wanglab/gogpt-training-data huggingface dataset:
Protein: CARD domain-containing protein (A0A060YD78)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Guanylate kinase-like domain-containing protein
- Uncharacterized protein
- Mucosa-associated lymphoid tissue lymphoma translocation protein 1
- NF-kappa-B essential modulator NEMO N-terminal domain-containing protein
- MALT paracaspase 2
- Death domain-containing protein
- Mucosa-associated lymphoid tissue lymphoma translocation protein 1-like
- Caspase family p20 domain-containing protein
- CARD domain-containing protein
- CARD domain-containing protein
Sequence:
MDSWCITDEDMAEVKKEALERLRPYLCEKLVADRHLDYLRSRRVLTRDDAEDICCSKKTGRMLDYLAENPRGLDYLVESICRVRTKDFVIGKITNEVEVVKMERREAAILSAAGSSSPVCICKERTPFVSLQSGSSDAQSIQTSLSNSEDKWGQNEASFSWSALPEGVSVSSLHSLPKPGEQGAPSVPLEDNEPGTLRV
Protein: Hexosyltransferase (EC 2.4.1.-) (Q57U24)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}.
Interaction partners:
- T. brucei spp.-specific protein
- T. brucei spp.-specific protein
- Dolichol-phosphate mannosyltransferase subunit 1
Sequence:
MVWSGHKYKRLLPLCLLTLLWFLSLSRFRRVEVPKQRENIQHSFEPTLTTLNEEDLQSVQFIPQATVDVLRRRDFFVAVGFLSPDNNERRRRRYLLRLTSFQYPGVATKSNNFSGELMIAFILARHPDHNYTFSAKLKEEAWHWNDIISLPMDEGKVSTNKTTGDGTHWGPATEIGMSRKVFHWYDFALRFFRNVTYISKADDDAFLHVPQFLADLHTLPRRRVYWGYMKPMTVKDPFYFAAGILYTLSRDVSEAFVAYEPLRKIIRVPYSKEREMEFKPLILENEDIMVARVISYLRLDNLRYYVESCCRFNDLNYGFCSGVRDTSVIIHGVKEGQYADIVNRLGKHRTVANPFYRGYLGWHASCT
Protein: Vacuolar protein 8 (A2R3P5)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Vacuole membrane {ECO:0000256|ARBA:ARBA00004592, ECO:0000256|RuleBase:RU369097}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004592, ECO:0000256|RuleBase:RU369097}.
Interaction partners:
Sequence:
MSGITNACLSCFSTVDRWCHISACLGPIGGRSRDGIYETTLADNEREAVSDLLGYLENRTETDFFAGEPLRALSTLVYSDNVDLQRSASLTFAEITERDVREVDRDTLEPILFLLQSSDIEVQRAASAALGNLAVNADNKVLIVALGGLAPLIRQMMSPNVEVQCNAVGCITNLATHEDNKAKIARSGALGPLIRLAKSKDMRVQRNATGALLNMTHSDDNRQQLVNAGAIPVLVQLLSSPDVDVQYYCTTALSNIAVDSSNRKRLAQTESRLVQSLVHLMDSSTPKVQCQAALALRNLASDEKYQLEIVRAKGLPPLLRLLQSSYLPLILSAVACIRNISIHPLNESPIIDAGFLKPLVDLLGSTDNEEIQCHAISTLRNLAASSDRNKELVLQAGAVQKCKDLVLRVPLSVQSEMTAAIAVLALSDELKPHLLNLGVFDVLIPLTESESIEVQGNSAAALGNLSSKVGDYSIFVRDWADPNGGIHGYLNRFLASGDPTFQHIAIWTLLQLLESEDQRLIGYIAKSDDIVQMVKSISDKNIESDEEDAEDGEGEVIALARRCLEFLGNGHKLVEA
Protein: Histone H1.X (Histone H1-like protein 1) (Q18336)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}.
