVIDDASKFAQQLPEILNSFGSKIAGDASKEGPVNVLQVGALSGDISIEDLEKATSANKDKLNMLGVRTVTALIPRGKKDPSYYSFPQCSGFKEDPLRRGMRPTFHHLLELGRLEENFALERIPAVGRNVQIYVGSEKTARRNAAQVVFLRAISHTPGLTTFSGARRALLQGLDELERAQANSKVSVQSSSRIYLHSLPEQSDATPEEIAKEFEGVIDKLKSRLAQRLTKLRVDEIETKVRVTVQDEDGSPRVVPVRLVASSMQGEWLKTSAYIDRPDPVTGVTRERCVIGEGIDEVCELESYDSTSTIQTKRSIARRVGSTYAYDYLGLLEVSLLGEWDKYLSSLSGPDTPTIPSNVFEAQELLEGPDGELVTGKREIGTNKVGMVAWVVTMKTPEYPEGRQVVVIVNDVTVQSGSFGVEEDEVFFKASKYARENKLPRVYIACNSGARIGLVDDLKPKFQIKFIDEASPSKGFEYLYLDDATYKSLPEGSVNVRKVPEGWAITDIIGTNEGIGVENLQGSGKIAGETSRAYDEIFTLSYVTGRSVGIGAYLVRLGQRIIQMKQGPMILTGYGALNKLLGREVYNSNDQLGGPQVMFPNGCSHEIVDDDQQGIQSIIQWLSFVPKTTDAVSPVRECADPVNRDVQWRPTPTPYDPRLMLSGTDEELGFFDTGSWKEYLAGWGKSVVIGRGRLGGIPMGAIAVETRLVEKIIPADPADPNSREAVMPQAGQVLFPDSSYKTAQALRDFNNEGLPVMIFGNWRGFSGGSRDMSGEILKFGSMIVDSLREYKHPIYIYFPPYGELRGGSWVVVDPTINEDKMTMFSDPDARGGILEPAGIVEIKFRLADQLKAMHRIDPQLKMLDSELESTDDTDVAAQEAIKEQIAAREELLKPVYLQAATEFADLHDKTGRMKAKGVIKEAVPWARSREYFFYLAKRRIFQDNYVLQITAADPSLDSKAALEVLKNMCTADWDDNKAVLDYYLSSDGDITAKISEMKKAAIKAQIEQLQKALEG
Protein: CLIP domain-containing serine protease HP8 (EC 3.4.21.-) (BzArgOEtase) (BAEEase) (Hemolymph proteinase 8) (HP8) [Cleaved into: CLIP domain-containing serine protease HP8 light chain; CLIP domain-containing serine protease HP8 heavy chain] (Q2VG86)
Organism: Bombyx mori (Silk moth)
Function: Endopeptidase with selective post-Arg cleavage site. Functions in the innate immune response to fungal and Gram-positive bacterial infections. Upon pathogen infection promotes nodulation; a cellular defense response in which hemocytes surround and isolate invading pathogens forming aggregates called nodules. Involved in activating nodule formation in response to infection with M.luteus, E.coli or S.cerevisiae. Able to bind the microbes M.luteus, E.coli or S.cerevisiae. According to another report, does not bind microorganisms.
Subcellular location: Secreted {ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:26707571, ECO:0000269|PubMed:7737188}. Cytoplasm {ECO:0000269|PubMed:26707571}. Note=In larvae, secreted in the hemolymph (PubMed:16399077, PubMed:26707571, PubMed:7737188). Only the uncleaved form is detected in hemolymph (PubMed:26707571). Uncleaved (42 kDa) and cleaved (29 kDa) forms, are weakly expressed in hemocytes (PubMed:26707571). Detected in the cytoplasm of various hemocytes including plasmatocytes, oenocytoids, granulocytes and prohemocytes (PubMed:26707571). Cleaved and uncleaved forms also localize to immune defense nodules that have been induced by injection with E.coli, M.luteus or S.cerevisiae cells (PubMed:26707571). {ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:26707571, ECO:0000269|PubMed:7737188}.
