wanglab/gogpt-training-data huggingface dataset:
Protein: Electron transfer flavoprotein subunit beta (Beta-ETF) (Q387N3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|PIRNR:PIRNR000090}.
Interaction partners:
- Electron transfer flavoprotein subunit alpha
- Electron transfer flavoprotein-ubiquinone oxidoreductase
- Acyl-CoA oxidase C-terminal domain-containing protein
- Acyl-CoA dehydrogenase, mitochondrial, putative
- Isovaleryl-coA dehydrogenase, putative
- Acyl-coa dehydrogenase, putative
- Adrenodoxin reductase, putative
- 2,4-dienoyl-coa reductase-like protein
- Succinate--CoA ligase subunit alpha, mitochondrial
- Cytochrome c
Sequence:
MLSRTVPGLFARCSVSRMKVMVGVKRVVDYTVKVRVRNNKIQTESLKMSINPFDEIAIEEAVRLKEKKIATEVIAVTVGNKKAEEGLRVAMALGCDKAIHIITPDGANGEIESLAVAKLFKKLHEEFKPDLWILGKQAVDWDLGTTAQLLAGLLNVPQGTFASKINISRDGVIKVTREVDVGHQMVELQMPCVVSADLRLNTPRLPKLPNIMKSRKKPIDVRNVLEMGVDVTPRLICETVKEPPVRQVGMQVKTVEELYEKLHNEAKVI
Protein: Histone acetyltransferase (EC 2.3.1.48) (D4ACX5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR003048}.
Interaction partners:
- Transcriptional adapter 3
- WD repeat-containing protein 5
- SAGA-associated factor 29
- Histone lysine acetyltransferase CREBBP
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 9B
- Transcription initiation factor TFIID subunit 12
- Transcriptional adapter 2-alpha
- Cysteine-rich protein 2-binding protein
- Transcriptional adapter
Sequence:
MAEPSQAPNPAPAAQPRPLQSPAPAPTSTPAPSPASAPTPAPTPAPAPAPAAAPAGSTGTGGAGVGSGGDPARPGLSQQQRASQRKAQVRGLPRAKKLEKLGVFSACKANETCKCNGWKNPKPPTAPRMDLQQPAANLSELCRSCEHPLADHVSHLENVSEDEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMTRPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPRERQTMFELSKMFLLCLNYWKLETPAQFRQRSQSEDVATYKVNYTRWLCYCHVPQSCDSLPRYETTHVFGRSLLRSIFTVTRRQLLEKFRVEKDKLVPEKRTLILTHFPKFLSMLEEEIYGANSPIWESGFTMPPSEGTQLVPRPATVSATVVPSTPIFSPSMGGGSNSSLSLDSTGTEPMPAGEKRKLPENLTLEDAKRLRVMGDIPMELVNEVMLTITDPAAMLGPETSLLSANAARDETARLEERRGIIEFHVIGNSLTPKANRRVLLWLVGLQNVFSHQLPRMPKEYIARLVFDPKHKTLALIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHSILYFLTYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIPYTELSHIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKEGVRQIPVESVPGIRETGWKPLGKEKGKELKDPDQLYTTLKNLLAQIKSHPSAWPFMEPVKKSEAPDYYEVIRFPIDLKTMTERLRSRYYVTRKLFVADLQRVIANCREYNPPDSEYCRCASALEKFFYFKLKEGGLIDK
Protein: WRKY transcription factor 8 (WRKY DNA-binding protein 8) (Q9FL26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-TTGAC[CT]-3'), a frequently occurring stress-responsive cis-acting element. Functions as positive regulator of salt stress response. Binds the W box of LTI78/RD29A stress-response gene and directly regulates its transcription under salt stress. Functions antagonistically with VQ9 to regulate sodium and potassium homeostasis under salt stress by regulating the expression of downstream SOS (SALT OVERLY SENSITIVE) stress-responsive genes. The DNA-binding activity of WRKY8 is decreased by VQ9. Functions as negative regulator of basal resistance to the bacterial pathogen P.syringae and as positive regulator of resistance to the fungal pathogen to B.cinerea. Functions as positive regulator of defense response againt tobamovirus (TMV) by regulating both the abscisic acid and ethylene signaling pathways. Positively regulates ABI4 expression and negatively modulates ACS6 and ERF104 expression by directly binding to the W box consensus motifs within their promoters.
