wanglab/gogpt-training-data huggingface dataset:
Protein: G-protein coupled receptors family 1 profile domain-containing protein (Serotonin receptor) (O17470)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha
- G-protein coupled receptors family 1 profile domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- Serotonin-gated chloride channel mod-1
- Biopterin-dependent aromatic amino acid hydroxylase family profile domain-containing protein
- Transporter
- Guanine nucleotide-binding protein G
Sequence:
MLIELFSHSAPPEDPYYVPANESFATTALTPHFSTTSVWSIRVQLIPTMGIYHFNGVALFLLPVLCLIGLIGNFLVCVAIATDRRLHNVTNYFLFSLALADLLVCCIVMPLSIVVEVRHGVWTWSVSMCLLYVYSDVFLCSASIVHMSVISLDRYLGISQPLRTRNRSKTLIFIKIAIVWVVTLLVSCPIAVLAMHDTANILRNNQCMIFSRYYIIYGSTMTFLIPLCIMGVTYAKTTQLLNKQASILSQKAGDKFNGNGLRRTMPHRKLGYARTYSATVNGTIANGKAIGAHGRTMSSISNIANGETADRLGTSRPSINTNGHKQLQKASTINKWKSRTSNLVTNFANKVGRRSSLQTATQDLANEHKATRVLAVVFACFFICWTPFFFINFLIGFGGENVQIPDWVASIFLWLGYVSSTINPIIYTVFNKRFRQAFVRILRCQCFHPLRDSHQMYSRNFTTTIVPDTYTCSRSNQERTTSVITRDETRSARSSERPEPSRARSEISEEPVARTNGKLTSEKKKISLPSFPRVSSSRDSRATTEASTTDEETKPLIPKSTVPATVINIPEQLINPIKKSLTTIINMPLLDETIPEKAQVHHKSQTLLTSSTLNFATFSTCPQQPTRSYSCVDCKKAEKMLSSDVSDMMTTSTASTASTVNGAPRKHLTLFNHFDSAIKETFL
Protein: UDP-glycosyltransferase 71C2 (EC 2.4.1.-) (O82382)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses low quercetin 3-O-glucosyltransferase, 7-O-glucosyltransferase and 3'-O-glucosyltransferase activities in vitro. Glucosylates other secondary metabolites in vitro like vanillin, trans-resveratrol, curumin and etoposide.
Interaction partners:
- Mucin-like protein
- Hydroxyproline-rich glycoprotein family protein
- soluble epoxide hydrolase
- F-box/kelch-repeat protein At1g55270
- Uncharacterized GPI-anchored protein At5g19250
- Bifunctional TENA-E protein
- At2g29210/F16P2.41
Sequence:
MAKQQEAELIFIPFPIPGHILATIELAKRLISHQPSRIHTITILHWSLPFLPQSDTIAFLKSLIETESRIRLITLPDVQNPPPMELFVKASESYILEYVKKMVPLVRNALSTLLSSRDESDSVHVAGLVLDFFCVPLIDVGNEFNLPSYIFLTCSASFLGMMKYLLERNRETKPELNRSSDEETISVPGFVNSVPVKVLPPGLFTTESYEAWVEMAERFPEAKGILVNSFESLERNAFDYFDRRPDNYPPVYPIGPILCSNDRPNLDLSERDRILKWLDDQPESSVVFLCFGSLKSLAASQIKEIAQALELVGIRFLWSIRTDPKEYASPNEILPDGFMNRVMGLGLVCGWAPQVEILAHKAIGGFVSHCGWNSILESLRFGVPIATWPMYAEQQLNAFTIVKELGLALEMRLDYVSEYGEIVKADEIAGAVRSLMDGEDVPRRKLKEIAEAGKEAVMDGGSSFVAVKRFIDGL
Protein: Glutamate--cysteine ligase catalytic subunit (EC 6.3.2.2) (GCS heavy chain) (Gamma-ECS) (Gamma-glutamylcysteine synthetase) (P19468)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the ATP-dependent ligation of L-glutamate and L-cysteine and participates in the first and rate-limiting step in glutathione biosynthesis.