Interaction partners:
Sequence:
MKTPFEKIRIISCILVIVSTNVVGQKCNGGANCIPLEECTDLFQQLKQGNSPQLTRLLRGLHCGFEDLNSPKICCPPEFLARRSAFSSAGTNSNPTSILPNEKVCGIQNNDRIFGGIQTEIDEHPWMALLRYDKPLGWGFYCGGVLIAPMYVLTAAHCVKGSDLPSSWQLSQVRLGEWNTSTETDCVEGDCSGPVQDIPVQQIIAHENYDPNDKDQQNDIALLRLSRNAQFNDFVSPICLPTSNELRQNEFESDYMEVAGWGKTETRSESDVKLKVRVPIVNREECANVYSNVDRRVTNKQICAGGLAGRDSCRGDSGGALMGQSPKANNWYVFGVVSYGPSPCGTEGWPGVYTRVGSFMDWILSKLEQ
Protein: GH15225p (Ulp1) (Q9VWK5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ubiquitin-related modifier
- LD37257p
- Dorsal interacting protein 4
- SUMO-activating enzyme subunit
- Ran GTPase-activating protein
- Activator of SUMO 1
- Nuclear pore complex protein Nup133
- DNA repair protein Rad60
- Ubiquitin-like protease family profile domain-containing protein
- JmjC domain-containing histone demethylation protein 1
Sequence:
MSLPPEDTDLSTNSAYESALQIASNVSAARVVGSAVGQRFSPSPAAHPNVIERVASHVDSRRSTFPSWGNPSVAPRGSEEAAANATATQLLWAENQGLPTSHLLPTEQAFETLNTNAYCSPPGDSRFTFPSQNYSPLLPRCVPVPNQRYSPDGSPIHQLHELQNCPLIDSPIRLRFPSPLPEPPSLPTITLTVDALIDLDQNNQVAYYVQQYNNQPVLYQQNIHIGTGIQLCDQASENNQPIILHIVEHNPQTITESQEQFHQVVPEIQINNIQEQDQKFENGISEQNHPIATEAQDQTLTEIRDENQIVLAVQEKNLTRASEIQDQNQQTLTEIPEKCLQIASPVTTDIQVQSPQVVIEIQEQNHQSVTEIQEEVHQTAPEIQVNVFQTSSDIQGQNHQIVTEEQNHQTITETQEDYSAVSEIQWENLSFSAEIQEQNQQIVTEVTKLASPSVTDIQAQSPQSVIEIQDDDDEDLKFESDDLHTIPEIQEKNQQSPQFVIEIHYDNEDLKFASDNQEQDQQTAELQKERFQFASEIEKRDLQIVTDTHKQNYHNVTDIPFATYIQEENEQLTPEDQEEDQHYLNFEGNQQFQLQKQDQLSVPQIQKQTHQFESKVKKRKLQPFSEYQQKGQKDHIQERQYIQQEFTIHSNQAYSKVQYIQTIQTATPYVPQLEISQENSFEVQPAYEVNEGQRDRELVSYTGHEHQNFVDEVSTPLPPAEAQPGSTSEDISDPVSPEHWEQLESLDPSTICIRKTFNLIRDISESLVADPEQPEAEAHRKSIFLLRQKLADVCHKVLTEIIHGRATDEIISILREILEQTKEIPPRPTPKRDLQEDISMGLEILKKIRGMLSGWYSSRESETDSTDTGTGFQAQNGKGFGAGRQPENSFLSQKRRNQEENPRLIKYRRVDNSFPRLITNETAEDLIPNNSMAKRDQPQSSKRLSIFNPPVYTQHRVRNDAPHVPTPFDDEESSQRLANAGPSSRPMTYSDAVRLGHNGISESRVNGHSSHTVRREPSRLHRSILSHEMNCKDQEQYNELIRTQTNYVGSRYLKPGTPPTFQRAKAQSATSSSCSLQDNQSNITDSFPSPHGRANPELTEYAKLINRQENEENRSPAPQQPKRNASNSSASHASTISSSASSSCSTCSTCSSSDTEPMLVKDSPEVKEANEANEANEANEANETKENDAPQPTTTRIKKPDFLHRRFANCIFLRNDFAENFKARANRRQLESMHLLGIAEQQANESKDERLAYEKKLREVMFRSGAPHRPFFEIGPLEQPEEKKETKLIPLTKEDHARFQEMTTIEVTTNLIFKYNLQITTDDIFTFVDGEWLNDAIINFYMSMLTERSEKRAGELPATYAMNTFFMPRLLQAGYAGVRRWTRKVDLFSKDIIPVPVHCGNVHWCMAIIHLRNKTIFYYDSMGRPNQPALDALVKYLHEESLDKRKQPFDMTGFVVENAQNIPRQGNSSDCGVFSCMFAEYITRDVPITFSQAEMLYFRTKMALEIADGKLWQ
