wanglab/gogpt-training-data huggingface dataset:
Protein: AGAMOUS-like 102 (MADS-box protein AGL102) (T2E6.17) (Q9FZF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- AGAMOUS-like 78
- Agamous-like MADS-box protein AGL103
- Agamous-like MADS-box protein AGL49
- Agamous-like MADS-box protein AGL82
- AGAMOUS-like 83
- At5g26880
- MADS-box protein AGL73
- Methyl-CpG-binding domain-containing protein 13
Sequence:
MGRRKIEIKFIEDSIERKATFSRRRNGIFKKADELAKLCNVEIAVLVISPTNIPYTYGYPCFNDVVERIQNPSASSKLRSLMKELEQIKEFQEDLRKKQQRNLEKSNMKENVDLKLEDLVAFKAKLEAYQAGLKRKHVEMEDLSSPSILSKNTKNKMMRTEYSSGQSKGMYEFRAFGPGFLGTI
Protein: Putative corazonin receptor (Q8ITC8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MEDEWGSFDRLPSVPSASMDLETENEVVSNWSTLANFTRLVAGAAPEIVNYTLNMIDVGVGMATDISNLSVSTTPLPAYAISNSSSLAHTNSRHEAPPMAEQVPEHVMDHAPQLSRSGLLKVYVLAVMALFSLLGNLLTIWNIYKTRISRRNSRHTWSAIYSLMFHLSIADVLVTWFCIIGEAAWCYTVQWLANELTCKLVKLFQMFSLYLSTYVLVLIGVDRWIAVKYPMKSLNMAKRCHRLLGGTYILSLVLSLPQFFIFHVARGPFVEEFYQCVTHGFYTADWQEQMYATFTLVFTFLLPLCILFGTYMSTFRTISSSEKMFQGSKLANYSTAKLPTQTNRQRLIHKAKMKSLRISVVIIIAFLICWTPYYVMMIMFMFLNPDKRLGDDLQDAIFFFGMSNSLVNPLIYGAFHLCPGKGGKSSGGGGNNNAYSLNRGDSQRTPSILTAVTQVDGTGGSSRQMRAFRQQSYYRSSSNGTAGPGAAPFKEQVGLLHVGPGNGTPGGSVSSGATPQLIRKGSALLARQPSCLREQEHQQRLLLHEKPSTLVVSYDSQRGGVGVGVASGLLDNNERVSSV
Protein: Myosin heavy chain-like protein (F4IGF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DNA repair protein REV1
- DNA polymerase zeta processivity subunit
- Proliferating cell nuclear antigen 2
- Proliferating cellular nuclear antigen 1
- DNA polymerase zeta catalytic subunit
- Protein PLANT CADMIUM RESISTANCE 3
- Serine/threonine-protein kinase ATG1t
- DNA polymerase epsilon catalytic subunit B
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase delta catalytic subunit
Sequence:
MDLNLDENENLKARIKQLEHERNELQKDIEQLCMQQGGPSILGVAARMHFQRTASLEQEIESLKLKLAACTREKHNLQEELAEAYRVKAQLADLHAGEVAKNLEAEKQVRFFQGSVAAAFSERDKSVMEAEKAEENAEMMSQKLSEIEMRLEELSSDCLVQKRLNDTLQADLAKLEEQTRTYAGVIEKFYDIRKASLCESLEMSLHEKCASLLDDPIESWTFNDPSTSDYVAALEGELGKVKNTVDNLQSKLRVGLEIENHLKKRVRALEKKNIVADGLIVNGITDIRHHHSQLRAYIIALLNEEGLYIKSISKNVEEKLKLHSSEVQNVVPPQHDLKPDESECRDVHMTTVVESCQVTKLAEASIAKIMAESRGDASEAFAQALQEKVGALLLLSQQEERHLHEENVNAALQQKVDELQRNILQVTNEKVRTLMELAQLRQEYQSLREHGTFCKWCKPSFKTNFALSSVLNKMSGTREEESTGNSGRIVISNEKDGRLKNMWKKSYINRWIDPSSRGGSHLNTEADYASNIEYSRMKVEYAAIKENLESMGHLTTSIRRLRLALLKVKELNDTETTARSCEVAIANILVEATHLKTALGISIPISWSAESDIESVTDGESSCERTDSVSAAGFEMVELVILAAEIMKEQHH
Protein: Pentraxin family member (A7E2J1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362112}.
