wanglab/gogpt-training-data huggingface dataset:
Protein: Casein kinase II subunit beta-1 (CK II beta-1) (P40228)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a complex role in regulating the basal catalytic activity of the alpha subunit. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor GBFl, resulting in stimulation of its DNA binding activity. CK2 phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis. CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation. Stimulates the binding of CCA1 to promoters (Probable).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16926165}. Nucleus {ECO:0000269|PubMed:16926165}.
Interaction partners:
- Casein kinase II subunit alpha-1
- Casein kinase II subunit alpha-2
- Casein kinase II subunit alpha-3
- Casein kinase II subunit alpha-4, chloroplastic
- Protein CCA1
- FACT complex subunit SSRP1
- Casein kinase II subunit beta-3
- Ribosomal RNA-processing 7 protein
- Nucleolar protein
- rRNA biogenesis protein RRP36
Sequence:
MYRDRGTVNSRPEVVDRKRINDALERPSPSTSRQVNGKGKGTVTAATTTANLIGKQQSNNINHRDSRSASLSKNNTVSDDESDTDSEESDVSGSDGEDTSWISWFCNLRGNEFFCEVDDDYIQDDFNLCGLSSLVPYYEYALDLILDVESSQGEMFTEEQNELIESAAEMLYGLIHARYILTSKGLAAMLDKYKNYDFGRCPRVYCCGQPCLPVGQSDLPRSSTVKIYCPKCEDIYYPRSKYQGNIDGAYFGTTFPHLFLMTYGHLKPAKATQNYVQRVFGFKLHKP
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 6 (BLOC-1 subunit 6) (Pallid protein homolog) (Q9VTM0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis and membrane trafficking in synapses. In response to high synaptic activity at neuromuscular junctions, plays a key role in promoting efficient synaptic vesicle recycling and re-formation through early endosomes.
Subcellular location: Synapse {ECO:0000269|PubMed:28317021}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28317021}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:28317021}. Note=At the neuromuscular junctions, present at both pre- and postsynaptic compartments where it associates with cytoskeletal neuronal microtubule structures and muscle Z-lines. {ECO:0000269|PubMed:28317021}.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Dysbindin protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- SNAPIN protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- Uncharacterized protein, isoform A
- Biogenesis of lysosome-related organelles complex 1 subunit 3
- BLOC-2 complex member HPS5 homolog
- Hermansky-Pudlak syndrome 4, isoform A
Sequence:
MLKSSNINSVLNELPNDPARDSTAQSSHNGKPKQDAETCCSSQDNEVMASLAALQLSAGVLQIAEPPLNHVRTQLRELIGRQNKTYIDLSKEKYKLDCSEVARLNDMMSDVKRYKDKLTKIKKEMQGVYQRTKELKKRAANVAACKQRDYQRKLERLQHEESLIGSQ
Protein: Prefoldin subunit 1 (O60925)
Organism: Homo sapiens (Human)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Interaction partners:
