wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase SIK1 (EC 2.7.11.1) (Protein kinase KID2) (Salt-inducible kinase 1) (SIK-1) (Serine/threonine-protein kinase SNF1-like kinase 1) (Serine/threonine-protein kinase SNF1LK) (Q9R1U5)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, CRTC1/TORC1 and CRTC2/TORC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators CRTC1/TORC1 and CRTC2/TORC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1. In concert with CRTC1/TORC1, regulates the light-induced entrainment of the circadian clock by attenuating PER1 induction; represses CREB-mediated transcription of PER1 by phosphorylating and deactivating CRTC1/TORC1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19244510}. Nucleus {ECO:0000269|PubMed:19244510}. Note=Following ACTH (adrenocorticotropic hormone) treatment and subsequent phosphorylation by PKA, translocates to the cytoplasm, where it binds to YWHAZ.
Interaction partners:
- CREB-regulated transcription coactivator 2
- CREB regulated transcription coactivator 3
Sequence:
MVIMSEFSAVPTGTGQGQQKPLRVGFYDVERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDSSNLEKIYREVQLMKLLNHPNIIKLYQVMETKDMLYIVTEFAKNGEMFDYLTSNGHLSENEARKKFWQILSAVEYCHNHHIVHRDLKTENLLLDGNMDIKLADFGFGNFYKPGEPLSTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPFFMSQDCETLIRRMLVVDPAKRITIAQIRQHRWMQADPTLLQQDDPAFSMQGYTSNLGDYNEQVLGIMQALGIDRQRTVESLQNSSYNHFAAIYYLLLERLREHRSTQPSSRATPAPARQPQLRNSDLSSLEVPQEILPCDPFRPSLLCPQPQALAQSVLQAEIDCDLHSSLQPLFFPLDTNCSGVFRHRSISPSSLLDTAISEEARQGPSLEEEQEVQEPLPGSTGRRHTLAEVSTHFSPLNPPCIIVSSSAAVSPSEGTSSDSCLPFSASEGPAGLGGGLATPGLLGTSSPVRLASPFLGSQSATPVLQSQAGLGATVLPPVSFQEGRRASDTSLTQGLKAFRQQLRKNARTKGFLGLNKIKGLARQVCQSSIRGSRGGMSTFHTPAPSSGLQGCTASSREGRSLLEEVLHQQRLLQLQHHSAVSSDYQQAPQLSPVPYVLTPCDGLLVSGIPLLPTPLLQPGMSPVASAAQLLDAHLHISAGPVALPTGPLPQCLTRLSPSCDPAGLPQGDCEMEDLTSGQRGTFVLVQ
Protein: Heat shock 70 kDa protein 14 (HSP70-like protein 1) (Heat shock protein HSP60) (Heat shock protein family A member 14) (Q0VDF9)
Organism: Homo sapiens (Human)
Function: Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16002468}.
Interaction partners:
- DnaJ homolog subfamily C member 2
- DnaJ homolog subfamily B member 4
- DnaJ homolog subfamily B member 1
- DnaJ homolog subfamily B member 6
- DnaJ homolog subfamily C member 5
- Heat shock protein HSP 90-beta
- Heat shock 70 kDa protein 12A
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 12B
- DnaJ homolog subfamily A member 1
Sequence:
MAAIGVHLGCTSACVAVYKDGRAGVVANDAGDRVTPAVVAYSENEEIVGLAAKQSRIRNISNTVMKVKQILGRSSSDPQAQKYIAESKCLVIEKNGKLRYEIDTGEETKFVNPEDVARLIFSKMKETAHSVLGSDANDVVITVPFDFGEKQKNALGEAARAAGFNVLRLIHEPSAALLAYGIGQDSPTGKSNILVFKLGGTSLSLSVMEVNSGIYRVLSTNTDDNIGGAHFTETLAQYLASEFQRSFKHDVRGNARAMMKLTNSAEVAKHSLSTLGSANCFLDSLYEGQDFDCNVSRARFELLCSPLFNKCIEAIRGLLDQNGFTADDINKVVLCGGSSRIPKLQQLIKDLFPAVELLNSIPPDEVIPIGAAIEAGILIGKENLLVEDSLMIECSARDILVKGVDESGASRFTVLFPSGTPLPARRQHTLQAPGSISSVCLELYESDGKNSAKEETKFAQVVLQDLDKKENGLRDILAVLTMKRDGSLHVTCTDQETGKCEAISIEIAS
Protein: Heparan-sulfate 6-O-sulfotransferase (EC 2.8.2.-) (Q9VDR6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Membrane {ECO:0000256|RuleBase:RU364122}; Single-pass type II membrane protein {ECO:0000256|RuleBase:RU364122}.