Interaction partners:
Sequence:
MLGFLFTLLNLTPAATEVGLGGKVLLFPTQTATSYVKLTPDKPLSLSAFTLCMRVATELQGGREVILFAYRTSEVDELNVWREKDGRLFMYIQSSSDGARFYLPPLSTFQTHLCVSWESATGLTALWVDGRRSLYQIYKKDASVRPGGTVLLGQDPDSYVGSFDANQCFIGEITDVKLWDYVLSEIQIKALYSNQDPLVPAGNVFDWNTVKYDVVGNVTVANDNL
Protein: Olfactory receptor 4E2 (Odorant receptor 244-3) (Odorant receptor 83) (Olfactory receptor 1509) (Q7TQQ0)
Organism: Mus musculus (Mouse)
Function: Olfactory receptor that is activated by the binding of organosulfur odorants with thioether groups such as (methylthio)methanethiol (MTMT) and bis(methylthiomethyl) disulfide. Also binds odorants cis-cyclooctene and tert-butyl mercaptan. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (Potential).
Subcellular location: Cell membrane {ECO:0000255, ECO:0000255|RuleBase:RU363047, ECO:0000269|PubMed:22328155, ECO:0000269|PubMed:27019154, ECO:0000269|PubMed:29659735, ECO:0000305|PubMed:25185561, ECO:0000305|PubMed:25901328}; Multi-pass membrane protein {ECO:0000255, ECO:0000255|RuleBase:RU363047, ECO:0000269|PubMed:27019154}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MGALNQTRVTEFIFLGLTDNWVLEILFFVPFTVTYMLTLLGNFLIVVTIVFTPRLHNPMYFFLSNLSFIDICHSSVTVPKMLEGLLLERKTISFDNCIAQLFFLHLFACSEIFLLTIMAYDRYVAICIPLHYSNVMNMKVCVQLVFALWLGGTIHSLVQTFLTIRLPYCGPNIIDSYFCDVPPVIKLACTDTYLTGILIVSNSGTISLVCFLALVTSYTVILFSLRKQSAEGRRKALSTCSAHFMVVALFFGPCIFLYTRPDSSFSIDKVVSVFYTVVTPLLNPLIYTLRNEEVKTAMKHLRQRRICS
Protein: FAS-associated factor 1 (P54731)
Organism: Mus musculus (Mouse)
Function: Ubiquitin-binding protein (By similarity). Required for the progression of DNA replication forks by targeting DNA replication licensing factor CDT1 for degradation (By similarity). Potentiates but cannot initiate FAS-induced apoptosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UNN5}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Nuclear protein localization protein 4 homolog
- UBX domain-containing protein 7
- UBX domain-containing protein 1
- Tumor necrosis factor receptor superfamily member 6
- UBX domain-containing protein 6
- FAS-associated death domain protein
- NSFL1 cofactor p47
- UBX domain-containing protein 2B
Sequence:
MASNMDREMILADFQACTGIENIDEAITLLEQNNWDLVAAINGVIPQENGILQSDFGGETMPGPTFDPASHPAPASTPSSSAFRPVMPSRQIVERQPRMLDFRVEYRDRNVDVVLEDSCTVGEIKQILENELQIPVPKMLLKGWKTGDVEDSTVLKSLHLPKNNSLYVLTPDLPPPSSSSHAGALQESLNQNFMLIITHREVQREYNLNFSGSSTVQEVKRNVYDLTSIPVRHQLWEGWPASATDDSMCLAESGLSYPCHRLTVGRRTSPVQTREQSEEQSTDVHMVSDSDGDDFEDASEFGVDDGEVFGMASSTLRKSPMMPENAENEGDALLQFTAEFSSRYGDCHPVFFIGSLEAAFQEAFYVKARDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDTNRARFLTMCNRHFGSVIAQTIRTQKTDQFPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIFSAQQQEDIKDEDEREARENVKREQDEAYRLSLEADRAKREAHEREMAEQFRLEQIRKEQEEEREAIRLSLEQALPPEPKEENAEPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEFKLLSTFPRRDVTQLDPNKSLLEVNLFPQETLFLQAKE
Protein: Proline-rich protein PRCC (Papillary renal cell carcinoma translocation-associated gene protein) (Q92733)
Organism: Homo sapiens (Human)
Function: May regulate cell cycle progression through interaction with MAD2L2.