- Prefoldin subunit 2
- Prefoldin subunit 6
- Prefoldin subunit 4
- Prefoldin subunit 3
- Prefoldin subunit 5
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit theta
Sequence:
MAAPVDLELKKAFTELQAKVIDTQQKVKLADIQIEQLNRTKKHAHLTDTEIMTLVDETNMYEGVGRMFILQSKEAIHSQLLEKQKIAEEKIKELEQKKSYLERSVKEAEDNIREMLMARRAQ
Protein: Gabrb2 protein (A4FUK8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MESIGKTPHIFLLCPLIVAVACAQSIRDPSNMPVVKDTVDRLMKGYDIRLRPDFGGAPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYSEIPLNLTLDNRVADQLWVPDTYFLNDKRSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGGDGAVSGVERIELPQFSIVDYKLISKNVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSIPITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFLALLEYAFVNYIFFGRGPQRQKKAAEKAATANNEKLRPDPNKWLVGSVVQRDDALYARMKQREIDGYDSMWGPIFAEDAALGLGDQRLKMTPDDIRLTTVEMKNEMGPSDLSRGLGDPRSTMLAYDSSTLQYRRAAMARQNYGHSALERHATQKKSRLRRRASQLKVNTPDLSDVNSIDKWSRMIFPTLFSFFNIVYWLYYVH
Protein: GDP-mannose 4,6-dehydratase (EC 4.2.1.47) (GDP-D-mannose dehydratase) (P0AC88)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
Interaction partners:
- GDP-L-fucose synthase
- GDP-mannose mannosyl hydrolase
- Mannose-1-phosphate guanylyltransferase
- Putative colanic acid biosynthesis glycosyl transferase WcaI
- UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase
- Putative colanic acid biosynthesis acetyltransferase WcaF
- Putative colanic acid biosynthesis glycosyl transferase WcaC
- Putative polysaccharide export protein Wza
- Phosphomannomutase
- Putative colanic acid biosynthesis glycosyl transferase WcaE
Sequence:
MSKVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVQPDEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQQEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGVEEKGIVVSVTGHDAPGVKPGDVIIAVDPRYFRPAEVETLLGDPTKAHEKLGWKPEITLREMVSEMVANDLEAAKKHSLLKSHGYDVAIALES
Protein: Cell cycle checkpoint control protein RAD9A (hRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A) (Q99638)
Organism: Homo sapiens (Human)
Function: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:12628935}.
Interaction partners:
- DNA topoisomerase 2-binding protein 1
- Cell cycle checkpoint protein RAD1
- Checkpoint protein HUS1
- Cell cycle checkpoint protein RAD17
- Replication factor C subunit 2
- Checkpoint protein HUS1B
- Serine/threonine-protein kinase ATR
- ATR-interacting protein
- Replication factor C subunit 5
- Replication protein A 70 kDa DNA-binding subunit
Sequence:
MKCLVTGGNVKVLGKAVHSLSRIGDELYLEPLEDGLSLRTVNSSRSAYACFLFAPLFFQQYQAATPGQDLLRCKILMKSFLSVFRSLAMLEKTVEKCCISLNGRSSRLVVQLHCKFGVRKTHNLSFQDCESLQAVFDPASCPHMLRAPARVLGEAVLPFSPALAEVTLGIGRGRRVILRSYHEEEADSTAKAMVTEMCLGEEDFQQLQAQEGVAITFCLKEFRGLLSFAESANLNLSIHFDAPGRPAIFTIKDSLLDGHFVLATLSDTDSHSQDLGSPERHQPVPQLQAHSTPHPDDFANDDIDSYMIAMETTIGNEGSRVLPSISLSPGPQPPKSPGPHSEEEDEAEPSTVPGTPPPKKFRSLFFGSILAPVRSPQGPSPVLAEDSEGEG