Protein: Suppressor of cytokine signaling 1 (V9Q5U6)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MVAHSTVEEQDTTSAPSSSSSSASSSSSSVSQSHRQHPSKQCVASPIPVPDLLDQQPPLPLLDPVPTHFPPFRCQVDFLIITRTASMLERSGFYWGPLGVEEAHSRLKDVATGTFLIRDSRQKDVFFTLSYRADGGPVSVRIIYKGQRFSLAGSEHSFPCLFLLLEHYINSSKKSLTVPYRKQRPTLQELCRKQVVESCSGDVERVARVPVNPVLKHFLLEFPYRI
Protein: Transmembrane protein 100 (Q9CQG9)
Organism: Mus musculus (Mouse)
Function: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor-dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons. Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23485812, ECO:0000269|PubMed:25640077}; Multi-pass membrane protein {ECO:0000269|PubMed:23485812, ECO:0000269|PubMed:25640077}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:23485812}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Colocalized with HSPA5 in the endoplasmic reticulum (ER). Enriched in ER microsome. Colocalized with BMP4 in neural cell bodies and neural fibers of the enteric nervous system (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MTEESTKENLGAPKSPTPVTMEKNPKREVVVTTGPLVSEVQLMAATGGAELSCYRCIIPFAVVVFITGIVVTAVAYSFNSHGSIISIFGLVLLSSGLFLLASSALCWKVRQRNKKVKRRESQTALVVNQRCLFA
Protein: Transcription factor CBF/NF-Y/archaeal histone domain-containing protein (Q2UK39)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Histone H2A/H2B/H3 domain-containing protein
- Transcriptional activator HAP2
- BZIP domain-containing protein
- Uncharacterized protein
Sequence:
MSSTSPSKEPEVEPEVQSGEEQEQMDKEQQDQAQNQGEFEVKEQDRWLPIANVARIMKLALPDNAKIAKEAKECMQECVSEFISFITSEASEKCQQEKRKTVNGEDILFAMTSLGFENYAEALKIYLSKYRETQSARGEHQNRPTSSGYASGGPVGGVSSAPGGRPATAGGFPDAADNTNSIMNPSLDPTEQDPSAYGYPPMVGQPHNGTAGDSY
Protein: Desmoglein 2 (F1LYX9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, desmosome {ECO:0000256|ARBA:ARBA00004568}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- Desmocollin 2
- Desmoplakin
- Junction plakoglobin
- Plakophilin-1
- Plakophilin-3
- Plakophilin-2
- Desmocollin 1
- Transmembrane protein 43
- Caspase-3
- Plakophilin 4
Sequence:
MARSPSGRCTLLLLLQLLAVVCLDFGDGLHLEVFSTRGEDRLFTKRTHLVRQKRAWITAPVALREGEDLSKKNPIAKIHSDLAEERGIKITYKYTGKGITEPPFGIFVFDRNTGDLNITSILDREETPFFLLTGYALDSRGNNLEKPLELRIKVLDINDNEPVFTQEVFVGSIEELSAAHTLVMKITATDADDPQTLNSKISYRIVSQEPANTPVFYLNKDTGEIYTTSFALDREEHSSYSLTVEARDGNGQITDKPVQQAQVQIRILDVNDNIPVVEYGTYEGVVEENQVNVEVMRIKVTDADEVGSDNWLANFTFASGNEGGYFHIETDTQTNEGIVTLVKELDYEEMKKLDLSILVTNKAAFHKSVVSKYKATPIPITVKVKNVVEGIHFKSSTVTFRASEAMDRSSLSRSIGKFQVFDEDTGKAADVTYVKVQDTDNWVSVDSETSEIKLVKIPDFESRHVQNGTYTVKVVAISKGHPQKTVTGTILINVEDVNDNCPVLVDSVRSVCADAPYVNVTAEDLDGPRNSGPFTFSIIDQPPGTAQKWKITHQESTSVLLQPSERKLGRSEIPFLISDSQGFSCLERQVLQLTVCECLEGGGCVAALYDNYVGLGPAAIALMILALLLLLLVPLLLLMCHCGEGAKGFAPIPGTIEMLHPWNNEGAPPEDKVVPSLLVTDHVENSGVRGGGGGGGGGVGGVKLKEGVSSSASITKGQHELIEVDGRWEEHRSLLTSGLTHHVATAGSIAANDTTIRTTRATGASRDMSGARGAVAMNEELLRSYFTEKAASYAGEDDFHLAKDCLLVYSQEDTDSLRGSVGCCSFIEGELDDLFLDDLGPKFKTLAEVCLGRKIDMDVDIEQRQKPVRETSVNAAPGSHYTQVTASSESTYSSNSGFQAPKPLHGAHTEKVTQEVVTESSVSSRQSQKVVPPPNPVASGNIIVTETSYAAGSAVPPSTVILAPRQPQSLIVTERVYAPASTLVDQHYANEENVLVTERVIQPNGGIPKPLEVTQHLNDAQYVMVRERESILAPSSGVQPTLAMPSVAAGGQNVTVTERVLTPASTLQSSYQIPSEASIKARKTVLSSVGGMGPLPNLDLEESGPPNSTVTTSSTRVTKHSTVQHSYS
Protein: Shaggy-related protein kinase iota (EC 2.7.11.1) (ASK-iota) (GSK3/shaggy-related protein kinase 1) (AtGSK1) (Protein BIN2-like 2) (Shaggy-related protein kinase 2-3) (AtSK2-3) (Shaggy-related protein kinase 22) (AtSK22) (Q39012)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phosphorylates BSK1, BSK3, BSK5, BSK6, BSK8 and BSK11 in vitro. May mediate extracellular signals to regulate transcription in differentiating cells (By similarity).
Interaction partners:
- Protein BRASSINAZOLE-RESISTANT 1
- Protein BRASSINAZOLE-RESISTANT 2
- Serine/threonine-protein phosphatase BSU1
- BES1/BZR1 homolog protein 2
- BES1/BZR1 homolog protein 1
- Shaggy-related protein kinase eta
- Serine/threonine-protein kinase BSK3
- Serine/threonine-protein kinase BSK1
- Serine/threonine-protein kinase BSK8
- Serine/threonine-protein kinase BSK11
Sequence:
MASLPLGPQPHALAPPLQLHDGDALKRRPELDSDKEMSAAVIEGNDAVTGHIISTTIGGKNGEPKQTISYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSRDELFLNLVMEYVPETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNPNYTDFRFPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLPNGRPLPPLFNFKQELGGASMELINRLIPEHVRRQMSTGLQNS
Protein: ATP-dependent zinc metalloprotease FtsH 2 (EC 3.4.24.-) (Q55700)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (By similarity).
Subcellular location: Cellular thylakoid membrane {ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:12953117}; Multi-pass membrane protein {ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:12953117}; Stromal side {ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:12953117}. Note=A fraction is found associated with PSII. Localization to the cell inner membrane has been specifically tested and not seen.
