wanglab/gogpt-training-data huggingface dataset:
Protein: NEDD8-activating enzyme E1 regulatory subunit (Amyloid beta precursor protein-binding protein 1, 59 kDa) (APP-BP1) (Amyloid protein-binding protein 1) (Proto-oncogene protein 1) (Q13564)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14557245}. Note=Colocalizes with APP in lipid rafts.
Interaction partners:
- NEDD8-conjugating enzyme Ubc12
- Ubiquitin-like protein NEDD8
- NEDD8-activating enzyme E1 catalytic subunit
- Amyloid-beta precursor protein
- NEDD8-conjugating enzyme UBE2F
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- Cullin-4A
- Sentrin-specific protease 8
- DCN1-like protein 1
Sequence:
MAQLGKLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILKNENGAPEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEGQGNLPVRGTIPDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAEEYGLDTINKDEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL
Protein: TATA-box binding protein associated factor, RNA polymerase I subunit C (H3BR71)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XSSSWRWADFTAHPRVLTVGDRTGVKMLDTQGPPGCGLLLFRLGAEASCQKGERVLLTQYLGHSSPKCLPPTLHLVCTQFSLYLVDERLPLVPMLKWNHGLPSPLLLARLLPPPRPSCVQPLLLGGQGGQLQLLHLAGLAAVVPPLPSAPTPGLVLFQLSAAGDVFYQQLRPQVDSSLRRDAGPPGDTQPDCHAPTASWTSQDTAGCSQWLKALLKVPLAPPVWTAPTFTHRQMLGSTELRREEEEGQRLGVLRKAMARGQLLLQRDLGSLPAAEPPPAPESGLEDKLSERLGEAWAGRGAAWWERQQGRTSEPGRQTRRPKRRTQLSSSFSLSGHVDPSEDTSSPHSPEWPPADALPLPPTTPPSQELTPDACAQGVPS
Protein: RIM-binding protein, isoform G (A0A0B4JCX2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHLCEFPSANVEEENRRPEKAAAAASKKQKHKQQKSRPRGSHSMPYESMHHHQSAAAAVAAGTTPNGMLDALSLQLRDAEMRRTEIERAHQETLAQIRNLSGSARPDAEAVENLQSRARELEKKVALENVRCEELQIELTSALKAKQASRSACSGMGSVSSGGGATIPTSASSSTVTWAPTISHQDQGSEIDIIMAKIEQDNRVLAELEQPRTSASASMSALPPSSMLSTVNSEFRTISKSELEEELNRYKRAVLGGSGGGGGGVGGGGGGVSALSSGYSSLPQSLASTLPNGGASTSLSGTSLGSHSAAAAAAAHSVSAGSGGVVGGGGQGGLSSISALVPNSISGISSSLSSHAIQSMQYGTGQTSVEKLLSGTSGITGIPPLPVNIHTMKAMPTALSQRGTIQLYNLQSTTMPLLSLNSHNLPPAGSTSYSALGAGGGTSLTHPTMANLGLLDTGTLLGSTGLSGLGVGPSVGGITGATSLYGLSGGGGGAGGLGSSYGPPFLDVASSASYPFTAAALRQASKMKMLDEIDIPLTRYNRSSPCSPIPPNNWGLDEFTDGLSVSMMHNRGGLALGALDLDTRNHGLNGASEPQVDMLDIPGKGRCCVFIARFPYDPPDVHNEFLSMPCREAEGELSLCAGDYLLVWTSGEPQGGYLDAELLDGRRGLVPASFVQRLVGDDLLEFHQAVLSTLRDAEDGSMQCDTTSLPSLPPHNPLLTHTHEDLARLSETHTDLEHDQDDISDNVPAPKHLTLERQLNKSVLIGWSPPEPVGYNLIDSYHVYVDGVLKVTVKANERTRALIEGVDSTRPHRISVRSVTQNRQTSRDAACTMIIGRDTAHLGPSAVRASHITCSSAVISWLPANSNHQHVVCVNNVEVRTVKPGMYRHTITGLAPSTQYRVTVRAKHLRAVGQHAANVGQTGGAGRPGQEEAPGAYADFRTLTKGLPDPPQEIQLEAGPQDGTILVTWQPVNRPTSTGPVTGYAVYADGKKVTDINSPTGDHALIDIGKLGVFNPRAVTIRTKSRDSQSADSAPILIPNTVRNAVARRGPNQMGMGPQLPQGPHGMTVQQQMGGMPGQPGQQGQHMMGGQQDHGQYDPNQMQQQQQQQGQPGQPGHQGYQPGQPGAQRGMVPIPGRPQGPQQQQQQPYGPQGPMGGPRFRGPVPGQLNMQGQQMQGQMQGQMQGQMQGQMSGQMPGQMPGQMPGQMPGQMAGQMAGQMPGQMPGQMPGQMSGQMPGQMMGPRGPLNQQQQQQQQMQQGQMMPGQQAGQQQAQPGQPGQPGQMPGAQKKPRYFVAMFDYDPSTMSPNPDGCDEELPFQEGDTIKVFGDKDADGFYWGELRGRRGYVPHNMVSEVEDTTASMTAGGQMPGQMPGQMGQGQGVGVGGTAQVMPGQGAPQQSMRNVSRDRWGDIYANMPVKRMIALYDYDPQELSPNVDAEQVELCFKTGEIILVYGDMDEDGFYMGELDGVRGLVPSNFLADAPDQYNNQMGPGGVAGRGGLSQRGRGQGPGARGPPPPPRDNMMPGMGGRGQPGKNARPASPTLLDNTGHPAPDHQTQGMIGRVGNVGLQQQQQQQQQQQQLQQQQQYGQQQTQMGQQQQQQQQMGQPGMMGQQMGQPMGQQMGQMGQMGQMGQQQMGQQQMGQQQQPPTTQAQTGGLFSGATSLLSGATSAATGGLFGSKQPPKTDPMQPQGGVQPAQQQANAFGAQQPGMGMQQQGGMQSGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQPGMQQQQQQPQQVPPQAQAPPPGPGAGLLGGLKGIAAAAPGGDVLSKGKDLFGKFGFGFGK
Protein: RNA-binding protein 14 (RNA-binding motif protein 14) (Q8C2Q3)
Organism: Mus musculus (Mouse)
Function: May function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1 (By similarity). Regulates centriole biogenesis by suppressing the formation of aberrant centriolar protein complexes in the cytoplasm and thus preserving mitotic spindle integrity. Prevents the formation of the STIL-CENPJ complex (which can induce the formation of aberrant centriolar protein complexes) by interfering with the interaction of STIL with CENPJ (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96PK6}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96PK6}. Cytoplasm {ECO:0000250|UniProtKB:Q96PK6}. Note=In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Cytoplasmic localization is crucial for its function in suppressing the formation of aberrant centriolar protein complexes. {ECO:0000250|UniProtKB:Q96PK6}.
Interaction partners:
- Non-POU domain-containing octamer-binding protein
- Splicing factor, proline- and glutamine-rich
- Paraspeckle component 1
- Runt-related transcription factor 2
- Matrin-3
- Heterogeneous nuclear ribonucleoprotein K
- RNA-binding protein FUS
- X-ray repair cross-complementing protein 5
- U1 small nuclear ribonucleoprotein 70 kDa
Sequence:
MKIFVGNVDGADTTPEELAALFAPYGTVMSCAVMKQFAFVHMRENAGAVRAIEALHGHELRPGRALVVEMSRPRPLNTWKIFVGNVSAACTSQELRSLFERRGRVIECDVVKDYAFVHMEKEADAKAAIAQLNGKEVKGKRINVELSTKGQKKGPALAIQSGDKTKKPGAGDTAFPGTGGFSATFDYQQAFGNSTGGFDGQARQPTPPFFGRDRSPLRRSPPRASYVAPLTAQPATYRAQPSVSLGAAYRAQPSASLGVGYRTQPMAAQAASYRAQPSVSLGAPYRGQLASPSSQSAAASSLGPYGGVQPSASALSTYGGQAAAASSLNSYGAQGSSLASYGNQPSSYGAQAASSYGVRAAASSYNTQGAASSLGSYGAQAASYGAQSAASSLAYGAQAASYSAQPSASYSAQSAPYAAQQAASYSSQPAAYVAQPATAAAYASQPAAYAAQATTPMAGSYGAQPVVQTQLNSYGAQASIGLSGSYGAQSAAAATGSYGAAAAYGAQPSATLAAPYRTQSSASLAASYAAQQHPQAAASYRGQPGSAYDGTGQPSAAYLSMSQGAVANANSTPPPYERTRLSPPRASYDDPYKKAVAMSKRYGSDRRLAELSDYRRLSESQLSFRRSPTKSSLDYRRLPDAHSDYARYSGSYNDYLRAAQMHSGYQRRM
Protein: Protein LEG1 homolog (Q6P5S2)
Organism: Homo sapiens (Human)
Function: May be involved in early liver development.