Protein: Casein kinase I isoform alpha (CKI-alpha) (EC 2.7.11.1) (CK1) (P42168)
Organism: Caenorhabditis elegans
Interaction partners:
- Armadillo repeat-containing protein wrm-1
- Beta-catenin/armadillo-related protein 1
- Beta-catenin-like protein hmp-2
- Axin-like protein pry-1
- Glycogen synthase kinase-3
- CULT domain-containing protein
- Adenomatous polyposis coli protein-related protein 1
- Ubiquitin-like domain-containing protein
- CULT domain-containing protein
- Beta-catenin homolog sys-1
Sequence:
MAGVMSVKDFIVATKYKLIRKIGSGSFGDIYVSINVTNGEEVAIKLESNRARHPQLLYESKVYRILQGGVGIPHIRWYGTEREYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHVKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDSRTRTHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGTLPWQGLKAATKKQKYEKISEKKMTTSVEHLCKGFPAEFPMYLSYTRGLRFDESPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAQQSQSSGVPGTNTTTQGATVPSAGVPAGVAPGGTTPQ
Protein: Kinesin, putative (Q582C4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Flagellar attachment zone protein 1
Sequence:
MSKAAVSRPRVYVRIRPLNEREKREGNGELICHGDQRMRDTLFVRKDESGAELQTRFDCVFDRDATQANIFDTIGPEVLNTLFSGYNASIFAYGQTGSGKTYTMEGDHSKPERLGVTPRLVRAIFERFKGNPDISRPVCEVSLVQIYQEKIQDLLAGQKQLEIHMDRTGQYIARDATWTRVRSLEESMKLYKKASEMRTTSSTDMNLVSSRSHMIMMMKLQWDEPSLPGSHAQLNLVDLAGSERIALSGATGDLMKEAIHINKSLSALGNVVSKLVEQAKHKGRRVHIPYKDSKLTYLLQSSIGGSNLIHFILAVSCSALWRSETNSTIEFGKRALQLVLRPVRNAIDYTRLAEMEEMIERMRSHIASLEEALRDKSSEAAEFLKLKQIPQDGDEGPGKFSDSRGRRQRKKLKMQTELARIMANLPETFDDLTSHCVLFPESKGSFRELGGLQHLVHFVDRSASTFYRSNAAQTIASVLDDKGRDMFVEIDGVEALTRLLHIKEERCKEAACVALEAVCRGSLKNKQSLSPAVYTELVDLIYSYPNQQVQEAACTAVATIVDLYPEARRTFERLDIVPKLLETIRNTPEEVVNLIKSATNCIGRLSHGDPEMQDVIASFGGIDLLIDVLFSNAGTRDHQVPILASYALVNLCCSNEQNLDIAQDHPRYGEVKFRLLEGLARAFGVNTAREGFGRATAHETGSPFPYYGVTIVDKWSFTSSGGRPIFSTFMDNPQFYLYVSRPTDVAFMIQDVLYETRMLKKKKNNTVYMGLALFEGDPELAKAGLKQVDFHGRMVEIGKYTSNCENVLHCTLQPSEVPYVVVPFTSQRGRQTEFALSAFADSSIELTAVPEQVGWVRTVLDGCWTEFTGRGGDGFDWRCNPQISIQPKENCRCVFVLSYLSLDQQRAYSRDEEAEEQNTRPRLYGRLFTNSNGEKRYLKALVPLPQKSTFVASNSFASNSYITTSANLTAGESYTYIPFTETPYEDTWRLSVYCDTDDVAIAPINGSKSEWYCTTSSGEWAGKPLSIQLDTKGRMVAVASSPGSFLRVRLFNAKGKKLEGIDAYWNAEASVEYKSQGAVTVQVEGMVRTENGQEPARGLKVDVFIFTENKCTVQHVDFPASPSSLLHPTKTTPIELLRYPVEVVENDAPFATLDQTDDDEEDATCDEDDSYESKELELKETLERRNTENAKLLDRIAEQQRELQELRMLQNMLPSSATHNESPGSGSPNDTRINSGMNQVNSKKDNISRKGDRNGAAASSNGSPVSSKAISPSHFPQSGGGGVSRSMREAIERSLVTLNRLECHTEPPKAGEWGAIRNEVKELRKLLGLALSQESLVRT
Protein: Tyrosine-protein phosphatase 3 (EC 3.1.3.48) (Protein-tyrosine phosphatase 3) (PTPase 3) (P32587)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Contributes to dephosphorylation of tyrosine 15 of cdc2.
Subcellular location: Cytoplasm.