Interaction partners:
- H15 domain-containing protein
- Fork-head domain-containing protein
Sequence:
MTTSLIHMANHLDASTEEISLNYVLLGHPHHERAQHHPSYMDMIKGAIQAIDNGTGSSKAAILKYIAQNYHVGENLPKVNNHLRSVLKKAVDSGDIEQTRGHGATGSFRMGKECEKNLQVGIPVQTKPMLMLKEVRQKLENISKAEKTKPSTSSMSTNKKGKPISTMKKRGVMSKKRSSKNKMAPKAKSHGLKKKGPATKSSGLVHKAAGAKNEAAPTTKMELRTGTRKSYC
Protein: Transmembrane protein (Q0WV86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Phosphatidylinositol 3-kinase VPS34
- Beclin-1-like protein
Sequence:
MGLLKTSWLLLLFWVVSSPLCFRFHYCYGSELSVKFLKAPPTTSRFTSAKFSFLAFEDGNRTCSSCKFRCKLDDRISLDCHQRKVSYSKLLDGDHTLEVCANRMHGFGCNHYNWTVDTVSPTAFVTASMPFTSAQNVSVNITFTEPCVGRGGFGCSSVNSCDLLVYGAGQVIPSSFTVLDQYLRYSLLVGLSPDAQYGRIVLVMNKSVCSDIAGNNFKRALGSRFFVHFDRRNVLVNLRTHVPEKLLKLNNQTRTVQATNDNNKLNVYLYFSEPVLNSSAEILRRLNTNQGDLLPIDGNTNGNRRFAFMVTNTSRRAIVTVTLDSNSIRSRHGTPASPTAPLTFLYDTERPHVILNTTSGMRTRKHTIPVWIKFMKPVFGFNSSFVSISGGYLDSFEELSGSIYIVYVKANTSTLSIKIPENVTQDVAGNKNLASNILKVKHYSVPMISSVISWVTTYIFLVTSFVAGLLTLSTTSLYSLGAFPRPSPYLISDPTRNLFRTACHIQFFALTRWLPVTLPVDYYELVRGIQWIIPYFPLPWETKIKEQIMVATSPYIGPHSFISKTHNNMINLKTSTNAESVFGLPLTAMEYRLFFETSNLKPEAEHVLGLPHSTVWRDFNRIMFWIAIIGGSLVLLHIVLSLILKFKKAHSEKKRSFGAFVFPRFELFLLILALPSICKAARSLIQGYFKHQGAAEASVIVGILVLCVVAILLLALFLFLSVGITFGKLLQYKEIHQEGQTFHWYQELIRVTLGPGKRGQWTWKTENSVYLTRLGPVFEDLRGPPKYMLTQISGSNPLKQQDDRIIASDDENEDAEAPCIQKLFGILRIYYTFLETVKRVCLGIIAGAFLDNETAKTPIVVLLSITSFQLFFLLLKKPFIKKKVQLVEIISIACQVGVFASCLMLLAKDFPEASGKKLGIFMVVLFLIGFIMLMCNEWYSLYKQTKRLDQINRSFLSGLKMFIIGLAALILPQKMIKNKIPVAQLEARSSSNGGTTPEFRYRNSSGSRSSGSLDKPWLKQIREMAKSSFTRDRSNSKVPSDPSCSKSGWSSSIWGTKTSGSSSKESSADYKSRPKGLYKDLEAIFASK
Protein: DNA transformation protein TfoX1 (Q5E6F5)
Organism: Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri)
Function: Required for DNA transformation jointly with TfoX2.
Interaction partners:
- Macrodomain Ter protein
- Conserved protein
- Primosomal replication protein N
- UPF0304 protein VF_1794
- ParB family protein
- Chromosome partitioning protein ParA
- DNA polymerase III subunit psi
- Card1 endonuclease domain-containing protein
- Fused chromosome partitioning protein: predicted nucleotide hydrolase
- Calcium-binding protein involved in chromosome partioning
Sequence:
MTGTGDVNLKIKEIEMSHLEERFFNFVKKLGRFNKRSMFGGVGLFNEDAMFSLVTDGRLYVRGGGEVDARFEELGCERFKHVKKTTIATVNYFDVTELFEKKPASLLSIVQEAMENSRLEREFKKSKENRRLRDLPNMQLTLERMVKKAGVPDVDSFLEIGAVDVFKKVNHTYGGDVDVKLLWKFAGAESGVHWTLLQEPAKQALLQQV
Protein: Probable tyrosyl-DNA phosphodiesterase (Tyr-DNA phosphodiesterase) (EC 3.1.4.-) (Protein glaikit) (Q9VQM4)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. May have low 3'exonuclease activity and may be able to remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate (By similarity). Required for normal polarization of epidermal cells, correct subcellular location of the Crb complex to the apical lateral membrane, and for normal neuronal development during embryonic development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NUW8}. Cytoplasm {ECO:0000269|PubMed:15556867}.