Subcellular location: Nucleus {ECO:0000269|PubMed:11717438}.
Interaction partners:
- Tether containing UBX domain for GLUT4
- Transcription factor E3
- Crooked neck-like protein 1
- Zinc finger protein 830
- Pre-mRNA-splicing factor SYF1
- SNW domain-containing protein 1
- RING-type E3 ubiquitin-protein ligase PPIL2
- RNA-binding protein 10
- Mitotic spindle assembly checkpoint protein MAD2B
- Clathrin heavy chain 1
Sequence:
MSLVAYASSDESEPDEAEPEPEEEEAVAPTSGPALGGLFASLPAPKGPALLPPPPQMLAPAFPPPLLLPPPTGDPRLQPPPPLPFGLGGFPPPPGVSPAEAAGVGEGLGLGLPSPRGPGLNLPPPIGGAGPPLGLPKPKKRKEPVKIAAPELHKGDSDSEEDEPTKKKTILQGSSEGTGLSALLPQPKNLTVKETNRLLLPHAFSRKPSDGSPDTKPSRLASKTKTSSLAPVVGTTTTTPSPSAIKAAAKSAALQVTKQITQEEDDSDEEVAPENFFSLPEKAEPPGVEPYPYPIPTVPEELPPGTEPEPAFQDDAANAPLEFKMAAGSSGAPWMPKPGDDYSYNQFSTYGDANAAGAYYQDYYSGGYYPAQDPALVPPQEIAPDASFIDDEAFKRLQGKRNRGREEINFVEIKGDDQLSGAQQWMTKSLTEEKTMKSFSKKKGEQPTGQQRRKHQITYLIHQAKERELELKNTWSENKLSRRQTQAKYGF
Protein: Ubiquitin carboxyl-terminal hydrolase 17 (USP17) (EC 3.4.19.12) (Deubiquitinating enzyme 17-like protein 2) (Deubiquitinating protein 3) (DUB-3) (Ubiquitin carboxyl-terminal hydrolase 17-like protein 2) (Ubiquitin thioesterase 17-like protein 2) (Ubiquitin-specific-processing protease 17-like protein 2) (Q6R6M4)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Regulates cell proliferation by deubiquitinating and inhibiting RCE1 thereby controlling the small GTPases NRAS and HRAS localization and activation. In parallel, mediates deubiquitination of CDC25A, preventing CDC25A degradation by the proteasome during the G1/S and G2/M phases promoting cell-cycle progression. Also regulates cell proliferation and apoptosis through deubiquitination of SUDS3 a regulator of histone deacetylation. Through activation of the Rho family GTPases RAC1A, CDC42 and RHOA, regulates cell migration. Through the cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains of the cytoplasmic innate immune receptors RIGI and IFIH1 stimulates the cellular response to viral infection.
Subcellular location: Nucleus {ECO:0000269|PubMed:21239494}. Endoplasmic reticulum {ECO:0000269|PubMed:19188362}.