Interaction partners:
- M-phase inducer phosphatase
- Mitosis inhibitor protein kinase mik1
- Mitosis inhibitor protein kinase wee1
Sequence:
MSFKEVSTENGVLTPLITIKEKAYMIIEGLNEEEIELLNTRLPKLSKKALARNRYSNIVPYENTRVRLDPMWKEACDYINASIVKIPSGKTFIATQGPTSNSIDVFWKMVWQSVPKSGIIVMLTKLRERHRLKCDIYWPVELFETLNIGDLSVILVKVYTLTSLNEVQVREFELNKDGVKKKILHFYYNGWPDFGAPHTFSLLSLTRYIKSLSYSPDFETAPIIVHCSAGCGRTGTFMALFEILSQTDDSTSTSKFEVDNIANIVSSLRSQRMQSVQSVDQLVFLYTVSQELLQGKEFLLPQL
Protein: Trans-alpha-bergamotene synthase (EC 4.2.3.81) (Terpene synthase 7) (LdTPS7) (J7LQ09)
Organism: Phyla dulcis (Aztec sweet herb) (Lippia dulcis)
Function: Sesquiterpene synthase converting farnesyl diphosphate to trans-alpha-bergamotene as the major product.
Interaction partners:
Sequence:
MEARRSGNFKASIWDDDFLQSLTSPYTAKEYLKQADKLKWQVKVIIKETKQRLDQLDLIDNIQRLGISHHFRDEIQRVLQNIYEKMRVECPDRMLMEKDLYSTSLQFRLLRQHGYHVSQDVFCSFMDGAGNFQAVDDLKGILALYEASFLSREGENILGSARDFSTRHLKQKLEEITDPILAEKIRRALELPLHWRLQKLEAIWFINIYESRFDANLILLQLAKLEFNMVQAQYQEDLKWLSRWYKETGLPEKMNFARDRLAECFLWALGFIPEAHLGQARKILTKIAVLIVIMDDFYDIYGTLDEIKVFTEELQRWDINALDNLPEYMRICFLAIFNTANEIAYDILRDQGINIISNLRRLWAELGRVYYTEAKWYHSGYFPSTEEYLNVAWISITGPVLLFHAYFSIMNPIDMKELQYLEQYPGIIRWPSTVLRLADDLGTASDEIKRGDVPKSIQCYMHETGCSEEEAREYVKQLIDTTLKKMNKEILMEKPTNDFGATAMNLARISLFFYQYGDGFGVPHNQTKENLVSLIVKPICLT
Protein: Low-density lipoprotein receptor-related protein (Q95V09)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MALEPYTKSAEIEPQLCQVIDNNEDVTTKATKCVKSNSGVGWRQMLIGFLLICFGISNSWQYKNVHMPSSSSLIASPPASAFVNTPATLLFTTRHDIQVANITRPTGGPQIDVIVRDLAEAMAIDFYYAKNLVCWTDSGREIIECAQTNSSALQPLLRAPKQTVISTGLDKPEGLAIDWYTDKIYWTDGEKNRIEVATLDGRYQKVLFWTDLDQPRAVAVVPARKLLIWTDWGEYPKIERASMDGDPLSRMTLVKEHVFWPNGLAVDLKNELIYWTDGKHHFIDVMRLDGSSRRTIVNNLKYPFSLTFYDDRLYWTDWQRGSLNALDLQTRELKELIDTPKAPNSVRAWDPSLQPYEDNPCAHNNGNCSHLCLLATNSKGFSCACPTGVKLISANTCANGSQEMMFIVQRTQISKISLDSPDYTIFPLPLGKVKYAIAIDYDPVEEHIYWSDVETYTIKRAHADGTGVTDFVTSEVRHPDGLALDWLARNLYWTDTVTDRIEVCRLDGTARKVLIYEHLEEPRAIAVAPSLGWMFWSDWNERKPKVERASLDGSERVVLVSENLGWPNGIALDIEAKAIYWCDGKTDKIEVANMDGSGRRVVISDNLKHLFGLSILDDYLYWTDWQRRSIDRAHKITGNNRIVVVDQYPDLMGLKVTRLREVRGQNACAVRNGGCSHLCLNRPRDYVCRCAIDYELANDKRTCVVPAAFLLFSRQEHIGRISIEYNEGNHNDERIPFKDVRDAHALDVSVAERRIYWTDQKSKCIFRAFLNGSYVQRIVDSGLIGPDGIAVDWLANNIYWSDAEARRIEVARLDGSSRRVLLWKGVEEPRSLVLEPRRGYMYWTESPTDSIRRAAMDGSDLQTIVAGANHAAGLTFDQETRRLYWATQSRPAKIESADWDGKKRQILVGSDMDEPYAVSLYQDYVYWSDWNTGDIERVHKTTGQNRSLVHSGMTYITSLLVFNDKRQTGVNPCKVNNGGCSHLCLAQPGRRGMTCACPTHYQLAKDGVSCIPPRNYIIFSQRNSFGRLLPNTTDCPNIPLPVSGKNIRAVDYDPITHHIYWIEGRSHSIKRSLANGTKVSLLANSGQPFDLAIDIIGRLLFWTCSQSNSINVTSFLGESVGVIDTGDSEKPRNIAVHAMKRLLFWTDVGSHQAIIRARVDGNERVELAYKLEGVTALALDQQSDMIYYAHGKRIDAIDINGKNKKTLVSMHISQVINIAALGGFVYWLDDKTGVERITVNGERRSAELQRLPQITDIRAVWTPDPKVLRNHTCMHSRTKCSHICIASGEGIARTRDVCSCPKHLMLLEDKENCGAFPACGPDHFTCAAPVSGISDVNKDCIPASWRCDGQKDCPDKSDEVGCPTCRADQFSCQSGECIDKSLVCDGTTNCANGHDEADCCKRPGEFQCPINKLCISAALLCDGWENCADGADESSDICLQRRMAPATDKRAFMILIGATMITIFSIVYLLQFCRTRIGKSRTEPKDDQATDPLSPSTLSKSQRVSKIASVADAVRMSTLNSRNSMNSYDRNHITGASSSTTNGSSMVAYPINPPPSPATRSRRPYRHYKIINQPPPPTPCSTDICDESDSNYTSKSNSNNSNGGATKHSSSSAAACLQYGYDSEPYPPPPTPRSHYHSDVRIVPESSCPPSPSSRSSTYFSPLPPPPSPVQSPSRGFT
Protein: Zinc finger protein ZIC 2-A (Zinc finger DNA-binding protein fZic) (Zinc finger protein ZIC 2) (XlZic2) (xZic2) (Zinc finger protein of the cerebellum 2-A) (Q91689)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional repressor that inhibits neurogenesis and induces neural and neural crest differentiation. Regulates anteroposterior patterning in early development by inhibiting expression of the nodal genes through the inhibition of vegt. Required for gastrulation movements and for proper anterior neural and axial development. May also act as a transcriptional activator. May bind to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'.
Subcellular location: Nucleus {ECO:0000269|PubMed:9634234}. Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MLLDAGPQFPALGVGTFARHHHHHHHHHAAVAAAAAAAAEMQERELSLAQNTFVEPTHMAAFKLNPGGGSGGGSGGGGGGGGAGPNGGAGASGPHDLSPPGQTSAFTSQAGYPTSALAPHSAYSGAAAFNSPRDFLFRGRGFAEGSAAAGGGQHGLFGPPAGSLHHHPHHHHQLSHAEHPQGHLLFPGIHDQHAAASQNTLGGQMRLGLPGEVFGRTEQYRQVSSPRGDPYTAAQLHNQYSPMNMGMNMAAHHHHHHHHHPGAFFRYMRQPCIKQELICKWIDPEQLNNPKKSCTKTFSTMHELVTHVSVEHVGGPEQSNHICFWEECPREGKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFQCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHESSPQGSESSPAASSGYESSTPPGLVSPNSETQNPNLSPAAAAVSAVHNVSSGASGALASNFNEWYV
Protein: Neutral metalloprotease ShpI (EC 3.4.24.-) (Q08002)
Organism: Staphylococcus hyicus
Function: Protease that has a low substrate specificity. Catalyzes the hydrolysis of glucagon, melittin and oxidized beta-insulin at various positions in vitro. Is not able to cleave elastin or the synthetic substrates FAGLA (a substrate for neutral proteinases) and FALGPA (a substrate for collagenase).