Interaction partners:
- Glutamate--cysteine ligase regulatory subunit
- Glutathione synthetase
- 5-oxoprolinase
- Glutathione hydrolase 6
- Aminopeptidase N
- Glutathione hydrolase 7
- NAD
- Glutathione hydrolase 5 proenzyme
- Gamma-glutamylcyclotransferase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
Sequence:
MGLLSQGSPLSWEETQRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDHENRKVQLLLNGGDVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTVEDNMRKRRKEATSVLGEHQALCTITSFPRLGCPGFTLPEHRPNPEEGGASKSLFFPDEAINKHPRFGTLTRNIRHRRGEKVVINVPIFKDKNTPSPFVETFPEDEEASKASKPDHIYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLEPLKNNRFKISKSRYDSIDSYLSKCGEKYNDIDLTIDTEIYEQLLEEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDIGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQERDAVLQGMFYFRKDICKGGNAVVDGCSKAQTSSEPSAEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEINYSLILKCNQIANELCECPELLGSGFRKAKYSGGKSDPSD
Protein: ALG-1 INteracting protein (Q17740)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein argonaute-1
- Protein argonaute-1
- RING-type E3 ubiquitin transferase
- ALG-1
- ATP-dependent RNA helicase cgh-1
- Hyaluronan/mRNA-binding protein domain-containing protein
- Endoribonuclease dcr-1
- m7GpppN-mRNA hydrolase dcap-2
- Protein LSM14 homolog car-1
- Protein lin-41
Sequence:
MESLAKNFNNISIDDAAWHPNDQQPVWGNNGLQQQRVWAPPVPQPQFPNRSPWQQESNDIEPNVNEALVGLSGTGSSSQSQWGGIQNTDYEKQIWGDPPLSDVQYPLQPHASFGELNSLGGQSAPWSIGSQPAHPVWSNGGMGKESDDFWKQQQPQQHQQYPMPLLQGAWNTGMRHGPPGQGQRSGPMMQQQQDYQGGWGGPNNMGGNKQMNRPWGQDSNRGMSGMPPRNGRPNHNQGRYSGNMGGGVDVSVPPPMDMHMGGGMGGMRNMGVAPNSGHGSWKNNNAGGGQGGHGGQRNYNNRGGMGHSGSQSGGGSNMWNSTGNNGSGGSMQQFMGGDQQYNNPFPIGGAADDLTLTVWHDPNGELKKWQRDTGVSYWGDPEKQTDRTISLWIVGEGADEDLETALNRCPVPQKKGEDNQRFPFPVPAKRPIVVTGWGELPENDPNNPSKSESTIFDENNRWNDLTTEQNPWYLPNQHTSTFSSDNTTGSWVQGGTIPLNEPGTNQHVAVAEMLKNAVDKGYLDQSVTMMANLPPMVLQYVNMLLVKIPALDSVENELKQIIESSLPEDVKEVDPQNQQKYMNDSQKLEHNRLIIEVTTAKIEVQEYSKKVNRALMDAGIVQPQEQRAPASTEDYHYSFLE
Protein: Chorismate pyruvate-lyase (EC 4.1.3.40) (4-HB synthase) (p-hydroxybenzoic acid synthase) (P9WIC5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Removes the pyruvyl group from chorismate to provide 4-hydroxybenzoate (4HB). Involved in the synthesis of glycosylated p-hydroxybenzoic acid methyl esters (p-HBADs) and phenolic glycolipids (PGL) that play important roles in the pathogenesis of mycobacterial infections.
Interaction partners:
- p-hydroxybenzoic acid--AMP ligase FadD22
- 4-hydroxyphenylalkanoate adenylyltransferase
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks15
- Putative isochorismate synthase MenF
- Rhamnosyl O-methyltransferase
- PGL/p-HBAD biosynthesis glycosyltransferase Rv2958c
- Intracellular chorismate mutase
- Secreted chorismate mutase
- Anthranilate synthase component 1
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks1
Sequence:
MTECFLSDQEIRKLNRDLRILIAANGTLTRVLNIVADDEVIVQIVKQRIHDVSPKLSEFEQLGQVGVGRVLQRYIILKGRNSEHLFVAAESLIAIDRLPAAIITRLTQTNDPLGEVMAASHIETFKEEAKVWVGDLPGWLALHGYQNSRKRAVARRYRVISGGQPIMVVTEHFLRSVFRDAPHEEPDRWQFSNAITLAR
Protein: Scopoletin glucosyltransferase (EC 2.4.1.128) (Phenylpropanoid:glucosyltransferase 1) (Q9AT54)
Organism: Nicotiana tabacum (Common tobacco)
Function: Glucosyltransferase acting preferentially on aromatic substrates of the phenylpropanoid types. The best substrates are scopoletin and esculetin. Required for full resistance to virus.