Subcellular location: Nucleus {ECO:0000269|PubMed:20367464, ECO:0000269|PubMed:23451802}.
Interaction partners:
- VQ motif-containing protein 9
- VQ motif-containing protein 10
- VQ motif-containing protein 22
- Sigma factor binding protein 1, chloroplastic
- Sigma factor binding protein 2, chloroplastic
- Protein HAIKU1
- VQ motif-containing protein 20
- VQ motif-containing protein 29
- Calmodulin-binding protein 25
- Protein MKS1
Sequence:
MSHEIKDLNNYHYTSSYNHYNINNQNMINLPYVSGPSAYNANMISSSQVGFDLPSKNLSPQGAFELGFELSPSSSDFFNPSLDQENGLYNAYNYNSSQKSHEVVGDGCATIKSEVRVSASPSSSEADHHPGEDSGKIRKKREVRDGGEDDQRSQKVVKTKKKEEKKKEPRVSFMTKTEVDHLEDGYRWRKYGQKAVKNSPYPRSYYRCTTQKCNVKKRVERSYQDPTVVITTYESQHNHPIPTNRRTAMFSGTTASDYNPSSSPIFSDLIINTPRSFSNDDLFRVPYASVNVNPSYHQQQHGFHQQESEFELLKEMFPSVFFKQEP
Protein: RecBCD enzyme subunit RecB (EC 3.1.11.5) (EC 5.6.2.4) (DNA 3'-5' helicase subunit RecB) (Exonuclease V subunit RecB) (ExoV subunit RecB) (Helicase/nuclease RecBCD subunit RecB) (P9WMQ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA.
Interaction partners:
- RecBCD enzyme subunit RecC
- RecBCD enzyme subunit RecD
- DNA repair protein RecO
- Protein RecA
- DNA polymerase I
- ATP-dependent DNA helicase RecG
- DNA repair protein RecN
- DNA ligase A
- Multifunctional non-homologous end joining DNA repair protein LigD
Sequence:
MDRFELLGPLPREGTTTVLEASAGTGKTFALAGLVTRYLAETAATLDEMLLITFNRAASRELRERVRGQIVEAVGALQGDAPPSGELVEHLLRGSDAERAQKRSRLRDALANFDAATIATTHEFCGSVLKSLGVAGDNAADVELKESLTDLVTEIVDDRYLANFGRQETDPELTYAEALALALAVVDDPCAQLRPPDPEPGSKAAVRLRFAAEVLEELERRKGRLRAQGFNDLLIRLATALEAADSPARDRMRERWRIVLVDEFQDTDPMQWRVLERAFSRHSALILIGDPKQAIYGFRGGDIHTYLKAAGTADARYTLGVNWRSDRALVESLQTVLRDATLGHADIVVRGTDAHHAGHRLASAPRPAPFRLRVVKRHTLGYDGTAHVPIEALRRHIPDDLAADVAALLASGATFAGRPVVAADIAVIVEHHKDARACRNALAEAGIPAIYTGDTDVFASQAAKDWLCLLEAFDAPQRSGLVRAAACTMFFGETAESLAAEGDALTDRVAGTLREWADHARHRGVAAVFQAAQLAGMGRRVLSQRGGERDLTDLAHIAQLLHEAAHRERLGLPGLRDWLRRQAKAGAGPPEHNRRLDSDAAAVQIMTVFVAKGLQFPIVYLPFAFNRNVRSDDILLYHDDGTRCLYIGGKDGGAQRRTVEGLNRVEAAHDNLRLTYVALTRAQSQVVAWWAPTFDEVNGGLSRLLRGRRPGQSQVPDRCTPRVTDEQAWAVFAQWEAAGGPSVEESVIGARSSLEKPVPVPGFEVRHFHRRIDTTWRRTSYSDLVRGSEAVTVTSEPAAGGRADEVEIAVVAAPGSGADLTSPLAALPSGASFGSLVHAVLETADPAAPDLAAELEAQVRRHAPWWTVDVDHAQLAPELARALLPMHDTPLGPAAAALTLRQIGVRDRLRELDFEMPLAGGDLRGRSPDVSLADVGELLASHLPGDDPLSPYADRLGSAGLGDQPLRGYLAGSIDVVLRLPGQRYLVVDYKTNHLGDTAADYGFERLTEAMLHSDYPLQALLYVVVLHRFLRWRQRDYAPARHLGGVLYLFVRGMCGAATPVTAGHPAGVFTWNPPTALVVALSDLLDRGRLQS
Protein: Histone deacetylase (EC 3.5.1.98) (Q8IR69)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
Sequence:
MELEHKLQLEHKYQFAVNSHGAFQELRNESMVTAAAAAVAQEQHRQQLHQQQQQHQQQQQQQQHQQQQQQQQARGRDGMKLKQNCSANASPEVKQILNCFILSRKSQAAASNGTTTTSPYRNRGVVKSSSGESLPAGTVTSAHPYKIPQPPPSLLKYESDFPLRKTASEPNLLKIRLKQSVIERKARIGGPAGARRHERLLQAAQRRQQKNSVLTNCNSTPDSGPNSPPSAAALAVGVVGSRGSPTSAPIQEENEEGSQYQPGQRSSINDLPLFSSPSLPNISLGRPHLPNSAQAHAQVNAQVAAQAQAQAQAQAQAHAMFAALAAAQGGCGQPGYYNPLGMAFVGRQPAPLAMIPATGIAPQQPSPVVRSASATSTSSSQASLVGDVAPPQAHAASTILPSSSSYMQQLGSVAGSGVNLHAAAVAAAAAAAAAAGSLPPTNSHGHGHGSHAHPHPHAHGHGHGHGHGIYAGHQHNVPITDAQVAQVHLHKQGHRPLGRTQSAPLPLGHPMLTGAVQLNVVQTHYENSEAERQAYEHQVVNQKVRQTVLTRSGAAAAAAAAAGVSVVREAQLKEEDDDSAAEVMDLTDKKKPPKTVLTSTIATSTSQNLPEALAAAAAAAAYRAPHNASSNSASATKSGIKLRDQEYLQQQREQLLLLQQEEELAKSLMRPLSRTLSSPLVPLGPHGLSQIPDTGQQPAPIATSSSADHIPPVNLSLPHRQHRQLMSTLYASQLRNHQPSASGSPPHKVTTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQCQLSRPKLENTLSASFVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRMPEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLGFNVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGKVVLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHWPCVRMLEHTVGLSALETLKVEHDESETINAMAGLSMQSMHRTLSRDDSEEPMDQDETK
Protein: Adenosine receptor A2b (Q60614)
Organism: Mus musculus (Mouse)
Function: Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Adenosine receptor A2a
- Ectonucleoside triphosphate diphosphohydrolase 1
- 5'-nucleotidase
- Adenosine deaminase
Sequence:
MQLETQDALYVALELVIAALAVAGNVLVCAAVGASSALQTPTNYFLVSLATADVAVGLFAIPFAITISLGFCTDFHGCLFLACFVLVLTQSSIFSLLAVAVDRYLAIRVPLRYKGLVTGTRARGIIAVLWVLAFGIGLTPFLGWNSKDSATSNCTELGDGIANKSCCPVTCLFENVVPMSYMVYFNFFGCVLPPLLIMLVIYIKIFMVACKQLQRMELMDHSRTTLQREIHAAKSLAMIVGIFALCWLPVHAINCITLFHPALAKDKPKWVMNVAILLSHANSVVNPIVYAYRNRDFRYSFHKIISRYVLCQAETKGGSGQAGAQSTLSLGL