Subcellular location: Secreted {ECO:0000250|UniProtKB:A5PF61, ECO:0000250|UniProtKB:Q4QRF7}.
Interaction partners:
- BPI fold-containing family B member 1
Sequence:
MAFLPSWVCVLVGSFSASLAGTSNLSETEPPLWKESPGQLSDYRVENSMYIINPWVYLERMGMYKIILNQTARYFAKFAPDNEQNILWGLPLQYGWQYRTGRLADPTRRTNCGYESGDHMCISVDSWWADLNYFLSSLPFLAAVDSGVMGISSDQVRLLPPPKNERKFCYDVSSCRSSFPETMNKWNTFYQYLQSPFSKFDDLLKYLWAAHTSTLADNIKSFEDRYDYYSKAEAHFERSWVLAVDHLAAVLFPTTLIRSYKFQKGMPPRILLNTDVAPFISDFTAFQNVVLVLLNMLDNVDKSIGYLCTEKSNVYRDHSESSSRSYGNNS
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FK29)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- GTP-binding protein RHO1
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MPNKHSISPSRHMPFWKNFVNNPKSVSSENLSTPSRPVYQRGHSYNHTAPKTGSPIKNEVGAAERQDFRDYRDQFLSGRNGFSGRVFGVSLEESLSVASAEVIVQSELVSFGRIPIVVAKCGAYLKSNGLSTSGVFRIAGNSKRIKELQYIFSTPPDYGAKFSNWEPYTVHDVASLLRRYLNNLEEPLIPLALYEKFRAPLMNRPRILKYMLNNEVSHPNANKENTLTMKLTESTKQDTDDRANDGDNENEDEQHITEEEAKRKQLRRKKKLSRCIRAAIKEYEELFTDLLSDSKQLTIYLLDLLSLFARQSQLNLMSGSNLAAIFQPSILSHPQHDLDPKEYELSRLVVEFLIEYTYKLLPHLLKSTKDDQQKKISESVHQKSTTESTTNRDKTSSPLPNIQIQTETTTIKGTPDNSKTTSTATSQQNNIHSKPEAKSPALQVPKYQRPHSRSIGSAPMVPDVIASNKRRSRLFPWLHKPGILSDTGDTATDGEGDDLLNDDENVDPHLSSPVHSSNHRQHLLSIPKVQRSVSGRSITSNSSGRPLSLILNRSEDNLPKNGSSSTEKFERPRSPIAYSQESIESKAKKRESWFARLTSRN
Protein: Intraflagellar transport protein 46 (Flagellar-associated protein 32) (IFT complex B protein) (A2T2X4)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. Plays a role in maintaining IFT complex B stability.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199, ECO:0000269|PubMed:19412537}. Cell projection, cilium {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199, ECO:0000269|PubMed:19412537}. Note=Expression is concentrated at the cilium basal body but is also detected along the length of the cilium. {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199, ECO:0000269|PubMed:19412537}.
Interaction partners:
Sequence:
MDDSMDYPDRDGDDLDQFQGTARSQVVQNQPHDEEVNLSESESFAGADEPPAAPRDASLIESHDMDEGPAAPARTLSPTGYEAGKHAPGGIANSDEAPPGAYNAQEYKHLNVGEDVRELFSYIGRYKPQTVELDTRIKPFIPDYIPAVGGIDEFIKVPRPDTKPDYLGLKVLDEPAAKQSDPTVLTLQLRQLSKEAPGAKADMVGRLEHTDENKAKKIQQWIASINDIHKAKPAATVNYSKRMPEIEALMQEWPPEVETFLKTMHMPSGDVELDIKTYARLVCTLLDIPVYDDPVESLHVLFTLYLEFKNNPIFRQHMEMENKLDGMSGGGGGMMGGGADVLGL
Protein: Opine/polyamine ABC transporter, permease protein (Q5LPZ6)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}.