Interaction partners:
- Zinc finger-containing ubiquitin peptidase 1
- CAAX prenyl protease 2
- Sin3 histone deacetylase corepressor complex component SDS3
- Zinc finger protein SNAI1
- Ubiquitin carboxyl-terminal hydrolase 17-like protein 24
- M-phase inducer phosphatase 1
Sequence:
MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSSEARVDLCDDLAPVARQLAPRKKLPLSSRRPAAVGAGLQNMGNTCYENASLQCLTYTPPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKLAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQEGQWYKMDDAKVTACSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDERLVERATQESTLDHWKFPQEQNKTKPEFNVRKVEGTLPPNVLVIHQSKYKCGMKNHHPEQQSSLLNLSSTTRTDQESVNTGTLASLQGRTRRSKGKNKHSKRALLVCQ
Protein: Tegument protein UL16 (I3TC73)
Organism: Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1)
Interaction partners:
Sequence:
MAPASGVCPPPAPGMAQLGPRRPLAPPGPPGTLPRPDSRAGARGTRDRVDDLGTDVDSIARIVNSVFVWRVVRADERLKIFRCLTVLTEPLCQVALPNPDPGRALFCEIFLYLTRPKALRLPPNTFFALFFFNRERRYCAIVHLRSVTHPLTPLLCTLTFARIRAATPPEETPDPTTEQLAEEPVVGELDGAYLVPAKTPPEPGACCALGPGAWWHLPSGQIYCWAMDSDLGSLCPPGSRARHLGWLLARITNHPGGCESCAPPPHIDSANALWLSSVVTESCPCVAPCLWAKMAQCTLAVQGDASLCPLLFGHPVDTVTLLQAPRRPCITDRLQEVVGGRCGADNIPPTSAGWRLCVFSSYISRLFATSCPTVARAVARASSSDPE
Protein: Mitochondrial ribosome-associated GTPase 1 (GTP-binding protein 7) (Mitochondrial GTPase 1) (Q9BT17)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity. Displays mitochondrial GTPase activity.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:12808030, ECO:0000269|PubMed:23396448}; Peripheral membrane protein {ECO:0000269|PubMed:12808030, ECO:0000269|PubMed:23396448}; Matrix side {ECO:0000269|PubMed:12808030, ECO:0000269|PubMed:23396448}.
Interaction partners:
- Mitochondrial assembly of ribosomal large subunit protein 1
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL24m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL17m
- Mitochondrial ribosome-associated GTPase 2
Sequence:
MRLTPRALCSAAQAAWRENFPLCGRDVARWFPGHMAKGLKKMQSSLKLVDCIIEVHDARIPLSGRNPLFQETLGLKPHLLVLNKMDLADLTEQQKIMQHLEGEGLKNVIFTNCVKDENVKQIIPMVTELIGRSHRYHRKENLEYCIMVIGVPNVGKSSLINSLRRQHLRKGKATRVGGEPGITRAVMSKIQVSERPLMFLLDTPGVLAPRIESVETGLKLALCGTVLDHLVGEETMADYLLYTLNKHQRFGYVQHYGLGSACDNVERVLKSVAVKLGKTQKVKVLTGTGNVNIIQPNYPAAARDFLQTFRRGLLGSVMLDLDVLRGHPPAETLP
Protein: Solute carrier family 2, facilitated glucose transporter member 12 (Glucose transporter type 12) (GLUT-12) (Q8TD20)
Organism: Homo sapiens (Human)
Function: Insulin-independent facilitative glucose transporter.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11832379}. Note=Localizes primarily perinuclear region in the absence of insulin. {ECO:0000269|PubMed:11832379}.
Interaction partners:
- Major facilitator superfamily
Sequence:
MVPVENTEGPSLLNQKGTAVETEGSGSRHPPWARGCGMFTFLSSVTAAVSGLLVGYELGIISGALLQIKTLLALSCHEQEMVVSSLVIGALLASLTGGVLIDRYGRRTAIILSSCLLGLGSLVLILSLSYTVLIVGRIAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVIGILSAYISNYAFANVFHGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEGAASKVLGRLRALSDTTEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAASLASTGVGVVKVISTIPATLLVDHVGSKTFLCIGSSVMAASLVTMGIVNLNIHMNFTHICRSHNSINQSLDESVIYGPGNLSTNNNTLRDHFKGISSHSRSSLMPLRNDVDKRGETTSASLLNAGLSHTEYQIVTDPGDVPAFLKWLSLASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTDLIGLPWVCFIYTIMSLASLLFVVMFIPETKGCSLEQISMELAKVNYVKNNICFMSHHQEELVPKQPQKRKPQEQLLECNKLCGRGQSRQLSPET
Protein: Lipoxygenase homology domain-containing protein 1 (C8YR32)
Organism: Mus musculus (Mouse)
Function: Required for normal function of hair cells in the inner ear.
Subcellular location: Cell projection, stereocilium {ECO:0000269|PubMed:19732867}.