Protein: Polyunsaturated fatty acid (12S)/(13S)-lipoxygenase, epidermal-type (EC 1.13.11.-) (Arachidonate (12S)-lipoxygenase, epidermal-type) (12-LOX-e) (e(12S)-LOX) (EC 1.13.11.31) (Linoleate (13S)-lipoxygenase) (D3ZQF9)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species. Shows increasing catalytic activity within the series arachidonic acid < 5,8,11-eicosatrienoic acid < linoleic acid < 8,11,14-eicosatrienoic acid (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
Interaction partners:
- Prostaglandin G/H synthase 2
- Prostaglandin G/H synthase 1
- Cytochrome P450 2C23
- Arachidonate 12-lipoxygenase, 12R-type
- Polyunsaturated fatty acid lipoxygenase ALOX15B
- Polyunsaturated fatty acid 5-lipoxygenase
- Cytochrome P450 2E1
- Cytochrome P450 4F3
- Cytochrome P450 4A12
- Cytochrome P450 4A10
Sequence:
MGKYKILVVTGDSLLAGSTNLVQLWLVGEHAEADLGKQLRPLRGRKTELEIDVPLHLGRLLVVKLRKHKGLLDSDWFCKWITVQGPGIQGEAFFPCYSWVQGKETIYLPEGTALKVNDDTKNLFRKYREQELEDRRNVYRWGSWKEGLILPIAGSTERDLPRNQRFMEDKDLDFSLSLAKVLKDFAIKGTLDFVSRVQHLEDYQKVFPHSKTALAGRVRDSWKEDALFGYQFLNGANPMLLRRSKRLPARLVLPPGMEDLQTQLEKELKAGSLFEADFSLLDGVKPNVIIFKQQHVAAPLVMLKLQSDGRLLPMVIQLQPPRHGCPPPLLFLPSDPPMAWLLAKIWVRSSDFQVHQLQSHLLRGHLMAEVISVATMRSLPSLHPIYKLLAPHFRYTMEINTLARNNLVSEWGIFDLVVSTGSGGHVDILQRATACLTYRSFCPPDDLADRGLLDVKSSLYARDALRLWEIISRYVGRMVELFYKNDREVKEDPELQVWCREVTEIGLLGAQDRGFPLSLESRAQLCRFVTMCIFTCTGQHASTHLGQLDWYSWIPNGPCTMRKPPPTSKNVTEGDILDALPCLQQARMQITFTKFLGRHQPVMVALGQHKEEYFSDPGARAVLKQFQEELAVMDKEIEVRNASLDLPYEYLRPSMVENSVTI
Protein: Glucocorticoid receptor (Nuclear receptor subfamily 3 group C member 1) (F1D8N4)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK
Protein: Cdc42 effector protein 4 (Binder of Rho GTPases 4) (Q9H3Q1)
Organism: Homo sapiens (Human)
Function: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.
Subcellular location: Endomembrane system; Peripheral membrane protein. Cytoplasm, cytoskeleton.