Interaction partners:
Sequence:
MGQLHFFFFPVMAHGHMIPTLDMAKLFASRGVKATIITTPLNEFVFSKAIQRNKHLGIEIEIRLIKFPAVENGLPEECERLDQIPSDEKLPNFFKAVAMMQEPLEQLIEECRPDCLISDMFLPWTTDTAAKFNIPRIVFHGTSFFALCVENSVRLNKPFKNVSSDSETFVVPDLPHEIKLTRTQVSPFERSGEETAMTRMIKTVRESDSKSYGVVFNSFYELETDYVEHYTKVLGRRAWAIGPLSMCNRDIEDKAERGKKSSIDKHECLKWLDSKKPSSVVYVCFGSVANFTASQLHELAMGIEASGQEFIWVVRTELDNEDWLPEGFEERTKEKGLIIRGWAPQVLILDHESVGAFVTHCGWNSTLEGVSGGVPMVTWPVFAEQFFNEKLVTEVLKTGAGVGSIQWKRSASEGVKREAIAKAIKRVMVSEEADGFRNRAKAYKEMARKAIEEGGSSYTGLTTLLEDISTYSSTGH
Protein: Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR8 (EC 3.1.3.95) (Myotubularin-related protein 6) (Myotubularin-related protein 8) (Phosphatidylinositol-3-phosphate phosphatase) (Q6TEL0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Phosphatase that acts on lipids with a phosphoinositol headgroup (By similarity). Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate (By similarity).
Subcellular location: Nucleus envelope {ECO:0000250|UniProtKB:Q96EF0}.
Interaction partners:
- Myotubularin-related protein 9
- 1-phosphatidylinositol 3-phosphate 5-kinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase.
- Myotubularin-related protein 14
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3-A
- Phosphatidylinositide phosphatase SAC2
- Phosphatidylinositol 4-kinase, catalytic, alpha a
- Phosphatidylinositol 4-kinase beta
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
Sequence:
MEHIITPKVENVKLLNRYTEKKSALGTLYLTATHLIYVEQTSNTRKETWVLHHHILSVEKLLLTASGCPLLIRCKTFQHLHLLFQKERDCQDVYQSLLRLFQPVKEEELYAFLYNPHQNEEERRRGWELISVVNDFNRMGLSNDYWEISHINKNFEMCSTYPSILGLPKSASVATVTGSAKFRSRGRLPVLSYYHKDTKAAICRCSQPLSGLNSRCVEDEQMLQAISQANPNSPFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIRFQFQGIENIHVMRSSLQKLLEVCSMKSPSMSDYLTGLENSGWLRHIKSVMDAGVFLAKAVCEERASVLVHCSDGWDRTAQVCSLACLLLDPYYRTIKGLMVLIEKEWISFGHKFSHRCGHLDSDPKEASPVFTQFLECVWQLSQQFPCVFEFNEHYLIEIHDQVYACQYGNFIGNCQKERLDMRLHEKTFSLWPHLLENQHQYRNPLYRRSLESTVLRPSTLPLHFKFWCGMYNHYDRGMHPKQSVLDTLLTLTQRQVEGERTMTELQRQLAVADGVLPDPAGPINTHADQNNQSEKMPAPPVVQSNGSCAPLINGNVKEVGPGAENSNQEDREEPAANEHDLSSKDKPVFVETEHSKEEVQESS
Protein: Dehydrodolichyl diphosphate synthase complex subunit RER2 (DEDOL-PP synthase) (EC 2.5.1.87) (Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)) (P35196)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11442630}; Peripheral membrane protein {ECO:0000269|PubMed:11442630}.