Subcellular location: Secreted {ECO:0000269|PubMed:8121397}.
Interaction partners:
Sequence:
MINKKKLVTSLVTSSLLATFTLGSFADAHTYIINNEDINKNAQESSIGTLKQNNFKQSTIDSMKPRNLQSFQEDKVFKAPKEKTPITERARKSENALSNSKLNDVRSFTTVNMRTNENERTAAKLKYNGKNTNVWVADNYITDKQAKNIGEEFDNKIDPLVKEKFGEPSDVDHDGKVNILVYDIKDDFETTGSYTGGYFHPRDLYDVPHSNKAEVFYMDTYPSMGTDKNNLNEKKVYSTLAHEYQHMVNANQKLLKEQKEDGMDVWLDEAFAMASEHMYLQKPLDHRIEYYNNSTSIANGHSLIKWNHRGDVLSNYALSYLFSQYLSAQSDNGDKIFKEILQDPANTSEALENAIHKHVDPKMSLGEFMTNFRVALEKKEATGLHGFNGAPGLNSISPKPVRELPQTLAPQGSVMFETTSPIKVPKDKDEKVNYVKVK
Protein: Probable geranyltranstransferase (Farnesyl-diphosphate synthase) protein (EC 2.5.1.10) (Q8XX94)
Organism: Ralstonia nicotianae (strain ATCC BAA-1114 / GMI1000) (Ralstonia solanacearum)
Interaction partners:
- Isoprenyl transferase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- 1-deoxy-D-xylulose-5-phosphate synthase
- Phytoene synthase protein
- Octaprenyl diphosphate synthase
- Exodeoxyribonuclease 7 small subunit
- D-lactate dehydrogenase
- Exodeoxyribonuclease 7 large subunit
Sequence:
MSDFAHWMASVVARTESALERALPGESVAPQRLHAAMRYATLGAGKRVRPLLAHAAGALGEASPEALDGVSCAVEMIHAYSLVHDDMPCMDDDDLRRGRPTVHRAYDEATALLVGDALQTQAFIALAELGAVSPATRAGLVGELARASGSLGMAGGQAIDLQSVGVALSQDALETMHRMKTGALLRASLRMGALCAGVNAAALEQVDAYAGAVGLAFQVVDDILDVTADTATLGKTAGKDEANDKPTYVSILGLERARALADALHAAAGAAVAQLSRELGEARTARLAGMADLIVWRGH
Protein: Cysteine protease RavZ (EC 3.4.22.-) (Region allowing vacuole colocalization protein Z) (Q5ZUV9)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Cysteine protease effector that inhibits host cell autophagy by targeting lipid-conjugated ATG8 family proteins on pre-autophagosomal structures. Specifically hydrolyzes the amide bond between the C-terminal glycine residue and an adjacent aromatic residue in ATG8 proteins conjugated to phosphatidylethanolamine (PE), producing an ATG8 protein that cannot be reconjugated by host ATG7 and ATG3. Mechanistically, Ravz interacts with ATG8 proteins conjugated to PE via its LIR motifs, extracts them from the membrane of autophagosomes and integrates the PE part into its own lipid-binding site. It then removes the lipid component of the ATG8 protein. Also able to mediate delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) during non-canonical autophagy. Inhibits host ubiquitin recruitment to bacteria-containing vacuoles, suggesting that it is able to mediate delipidation of other proteins in addition to ATG8 proteins. It is however not involved in the exclusion of autophagy adapters from bacteria-containing vacuoles decorated with ubiquitin.
Subcellular location: Secreted {ECO:0000269|PubMed:20880356}. Host cytoplasmic vesicle membrane {ECO:0000269|PubMed:23112293, ECO:0000269|PubMed:26343456, ECO:0000269|PubMed:31719622, ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33298241}. Note=Translocated into the host cell via the type IV secretion system (T4SS) (Probable). In host cells, localizes to mature autophagosome membranes (PubMed:23112293, PubMed:26343456, PubMed:31719622, PubMed:31722778, PubMed:33298241). {ECO:0000269|PubMed:23112293, ECO:0000269|PubMed:26343456, ECO:0000269|PubMed:31719622, ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33298241, ECO:0000305|PubMed:23112293}.