Interaction partners:
- Rho-related GTP-binding protein RhoQ
- Cell division control protein 42 homolog
- Septin-7
- Septin-6
- Septin-8
- Neuronal-specific septin-3
- Septin-11
- Uncharacterized protein C17orf47
- Septin-9
- Septin-5
Sequence:
MPILKQLVSSSVHSKRRSRADLTAEMISAPLGDFRHTMHVGRAGDAFGDTSFLNSKAGEPDGESLDEQPSSSSSKRSLLSRKFRGSKRSQSVTRGEREQRDMLGSLRDSALFVKNAMSLPQLNEKEAAEKGTSKLPKSLSSSPVKKANDGEGGDEEAGTEEAVPRRNGAAGPHSPDPLLDEQAFGDLTDLPVVPKATYGLKHAESIMSFHIDLGPSMLGDVLSIMDKEEWDPEEGEGGYHGDEGAAGTITQAPPYAVAAPPLARQEGKAGPDLPSLPSHALEDEGWAAAAPSPGSARSMGSHTTRDSSSLSSCTSGILEERSPAFRGPDRARAAVSRQPDKEFSFMDEEEEDEIRV
Protein: Transmembrane serine protease 2 (C9J5Y1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFIRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG
Protein: Sulfotransferase 4A1 (ST4A1) (EC 2.8.2.-) (Brain sulfotransferase-like protein) (mBR-STL) (Nervous system sulfotransferase) (NST) (P63046)
Organism: Mus musculus (Mouse)
Function: Atypical sulfotransferase family member with very low affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in the metabolism of drugs and neurotransmitters in the CNS.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Sulfotransferase 1A1
Sequence:
MAESEAETPGTPGEFESKYFEFHGVRLPPFCRGKMEDIADFPVRPSDVWIVTYPKSGTSLLQEVVYLVSQGADPDEIGLMNIDEQLPVLEYPQPGLDIIKELTSPRLIKSHLPYRFLPSDLHNGDSKVIYMARNPKDLVVSYYQFHRSLRTMSYRGTFQEFCRRFMNDKLGYGSWFEHVQEFWEHRMDANVLFLKYEDMHRDLVTMVEQLARFLGVSCDKAQLESLIEHCHQLVDQCCNAEALPVGRGRVGLWKDIFTVSMNEKFDLVYKQKMGKCDLTFDFYL
Protein: Uncharacterized protein (Q86K54)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Metabotropic glutamate receptor-like protein M
Sequence:
MIIISLILMTIKLFFFATPLVGLVASSIFLDYRSTLRISLVLLICQLISLLVQSLFVKGGIEKWNFIKFIIDIPILALSYYIYPLIPDQVIDFYYYCFQWIFPLLVYTVESYQAILLIVFKSRSLSNQLISSDSNNIIFKTFVILISIFSYSLSFFIIYQIFNYNIISTLNSCLLSSLGTLMILLLPYMYMVEESMLSDISLITLTICLNLYSFFFQFDTSSIINTVNILKSLSYLVTFILISYPIINNKLDSDSTDQFINGDDDDESVLLKLKSKIFHIGLVIALTYLPLSMTNIVSNGNLVFRYLQGVFTVLCYFALLSQSNSDPFKFKYD
Protein: WAS/WASL-interacting protein family member 1 (Protein PRPL-2) (Wiskott-Aldrich syndrome protein-interacting protein) (WASP-interacting protein) (O43516)
Organism: Homo sapiens (Human)
Function: Plays a role in the reorganization of the actin cytoskeleton. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation. Plays a role in the formation of cell ruffles (By similarity). Plays an important role in the intracellular motility of vaccinia virus by functioning as an adapter for recruiting WASL to vaccinia virus.
Subcellular location: Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle {ECO:0000269|PubMed:19910490}. Note=Vesicle surfaces and along actin tails. Colocalizes with actin stress fibers. When coexpressed with WASL, no longer associated with actin filaments but accumulated in perinuclear and cortical areas like WASL (By similarity). {ECO:0000250}.
Interaction partners:
- SH2/SH3 adapter protein NCK1
- Actin nucleation-promoting factor WASL
- Actin nucleation-promoting factor WAS
- Growth factor receptor-bound protein 2
- Cell division control protein 42 homolog
- Src substrate cortactin
- Cytoplasmic protein NCK2
- Hematopoietic lineage cell-specific protein
- Formin-binding protein 1-like
- WAS/WASL-interacting protein family member 3
Sequence:
MPVPPPPAPPPPPTFALANTEKPTLNKTEQAGRNALLSDISKGKKLKKTVTNDRSAPILDKPKGAGAGGGGGGFGGGGGFGGGGGGGGGGSFGGGGPPGLGGLFQAGMPKLRSTANRDNDSGGSRPPLLPPGGRSTSAKPFSPPSGPGRFPVPSPGHRSGPPEPQRNRMPPPRPDVGSKPDSIPPPVPSTPRPIQSSPHNRGSPPVPGGPRQPSPGPTPPPFPGNRGTALGGGSIRQSPLSSSSPFSNRPPLPPTPSRALDDKPPPPPPPVGNRPSIHREAVPPPPPQNNKPPVPSTPRPSASSQAPPPPPPPSRPGPPPLPPSSSGNDETPRLPQRNLSLSSSTPPLPSPGRSGPLPPPPSERPPPPVRDPPGRSGPLPPPPPVSRNGSTSRALPATPQLPSRSGVDSPRSGPRPPLPPDRPSAGAPPPPPPSTSIRNGFQDSPCEDEWESRFYFHPISDLPPPEPYVQTTKSYPSKLARNESRSGSNRRERGAPPLPPIPR
Protein: Riboflavin biosynthesis protein VVA0006 [Includes: Riboflavin biosynthesis intermediates N-glycosidase (EC 3.2.2.-); GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II)] (Q7MGG3)
Organism: Vibrio vulnificus (strain YJ016)
Function: Catalyzes the hydrolysis of the N-glycosidic bond in the first two intermediates of riboflavin biosynthesis, which are highly reactive metabolites, yielding relatively innocuous products. Thus, can divert a surplus of harmful intermediates into relatively harmless products and pre-empt the damage these intermediates would otherwise do. Has no activity against GTP, nucleoside monophosphates or ADP-ribose.