Interaction partners:
- Stereocilin
- Myosin-IIIa
- Cytosolic carboxypeptidase 4
- Cell adhesion molecule CEACAM16
- Solute carrier family 4 member 11
- Unconventional myosin-XV
- E3 ubiquitin-protein ligase ARK2C
Sequence:
MMAQKKKRRKKDIDFLGLYEEELLNYDSEDGEDELEHEYYKAKVYEVVTATGDVRGAGTDANVFITLFGENGLSPKLHLTSKSESAFEKANVDVFRVRTNNVGLIYKIRIEHDNTGLNASWYLDRVIVTDMKRPHLRYYFNCNNWLSKVEGDRQWCRDLLASFDPMDMPRGNKYEIKVYTGDVIGAGTDADVFINIFGEYGDTGERRLENEKDNFEKGAEDKFTLDAPDLGQLMKINVGHNNKGGSAGWFLSKIIIEDIGNKRKYDFPLNRWLALDEDDGKIQRDILVGGAETTAITYIVTVFTGDIRGAGTKSKIYLVMYGARGNKNSGKIFLEGGVFDRGRTDIFHIDLAVLLSPLSRVSIGHGNIGVNRGWYCEKVVILCPFTGIQQTFPCSNWLDEKKADGLIERQLYEMVSLRKKRLKKYPWSLWVWTTDLKKAGTNSPIFIQIYGKKGRTDEILLNPNNKWFKPGIIEKFRMELPDLGRFYKIRAWHDRQNPGSGWHLEKMTLMNTINKDKYNFNCNRWLDANEDDNEIVREMTAEGPTVRRIMGMARYRVTVCTGELEGAGTDANVYLCLFGDVGDTGERLLYNCRNNTDLFEKGNADEFTIESVTMRKVRRVRVRHDGKGSGSGWYLDRVLVREEGQPESDNVEFPCLRWLDKDKDDGQLVRELLPSDSNATLKNFRYHISVKTGDVSGASTDSRVYIKLYGEKSDTIKQVLLVSDNNLKDYFERGRVDEFTLETLNIGTINRLVIGHDSTGMHAGWFLGSVQIRVPRQGKQYTFPANRWLDKNQADGRLEVELYPSEVVEIQKLVHYEIEIWTGDVGGAGTTSRVFVQIYGEEGKTEVLFLSSRSKVFDRGSKDIFQTDTFTIYAIDLGALTKIRIRHDNTGNRPGWFLDRVDITDVNNETTYYFPCQRWLAVEEDDGQLSRELLPVDESYVLPSEDEEGGGQGDNNPLDNLALEQKDKSTTFSVTIKTGDKKNAGTDANVFITLFGTQDNNGMTLLKSSKTNSDKFERDSIEIFTVETLDLGDLWKVRIGHDNTGKAPGWFVDWVEVDAPSLGKCMTFPCGRWLAKNEDDGSIVRDLFHAELQTRLYTPFVPYEITLYTSDVFAAGTDANIFIVIYGCDAVCTRQKFLCTNKREQKLFFERKSASRFIVELEDVGEIIEKIRIGHDNTGINPGWHCSHVDIRRLLPEKDGTETLTFPCDRWLATSEDDKKTIRELVPYDIFTEKYMKDGSLRQVYKEVEEPLDIVLYSVQIFTGNVPGAGTDAKVYITIYGDLGDTGERYLGKSENRTNKFEKGTADTFIIEAADLGVIYKIKLRHDNTKWCADWYVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLFYEKEYTGDRSSNCSSPADFWEIALSSKMADVDIDTVTGPMVDYVQDGPVIPYYVSVTTGKHKEAATDSRAFVLLIGEDDECTNRIWLDYPQGKRGFSCGSVEEFYVGGLDVGIIKKIELGHDGASPESCWLVEELCLAVPTQGTKYTLRCNCWLAKDRGDGVTSRVFDLLDAMVVNIGKKVLYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEVQLDKKKARFEREQNDTFIMEILDIAPFTKMRIRIDGMGSRPEWFLERILLKNMNTGDLTMFYYGDWLSQKKGKKTLVCEICAVIDGEEMMEWTSYTVSVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFSDMLSLGHLCKLRVWHDNKGIFPGWHLSYVDVKDNSRDETFRFQCDCWLSKSEGDRQTLRDFACANNEIRDELEETTYEIVIETGNGGETRENVWLILEGRKNRSKEFLVENSSRQRAFRKGTTDTFEFDSIFLGDIASLCVGHLAREDRFIPKRELVWHVKTITITEMEYGNVYFFNCDCLIPLKRKRKYFKVFEVTKTTESFASKIQSLVPVKYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKMRNLFERGSTDRFFLETLELGELRKVRLEHDSSGYYSGWLVEKVEVTNTSTGVATIFSCGRWLDKSRGDGLTWRELFPSV
Protein: Pyruvate dehydrogenase E1 component subunit alpha (EC 1.2.4.1) (Q5B2R8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Acetyltransferase component of pyruvate dehydrogenase complex