Interaction partners:
- Heparin sulfate O-sulfotransferase
- Heparan sulfate 3-O sulfotransferase-B, isoform A
- heparosan-N-sulfate-glucuronate 5-epimerase
- GH20068p
- Extracellular sulfatase SULF-1 homolog
- Dally-like, isoform A
- Syndecan
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase
- Division abnormally delayed protein
- Exostosin-1
Sequence:
MPGDMHKNVSVQVDSDFALLLPSGVYEIKKMEPRSKIRTIIVFCLFLAIAGIIGFGYFCQDQVCALSKRAVILQSSDILAYNELPLHQANSINGNANGNSNGNGNSVGGITAMASKSSAPQNIIANAGLSYEDVLNDDFQFDMDGHDVMVFLHIQKTGGTSFGRHLVRDLDLKRPCECQRQRKRCYCFRPHRNENWLFSRYSTGWKCGLHADWTELTSCVDVELDKNEGETAKRRYFYISLLRQPIARYMSEYRHVRRGATWKGSRHWCLGRQATAAELPACYKGKDWLDVDLDQFAGCESNLAANRQTRMLADLALVGCYNKSSMPAHERDRVMLASAKRNLAAMAYFGLTEYQKMSQYIFEETFNLRFAIPFEQHNTTISATAVQNLRPDQKRRIEKLNSLDIELYAFAKTLLFQRFEHLKAKDTNFEQRYANLGNIYFKQGVTEFNWDSNVEDGLSTDH
Protein: Selina-4(15),7(11)-diene synthase ((2E,6E)-farnesyl diphosphate cyclizing) (EC 4.2.3.181) (Selinadiene synthase) (SdS) (Terpene synthase) (Type I terpene cyclase) (B5HDJ6)
Organism: Streptomyces pristinaespiralis (strain ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / KCC S-0507 / NBRC 13074 / NRRL 2958 / 5647)
Function: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene selina-4(15),7(11)-diene via a 1,10-cyclization, which requires the abstraction of the pyrophosphate from FPP leading to a (E,E)-germacradienyl cation. The only accepted substrate is (2E,6E)-farnesyl diphosphate (FPP).
Interaction partners:
Sequence:
MEPELTVPPLFSPIRQAIHPKHADIDVQTAAWAETFRIGSEELRGKLVTQDIGTFSARILPEGREEVVSLLADFILWLFGVDDGHCEEGELGHRPGDLAGLLHRLIRVAQNPEAPMMQDDPLAAGLRDLRMRVDRFGTAGQTARWVDALREYFFSVVWEAAHRRAGTVPDLNDYTLMRLYDGATSVVLPMLEMGHGYELQPYERDRTAVRAVAEMASFIITWDNDIFSYHKERRGSGYYLNALRVLEQERGLTPAQALDAAISQRDRVMCLFTTVSEQLAEQGSPQLRQYLHSLRCFIRGAQDWGISSVRYTTPDDPANMPSVFTDVPTDDSTEPLDIPAVSWWWDLLAEDARSVRRQVPAQRSA
Protein: CRC-A (Q9NIR4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MESLQLPKELYWDLKMEPQSPTSVLGSDLFPLTDSNDTEWLYDDNFANGITLIGDDEALTLEEVASLQLLSDEEMVVEIFDLKDEECLLDQKATLNCIDYDSNSFQPNINVITQAIVPANKVQFGASSDAASLPSAADYQLNDGPSLILQQLTPPQSPPQFDAYKQAGDAQPKPVLVKAEQKVQCYTPDVTHAASATPFNFTNWVGGSEIARENQLVDDIVNMRAKELELSTNWQQLNEDCESQASSSLDSRSTGSGVCSSIADADEDWVPELISSSSSPAPTTIEQSASQPKKRTRTYGRGVEDRKIRKKEQNKNAATRYRQKKKLEMENVLGEEHVLSKENEQLRRTLQERHNEMRYLRQLIREFYHERKR
Protein: Invertebrate-type lysozyme (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase) (Destabilase) (Q8IU26)
Organism: Ruditapes philippinarum (Japanese carpet shell) (Venerupis philippinarum)
Function: Bacteriolytic activity against Gram-positive bacterium M.luteus and thereby probably protects against bacterial infection. Also has chitinase activity. May act as an ispopeptidase, cleaving isopeptide bonds between the side chains of Lys and Gln residues in proteins or in the cross-linking peptide of peptidoglycan in bacterial cell walls.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P83673}.