Interaction partners:
- Riboflavin biosynthesis protein RibD
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- 6,7-dimethyl-8-ribityllumazine synthase
- Riboflavin synthase
- GTP cyclohydrolase 1
- Riboflavin synthase
- GTP cyclohydrolase-2
- GTP 3',8-cyclase
- Nucleoside diphosphate kinase
Sequence:
MHFVSYSLCYDVRSNIMEQPIYFYEPDENHGFLANFYPCSITVSGTCWPSSEHYYQAQKFDDVRLQEKVLRAEDAAQAFRLSREYQQWQRHDWYDIRVEVMRFIVREKFLQNTPLAHQLLATGDTELKEHSHKDAFWGDGGDGHGRNELGRILMMVREELQEHAPYNLVQFIDSAKLPTQWGTFQMYGFIEKATGKEHLALVYGDIEQQAAPLIRLHSECLTGDALFSARCDCGFQLAKALQNIVAEGAGVLLYLRQEGRGIGLINKIRAYHLQDDGADTVEANEQLGFGADMRDYAFCRGILSFLGIERVRLMTNNPRKVKALQLANIEVTERVPLQEGNNPHNHQYLRTKADKLGHMFDRNFVKP
Protein: Tissue factor pathway inhibitor (Q8CF99)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|PIRNR:PIRNR001620}.
Interaction partners:
Sequence:
MDPATSLRLWNLPLLLVGSALGLASVSAQGNNLEICLLPLDMGPCKALIPKFYYDRDQKKCRRFKYGGCLGNANNFHSRKLCEHTCGNKEKVPWVCRSAVRTYPCDKPNTEFFFNLKTMTCEPLRPGLCSRTTNVFPEEAMCKSLCEPRKSIPSFCSSPKDEGLCSANVTRYYFNSRNKTCETFTYTGCGGNENNFYYLDACNRACVKALKKPKRRKIGDFLPRFWKLRS
Protein: Death domain-containing protein CRADD (Caspase and RIP adapter with death domain) (RIP-associated protein with a death domain) (O88843)
Organism: Mus musculus (Mouse)
Function: Adapter protein that associates with PIDD1 and the caspase CASP2 to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis. Also recruits CASP2 to the TNFR-1 signaling complex through its interaction with RIPK1 and TRADD and may play a role in the tumor necrosis factor-mediated signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22279524}. Nucleus {ECO:0000269|PubMed:22279524}.
Interaction partners:
- Caspase-2
- p53-induced death domain-containing protein 1
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- FAS-associated death domain protein
- Receptor-interacting serine/threonine-protein kinase 1
- Suppressor of cytokine signaling 2
Sequence:
MEARDKQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEIKAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQEFPWVREKLEKAREEVTAELPTGDWMAGIPSHILSSSPSDQQINQLAQRLGPEWEPVVLSLGLSQTDIYRCKANHPHNVHSQVVEAFVRWRQRFGKQATFLSLHKGLQAVEADPSLLQHMLE
Protein: Ubiquitin carboxyl-terminal hydrolase 35 (EC 3.4.19.12) (Deubiquitinating enzyme 35) (Ubiquitin thioesterase 35) (Ubiquitin-specific-processing protease 35) (Q9P2H5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25915564}. Mitochondrion {ECO:0000269|PubMed:25915564}. Note=Only associates with polarized mitochondria, and rapidly translocates to the cytosol during mitophagy. {ECO:0000269|PubMed:25915564}.