Interaction partners:
- Opine/polyamine ABC transporter, permease protein
- Polyamine ABC transporter, permease protein
- Opine/polyamine ABC transporter, ATP-binding protein
- Opine/polyamine ABC transporter, periplasmic substrate-binding protein
- Putrescine ABC transporter, permease protein
- Spermidine/putrescine import ATP-binding protein PotA
- Spermidine/putrescine transport system permease protein PotC
- Spermidine/putrescine ABC transporter, permease protein
- Polyamine ABC trasnporter, periplasmic polyamine-binding protein
- Polyamine ABC transporter, permease protein
Sequence:
MVGAALRNTDMNAVARHIHPGWAIIAPLLVLVVALYLGPILNIMWLSVTDPEPGLGNYRMLYESDSLLRIVWTTLRICVITTVFSVTLGYSIAYAMVHCHQRQKNYMLTLLLVSFWISILVRTFSWLMLLGRSGLINNTLETLGLVSAPIAFMRNELGVLIGMVHYMIPYAVLPLLVSMQSLDSRVMDASRNLGASGSQTFWRIYLPLTLPGIVASTLLVFILSLGFYVTPAVLGGGKVLMVAEYISVQLLVTLKWGTAAMLAALMLAGVLAMLWIMSRFMKLSAVFGGSTR
Protein: Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) (Q55EZ0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
Sequence:
MGDNNNNNNNEIREDENEPIPPFKCPEWASKPISNVYLEIIKNGVNIDRVDISKDKFTVFGRSSEVASVLLDHPSVSRRHAALVYHGANNRFYLIDLQSATGTQVNDEQVKPLTPTTVKENFTFKFGSSSKHFILKGTVNTNPSSSSSSSSSSSSEPKTVTCRHLLVKHQGSRNPSSWRESKITRTKERAIAKLNEYRATIISGSATFEDLAHKNSDCSSAKRGGYLDPFKRGQMQRPFEDCAFSLKVGEVSGIVDTDSGVHIIERLA
Protein: Methenyltetrahydromethanopterin cyclohydrolase (EC 3.5.4.27) (Methenyl-H4MPT cyclohydrolase) (P51616)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+).
Subcellular location: Cytoplasm.
Interaction partners:
- Formylmethanofuran--tetrahydromethanopterin formyltransferase
- Formylmethanofuran--tetrahydromethanopterin formyltransferase-like protein
- F420-dependent methylenetetrahydromethanopterin dehydrogenase
- Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C
- Tungsten formylmethanofuran dehydrogenase, subunit A
- 5,10-methenyltetrahydromethanopterin hydrogenase
- Putative thymidylate synthase
- Methionine synthase
- DUF1894 domain-containing protein
- DUF1890 domain-containing protein
Sequence:
MVSVNIEAKKIVDRMIEGADDLKISVDKLENGSTVIDCGVNVDGSIKAGELYTAVCLGGLADVGISIPGDLSERFALPSVKIKTDFPAISTLGAQKAGWSVSVGDFFALGSGPARALALKPAETYEEIGYQDEADIAVLTLEADKLPGEDVTDKIAEECDVSPENVYVLVAPTSSLVGSIQISGRVVENGTYKMLEALHFDVNKVKYAAGIAPIAPVDPDSLKAMGKTNDAVLFGGRTYYYIESEEGDDIKSLAENLPSSASEGYGKPFYDVFKEADYDFYKIDKGMFAPAEVVINDLRTGEVFRAGFVNEELLMKSFGL
Protein: CD226 antigen (DNAX accessory molecule 1) (DNAM-1) (CD antigen CD226) (Q15762)
Organism: Homo sapiens (Human)
Function: Involved in intercellular adhesion, lymphocyte signaling, cytotoxicity and lymphokine secretion mediated by cytotoxic T-lymphocyte (CTL) and NK cell. Cell surface receptor for NECTIN2. Upon ligand binding, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Competes with PVRIG for NECTIN2-binding.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15684041}; Single-pass type I membrane protein {ECO:0000305}. Note=Localizes to lipid rafts. {ECO:0000269|PubMed:15684041}.