Interaction partners:
Sequence:
METVSVEEGLDFAPGMVSQKCLLCMCKLESGGCKPIGCRMDVGSLSCGYFQIKQPYWIDCGKPGKDWKSCSNDINCSSKCVQQYMKRYATHYRCPLNCEGFAREHNGGPNGCHSSRTLKYWELLQKIPGCKGVKFS
Protein: Glutathione S-transferase L1 (AtGSTL1) (EC 2.5.1.18) (GST class-lambda member 1) (Q6NLB0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the glutathione-dependent reduction of S-glutathionylquercetin to quercetin. In vitro, possesses glutathione-dependent thiol transferase activity toward 2-hydroxyethyl disulfide (HED).
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase Z1
- Glutathione S-transferase U25
- Glutathione S-transferase U11
- Glutathione S-transferase F7
- Glutathione S-transferase F3
- Putative F-box protein PP2-B6
- Protein MODIFYING WALL LIGNIN-2
- Putative U-box domain-containing protein 50
- Glutathione S-transferase DHAR2
- Glutathione S-transferase T2
Sequence:
MALSPPKIFVEDRQVPLDATSDPPALFDGTTRLYISYTCPFAQRVWITRNLKGLQDEIKLVPIDLPNRPAWLKEKVNPANKVPALEHNGKITGESLDLIKYVDSNFDGPSLYPEDSAKREFGEELLKYVDETFVKTVFGSFKGDPVKETASAFDHVENALKKFDDGPFFLGELSLVDIAYIPFIERFQVFLDEVFKYEIIIGRPNLAAWIEQMNKMVAYTQTKTDSEYVVNYFKRFM
Protein: SCP domain-containing protein (Q20608)
Organism: Caenorhabditis elegans
Interaction partners:
- SCP domain-containing protein
- NADH:flavin oxidoreductase/NADH oxidase N-terminal domain-containing protein
- SCP domain-containing protein
- Trifunctional purine biosynthetic protein adenosine-3
- SCP domain-containing protein
- SCP domain-containing protein
Sequence:
MYFILCLLAIGVNAQFTSTGQSSIVDAHNKLRSAIAKSTYVAKGTKKEPATDMRKMVVDSTVAASAQNYANTCPTGHSKGTGYGENLYWSWTSADVGSLDSYGEIAAAAWEKEFQDFGWKSNAMDTTLFNSGIGHATQMAWANTSSIGCGVKNCGRDASMRNMNKIAVVCQYSPPGNTMGRPIYKEGTTCSSCSGSTKCDTASGLCG
Protein: 2-dehydropantoate 2-reductase (EC 1.1.1.169) (Ketopantoate reductase) (KPA reductase) (KPR) (P0A9J4)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Pantothenate synthetase
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Protein/nucleic acid deglycase 3
- Aspartate 1-decarboxylase
- Ketol-acid reductoisomerase
- Coenzyme A biosynthesis bifunctional protein CoaBC
Sequence:
MKITVLGCGALGQLWLTALCKQGHEVQGWLRVPQPYCSVNLVETDGSIFNESLTANDPDFLATSDLLLVTLKAWQVSDAVKSLASTLPVTTPILLIHNGMGTIEELQNIQQPLLMGTTTHAARRDGNVIIHVANGITHIGPARQQDGDYSYLADILQTVLPDVAWHNNIRAELWRKLAVNCVINPLTAIWNCPNGELRHHPQEIMQICEEVAAVIEREGHHTSAEDLRDYVMQVIDATAENISSMLQDIRALRHTEIDYINGFLLRRARAHGIAVPENTRLFEMVKRKESEYERIGTGLPRPW
Protein: CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2 (Alpha 2,3-ST 2) (Beta-galactoside alpha-2,3-sialyltransferase 2) (EC 2.4.3.4) (Gal-NAc6S) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (Monosialoganglioside sialyltransferase) (EC 2.4.3.2) (ST3Gal II) (ST3GalII) (ST3GalA.2) (Sialyltransferase 4B) (SIAT4-B) (Q11205)
Organism: Rattus norvegicus (Rat)