Interaction partners:
- Dehydrodolichyl diphosphate synthase complex subunit NUS1
- Farnesyl pyrophosphate synthase
- Dolichol kinase
- Dolichol-phosphate mannosyltransferase
- Hexaprenyl pyrophosphate synthase, mitochondrial
- Geranylgeranyl pyrophosphate synthase BTS1
- Dehydrodolichyl diphosphate synthase complex subunit SRT1-farnesyl diphosphate specific))
- Dolichyldiphosphatase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein farnesyltransferase subunit beta
Sequence:
METDSGIPGHSFVLKWTKNIFSRTLRASNCVPRHVGFIMDGNRRFARKKEMDVKEGHEAGFVSMSRILELCYEAGVDTATVFAFSIENFKRSSREVESLMTLARERIRQITERGELACKYGVRIKIIGDLSLLDKSLLEDVRVAVETTKNNKRATLNICFPYTGREEILHAMKETIVQHKKGAAIDESTLESHLYTAGVPPLDLLIRTSGVSRLSDFLIWQASSKGVRIELLDCLWPEFGPIRMAWILLKFSFHKSFLNKEYRLEEGDYDEETNGDPIDLKEKKLN
Protein: 60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (HSP-65) (Heat shock protein 60) (HSP-60) (Hsp60) (Mitochondrial matrix protein P1) (P63038)
Organism: Mus musculus (Mouse)
Function: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P10809}.
Interaction partners:
- Toll-like receptor 4
- 10 kDa heat shock protein, mitochondrial
- Stress-70 protein, mitochondrial
- Toll-like receptor 2
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- 10 kDa heat shock protein, mitochondrial
- Heat shock 70 kDa protein 1B
- Endoplasmic reticulum chaperone BiP
- T-complex protein 1 subunit alpha
Sequence:
MLRLPTVLRQMRPVSRALAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLNLNLEDVQAHDLGKVGEVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDPGMGAMGGMGGGMGGGMF
Protein: ArfGAP with dual PH domains 1 (H7C324)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
YFNRNDAKEPKAVMKIEHLNATFQPAKIGHPHGLQVTYLKDNSTRNIFIYHEDGKTCLSYKIRIFIKIAPSERKASWPRPQQHQGHREIVDWFNALRAARFHYLQVAFPGAGDADLVPKLSRNYLKEGYMEKTGPKQTEGFRKRWFTMDDRRLMYFKDPLDAFARGEVFIGSKESGYTVLHGFPPSTQGHHWPHGITIVTPDRKFLFACETESDQREWVAAFQKAVDRPMLPQEYAVEAHFKHKP
Protein: Translation initiation factor eIF2B subunit gamma (eIF2B GDP-GTP exchange factor subunit gamma) (Q9GQ88)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MTEFRAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFSEVIVVVLEQEKLEIQSALENTPLKLRLDYATIPSDGDFGTADSLRYIYDKIKSDFLVVSCDLVSNVSLYPLINKFREHDAALAMLLFPSGFESDVVMPGPKSKHKPERDLIGIHAATQRLAFVSAASDCEETLNIQRHLLKNRGRLDVYSRLVDAHVYVLKKWVIDYLRRKENISTFKGEFLPHLIKKQHSKRPPKTVQDTTSEVGVVTKNEDHVLHYVGHTILDQKITQTSLFNQSLSQSPYHGDIVRCYGIQAPRDAIGVRVNNTLSFLAINRKLASIWNNLCGEKHPLISPGAVVKSTQTKEIIAADNAKLSEKTSLNFSVFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGTHSQAVHLSNADQFMEIDIQ
Protein: Elongation factor Tu (EF-Tu) (EC 3.6.5.3) (P74227)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
Interaction partners:
- Elongation factor Ts
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL16
Sequence:
MARAKFERTKDHVNIGTIGHVDHGKTTLTAAITMTLAELGGAKARKYEDIDAAPEEKARGITINTAHVEYETDSRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPKLVVFLNKKDMVDDEELLELVELEVRELLSDYDFPGDDIPIVAGSALKAIEGEKEYKDAILELMKAVDDYIDTPEREVDKPFLMAVEDVFSITGRGTVATGRIERGKVKVGEEISIVGIKDTRKATVTGVEMFQKTLEEGMAGDNVGLLLRGIQKEDIERGMVLAKPGSITPHTEFEGEVYVLKKEEGGRHTPFFANYRPQFYVRTTDVTGTIKSYTADDGSAVEMVMPGDRIKMTVELINPIAIEQGMRFAIREGGRTIGAGVVSKILK
Protein: GID complex subunit 1 (Glucose-induced degradation protein 1) (Vacuolar import and degradation protein 30) (P53076)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1).