Interaction partners:
- Poliovirus receptor
- Nectin-2
- Nectin-1
- T-cell immunoreceptor with Ig and ITIM domains
- Integrin beta-2
- Integrin alpha-L
- Natural cytotoxicity triggering receptor 3
- NKG2-D type II integral membrane protein
- Natural cytotoxicity triggering receptor 1
- UL16-binding protein 1
Sequence:
MDYPTLLLALLHVYRALCEEVLWHTSVPFAENMSLECVYPSMGILTQVEWFKIGTQQDSIAIFSPTHGMVIRKPYAERVYFLNSTMASNNMTLFFRNASEDDVGYYSCSLYTYPQGTWQKVIQVVQSDSFEAAVPSNSHIVSEPGKNVTLTCQPQMTWPVQAVRWEKIQPRQIDLLTYCNLVHGRNFTSKFPRQIVSNCSHGRWSVIVIPDVTVSDSGLYRCYLQASAGENETFVMRLTVAEGKTDNQYTLFVAGGTVLLLLFVISITTIIVIFLNRRRRRERRDLFTESWDTQKAPNNYRSPISTSQPTNQSMDDTREDIYVNYPTFSRRPKTRV
Protein: Rabaptin, RAB GTPase binding effector protein 2 (H3BNR2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
METMKAVAEVSESTKAEAVAAVQRQCQEEVASLQAILKDSISSYEAQITALKQERQQQQQDCEEKERELGRLKQLLSRAYPLDSLEKQMEKAHEDSEKLREIVLPMEKEIEELKAKLLRAEELIQEIQRRPRHAPSLHGSTELLPLSRDPSPPLEPLEELSGDGGPAAEAFAHNCDDSASISSFSLGGGVGSSSSLPQSRQGLSPEQEETASLVSTGTLVPEGIYLPPPGYQLVPDTQWEQLQTE
Protein: Probable purine permease 13 (AtPUP13) (Q8RY83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDEEEAMLLLKEEDEGTRRTSVPTQLMKLKRTHWWILVFISIFFLISAQAIAVLLGRFYYNEGGNSKWISTLVQTCGFPILYLPLCFLPASHSSSSSCSFKTLVWIYLSLGFAIGLDNLLYSFGLLYLSASTYSILCSSQLAFNGVFSYYINSQKITCLILFSVLFLSVSAVLVSLDDDSNSPSGDSKWSYLIGCLCTVFASLIYSLQLSLMQFSFENVLKSETFSMVLEMQIYTSLVASCVAVIGLFASGEWMLLSVEMEEFHEGQVIYVLTLVGTAVSWQLGSVGAVALIFLVSSLFSNLIGTLSLIVTPLAAIAVFHDKLTEVKMVAMLIAFMGFGFYIYQNYLDDLKVQRAREAQAE
Protein: RASD family member 3 (Zgc:152698) (Q0V963)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004193}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}.
Interaction partners:
Sequence:
MSLLVQERRTVRFVFLGAAGVGKTALITRFLQDRFDSKYTRTVEELHALEYDTEGARVRIEILDTSGSYSFPAMRALCIRTGDAFALVYAADEPDSLEEVQRLREEILELKGESFTGITVIENKADLCSRSRQATAEAMRAVEEDWGAGFVETSARTGDNVTAVFRDLLQQMKLPSRVSPALRRRTQTMSRELTEKREKPPMKKNNSCILS
Protein: SET domain containing 5 (E7EWN3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSIAIPLGVTTSDTSYSDMAAGSDPESVEASPAVNEKSVYSTHNYGTTQRHGCRGLPYADHNYGAPPPPTPPASPPVQTIIPRSDLNGLPSPVEERCGDSPNSEGETVPTWCPCGLSQDGFLLNCDKCRGMSRGKVIRLHRRKQDNISGGDSSATESWDEELSPSTVLYTATQHTPTSITLTVRRTKPKKRKKSPEKGRAAPKTKKIKNSPSEAQNLDENTTEGWENRIRLWTDQYEEAFTNQYSADVQNALEQHLHSSKEFVGKPTILDTINKTELACNNTVIGSQMQLQLGRVTRVQKHRKILRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKKPYPFVLFYSKFNGVEMCVDARTFGNDARFIRRSCTPNAEVRHMIADGMIHLCIYAVSAITKDAEVTIAFDYEYSNCNYKVDCACHKGNRNCPIQKRNPNATELPLLPPPPSLPTIGAETRRRKARRKELEMEQQNEASEENNDQQSQEVPEKVTVSSDHEEVDNPEEKPEEEKEEVIDDQENLAHSRRTREDRKVEAIMHAFENLEKRKKRRDQPLEQSNSDVEITTTTSETPVGEETKTEAPESEVSNSVSNVTIPSTPQSVGVNTRRSSQAGDIAAEKLVPKPPPAKPSRPRPKSRISRYRTSSAQRLKRQKQANAQQAELSQAALEEGGSNSLVTPTEAGSLDSSGENRPLTGSDPTVVSITGSHVNRAASKYPKTKKYLVTEWLNDKAEKQECPVECPLRITTDPTVLATTLNMLPGLIHSPLICTTPKHYIRFGSPFIPERRRRPLLPDGTFSSCKKRWIKQALEEGMTQTSSVPQETRTQHLYQSNENSSSSSICKDNADLLSPLKKWKSRYLMEQNVTKLLRPLSPVTPPPPNSGSKSPQLATPGSSHPGEEECRNGYSLMFSPVTSLTTASRCNTPLQFELCHRKDLDLAKVGYLDSNTNSCADRPSLLNSGHSDLAPHPSLGPTSETGFPSRSGDGHQTLVRNSDQAFRTEFNLMYAYSPLNAMPRADGLYRGSPLVGDRKPLHLDGGYCSPAEGFSSRYEHGLMKDLSRGSLSPGGERACEGVPSAPQNPPQRKKVSLLEYRKRKQEAKENSAGGGGDSAQSKSKSAGAGQGSSNSVSDTGAHGVQGSSARTPSSPHKKFSPSHSSMSHLEAVSPSDSRGTSSSHCRPQENISSRWMVPTSVERLREGGSIPKVLRSSVRVAQKGEPSPTWESNITEKDSDPADGEGPETLSSALSKGATVYSPSRYSYQLLQCDSPRTESQSLLQQSSSPFRGHPTQSPGYSYRTTALRPGNPPSHGSSESSLSSTSYSSPAHPVSTDSLAPFTGTPGYFSSQPHSGNSTGSNLPRRSCPSSAASPTLQGPSDSPTSDSVSQSSTGTLSSTSFPQNSRSSLPSDLRTISLPSAGQSAVYQASRVSAVSNSQHYPHRGSGGVHQYRLQPLQGSGVKTQTGLS
Protein: Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Polyadenylate-specific ribonuclease) (A0A8J8Y7Y5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDFLLFQFGLCAFKYDHANSKHVTKSFNFYVFPKPFSRSSPDVKFVCQSSSIDFLASQGFDFNKVFCSGIPYLNQEEERQLREQFDEKRSQANGAGALTKCPVTIPEDQKKFIDQVIEKIEGFLQREEKRTLELNPCTGFQRKLIYQTLSWKYPKGIHVETLETDKKERHIVISKVDEEERKRREQEKYAKEQEELNDAVGFSRVIHAIANSGKLVVGHNMLLDVMHTIHQFYCPLPVDLNEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFDPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSLLSPPKTCVSARSKLIEPFFNKGRDTLLHAALLQRLSSALHRVLLHPFRHVCVCDHHLPVAHGYHGAGASRLLRAPREGAGAAQAAEDSGSLLKPWHWLLDKYGLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVQIAVNTSKYAESYRIQTYAEYVGKKQESKQVKRKWTEDSWKEVDRKRPHVPGPCYHTNSFTAAGIVGKRTLSPDPREAGVVDRESEGISDPELEQTDYCADPLPEGRKKAKKLKRMKKEFSLAGSASDSPAVLFEVPDTW
Protein: Potassium channel subfamily K member 18 (TWIK-related individual potassium channel) (TWIK-related spinal cord potassium channel) (Q7Z418)
Organism: Homo sapiens (Human)
Function: Outward rectifying potassium channel. Produces rapidly activating outward rectifier K(+) currents. May function as background potassium channel that sets the resting membrane potential. Channel activity is directly activated by calcium signal. Activated by the G(q)-protein coupled receptor pathway. The calcium signal robustly activates the channel via calcineurin, whereas the anchoring of 14-3-3/YWHAH interferes with the return of the current to the resting state after activation. Inhibited also by arachidonic acid and other naturally occurring unsaturated free fatty acids. Channel activity is also enhanced by volatile anesthetics, such as isoflurane. Appears to be the primary target of hydroxy-alpha-sanshool, an ingredient of Schezuan pepper. May be involved in the somatosensory function with special respect to pain sensation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:20006580}; Multi-pass membrane protein {ECO:0000269|PubMed:20006580}.