- Pyruvate dehydrogenase E1 component subunit beta
- 3-methyl-2-oxobutanoate dehydrogenase
- Probable mitochondrial E3-binding protein of the pyruvate dehydrogenase complex
- Pyruvate kinase
- Pyruvate carboxylase
- Glucose-6-phosphate isomerase
- Malic enzyme
- Malic enzyme
- Glucose-6-phosphate 1-dehydrogenase
Sequence:
MLFRTAWARQAAPLRRQAFAPLARRSVTTDAASSHAENIPEDENKPFTVRLSDESFETYEIDPPPYTLEVTKKELKQMYYDMVAMRRMEMAADRLYKEKKIRGFCHLSTGQEAVAVGIEHALTREDKIITAYRCHGYAMMRGGTIRSIIGELLGRREGIAYGKGGSMHMFAPNFYGGNGIVGAQVPVGAGLAFAQQYNEEKSTSVVLYGDGASNQGQVFEAFNMAKLWNLPVLFGCENNKYGMGTSAARSSALTDYYKRGQYIPGIKVNGMDVLATKAAVKYGKDYAISGNGPLVYEYVTYRYGGHSMSDPGTTYRSREEIQRMRSTQDPIQGLKQKILDWGVMSEEDLKGLDKSARAHVDEEVAIAEKMPLPENNSRILFEDIYVRGSEPRWMRGRTVDETFYY
Protein: Rho GTPase activating protein 45 (K7ES98)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLGRRLGARASYSPYRAGRQGPQQRGRDPGIQLTELPRKDGADAVFPGPSLEPPAGSSGVKATGTLKRPTSLSRHASAAGFPLSGAASWTLGRSHRSPLTAASPGELPTEGAGPDVVEDISHLLADVARFAEGLEKLKECVLRDDLLEARRPRAHECLGEALRVMHQIISKYPLLNTVETLTAAGTLIAKVKAFHYESNNDLEKQEFEKALETIAVAFSSTVSEFLMGEVDSSTLLAVPPGDSSQSMESLYGPGSEGTPPSLEDCDAGCLPAEEVDVLLQRCEGGVDAALLYAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHMPLLSIYSLALEQDLEFGHSMVQAVGTLQTQTFMQPLTLRRLEHEKRRKEIKEAWHRAQRKLQEAESNLRKAKQGYVQRCEDHDKARFLVAKAEEEQAGSAPGAGSTATKTLDKRRRLEEEAKNKAEEAMATYRTCVADAKTQKQELEDTKVTALRQIQEVIRQSDQTIKSATISYYQMMHMQTAPLPVHFQMLCESSKLYDPGQQYASHVRQLQRDQEPDVHYDFEPHVSANAWSPVMRARKSSFNVSDVARPEAAGSPPEEGGCTEGTPAKDHRAGRGHQVHKSWPLSISDSDSGLDPGPGAGDFKKFERTSSSGTMSSTEELVDPDGGAGASAFEQADLNGMTPELPVAVPSGPFRHEGLSKAARTHRLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCGHKKLQGRLQLFGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHELVGLAKDSLKAEAEAKAASRGRQDGSESEAVAVALAGRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDYPHQARVIETLIVHYGLVFEEEPEETPGGQDESSNQRAEVVVQVPYLEAGEAVVYPLQEAAADGCRESRVVSNDSDSDLEEASELLSSSEASALGHLSFLEQQQSEASLEVASGSHSGSEEQLEATAREDGDGDEDGPAQQLSGFNTNQSNNVLQAPLPPMRLRGGRMTLGSCRERQPEFV
Protein: Dual oxidase 2 (EC 1.11.1.-) (EC 1.6.3.1) (Large NOX 2) (Long NOX 2) (NADH/NADPH thyroid oxidase THOX2) (Thyroid oxidase 2) (Q9ES45)
Organism: Rattus norvegicus (Rat)
Function: Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q9NRD8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NRD8}. Cell junction {ECO:0000250|UniProtKB:Q9NRD8}. Note=Localizes to the apical membrane of epithelial cells. Localizes on internal membrane structures under resting conditions, translocates to the plasma membrane and cell-cell junctions upon challenge with enteric pathogens. {ECO:0000250|UniProtKB:Q9NRD8}.