Function: A beta-galactoside alpha2-3 sialyltransferase primarily involved in terminal sialylation of ganglio and globo series glycolipids. Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through an alpha2-3 linkage. Sialylates GM1/GM1a, GA1/asialo-GM1 gangliosides to form GD1a and GM1b, respectively. Together with ST3GAL3, primarily responsible for biosynthesis of brain gangliosides that function as ligand for myelin-associated glycoprotein MAG on axons, regulating MAG expression and axonal myelin stability and regeneration (By similarity). Responsible for the sialylation of the pluripotent stem cell- and cancer stem cell-associated antigen SSEA3, forming SSEA4 (By similarity). Sialylates with low efficiency asialofetuin, presumably onto O-glycosidically linked Galbeta-(1->3)-GalNAc-O-Ser.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q16842}; Single-pass type II membrane protein. Secreted. Note=Membrane-bound form distributed along the Golgi cisternae, mainly in proximal compartments (By similarity). Secreted into the body fluid. {ECO:0000250|UniProtKB:Q16842}.
Interaction partners:
- Beta-1,3-galactosyltransferase 4
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Glucosaminyl
- Galactoside alpha-
- Hexosyltransferase
- Galactoside alpha-
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide6-alpha-sialyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6
- C1GALT1-specific chaperone 1
Sequence:
MKCSLRVWFLSMAFLLVFIMSLLFTYSHHSMATLPYLDSGTLGGTHRVKLVPGYTGQQRLVKEGLSGKSCTCSRCMGDAGTSEWFDSHFDSNISPVWTRDNMNLTPDVQRWWMMLQPQFKSHNTNEVLEKLFQIVPGENPYRFRDPQQCRRCAVVGNSGNLRGSGYGQEVDSHNFIMRMNQAPTVGFEKDVGSRTTHHFMYPESAKNLPANVSFVLVPFKALDLMWIASALSTGQIRFTYAPVKSFLRVDKEKVQIYNPAFFKYIHDRWTEHHGRYPSTGMLVLFFALHVCDEVNVYGFGADSRGNWHHYWENNRYAGEFRKTGVHDADFEAHIIDILAKASKIEVYRGN
Protein: Mitochondria-eating protein (Spermatogenesis-associated protein 18) (Q503Q1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Key regulator of mitochondrial quality that mediates the repairing or degradation of unhealthy mitochondria in response to mitochondrial damage. Mediator of mitochondrial protein catabolic process (also named MALM) by mediating the degradation of damaged proteins inside mitochondria by promoting the accumulation in the mitochondrial matrix of hydrolases that are characteristic of the lysosomal lumen. Also involved in mitochondrion degradation of damaged mitochondria by promoting the formation of vacuole-like structures (named MIV), which engulf and degrade unhealthy mitochondria by accumulating lysosomes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8TC71}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8TC71}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q8TC71}. Note=Localizes to the cytoplasm under normal conditions. Relocalizes to mitochondrion outer membrane following cellular stress. May form molecular condensates in the mitochondrial matrix. {ECO:0000250|UniProtKB:Q8TC71}.