Interaction partners:
- Photosystem II CP47 reaction center protein
- Prohibitin
- Chaperone protein dnaK1
- Chaperone protein dnaK3
- Chaperone protein DnaK2
- Chaperonin GroEL 1
- Iron stress-induced chlorophyll-binding protein
- Uncharacterized protein slr1128
- Protein translocase subunit SecY
- Membrane protein insertase YidC
Sequence:
MKFSWRTALLWSLPLLVVGFFFWQGSFGGADANLGSNTANTRMTYGRFLEYVDAGRITSVDLYENGRTAIVQVSDPEVDRTLRSRVDLPTNAPELIARLRDSNIRLDSHPVRNNGMVWGFVGNLIFPVLLIASLFFLFRRSSNMPGGPGQAMNFGKSKARFQMDAKTGVMFDDVAGIDEAKEELQEVVTFLKQPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCLIFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFEGNTGIIIIAATNRPDVLDSALMRPGRFDRQVMVDAPDYSGRKEILEVHARNKKLAPEVSIDSIARRTPGFSGADLANLLNEAAILTARRRKSAITLLEIDDAVDRVVAGMEGTPLVDSKSKRLIAYHEVGHAIVGTLLKDHDPVQKVTLIPRGQAQGLTWFTPNEEQGLTTKAQLMARIAGAMGGRAAEEEVFGDDEVTTGAGGDLQQVTEMARQMVTRFGMSNLGPISLESSGGEVFLGGGLMNRSEYSEEVATRIDAQVRQLAEQGHQMARKIVQEQREVVDRLVDLLIEKETIDGEEFRQIVAEYAEVPVKEQLIPQL
Protein: Prothoracicostatic peptide (Bom-PTSP) (P82003)
Organism: Bombyx mori (Silk moth)
Function: Inhibits ecdysteroid biosynthesis in the prothoracic gland of fifth instar larvae, with maximum inhibition during the spinning stage. When administered to day 8 fifth instar larvae it produces a significant delay in the commencement spinning behavior.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MRWCLFALWVFGVATVVTAAEEPHHDAAPQTDNEVDLTEDDKRAWSSLHSGWAKRAWQDMSSAWGKRAWQDLNSAWGKRGWQDLNSAWGKRAWQDLNSAWGKRGWQDLNSAWGKRDDDEAMEKKSWQDLNSVWGKRAWQDLNSAWGKRAWQDLNSAWGKRGWNDISSVWGKRAWQDLNSAWGKRAWQDMSSAWGKRAPEKWAAFHGSWGKRSSIEPDYEEIDAVEQLVPYQQAPNEEHIDAPEKKAWSALHGTWGKRPVKPMFNNEHSATTNEA
Protein: RING-type domain-containing protein (Tandem-array-modifier protein) (G5ED20)
Organism: Caenorhabditis elegans
Interaction partners:
- Runt-related transcription factor rnt-1
- Tat-binding homolog 7
- Protein lin-36
- Acyltransferase
Sequence:
MDIPGTSGTSNYQQWAHVVECPICYNIYDKPMQMGCGHTLCSTCIGRLVDQVKTNMAEELGRPRGPLLHPDDIGPGFGGLGGFADQEDQPHFIDLPRLDPRMNPNDPNMVRGIVVLPRRGPEARATEIKCPECRKPTLVPADGLPVNYRVQEIVQKVAPLFKDRHLVKLCNQCEAVLSQGVYFDCSQCEETGRKICSTCAIRLHNGHQLVEKKALTSDDVREMKQKISDASHAAFQSLENLKPRLQSVGGTIEAKALDKLTSLIKIFEFMLSTFDSKIKENSTMDELMEEVKKAEKISKVYSEAGGRVDVMLTAIESAFNSYWDPFEKLKQEMGFQIDEPTGSVNQIPASEGGAERVNEVAAPAAGRPIPQNARNLRGALNHFAQVARNRNRQARGVQQQQDLPFLPPPPPHQLVMPPPAMPPPQHMQAQRLWGGPQPQRMNQPMMAQVGGRPGQYIMGHPPPMHHQMQQGPPRMMYMHQQHHPMHQVEDQMQRQHQRMQQPNMNNIMHGNMQIAFQQHMHNNANVPMPPQMPAHPQQQQQQRHPNEGQQFQQGPPPPPPQRIQNHQQQMQQYHQQLQVQQQQQPQPRAQPFRPPIQQQQQLQQIDLQAMNDRQFQQLADEIVAEDQMVQNAVDPAAPADIPRADWEEIQVAQRGAGDFGINFHPEPIVEEVEEEQPEVDQQVVVNGQVVENYRAGDINNVIHFEEVPVVLEPDVDGNVDHNNGILENNVEEQEQFDDVPPQINNFVEFDDMREQVDAIEDEEFEPVLHRAAIEFQEAADQDALEQDVRERNLLDHEAENEEEDDGDLPYEEEDDEEEEVHVRNSVVRRRVQRPRDAAHISEVETRRSARRLARNSNNPTDEPSTSSGAAGPSNRPPHSPTPPPGNKRRRVDRKPKTEEPEQMETEPVDPVHRAPKRRGTSAASSSSNGMPSSSAPTTRSQTRL