Interaction partners:
- Dual oxidase maturation factor 2
- Dual oxidase maturation factor 1
- Cytochrome b-245 light chain
- Dual oxidase 1
- NADPH oxidase 1
- NADPH oxidase organizer 1
- NADPH oxidase activator 1
- Neutrophil cytosol factor 4
- Neutrophil cytosolic factor 1
- NADPH oxidase 3
Sequence:
MLPTSLKTLVLLGALLTGPLGPAGGQDAPSLPREVQRYDGWFNNLKYHQRGAAGSQLRRLVPANYADGVYQALQEPLLPNARLLSDAVSKGKAGLPSAHNRTVLGLFFGYHVLSDLVSVETPGCPAEFLNIYIPRGDPVFDPDKRGNVVLPFQRSRWDRSTGQSPSNPRDLTNQVTGWLDGSAIYGSSHSWSDTLRSFSGGQLASGPDPAFPRNSQNSLLMWMAPDPATGQGGPQGLYAFGAQRGNREPFLQALGLLWFRYHNLCAKRLAQEHPHWGDEELFQHARKRVIATYQNIALYQWLPSFLQKTPPEYSGYRPFMDPSISPEFVAASEQFLSTMVPPGVYMRNSSCHFREFPKEGSSSSPALRVCNNYWIRENPSLKTAQDVDQLLLGMASQISELEDRIVIEDLRDYWPGPDRYSRTDYVASSIQSGRDMGLPSYSQALQALGLEPPKNWSALNPKVDPQVLEATAALYNQDLSRLELFLGGLLESHGDPGPLFSNIILDQFVRLRDGDRYWFENTRNGLFSKEEIAEIRNTTLRDVLVAVSNVDPSALQPNVFFWQEGAPCPQPQQLTTEGLPQCVPVTVIDYFEGSGAGYGVTLLAVCCFPVVSLIIAWVVARFRNRERKMLLKKGKESLKKQTASDGVPAMEWPGPKESSYPVTVQLLPDRSLKVLDKRLTVLRTIQLQPTQQVNLILSSSHGRRTLLLKIPKEYDLVLMFNSEEDRDAFVQLLQDLCVCSTPGLRIAEMDEKELLRKAVTKQQRAGILEIFFRQLFAQVLDINQADAGTLPLDSSQQVREALTCELSRAEFADSLGLKPQDMFVESMFSLADKDGNGYISFREFLDILVVFMKGSPQDKSRLMFTMYDLDGNGFLSKEEFFTMMRSFIEISNNCLSKDQLAEVVESMFRESGFQDKEELTWEDFHFMLRDHDSDLRFTQLCVKGGAGGTGDIFKQSNACRVSFLTRTPGNRVMAPSPRLYTEALQEKMQRGFLAQKLKQFKRFVENYRRHIVCVTIFSAICAGLFADRAYYYGFASPPTDIEETTYVGIILSRGTAASISFMFSYILLTMCRNLITFLRETFLNRYIPFDAAVDFHRWIAMAAVVLAVVHSLGHAVNVYIFSVSPLSLMTCVFPSVFVNDGSKLPPKYYWWFFETVPGMTGVLLLLVLAIMYVFASHHFRRHSFRGFWLTHHLYVVLYALIIIHGSYALIQLPSFHIYFLVPAIIYVGDKLVSLSRKKVEISVVKVELLPSGVTYLQFQRPKTFEYKSGQWVRIACLSLGTNEYHPFTLTSAPHEDTLSLHIRAVGPWTTRLREIYSPPVGGTSARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSMGTQMLCKKIYFIWVTRTQRQFEWLADIIREVEENGSRDLVSVHIYITQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSVTHFGRPPFELFLDSLQEVHPQVHKIGVFSCGPPGMTKNVEKACQLINRQDRAHFVHHYENF
Protein: Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) (Q6FGX9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_03171}.