Interaction partners:
- DNA topoisomerase 1
- FI07206p
- Aprataxin-like protein
- FI04011p
- DNA ligase 4
- Crossover junction endonuclease MUS81
- DNA topoisomerase 2
- N-glycosylase/DNA lyase
- DNA ligase
- DNA repair endonuclease XPF
Sequence:
MKECPYGEKCYRKNPIHFGEFSHAHLDAIYAKGNESGDYEIPANYSSEMIHTQLKLLEKLFPKQATNKEQEAHSSSSKPAVTAPVASGSSSSGSLDTNPSGSSASGPAASQDTSNLAKKQKLNAKNIRDYIPVVIEKGGMAKKLERAAPYNMFLTAITDSKPTHSEPLSITLQEILDESLGEIESTVQINFMVDIGWLLGHYYFAGILDKPLLLLYGDESPELLSIGKFKQQVTAIRVKMPTPFATSHTKMMFLGYSDGSMRVVISTANLYEDDWHNRTQGLWISPKLPALPVDADTGAGESLTGFKQDLMLYLVEYKISQLQPWIARIRNSDFSAINVFFLGSVPGGHREGSVRGHPWGHARLASLLAKHAAPIDDRIPVVCQSSSIGSLGANVQAWIQQDFVNSLKKDSTPVGKLRQMPPFKMIYPSYGNVAGSHDGMLGGGCLPYGKNTNDKQPWLKDYLQQWKSSDRFRSRAMPHIKSYTRFNLEDQSVYWFVLTSANLSKAAWGCFNKNSNIQPCLRIANYEAGVLFLPRFVTGEDTFPLGNNRDGVPAFPLPYDVPLTPYAPDDKPFLMDYLQG
Protein: Gamma tubulin complex adapter mto2 (Microtubule organizer protein 2) (Q9USP7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10759889}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:15659644, ECO:0000269|PubMed:15800064}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:15659644, ECO:0000269|PubMed:15800064}. Note=Localizes at the interphase MTOC (iMTOC) and at the equatorial MTOC (eMTOC) at the end of mitosis. {ECO:0000269|PubMed:15800064}.
Interaction partners:
- Gamma tubulin complex adapter mto1
- Mitotic-spindle organizing protein 1
- Spindle pole body protein pcp1
- Spindle pole body component alp4
- DnaJ-related protein rsp1
- Spindle pole body component alp16
- Gamma-tubulin complex subunit mod21
- Gamma-tubulin complex component gfh1
- Spindle pole body component alp6
Sequence:
MSEHNYQSDREVAEDPFLNYEASANQLSSNSRESTPRGSPWRAGMRSASLMTEPLEDSMYSDNNYLDNGVSFTKDENPLYSPSWPSLADANVNSMKSNNAIQEHKAAKFVSEKSLEKVSTADNNLVLQELENLRERLNQVELQLSERPSSYLGYHNNLSPYRSPNSYPSLLPSTHSPHSPAPLSTMQTALMRLRTYHPSPIILKPVEQAVNHAITLVNTSPSSVVDALCRSLAELCLGLVQEAIDASILSQQESSNSLDLVRHTPPLNYTSSVDSSPQRMASDSYGRPSLHLNDPFPSVDLQSNELSHHNVRTTLFSDDSRFHSKIHTHSTPPSQMYSAASHFRYRSDPSTRHVSNSTNKSSLHPSPTSLRVAHPIIPQRASPASQSFPSLQDTPSP
Protein: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (PDHE1-B) (EC 1.2.4.1) (P49432)
Organism: Rattus norvegicus (Rat)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Ac1164
- Pyruvate kinase PKM
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- [Pyruvate dehydrogenase
Sequence:
MAAVAGLVRGPLRQASGLLKRRFHRSAPAAVQLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNPVVMLENELMYGVAFELPTEAQSKDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI
Protein: NECAP endocytosis associated 1, isoform CRA_a (cDNA FLJ78563) (A8K3C2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDARPKLDLGFKEGQTIKLCIGNITNKKGGASKPRTARGGGLSLLPPPPGGKVTIPPPSSSVAISNHVTPPPIPKSNHGGSDADILLDLDSPAPVTTPAPTPVSVSNDLWGDFSTASSSVPNQAPQPSNWVQF
Protein: Tubulin gamma chain (Gamma-tubulin) (P18695)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle pole or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. Interacts physically with beta-tubulin and is involved in microtubule function.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000305}.