Interaction partners:
- Radial spoke head 14 homolog.
- Coiled-coil domain-containing 146
- DLEC1 cilia and flagella-associated protein.
- Cilia- and flagella-associated protein 161
- Stabilizer of axonemal microtubules 2.
- Leucine-rich repeat-containing 23.
- Leucine-rich repeat-containing 34
- Translin-associated factor X-interacting protein 1
- Adenylate kinase 8
- Calcium channel, voltage-dependent, L type, alpha 1D subunit, b.
Sequence:
MADTLRRLVNSSPYSVLQDKLDAWYKDYHVYSCDQNLNRCCELVELTSKIQGQLFTILNLTAQEGGHYSGVDTLKSRLLPWLGSCFTIAASAVSSDTSLSLIQESVEKDRKIRELSSVHESNLQKIEDQLCSTRIELDSVKRELVDTHIELDSTKNKSATTLLATEDEILHLKSELRVAQDQLDLYKRKLDVLDDYERQVRILRDEVSFLNAEKTVLQDRLARSRSPSPLLRRSRSVSPVRGESPTRAQLTSSSRHARLVSRFSDLYATERLESQSLLLKYIDDLETVQRILFIAAVESFQAAKLAYRQFKSRVRKTLSSTHIGPESLEDAVVDYIVRNLDLYDVQTSINDVINAMNVNPRISFPPEVDFVLISSFIREACRIAFAMQTLDPPLDLAFSSDGELYSDVKYRRSFDSEFTAPLVAFHVWPALLEGDTVILKGEAVTRRGALWKSRSRSSSPVRSRSGSPSRTFMASHSRSPSPGRLSSSRL
Protein: DNA repair and recombination protein RAD26 (EC 3.6.4.12) (ATP-dependent helicase RAD26) (P40352)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in the preferential repair of active genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB9
- RNA polymerase II degradation factor 1
- DNA repair protein RAD7
- DNA repair protein RAD2
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerase II subunit RPB3
- DNA repair protein RAD14
- DNA-directed RNA polymerase II subunit RPB7
Sequence:
MEDKEQQDNAKLENNESLKDLGVNVLSQSSLEEKIANDVTNFSNLQSLQQEETRLERSKTALQRYVNKKNHLTRKLNNTTRISVKQNLRDQIKNLQSDDIERVLKDIDDIQSRIKELKEQVDQGAENKGSKEGLQRPGETEKEFLIRTGKITAFGHKAGFSLDTANREYAKNDEQKDEDFEMATEQMVENLTDEDDNLSDQDYQMSGKESEDDEEEENDDKILKELEDLRFRGQPGEAKDDGDELYYQERLKKWVKQRSCGSQRSSDLPEWRRPHPNIPDAKLNSQFKIPGEIYSLLFNYQKTCVQWLYELYQQNCGGIIGDEMGLGKTIQVIAFIAALHHSGLLTGPVLIVCPATVMKQWCNEFQHWWPPLRTVILHSMGSGMASDQKFKMDENDLENLIMNSKPSDFSYEDWKNSTRTKKALESSYHLDKLIDKVVTDGHILITTYVGLRIHSDKLLKVKWQYAVLDEGHKIRNPDSEISLTCKKLKTHNRIILSGTPIQNNLTELWSLFDFIFPGKLGTLPVFQQQFVIPINIGGYANATNIQVQTGYKCAVALRDLISPYLLRRVKADVAKDLPQKKEMVLFCKLTKYQRSKYLEFLHSSDLNQIQNGKRNVLFGIDILRKICNHPDLLDRDTKRHNPDYGDPKRSGKMQVVKQLLLLWHKQGYKALLFTQSRQMLDILEEFISTKDPDLSHLNYLRMDGTTNIKGRQSLVDRFNNESFDVFLLTTRVGGLGVNLTGANRIIIFDPDWNPSTDMQARERAWRIGQKREVSIYRLMVGGSIEEKIYHRQIFKQFLTNRILTDPKQKRFFKIHELHDLFSLGGENGYSTEELNEEVQKHTENLKNSKSEESDDFEQLVNLSGVSKLESFYNGKEKKENSKTEDDRLIEGLLGGESNLETVMSHDSVVNSHAGSSSSNIITKEASRVAIEAVNALRKSRKKITKQYEIGTPTWTGRFGKAGKIRKRDPLKNKLTGSAAILGNITKSQKEASKEARQENYDDGITFARSKEINSNTKTLENIRAYLQKQNNFFSSSVSILNSIGVSLSDKEDVIKVRALLKTIAQFDKERKGWVLDEEFRNNNAS