Interaction partners:
Sequence:
MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEIMEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDAGPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDSVFSQVCTHLDALK
Protein: Ubiquitin-like protein 4B (Q8N7F7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Testis-expressed protein 15
- Sodium-dependent neutral amino acid transporter SLC6A17
- Homeobox protein aristaless-like 3
- Large proline-rich protein BAG6
- Ribosomal protein uL16-like
Sequence:
MFLTVKLLLGQRCSLKVSGQESVATLKRLVSRRLKVPEEQQHLLFRGQLLEDDKHLSDYCIGPNASINVIMQPLEKMALKEAHQPQTQPLWHQLGLVLAKHFEPQDAKAVLQLLRQEHEERLQKISLEHLEQLAQYLLAEEPHVEPAGERELEAKARPQSSCDMEEKEEAAADQ
Protein: calcium/calmodulin-dependent protein kinase (EC 2.7.11.17) (Q4V9P8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Calmodulin
- Calmodulin-like protein 4
- Phosphoinositide phospholipase C.
- PH_14 domain-containing protein.
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Cytochrome b-245, beta polypeptide
- Ryanodine receptor 2b
- Receptor-interacting serine-threonine kinase 3.
- F-box only protein 43
Sequence:
MATIVTSTRFTDEYQLYEELGKGAFSVVRRCVKKSTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCISQILESVNHIHQHDIVHRDLKPENLLLASKMKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAEQALKHPWVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSACKSLLNKKADGVKHQTNNTKNSVVSAVVNAMKESNTASSTPMEPQTTVVHNPVDGPKGSTESCNTNEEEDMKGRKAESAQGASSDSAVMSQCSAGEEPPALVASPQGSPSTRKQEIIKITEQLIEAVNNGDFEAYTRICDPGLTSFEPEALGNLVEGMDFHKFYFEHLLSKNNKPVHTTILNPHVHLIGEDAACIAYIRLTQYIDGQGRPRSCQSEETRVWHRRDSKWLNVHFHCSGAPAAPLQ
Protein: Alpha-amylase A type-3 (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) (Taka-amylase A) (TAA) (P0C1B4)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0C1B3}.
Interaction partners:
- 1,4-alpha-glucan-branching enzyme
- Alpha-amylase A type-1/2
- Glucoamylase
Sequence:
MMVAWWSLFLYGLQVAAPALAATPADWRSQSIYFLLTDRFARTDGSTTATCNTADRKYCGGTWQGIIDKLDYIQGMGFTAIWITPVTAQLPQTTAYGDAYHGYWQQDIYSLNENYGTADDLKALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFCLIQNYEDQTQVEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSIDGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTCPYQNVMDGVLNYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPRFASYTNDIALAKNVAAFIILNDGIPIIYAGQEQHYAGGNDPANREATWLSGYPTDSELYKLIASANAIRNYAISKDTGFVTYKNWPIYKDDTTIAMRKGTDGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGNVPVPMAGGLPRVLYPTEKLAGSKICSSS
Protein: Lipid A palmitoyltransferase PagP (EC 2.3.1.251) (Lipid A acylation protein) (Q8XBR9)
Organism: Escherichia coli O157:H7
Function: Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00837}.
Interaction partners:
- Lipid A biosynthesis myristoyltransferase
- Lipid A biosynthesis myristoyltransferase
- Lipid A 1-diphosphate synthase
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Lipid A 1-diphosphate synthase
- Membrane-associated metal-dependent hydrolase
- Phosphoethanolamine transferase EptA
- Kdo
- Lipid A 3'-O-deacylase
Sequence:
MNVSKYVAIFSFVFIQLISVGKVFANADEWMTTFRENIVQTWQQPEHYDLYIPAITWHARFAYDKEKTDRYNERPWGGGFGLSRWDEKGNWHGLYAMAFKDSWNKWEPIAGYGWESTWRPLADENFHLGLGFTAGVTARDNWNYIPLPVLLPLASVGYGPVTFQMTYIPGTYNNGNVYFAWMRFQF