Interaction partners:
- Gamma-tubulin complex protein 3
- Spindle pole body component
- Spindle pole body component
- Spindle pole body component
- Mitotic-spindle organizing protein 1
- Spindle pole body component
- DASH complex subunit ASK1
- Polo-like kinase
- Kinesin-like protein klpA
Sequence:
MPREIITIQAGQCGNNVGSQFWQQLCLEHGISQDGNLEEFATEGGDRKDVFFYQSDDTRYIPRAILLDLEPRVLNGIQSGPYKNIYNPENFFIGQQGIGAGNNWGAGYAAGEVVQEEVFDMIDREADGSDSLEGFMFLHSIAGGTGSGLGSFLLERMNDRFPKKLIQTYSVFPDTQAADVVVNPYNSLLAMRRLTQNADSVVVLDNAALSRIVADRLHVQEPSFQQTNRLVSTVMSASTTTLRYPGYMHNDLVGIIASLIPTPRSHFLLTSYTPFTGDNIDQAKTVRKTTVLDVMRRLLQPKNRMVSINPSKSSCYISILNIIQGEADPTDVHKSLLRIRERRLASFIPWGPASIQVALTKKSPYIQNTHRVSGLMLANHTSVATLFKRIVQQYDRLRKRNAFLEQYKKEAPFQDGLDEFDEARAVVMDLVGEYEAAERENYLDPDAGKDEVGV
Protein: RRM domain-containing protein (Q38AR0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDPSKRICLKNIPPECTKREIAEFIRNRTGGQPHSIDLGLDSNGRVRRYAHFSVEGAKNVVSALTGATWKGVTVSALHANPHYTYRLAESRRRREHLESEEKQQREELLRRKTERWLAKTGGELPKGRPPKPFFASRQRYAEVASEIAKKSREEHRAKRLQGRMQQTVGGPSRRWARESLIDKATSGPVQPGVSFSNYLRSSSHCEHEGGSTDPNSRVLKRQKTERAGNPAMKPVQQQETPQTVGPTREERKLSGLKAKLEALRAKMK
Protein: Uncharacterized protein IRC16 (Increased recombination centers protein 16) (Q6B0V8)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MVCFSISFNRASFFSAAAPCTSSIPDFALIRPGVAMDSSLDEKNIHRPMIPNAATILMAWLLLTICFIPSFLAQSVQTFLFTNHQPSRLLVFITHVYCLMIKPFVLYFWFLFPLRLPGG
Protein: WUSCHEL-related homeobox 13 (O81788)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in the regulation of fruit patterning. Promotes replum development by down-regulating JAG and YAB1/FIL genes activity in medial tissues. Seems to inhibit fruit dehiscence, maybe by controlling valve margin lignification. Promotes callus formation at wound sites. Is required for the formation of highly vacuolated large cells in callus and for the establishment of organ reconnection. Targets directly genes involved in stress-induced cellular reprogramming, and cell wall modifier genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- AT-hook motif nuclear-localized protein 12
- Zinc finger protein JAGGED
- Axial regulator YABBY 1
Sequence:
MMEWDNQLQPNNHHSSNLQGIDVNGGSGAGGGMYVKVMTDEQYETLRKQIAIYGTICERLVEMHKTLTAQQDLAGGRMGGLYADPMMSSLGHKMTARQRWTPTPVQLQILERIFDQGTGTPSKQKIKDITEELSQHGQIAEQNVYNWFQNRRARSKRKQHGGGSSGNNNGESEVETEVEALNEKRVVRPESLLGLPDGNSNNNGLGTTTATTTAPRPEDLCFQSPEISSDLHLLDVLSNPRDEHLVGKMGLAESYNLYDHVEDYGMSG
Protein: fructokinase (EC 2.7.1.4) (A0A0H2UR62)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MTKLYGSLEAGGTKFVCAVGDENFNVVEKTQFPTTTPIETIDKTIEFFSKFDNLAGLAVGSFGPIDIDKNSKTYGFITTTPKPNWANVDLLGALRRALNVPMYFTTDVNSSAYGEMVARNNAGGRIENLVYYTIGTGIGAGVIQRGEFIGGVGHPEMGHYYVARHPMDIEKEFKGVCPFHKGCLEGYAAGPSLEARTGVRGETIELNNPVWDVQAYYIAQAAVNATVTFRPDVIVFGGGVMAQQHMLDRVREKFTSLLNGYLPVPDVRDYIVTPAVAGNGSATLGNFVLAKEVSK
Protein: Latent-transforming growth factor beta-binding protein 3 (LTBP-3) (Q61810)
Organism: Mus musculus (Mouse)
Function: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9NS15}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9NS15}. Note=Secretion occurs after coexpression with TGFB1 and requires complexing with 'Cys-33' of the TGFB1 propeptide. {ECO:0000250|UniProtKB:Q9NS15}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-2 proprotein
- Transforming growth factor beta-3 proprotein
- Growth/differentiation factor 8
- Lysyl oxidase homolog 1
- Latent-transforming growth factor beta-binding protein 1
- Integrin beta-6
- Elastin
Sequence:
MPGPRGAAHGLAPAMRQAGALGLLALLLLALLGPGGGAEGGPAGERGTGGGGALARERFKVVFAPVICKRTCLKGQCRDSCQQGSNMTLIGENGHSTDTLTGSGFRVVVCPLPCMNGGQCSSRNQCLCPPDFTGRFCQVPAAGTGAGTGSSGPGLARTGAMSTGPLPPLAPEGESVASKHAIYAVQVIADPPGPGEGPPAQHAAFLVPLGPGQISAEVQAPPPVVNVRVHHPPEASVQVHRIEGPNAEGPASSQHLLPHPKPQHPRPPTQKPLGRCFQDTLPKQPCGSNPLPGLTKQEDCCGSIGTAWGQSKCHKCPQLQYTGVQKPGPVRGEVGADCPQGYKRLNSTHCQDINECAMPGMCRHGDCLNNPGSYRCVCPPGHSLGPSRTQCIADKPEEKSLCFRLVSTEHQCQHPLTTRLTRQLCCCSVGKAWGARCQRCPADGTAAFKEICPAGKGYHILTSHQTLTIQGESDFSLFLHPDGPPKPQQLPESPSRAPPLEDTEEERGVTMDPPVSEERSVQQSHPTTTTSPPRPYPELISRPSPPTFHRFLPDLPPSRSAVEIAPTQVTETDECRLNQNICGHGQCVPGPSDYSCHCNAGYRSHPQHRYCVDVNECEAEPCGPGKGICMNTGGSYNCHCNRGYRLHVGAGGRSCVDLNECTKPHLCGDGGFCINFPGHYKCNCYPGYRLKASRPPICEDIDECRDPSTCPDGKCENKPGSFKCIACQPGYRSQGGGACRDVNECSEGTPCSPGWCENLPGSYRCTCAQGYEPAQDGLSCIDVDECEAGKVCQDGICTNTPGSFQCQCLSGYHLSRDRSRCEDIDECDFPAACIGGDCINTNGSYRCLCPQGHRLVGGRKCQDIDECSQDPGLCLPHGACENLQGSYVCVCDEGFTLTQDQHGCEEVEQPHHKKECYLNFDDTVFCDSVLATNVTQQECCCSLGAGWGDHCEIYPCPVYSSAEFHSLCPDGKGYTQDNNIVNYGIPAHRDIDECILFGAEICKEGKCVNTQPGYECYCKQGFYYDGNLLECVDVDECLDESNCRNGVCENTRGGYRCACTPPAEYSPAQRQCLSPEEMEHAPERREVCWGQRGEDGMCMGPLAGPALTFDDCCCRQGRGWGTQCRPCPPRGTGSQCPTSQSESNSFWDTSPLLLGKSPRDEDSSEEDSDECRCVSGRCVPRPGGAVCECPGGFQLDASRARCVDIDECRELNQRGLLCKSERCVNTSGSFRCVCKAGFTRSRPHGACVPQRRR
Protein: GH27027p (Sodium chloride cotransporter 69, isoform A) (Sodium chloride cotransporter 69, isoform G) (Q9VTW8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSDTISFELGSAADRPPNRFQVNPVNGNSRKSQGADGPGSGSGAGAGAGAGAGEDGPHEVYRRLTNAEGELLEDDTFDATQMLNQRQPRQQRQSIKSSFRDKDKPSRFKDLQTTTRFQVDPQNEESDESNDSQEERELLDNEYDTKYGKSFRHFTREALPRLDNYRNMMSIQAAYRPTLDELHNATLVGKNTHSLTRNQDPESGILNGVLKFGWIKGVLVRCLLNIWGVMLFLRLSWVVGQAGVIEGFVLILTTTAVTTITALSMSAISTNGVIKGGGTYYMISRSLGPEFGGSIGLIFSLANAVACAMYVVGFCESMLAMMTTFGWEIIDGGVQDVRIIGCITILLLLIIVVVGMEWEAKAQIGLLIILLVAIGDFVIGSFIGPKSDAEMAKGFLGYNATLFKNNLFADYRPEKGGIQHDFFSVFAIFFPAATGILAGANISGDLKDPQKSIPKGTILAIVITTGTYLIMVLQCGATVARDATGNLSDVVNGTFAFLDCQPGECNYGLQNSFQVIELVSAFGPLIYAGCYAATLSSALASLVSAPKVFQALCKDELYPKIVWFAKGYGKNNEPVRGYVLTFIIACAFILIGELNLIAPLISNFFLAAYMLINFSTFHASLAKPVGWRPTFKYYNMWLSLLGAILCVAVMFLISWATALITFAAVLALYLIVAYRKPDVNWGSTTQAQTYKNALMSVQQLNNVEEHVKNYRPQILVLSGLPNTRPVLVDLAYMLTKNLSLLVCGHVLKGSSSQKYRTYLQERAGNWFRKHRVKGFYALVDGEDFESGTRALMQATGIGKLKPNIILMGYKTDWQTCDHKELDQYFNVMHKALDMYLSVAILRVPQGLDCSQVLGSQDGWKTVSDVPRTLQPNESSGDLQAVDSSVRNGLSGSIDSLSRNVSQASSTSDLSFIAGNQSKDVSGMPDPLDAKSANLVSNSLRKSKLKHDDPASLYKGPGGAELPKEVLADLTQFTRKRSHAVIDVWWLYDDGGLTLLLPYIISTRRTWQSCKLRVYALANKNSELEFEQRSMASLLSKFRIDYSDLTLIPDITKKPQETSTQFFNELIKDFVVTEKDGENGTSSRATLNEDDALITDDDLLAVQDKTNRYLRLREYLREQSTKSDLVVMTLPMPRKNIVSAPLYMAWLESLSRDMPPFLFVRGNQTSVLTFYS
Protein: Aminoaldehyde dehydrogenase 2, peroxisomal (PsAMADH2) (EC 1.2.1.-) (Aminobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.19) (Gamma-guanidinobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.54) (Q93YB2)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 3-aminopropanal to beta-alanine. Catalyzes the oxidation of 4-aminobutanal to 4-aminobutanoate. Catalyzes the oxidation of 4-guanidinobutanal to 4-guanidinobutanoate.
Subcellular location: Peroxisome {ECO:0000255}.