Interaction partners:
Sequence:
MKGKLTGKDKLIVDEFEELGEQESDIDEFDLLEGDEKLPGDSELDKTTSIYPPETSWEVNKGMNSSRLHKLYSLFFDKSSAFYLGDDVSVLEDKPLTGAYGFQSKKNDQQIFLFRPDSDYVAGYHVDAKSDAGWVNDKLDRRLSEISEFCSKATQPATFILPFVEMPTDITKGVQHQVLLTISYDPKSKQLTPTVYDSIGRDTYSESLSSYFKGKYRTTCDEILTQSIEKAIKSTDFTLGKFTRAAYNHQNRLTEGNCGSYTFRTIKEVISSSAQGTEVKIPGSGYITSNSYLTSQHVQDIESCIKYRNLGVVDIESALTEGKTLPVQLSEFIVALEDYGKLRSQQSEKSMLNFIGYSKTAKLTAVELLIGILNDIKGKNEISESQYDKLVKEVDCLMDSSLGKLVQFHLKNLGAESLQKLVLPCVKFDDTIDDFVTIEKDELFDVPDITGEELASKKGIEQGALDKEALLKQKQIKTDLLDLREEDKTGLKKPLHGGIKVK
Protein: TM2 domain-containing protein 1 (Amyloid-beta-binding protein) (mBBP) (Q99MB3)
Organism: Mus musculus (Mouse)
Function: May participate in amyloid-beta-induced apoptosis via its interaction with beta-APP42.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- TM2 domain-containing protein 2
Sequence:
MAAAWPAGRASPAAGPPGLLRTLWLVTVAAGHCGAAASGAVGGEETPKCEDLRVGQYICKEPKINDATQEPVNCTNYTAHVQCFPAPKITCKDLSGNETHFTGSEVGFLKPISCRNVNGYSYKVAVALSLFLGWLGADRFYLGYPALGLLKFCTVGFCGIGSLIDFILISMQIVGPSDGSSYIIDYYGTRLTRLSITNETFRKTQLYP
Protein: Catalase (EC 1.11.1.6) (P00432)
Organism: Bos taurus (Bovine)
Function: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells.
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:7082009}.
Interaction partners:
- Superoxide dismutase, mitochondrial
- Regucalcin
- Sterol carrier protein 2
- Superoxide dismutase
- Superoxide dismutase
- Superoxide dismutase
- Trehalase
- Protein YIPF6
- Hydroxysteroid dehydrogenase-like protein 2
- Peroxiredoxin-2
Sequence:
MADNRDPASDQMKHWKEQRAAQKPDVLTTGGGNPVGDKLNSLTVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDALLFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLAHEDPDYGLRDLFNAIATGNYPSWTLYIQVMTFSEAEIFPFNPFDLTKVWPHGDYPLIPVGKLVLNRNPVNYFAEVEQLAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPYRARVANYQRDGPMCMMDNQGGAPNYYPNSFSAPEHQPSALEHRTHFSGDVQRFNSANDDNVTQVRTFYLKVLNEEQRKRLCENIAGHLKDAQLFIQKKAVKNFSDVHPEYGSRIQALLDKYNEEKPKNAVHTYVQHGSHLSAREKANL
Protein: 15-cis-phytoene desaturase, chloroplastic/chromoplastic (EC 1.3.5.5) (Phytoene dehydrogenase) (Phytoene desaturase) (P80093)
Organism: Capsicum annuum (Capsicum pepper)
Function: Converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene with a concomitant isomerization of two neighboring double bonds at the C9 and C9' positions from trans to cis.
Subcellular location: Plastid, chloroplast. Plastid, chromoplast {ECO:0000269|PubMed:1396714}. Membrane {ECO:0000269|PubMed:1396714}; Peripheral membrane protein {ECO:0000250|UniProtKB:A2XDA1}.