Protein: PAK1 interacting protein 1 isoform 1 (A0A0S2Z5C3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MELVAGCYEQVLFGFAVHPEPEACGDHEQWTLVADFTHHAHTASLSAVAVNSRFVVTGSKDETIHIYDMKKKIEHGALVHHSGTITCLKFYGNRHLISGAEDGLICIWDAKKWECLKSIKAHKGQVTFLSIHPSGKLALSVGTDKTLRTWNLVEGRSAFIKNIKQNAHIVEWSPRGEQYVVIIQNKIDIYQLDTASISGTITNEKRISSVKFLSESVLAVAGDEEVIRFFDCDSLVCLCEFKAHENRVKDMFSFEIPEHHVIVSASSDGFIKMWKLKQDKKVPPSLLCEINTNARLTCLGVWLDKVADMKESLPPAAEPSPVSKEQSKIGKKEPGDTVHKEEKRSKPNTKKRGLTGDSKKATKESGLISTKKRKMVEMLEKKRKKKKIKTMQ
Protein: Euchromatic histone lysine methyltransferase 1 (A0A0D9SEQ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XGEETPMAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSS
Protein: Cathepsin L (P79722)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MMFALLVTLYISAVFAAPSIDIQLDDHWNSWKSQHGKSYHEDVEVGRRMIWEENLRKIEQHNFEYSYGNHTFKMGMNQFGDMTNEEFRQAMNGYTHDPNQTSQGPLFMEPSFFAAPQQVDWRQRGYVTPVKDQKQCGSCWSFSSTGALEGQLFRKTGKLISMSEQNLVDCSRPQGNQGCNGGLMDQAFQYVKENKGLDSEQSYPYLARDDLPCRYDPRFNVAKITGFVDIPSGNELALMNAVAAVGPVSVAIDASHQSLQFYQSGIYYERACSSSRLDHAVLVVGYGYQGADVAGNRYWIVKNSWSDKWGDKGYIYMAKDKNNHCGVATKASYPLM
Protein: S-adenosylmethionine-dependent methyltransferase (Q4KCD2)
Organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Interaction partners:
- Polyketide synthase/nonribosomal peptide synthetase hybrid RzxA
- Polyketide synthase RzxC
- Polyketide synthase RzxE
- Polyketide synthase/nonribosomal peptide synthetase hybrid RzxB
- Cytochrome P450 monooxygenase
- Polyketide synthase RzxF
- Polyketide synthase RzxD
Sequence:
MTTPATETVSPISQWYDMMTRMFPDQRLTFLNYGYLAQDSDFDWINDADLEQKCSVNLIRTLLGDSDLRGKKVLEIGSGRGGNCSYLARYTGAASVTGLDFCPAHIELCNRVHALPGLSFVGGDAMALPFADNEFDVVINIESSHCYPDLNTFGAEVQRVLKQDGRFFYADTMKGDNTSALSEPDSIGVDFFSNVLAQHQAMIEHARFKVEEHRDISDGVIRAFESQDGHLKHLLRSLVEEKKQQREPLPPEVWHAFDTMFHFFDDSGIKAYKNGHLAYKFWRLQKAA
Protein: F-box only protein 22 (Q78JE5)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22972877}.