Protein: Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE (EC 2.1.1.163) (EC 2.1.1.201) (2-methoxy-6-polyprenyl-1,4-benzoquinol methylase) (Demethylmenaquinone methyltransferase) (P0A887)
Organism: Escherichia coli (strain K12)
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). In vitro, can use demethylphylloquinol, an intermediate in the biosynthesis of phylloquinone (vitamin K1) in plants and cyanobacteria.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30686758}.
Interaction partners:
- Ubiquinone biosynthesis accessory factor UbiJ
- Ubiquinone biosynthesis O-methyltransferase
- 3-demethoxyubiquinol 3-hydroxylase
- 2-octaprenyl-6-methoxyphenol hydroxylase
- 2-octaprenylphenol hydroxylase
- Probable protein kinase UbiB
- Ubiquinone biosynthesis accessory factor UbiK
- 3-octaprenyl-4-hydroxybenzoate carboxy-lyase
- 4-hydroxybenzoate octaprenyltransferase
- 1,4-dihydroxy-2-naphthoate octaprenyltransferase
Sequence:
MVDKSQETTHFGFQTVAKEQKADMVAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRLVGETGKVVLADINESMLKMGREKLRNIGVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTDKDKALRSMYRVLKPGGRLLVLEFSKPIIEPLSKAYDAYSFHVLPRIGSLVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYKF
Protein: Probable indole-3-acetic acid-amido synthetase GH3.4 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 4) (OsGH3-4) (Q60EJ6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May catalyze the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin.
Interaction partners:
Sequence:
MPEAVAAAVSPAAAAATAMCAEHREKLEHIERVTRNAGQEQRRVLEEILAQNAQAEYLRRLGVPGDAPGADEAFRRLAPLVTYEDILPDVLRIANGDTSPILSGKPVSEFLTSSGTSGGERKLMPTIEEEMERRSGLYSLLMPVMSRQVPGLDKGKAMYLYFVKSEWRTPGGLPARPVLTSFYRSRYFLERPHDPYTVYTSPDEAVLCEDAYQSMYAQLICGLVHRADVLRVGAVFASGFLRAIRFLEKHWPSLCRDIRAGELDGGVTDPAVRGAVGRVLRGADPALADAIEAECARPSWQGIIRRVWPSTKYIDVIVTGAMAQYIPTLEFYGGGLPLACTMYASSECYFGLNLNPMCKPSEVAYTLIPTMCYFEFLPVNSGANDVAAPEPDHRGLVDLVDVKLGHEYELVVTTYSGLYRYRVGDVLRVAGFKNAAPMFAFVRRKNVALSIDSDKTDEAELHAAVTEAVQHLAPFGASLVEYTSYADTATTIPGHYVLFWELRSPAGGTPVPASVFEDCCLAVEEGLNSVYRQCRAADRSIGPLEIRVVADGTFDKLMDYALSRGASINQYKAPRCVRPGPVVELLDGRVQATYFSPKCPKWCAGGNKQWISSGAAAKKTTTTCDSLAV
Protein: Atos homolog protein A (Q32MH5)
Organism: Homo sapiens (Human)
Function: Transcription regulator that syncronizes transcriptional and translational programs to promote macrophage invasion of tissues.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q7JXG9}.