Interaction partners:
Sequence:
MPQIGLVSAVNLRVQGNSAYLWSSRSSLGTDSQDGCSQRNSLCFGGSDSMSHRLKIRNPHSITRRLAKDFRPLKVVCIDYPRPELDNTVNYLEAAFLSSSFRSSPRPTKPLEIVIAGAGLGGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDDDGDWYETGLHIFFGAYPNMQNLFGELGINDRLQWKEHSMIFAMPNKPGEFSRFDFPEALPAPLNGILAILKNNEMLTWPEKVKFAIGLLPAMLGGQSYVEAQDGISVKDWMRKQGVPDRVTDEVFIAMSKALNFINPDELSMQCILIALNRFLQEKHGSKMAFLDGNPPERLCMPIVEHIESKGGQVRLNSRIKKIELNEDGSVKCFILNDGSTIEGDAFVFATPVDIFKLLLPEDWKEIPYFQKLEKLVGVPVINVHIWFDRKLKNTSDNLLFSRSPLLSVYADMSVTCKEYYDPNKSMLELVFAPAEEWVSRSDSEIIDATMKELAKLFPDEISADQSKAKILKYHVVKTPRSVYKTVPGCEPCRLLQRSPVEGFYLAGDYTKQKYLASMEGAVLSGKLCAQAIVQDYELLVGRSQRKLAETSVV
Protein: RIC (Ras which interacts with Calmodulin) (Ras-related protein interacting with calmodulin, isoform A) (Ras-related protein interacting with calmodulin, isoform B) (Q7JMZ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046278}; Lipid-anchor {ECO:0000256|ARBA:ARBA00046278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00046278}.
Interaction partners:
- non-specific serine/threonine protein kinase
Sequence:
MAGDMSIGCAALKRSSKLRSCTSAADTDSMRVPSDHRDNGSLIKPPPVPPQNMRGGLRVYKIVILGDGGVGKSAVTLQFVSHSFLDYHDPTIEDSYQQQAVIDNEAALLDILDTAGQVEFTAMRDQYMRCGEGFIICYSVTDRHSFQEASEYRKLITRVRLSEDIPLVLIANKVDLESQRRVTTEEGRNLANQFGCPFFETSAALRHYIDEAFYTLVREIRRKEMHKALGTDSNSEKIHTGRRSRWWRIRSIFALVFRRRRNLN
Protein: Phenylalanine--tRNA ligase, mitochondrial (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase) (O74952)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit
- Phenylalanine--tRNA ligase alpha subunit
- Putative leucine--tRNA ligase, mitochondrial
- Probable proline--tRNA ligase, mitochondrial
- Putative proline--tRNA ligase C19C7.06
- Putative leucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
- NADPH-dependent diflavin oxidoreductase 1
- Tyrosine--tRNA ligase, mitochondrial
- Aspartate--tRNA ligase, mitochondrial
Sequence:
MFPHRVSHLSKLFSRRFPNWKRKVQTDSWSNVPEHIHSKIGRNLFQKEGHPICSLRQLLEQQFQKFEMNNVQKESPIVSVETNFDSLGFPKTHVSRSKSDTYYMNNKTCLRTHTSAHQPEEFSRLAKEGFKKNGFLITADVYRRDEVDSSHYPIFHQMEGALVWNRNDTAKMKNDLKKVALSPSLKSMVDDETTALETHNDMQDIYSLEETKFVSQHLKDTLTTVIHDLVSLAPSISSGAEQVRYRWTYDSFPFTKPSFQLEIDWKGKWLEILGCGVVQDRLLKGAGLNNYIGWAFGIGLERLAMILYGIPDIRLFWSLDERFSKQFLPNKISTFKPFSKYPACFKDIAFWINNDFNPNDFYEIIRDVCQDMVESVNLIDQYTAKSGKTSLCYRVNYRSMERSLRNEEIDKLQEKLRNRVANSLRVELR