Interaction partners:
Sequence:
MDIPIPTRQLFINGDWKAPVLNKRIPVINPATQNIIGDIPAATKEDVDVAVAAAKTALTRNKGADWATASGAVRARYLRAIAAKVTEKKPELAKLESIDCGKPLDEAAWDIDDVAGCFEYYADLAEKLDARQKAPVSLPMDTFKSHVLREPIGVVGLITPWNYPMLMATWKVAPALAAGCAAILKPSELASLTCLELGEICKEVGLPPGVLNILTGLGPEAGAPLATHPDVDKVAFTGSSATGSKIMTAAAQLVKPVSLELGGKSPLVVFEDVDLDKAAEWAIFGCFWTNGQICSATSRLILHESIATEFLNRIVKWIKNIKISDPLEEGCRLGPVVSEGQYEKILKFVSNAKSEGATILTGGSRPEHLKKGFFIEPTIITDVTTNMQIWREEVFGPVLCVKTFSTEEEAIDLANDTVYGLGAAVISNDLERCERVTKAFKAGIVWVNCSQPCFTQAPWGGVKRSGFGRELGEWGLDNYLSVKQVTQYISEEPWGWYQPPAKL
Protein: Trehalose-6-phosphate phosphatase (C8VHC8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Alpha,alpha-trehalose-phosphate synthase
- Large subunit of trehalose 6-phosphate synthase
- Synthase subunit of trehalose-6-phosphate synthase/phosphatase complex
- Cytosolic neutral trehalase
Sequence:
MSLQQDPSKPDGRPGEVRFDSFTDASAPNVSSNFNNASKTASALSEADKGTQSGSDLLHRLSLKEILTMRAPDFQKQYQGLNLSGRIISAAFCIPHKLYFRAGRDWELKPRPGSSALFDSFAYLASEKSGWSHTLVGWTGEVEPLNEGSNPLQALNSNANTNLPAALDNTSRSLSKGSAPVVPDISLLQSNSSVAETSTVGPDDRKRLEDQLSSSRHGKVVPVWLSDESDVPEDTIILGDQSRWRRYAEKELYALLHYKQNGPTDGRFERDSWTDYVRMNQLFAERILQEYKEGDIVWIHDYHLFLLPSILRQHVPNIYIGFYLHSPFPSSEYMRCLAKRKEILTGVLGANMIGFQTFSYSRHFSSCCTRVLGFESDSAGVDAYGAHVAVDVFPIGIDAEAIQKIAFENADTEKAVEGLRQLYAGKKIIVGRDRLDSARGVAQKLQAFETFLERFPEWRDKVVLIQVTSPTSVEEEKEEQKIASRISNLVSTINGRFGSLSFSPVKYYPQYLSPHEYFALLRVADVGLITTVRDGMNTTSLEYILCQQENHSPLILSEFSGTAGALSSAIHINPWDTIGVSEAINKALTESVADKKEQHLKLYKHVTTNTVSAWSNQFISRLLANLSSFDQSMATPALDRTKLLKQYRKSRKRLFMFDYDGTLTPIVKDPQSAIPSDRVLRTLKTLAADPRNAVWIISGRDQAFLDEWMGHIPELGLSAEHGCFIRMPRSDNWQNLAETTDMGWQKEVMEIYQHFTERTQGSFIERKKVALTWHYRRADPEYGAFQARECRKQLEEHVSKTWDVEVMAGKANLEVRPRFVNKGFIATRLVQAYEDGKVPEFILCSGDDFTDEDMFRALKKFELPGDHVYTVTVGASSKQTEASWHLLEPSDVIETITMLNNSASGQDY
Protein: TNF receptor-associated factor 6-A (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6-A) (Q3MV19)
Organism: Xenopus laevis (African clawed frog)
Function: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet {ECO:0000250|UniProtKB:P70196}.