Interaction partners:
- E3 ubiquitin-protein ligase HERC2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin carboxyl-terminal hydrolase 30
Sequence:
MDKILEAVVTSSYPVSVKQGLVRRVLEAARQPLEREQCLALLALGARLYVGGAEELPRRVGCQLLHVAGRHHPDVFAEFFSARRVLRLLQGGAGPPGPRALACVQLGLQLLPEGPAADEVFALLRREVLRTVCERPGPAACAQVARLLARHPRCVPDGPHRLLFCQQLVRCLGRFRCPAEGEEGAVEFLEQAQQVSGLLAQLWRAQPAAILPCLKELFAVISCAEEEPPSSALASVVQHLPLELMDGVVRNLSNDDSVTDSQMLTAISRMIDWVSWPLGKNIDKWIIALLKGLAAVKKFSILIEVSLTKIEKVFSKLLYPIVRGAALSVLKYMLLTFQHSHEAFHLLLPHIPPMVASLVKEDSNSGTSCLEQLAELVHCMVFRFPGFPDLYEPVMEAIKDLHVPNEDRIKQLLGQDAWTSQKSELAGFYPRLMAKSDTGKIGLINLGNTCYVNSILQALFMASDFRHCVLRLTENNSQPLMTKLQWLFGFLEHSQRPAISPENFLSASWTPWFSPGTQQDCSEYLKYLLDRLHEEEKTGTRICQKLKQSSSPSPPEEPPAPSSTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSLAFPPPERCRRRRLGSVMRPTEDITARELPPPTSAQGPGRVGPRRQRKHCITEDTPPTSLYIEGLDSKEAGGQSSQEERIEREEEGKEERTEKEEVGEEEESTRGEGEREKEEEVEEEEEKVEKETEKEAEQEKEEDSLGAGTHPDAAIPSGERTCGSEGSRSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLLLRLPLAGGRGQAYDLCSVVVHSGVSSESGHYYCYAREGAARPAASLGTADRPEPENQWYLFNDTRVSFSSFESVSNVTSFFPKDTAYVLFYRQRPREGPEAELGSSRVRTEPTLHKDLMEAISKDNILYLQEQEKEARSRAAYISALPTSPHWGRGFDEDKDEDEGSPGGCNPAGGNGGDFHRLVF
Protein: Uncharacterized protein (Q383S0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tubulin alpha chain
- Cilia- and flagella-associated protein 45
- CFA20 domain-containing protein
- ODAD1 central coiled coil region domain-containing protein
- Enkurin domain-containing protein
- Enkurin domain-containing protein
Sequence:
MSSPMCSVHSNPLGGSRSRLHIAPQIIPAGRQGSRDGTTVRELTSNHYSSGRVTPELQRTYHRFGEVGCTRRHYGRARDPPIDETFRHGIRTEAGEGARGCLQPETGGRMMALMEQQLERAYLSNVRRPLGKVPAAMYDVQVPHSGFGIPSEKSESVKTLLYAGRDSGTVHPVGECKNRGYDWERAGINPMHHRFGWCEQRGEATAGEVMCETKLVTRLLPKVVTDVRKLTKQEVGKGLPPPWDTKYFDDTLESRTIRRNGRGEGDAVRQLLSSWMHHPFPPKRQLVAEEEDASLKGTGSLEGSRKEGLEKDALRSRFLCTYRRGGRYNSADHTRLDDDVRAPHVLYPCHYVQMGVNSSRFAGGCTLENVRDLCKSVGMDLAENQMQEVFNHVAVDGVCGIEQFKNKAVEMGYLS