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- GID complex subunit 5
- GID complex substrate-recognition subunit 4
- GID complex subunit 9
- GID complex subunit 7
- GID complex subunit 8
- E3 ubiquitin-protein ligase RMD5
- GID complex substrate-recognition subunit 10
- GID complex associated protein 12
- Fructose-1,6-bisphosphatase
- Protein yippee-like MOH1
Sequence:
MSEYMDDVDREFINCLFPSYLLQQPVAYDLWILYLQHRKLFHKLKNTNLINADENPTGVGMGRTKLTALTRKEIWSKLMNLGVLGTISFEAVNDDYLIQVYKYFYPDVNDFTLRFGVKDSNKNSVRVMKASSDMRKNAQELLEPVLSEREMALNSNTSLENDRNDDDDDDDDDDDDDDDDDDDDDESDLESLEGEVDTDTDDNNEGDGSDNHEEGGEEGSRGADADVSSAQQRAERVADPWIYQRSRSAINIETESRNLWDTSDKNSGLQYYPPDQSPSSSFSSPRVSSGNDKNDNEATNVLSNSGSKKKNSMIPDIYKILGYFLPSRWQAQPNNSLQLSQDGITHLQPNPDYHSYMTYERSSASSASTRNRLRTSFENSGKVDFAVTWANKSLPDNKLTIFYYEIKVLSVTSTESAENSNIVIGYKLVENELMEATTKKSVSRSSVAGSSSSLGGSNNMSSNRVPSTSFTMEGTQRRDYIYEGGVSAMSLNVDGSINKCQKYGFDLNVFGYCGFDGLITNSTEQSKEYAKPFGRDDVIGCGINFIDGSIFFTKNGIHLGNAFTDLNDLEFVPYVALRPGNSIKTNFGLNEDFVFDIIGYQDKWKSLAYEHICRGRQMDVSIEEFDSDESEEDETENGPEENKSTNVNEDLMDIDQEDGAAGNKDTKKLNDEKDNNLKFLLGEDNRFIDGKLVRPDVNNINNLSVDDGSLPNTLNVMINDYLIHEGLVDVAKGFLKDLQKDAVNVNGQHSESKDVIRHNERQIMKEERMVKIRQELRYLINKGQISKCINYIDNEIPDLLKNNLELVFELKLANYLVMIKKSSSKDDDEIENLILKGQELSNEFIYDTKIPQSLRDRFSGQLSNVSALLAYSNPLVEAPKEISGYLSDEYLQERLFQVSNNTILTFLHKDSECALENVISNTRAMLSTLLEYNAFGSTNSSDPRYYKAINFDEDVLNL
Protein: RALY RNA binding protein like (E5RJ39)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTMYKSKRRHQRYINMAGEPKPYRPKPGNKRPLSALYRLESKEPFLSVGLFDYHGRVPPPPRAVIPLKRPRVAVTTTRRGKGVFSMKGGSRSTASGSTGSKLKSDELQTIKKELTQIKTKIDSLLGRLEKIEKQQKAEAVSTDKVI
Protein: LD29482p (Q95TR0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKGFDPFKPLSINTSALESSASTSSTSATTTVKKQSVLYESLQQHPLAKYHQTQQQTTTTTTVDGQTSSRMELHKATLANATIDPVPVGSSTAAIVDSASGSGNVVRRYKPLSSSSFDEGKPMRRISYLRATNNETDFNAEAAAGGDAAATGASGPASASAASSAPGPTPSSAPAPAPAPAPLPISIPIPVAAVVEPQKTKSLVEEHPDPTYDVIGGTGGGHEFIETPNGLEDVRLSAHGSRRASMSSDMRSSIHIDAELNGKYVPNELEAFETEIEIKSSCINGKRMSEYRSWRQVKLEIKGDLLRIYSGRHAKSEHNVIELDIRNFKFFDESMDKKKYLIRMQSKPSPSGAHLASLGNELNLDEGHDKLLTSSGSSSANEPAANAASALTASTSSSTCSSGPYTEILFKTKSSNEMKRLFGLLQWKDSLNYDDNEHQPQGKQLAEPQKTVASASYLDDVQGGASAADSSPLSSHSGGIADASGSHHVSALPAAAAIVAATSDSISPVMKARKSSSHKHIPDKDLGSPKSKNWKDLLFRRGGSGSGGVSHHDLASPSACAAKQIGSIGVPLRSCPMSKVNAYVPHLVEVCTNIVETKGLGVVGIYRIPGNKAAISELSELVNTKDFQFESCASDDRWEDVNVVSSLLKLFIRSLPDALMPASYYINFIEADKKFGLERIVLLREIVESLPRHPYETMKHLIRHLCRVSGNCDVNRMEPKNLAIIFGPSIIRTPNDTLETAVKDMKHQCRIVELLVTQYDYFFEGGSLPDIAEVSGGTAAVSAAQPQQQTQEDQTSMLLHNLSKIERITERETTRTSRFMPQLRRKTHGKRSAVNSDTYSGESVLVSGSSSNTTTTTTTTTHTTSSTSSSNTITTTISTTTIQQRRAQRKAVQSICDQALILLLPTPVSSVSLPFQSLDYAKASASASASASSTASTSSSSTLHSGGKASASSSSSSTTKFSSSSSSACSTTAVAISSSISATSSKLLSANFKKRSTGGFLGSRSSHQTRKASLDEKDSGQSSGSLGHSLGVGINLAKEQQRSSVDISILLTDDDSSSRLSDTGSMSLTTITDTLDSKLRNLRSGSESNDENGSPEFPKNRRHTLGQPLHMHSENIPYADESPERLFHQFCNPLETAPLSLHLSRSCTATNTIGGDEKPSKQSGGVAPLPPSLLKAAHKLQHSATVPIHQGSSTAPTSGAATPVGTPTGSGGAGAIPSRSSSSSVTTLTKSIQPRFSNYLSYERGNAAAGGAERVVGSAGGAASDDDSEGSTTSDPKEKLLLGERPSPSFFIERYNKKRRDHRLFRSASFNCRNYSTRHITAQTSGGVAAGVSGGVAGAVAVGVACCQALSTTGLTKDEKTDMNLTKKRQIQNKQNRSIKRRHTVGGPHDYSASNGGCSNHSHGHDLAAINYNHHNRHHQQQLLKLGSATSGGGGSGAAAAETTTTTTTTTTVLRRLGTGQAGAEASVALPASSSGSSSNNNNSPQSDGSNGNGGGVAGVASNAPPTGVGVGGNNSSGSSSNSSSTSTTPAGNGDQVLEVGIRIKNISRGRF
Protein: Sp185/333 (Q3LS93)
Organism: Strongylocentrotus purpuratus (Purple sea urchin)
Interaction partners:
Sequence:
MEVKVTLIVAIVAALAISAHAQRDFNERRGKENDTERGQGGFGGRPGGMQMGGRRQDGGPMGEMRFDGPESGAPQMDGRRQNGGPMGGRRFDGPVFGGSRPDGAGGRPFFGQGGRRGDGEEETDAAQQIGDGLGGRGQFDGPGRRHHGRKPFGDRPFGRRNHTEGHQGHNETGDHPHDGHGRGHHGHRQGPPQDRPEEQPFGQRNESSDEDGRPHPRHHGRHHQHHHRNHTEGHQGHNETGDHPHRHHNKTGDGDQDRPMFEMRPFRFNPFGRKPFGDRPFGRRNGTEEGSARRDGQRRPYGNRGRWGENESEEEEHPTTESVTTSSPP
Protein: Klf1 protein (B0BNN2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
PEAQGGQQPVMASAETVLPSISTLTTLGQFLDTQEDFLKWWRSEETQDLGPGPPNPTEPSFHVSLKSEDPPGEDDERDVTCAWDPDLFLTNFSGPEPPSTPRTCALAPSGGPVAQFAPPESLSAYAGGPGLVTGPLGSEEHAGWAHPTPRPPTPEPFVAPVLAPGLAPKAQPAFSESRAVSAGGFFPRAGLAVPAAPSAPYGLLSGYPALYPAPQYQGHFQLFRGLAAPSAGPTAPPSFLNCLGPGAVGTELGATAIAGDAGLSPGAAPPKRSRRTLAQKRQAAHTCGHEGCGKSYTKSSHLKAHLRTHTGEKPYACSWDGCNWRFARSDELTRHYRKHTGHRPFCCGLCPRAFSRSDHLALHMKRHL
Protein: S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) (Alcohol dehydrogenase SFA) (EC 1.1.1.1) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (FLD) (GSH-FDH) (EC 1.1.1.-) (P32771)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Mitochondrion {ECO:0000269|PubMed:16823961}.