Interaction partners:
Sequence:
MSILNPRTSLEAGDSEDACCAAMASVCCINTKEDADSPSAGLPSGTTQNLDVEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACILKSLRNAGHKCPVDNEILMEKQLFPDNFAKREILSLRVKCPNLGCTDTMELRHLEHHLVQCQFASVECSQCQGSFLKLLLDKHMEHECGRRRTFCDNCGLAMAYEDKSGHELICPMAYVTCDYCQTNLIREQMPAHYSMDCTMAPIPCMYCEFGCREKMQRHNLAGHLQDFTQAHMRMMAQTLRSFSTTPTSHISDISFCDPNQFEPVPLSVAPAHPSHMPSQQDCSQETRNLRETVEQLEGRLVRQDHQIRELIAKMETQCTYVNELKHTIHSLEDKVADMDAHRCNGVFIWRIKGFSGLQKSQEEEKPVVIHSPGFYTGDPGYKLCLRLHLQLPSAQRCANYISLFVHTMQGDYDSLLPWPLQGTIRLSILDQSESTARQDQVEVMDTKPDLLAFQRPTAPRNPKGFGYVTFMHLNTLKQRQYVKNDTLLVRCSVNIHLDLTSPRREGFQPRSGEGTL
Protein: Chordin-like 2 (Chordin-like protein) (B4XEZ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKKRMTCLKHFFILVTMRCFVQGETEALRPGKNVFCTFKEKTYRPGDSWHPYLEPFGFMFCMRCTCTEPGLVKCNSIKCPSLRCENPVTNSQQCCPRCADEHRTPAGLRAPIKTCRYNGSIYQTGETFANHELFPTRQSNQCVMCTCSNGNIFCALKSCQPITCSSPVPVPDTCCLVCKESAIDINSALFEDGGQQLNRGARHSVDQCAADQVRGRSVRATPSTLRGSPRGLNLQTLHLKGASETTVKILLQRKHQRACVYSGKTYSHGDVWHPVLGKILECILCTCRDGFQECKRVTCPNQYPCQHPIKIEGKCCKICPELKPESNKSECYLAQDNNSLLVYKFEPSSGTQTEDKVRMIAIERQGATEVEVQVWKTVEGVLHLMETGDVKKKDLIENPEQYILLTTLDEDTWRKFKEDEDKQKDLSKIRSCEDGIKEVVKYLNPEQLDSLCTS
Protein: D-proline reductase proprotein PrdA (EC 1.21.4.1) [Cleaved into: D-proline reductase subunit beta (D-proline reductase 45 kDa subunit); D-proline reductase subunit alpha (D-proline reductase 23 kDa subunit)] (Q9Z4P6)
Organism: Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii)
Function: D-proline reductase catalyzes the reductive cleavage of a C-N bond in D-proline resulting in the formation of 5-aminovalerate. The alpha subunit has been shown to bind D-proline, presumably via the pyruvoyl group.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10085076}.
Interaction partners:
- D-proline reductase subunit gamma
- Proline racemase
- Electron transfer protein
- Uncharacterized protein
- 2,4-diaminopentanoate dehydrogenase
- Probable membrane transporter protein
- Proton-dependent oligopeptide transporter
Sequence:
MSITLESAKEHANDLAVLCCRAEEGTVIGPSNLEDPAIFGDLEDSGLLTIPANCLKIGEVLGAKLVKTADSLTPLTPELLEGVNSISEEAPKQEASAPVEAPVAEVAPAAMPVANVTGSMLKIHIGEGKDINLEIPLTIAGQMGVVAPTAAAPAGVAMPVASATEQVVAPAGEPKLVRTLQKKHFKIEKVEFGPETKIENNTIYIRENICEDAVKVSNLVTDIKVEIITPADYGKYSETIMDVQPIATKEGDGKIGQGVTRVIDGAIIMVTGTDEDGVQIGEFGSSEGELDANIMWGRPGAPDKGEILIKTQVTIKAGTNMERPGPLAAHKATDFITQEIREALKKLDDSEVVETEELAQYRRPGKKKVVIIKEIMGQGAMHDNLILPVEPVGVIGAKPNVDLGNVPVVLSPLEVLDGGIHALTCIGPASKENSRHYWREPLVIEVMNDEEFDLAGVVFVGSPQVNAEKFYVSERLGMLVETMDVEGAFITTEGFGNNHIDFASHHEQVGMRGIPVVGMSFCAVQGALVVGNKYMKYMVDNNKSEQGIENEILSNNTLCPEDAIRAVAMLKAAIAEEEVKVAERKFNKNVKENNVDLIEEQAGKEITLLPNEQVLPMSKKRKEIYEADK