Interaction partners:
Sequence:
MKPDRDTLDEYFEYDAEEFLVSLALLITEGRTPECSVKGRTESFHCPPAQSCYPVTTKHECSDKLAQCRQARRTRSEVTLLWKNNLPIMVEMMLLPDCCYSDDGPTTEGIDLNDPAIKQDALLLERWILEPVPRQNGDRFIEEKTLLLAVRSFVFFSQLSAWLSVSHGAIPRNILYRISAADVDLQWNFSQTPIEHVFPVPNVSHNVALKVSVQSLPRQSNYPVLTCSIHTNIGLYEKRIQQHKLKTHQHHNPNEAEQCGTNSSQRLCSKQTWTMAPESVLHAKSGPSPEYTAAVKNIKLYPGTGSKSDHGTSQANILGFSGIGDIKSQETSVRTLKSFSMVDSSISNRQSFWQSAGETNPLIGSLIQERQEIIARIAQHLIHCDPSTSHVSGRPFNTQESSSLHSKLFRVSQENENVGKGKEAFSMTFGSPEFSSPEDTNEGKIRLKPETPRSETCISNDFYSHMPVGETNPLIGSLLQERQDVIARIAQHLEHIDPTASHIPRQSFNMHDSSSVASKVFRSSYEDKNLLKKNKDESSVSISHTKCSLLGDISDGKNLVPNKCFTSFKNNSKEKCSLKHQTRNQCQNNPSEIIQSTYQETQNKSSSLSTSSILSQHKENNLDLTSRFKEQEMSNGIDKQYSNCTTIDKQICTNKYKEKIINENYNPKFFGNLQSDDSKKNDSKIKVTVLEMSEYLNKYESMSSNKDSKRPKTCEQNTQLNSIENYLNKDNEGFKCKKSDQLKNEQDKQEDPTNEKSQNYSQRRSIKDCLSTCEQPKNTEVLRTTLKHSNVWRKHNFHSLDGTSTRAFHPQTGLPLLSSPVPQRKTQSGCFDLDSSLLHLKSFSSRSPRPCLNIEDDPDIHEKPFLSSSAPPITSLSLLGNFEESVLNYRFDPLGIVDGFTAEVGASGAFCPTHLTLPVEVSFYSVSDDNAPSPYMGVITLESLGKRGYRVPPSGTIQVTLFNPNKTVVKMFVVIYDLRDMPANHQTFLRQRTFSVPVKQEVKRSVNKENIRHTEERLLRYLIHLRFQSSKSGKIYLHRDVRLLFSRKSMEVDSGAAYELKSYTESPTNPQFSPRC
Protein: Acetyl-CoA carboxylase alpha (A0A087X126)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLSDLGISSLQDGLALHISSWIKRSGSVVLGSHCSSESPRGALGDKPHPQRFRFI
Protein: Hypoxia-inducible lipid droplet-associated protein (Hypoxia-inducible gene 2 protein) (Q9Y5L2)
Organism: Homo sapiens (Human)
Function: Increases intracellular lipid accumulation. Stimulates expression of cytokines including IL6, MIF and VEGFA. Enhances cell growth and proliferation.
Subcellular location: Lipid droplet. Secreted. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Frizzled-10
Sequence:
MKHVLNLYLLGVVLTLLSIFVRVMESLEGLLESPSPGTSWTTRSQLANTEPTKGLPDHPSRSM