Interaction partners:
- S-phase kinase-associated protein 1
- NF-kappa-B inhibitor alpha
Sequence:
MEPAGGGGGVSSSTDPRSTYVLSNLAEVVERVFTFLPAKALLRVAGVCRLWRECVRRVLRTHRSVTWISAGVAEAGHLEGHCLVRVVAEALENVRILPQTVLYMADSETFISLEECRGHKRARKRTTMETACALEKLFPKQCQVLGIVTPGIVVTPMGSGSNRPQEIEIGESGFALLFPQIEGIKIQPFHFIKDSKNLTLERHQLTEVGLLDNPELRVVLVFGYNCCKVGASNYLHRVVSTFSDMNIILAGGQVDNLSSLTCEKNPLDIDATGVVGLSFSGHRIQSATVLLTEDVNDAKTVEAAMQRLKAANIPEQNTIGFMFACVGRGFQYYRAKGNVEADAFRKFFPSVPLFGFFGNGEIGCDRIVTGNFILRRCNEVKEEDLFHSYTTIMALVHLGTSK
Protein: Paraxial protocadherin (O93509)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLLLFRAIPMLLLGLMVLQTDCEIAQYYIDEEEPPGTVIAVLSQHSIFNTTDIPATNFRLMKQFNNSLIGVRESDGQLSIMERIDREQICRQSLHCNLALDVVSFSKGHFKLLNVKVEVRDINDHSPHFPSEIMHVEVSESSSVGTRIPLEIAIDEDVGSNSIQNFQISNNSHFSIDVLTRADGVKYADLVLMRELDREIQPTYIMELLAMDGGVPSLSGTAVVNIRVLDFNDNSPVFERSTIAVDLVEDAPLGYLLLELHATDDDEGVNGEIVYGFSTLASQEVRQLFKINSRTGSVTLEGQVDFETKQTYEFEVQAQDLGPNPLTATCKVTVHILDVNDNTPAITITPLTTVNAGVAYIPETATKENFIALISTTDRASGSNGQVRCTLYGHEHFKLQQAYEDSYMIVTTSTLDRENIAAYSLTVVAEDLGFPSLKTKKYYTVKVSDENDNAPVFSKPQYEASILENNAPGSYITTVIARDSDSDQNGKVNYRLVDAKVMGQSLTTFVSLDADSGVLRAVRSLDYEKLKQLDFEIEAADNGIPQLSTRVQLNLRIVDQNDNCPVITNPLLNNGSGEVLLPISAPQNYLVFQLKAEDSDEGHNSQLFYTILRDPSRLFAINKESGEVFLKKQLNSDHSEDLSIVVAVYDLGRPSLSTNATVKFILTDSFPSNVEVVILQPSAEEQHQIDMSIIFIAVLAGGCALLLLAIFFVACTCKKKAGEFKQVPEQHGTCNEERLLSTPSPQSVSSSLSQSESCQLSINTESENCSVSSNQEQHQQTGIKHSISVPSYHTSGWHLDNCAMSISGHSHMGHISTKDSGKGDSDFNDSDSDTSGESQKKSIEQPMQAQASAQYTDESAGFRHADNYFSHRINKGPENGNCTLQYEKGYRLSYSVAPAHYNTYHARMPNLHIPNHTLRDPYYHINNPVANRMHAEYERDLVNRSATLSPQRSSSRYQEFNYSPQISRQLHPSEIATTF
Protein: Uncharacterized fimbrial-like protein YfcP (P76499)
Organism: Escherichia coli (strain K12)
Function: Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes.
Subcellular location: Fimbrium {ECO:0000305}.