Interaction partners:
- Keratin, type II cytoskeletal 2 oral
- Potassium channel subfamily K member 13
- Potassium channel subfamily K member 12
- Potassium channel subfamily K member 7
- Potassium channel subfamily K member 17 channel 4) channel 2)
- Sodium/potassium-transporting ATPase subunit alpha-2
- Potassium channel subfamily K member 3 channel 1)
- Potassium channel subfamily K member 10
- Sodium channel protein type 1 subunit alpha
- Potassium channel subfamily K member 1
Sequence:
MEVSGHPQARRCCPEALGKLFPGLCFLCFLVTYALVGAVVFSAIEDGQVLVAADDGEFEKFLEELCRILNCSETVVEDRKQDLQGHLQKVKPQWFNRTTHWSFLSSLFFCCTVFSTVGYGYIYPVTRLGKYLCMLYALFGIPLMFLVLTDTGDILATILSTSYNRFRKFPFFTRPLLSKWCPKSLFKKKPDPKPADEAVPQIIISAEELPGPKLGTCPSRPSCSMELFERSHALEKQNTLQLPPQAMERSNSCPELVLGRLSYSIISNLDEVGQQVERLDIPLPIIALIVFAYISCAAAILPFWETQLDFENAFYFCFVTLTTIGFGDTVLEHPNFFLFFSIYIIVGMEIVFIAFKLVQNRLIDIYKNVMLFFAKGKFYHLVKK
Protein: ATP synthase subunit alpha, mitochondrial (Q9XPJ9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
Subcellular location: Mitochondrion. Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- ATP synthase F
- ATP synthase subunit a
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase subunit 9, mitochondrial
- ATP synthase F
- V-type proton ATPase proteolipid subunit
- V-ATPase proteolipid subunit C-like domain-containing protein
- Centrosomal protein 148 kDa
Sequence:
MQLEKMLTEVNIERSKFNTYNVLLQYIKAVTQKYNLNKVSSKYGKVLFIKDGVVKVSGLSQIKIGEKVEFVGKNLYGMALNLEATSVGIVIFGEDTAIYEGVIVKRCEQNFAIKVDKTMLGRVVDVLGQPIDGLGELKDTKTTRVMSVERKAPGIVTRKSVHESMLTGVKIVDALLPIGRGQRELIIGDRQTGKSAIAVDAILNQQVNKDIVCIYVAVGQKKSTVRRLVEMLNTKGALEYTIVVVSTASDAAPLQFLAPYTGCTIGEYFRDEGKHALIVYDDLSKHAVAYRQMSLLLRRPPGREAYPGDVFYIHSRLLERAAKLNEKYGCGSLTAFPIVETQAGDVSAYIPTNIISITDGQIFLEKELFNKGIRPAVNVGLSVSRVGSAAQSAVMKKLAGALKLELAQYRELARFEQFSSNADAVTTQILKKGKLTIELLKQVNNNPMSIGLEALMIYAMGTSYFQNLDLSLVRSEETKLLNYINSIASFKLYAACVDAVKAFNPKDTVFAEMCQSYVK
Protein: Cytosolic acyl coenzyme A thioester hydrolase (EC 3.1.2.2) (Acyl-CoA thioesterase 7) (Brain acyl-CoA hydrolase) (BACH) (hBACH) (CTE-IIa) (CTE-II) (Long chain acyl-CoA thioester hydrolase) (O00154)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18. May play an important physiological function in brain.
Subcellular location: [Isoform 4]: Cytoplasm, cytosol {ECO:0000305|PubMed:12435388}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytosol {ECO:0000305|PubMed:12435388}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:12435388}.; SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion {ECO:0000269|PubMed:12435388}.
Interaction partners:
- Acyl-coenzyme A thioesterase 1
- Acyl-coenzyme A thioesterase 2, mitochondrial
- Peroxisomal succinyl-coenzyme A thioesterase
- Acyl-coenzyme A thioesterase THEM5
- Acyl-coenzyme A thioesterase THEM4
- Very-long-chain enoyl-CoA reductase
- Acyl-coenzyme A thioesterase 13
- Glyceraldehyde-3-phosphate dehydrogenase
Sequence:
MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVVYSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHAEPQP
Protein: LD19086p (Q95RN4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMWYPPRMLPVPRRRPLWHPRFQKNLPVRHQRKSPPALKKAAVPRRTPPPWPLKFRRNPPLRHRRKAPPTLRMVAVLRIPLRLRKKPPPRSLKNPPARLPKNPPARRPKNPPQRSPKNRQPRRL