Interaction partners:
- Uncharacterized fimbrial-like protein YfcQ
- Uncharacterized fimbrial-like protein YfcR
- Uncharacterized protein YfcO
- Probable fimbrial chaperone YfcS
- Uncharacterized fimbrial-like protein YadL
- Outer membrane usher protein HtrE
- Uncharacterized fimbrial-like protein YadM
- Probable fimbrial chaperone YehC
Sequence:
MNKSMIQSGGYVLLAGLILAMSSTLFAADNNLHFSGNLLSKSCALVVDGQYLAEVRFPTVSRQDLNVAGQSARVPVVFKLKDCKGPAGYNVKVTLTGVEDSEQPGFLALDTSSTAQGVGIGMEKTDGMQVAINNTNGATFALTNGNNDINFRAWLQAKSGRDVTIGEFTASLTATFEYI
Protein: Opioid receptor-like protein ZFOR3 (Q98U14)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDSNVVQIFKEDKCPSSHPEKCLPNFTWQSAVSDIYNSSLNESWTTEQEAMSPLIPIITAVYSVVFVVGLVGNCLVMYVIIRHTKMKTATNIYIFNLRVADALVTTTMPFQSTDYLLNSWPFGEVVCKVFISIDYYNMFTSIFTLTMMSVDRYVAVCHPVKALDFRTPMKAKIINILIWVLSSAAGIPAMVLGSTQTNNGTTECALQFPDPYVYWDTLMKICVFIFGFVAPLLIITVCYTLMVLRLKSVRLLSGSREKDRNLRRITRLVLVVVAVFVVCWTPIHIFILVKALSHGVPETTSVMAAYFFCVALGYTNSSLNPILYAFLDENFKRCFRDFCCPGRTAGDGRGVSRVRSTLREHTCPAEAKNDGGQGRPV
Protein: Phosphoenolpyruvate carboxylase 1 (PEPC 1) (PEPCase 1) (ppcB) (EC 4.1.1.31) (Q9FV66)
Organism: Flaveria trinervia (Clustered yellowtops) (Oedera trinervia)
Function: Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. May be involved in phloem loading with sucrose and in anions and cations uptake and amino acid biosynthesis in roots.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P27154}.
Interaction partners:
Sequence:
MANRNLEKLASIDAHLRLLVPGKVSEDDKLIEYDALLLDKFLDILQDLHGEDLKETVQECYELSAEYEGKRDPKKLEELGSVLTSLDPGDSIVIAKAFSHMLNLANLAEEVQIAYRRRIKLKKGDFADEAHATTESDMEETLKKLVYKLNKSPEEVFDALKNQTVDLVLTAHPTQSVRRSLLQKHGRIRNCLAQLYAKDITPDDKQELDEALHREIQAAFRTDEIRRTQPTPQDEMRAGMSYFHETIWKGVPKFLRRVDTALKNIGINERVPYNAPLIQFSSWMGGDRDGNPRVTPEVTRDVCLLARMMAANMYFSQIEDLMFEMSMWRCTDELRVRAEELFRTARRDVKHYIEFWKQVPPTEPYRVILGDVRDKLYNTRERARHLLAHDISDIPEEAVYTNVEQFLEPLELCYRSLCACGDRVIADGSLLDFLRQVSTFGLSLVKLDIRQESDRHTDVLDAITQHLEIGSYREWSEEKRQEWLLAELSGKRPLFGSDLPKTEEIKDVLDTFNVLAELPSDCFGAYIISMATSPSDVLAVELLQRECHVKQPLRVVPLFEKLADLEAAPAAMARLFSIDWYKNRINGKQEVMIGYSDSGKDAGRFSAAWQLYKAQEELKNVAKEFGVKLVMFHGRGGTVGRGGGPTHLAILSQPPDTIQGSLRVTVQGEVIEQSFGEEHLCFRTLQRFCAATLEHGMNPPISPRPEWRELMDQMAVVATEQYRSIVFKEPRFVEYFRLATPELEYGRMNIGSRPSKRKPSGGIESLRAIPWIFAWTQTRFHLPVWLGFGAAFKQAIQKDSKNLQMLQEMYKTWPFFRVTIDLVEMVFAKGDPGIAALNDKLLVSEDLWPFGESLRANYEETKDYLLKIAGHKDLLEGDPYLKQRLKLRDSYITTLNVCQAYTLKRTRDPNYHVTLRPHISKEYAEPSKPADELIHLNPTSEYAPGLEDTLILTMKGIAAGMQNTG