Interaction partners:
- Alcohol dehydrogenase 4
- S-formylglutathione hydrolase
- Alcohol dehydrogenase 1
- Alcohol dehydrogenase 3, mitochondrial
- Alcohol dehydrogenase 2
- Alcohol dehydrogenase 5
- Pyruvate decarboxylase isozyme 3
- Pyruvate decarboxylase isozyme 2
- Pyruvate decarboxylase isozyme 1
- Thiamine metabolism regulatory protein THI3
Sequence:
MSAATVGKPIKCIAAVAYDAKKPLSVEEITVDAPKAHEVRIKIEYTAVCHTDAYTLSGSDPEGLFPCVLGHEGAGIVESVGDDVITVKPGDHVIALYTAECGKCKFCTSGKTNLCGAVRATQGKGVMPDGTTRFHNAKGEDIYHFMGCSTFSEYTVVADVSVVAIDPKAPLDAACLLGCGVTTGFGAALKTANVQKGDTVAVFGCGTVGLSVIQGAKLRGASKIIAIDINNKKKQYCSQFGATDFVNPKEDLAKDQTIVEKLIEMTDGGLDFTFDCTGNTKIMRDALEACHKGWGQSIIIGVAAAGEEISTRPFQLVTGRVWKGSAFGGIKGRSEMGGLIKDYQKGALKVEEFITHRRPFKEINQAFEDLHNGDCLRTVLKSDEIK
Protein: Chitin elicitor receptor kinase 1 (AtCERK1) (EC 2.7.11.1) (LysM domain receptor-like kinase 1) (LysM RLK1) (LysM-containing receptor-like kinase 1) (A8R7E6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity toward both biotic and abiotic stresses (e.g. tolerance to salinity, heavy-metal stresses, and Botrytis cinerea infection). Recognizes microbe-derived N-acetylglucosamine (NAG)-containing ligands. Involved in the resistance to pathogenic fungi Alternaria brassicicola and Erysiphe cichoracearum, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated molecular patterns (PAMP). Plays an essential role in detecting peptidoglycans (e.g. PGNs) and restricting bacterial growth. Target of the bacterial type III effector E3-ligase protein hopAB2/avrPtoB of Pseudomonas syringae pv. tomato DC3000 that mediates ubiquitination and subsequent proteolysis, thus blocking all defense responses by suppressing PAMP-triggered immunity (PTI). Mediates chitin-induced phosphorylation of PBL27.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18042724, ECO:0000269|PubMed:24750441, ECO:0000269|PubMed:27679653}; Single-pass membrane protein {ECO:0000269|PubMed:18042724}.
Interaction partners:
- LysM domain-containing GPI-anchored protein 1
- LysM domain-containing GPI-anchored protein 3
- Elongation factor Tu, chloroplastic
- Guanine nucleotide-binding protein subunit gamma 1
- Protein LYK5
- LysM domain-containing GPI-anchored protein 2
- Guanine nucleotide-binding protein subunit gamma 2
- Elongation factor Tu
- Guanine nucleotide-binding protein alpha-1 subunit
- Extra-large guanine nucleotide-binding protein 2
Sequence:
MKLKISLIAPILLLFSFFFAVESKCRTSCPLALASYYLENGTTLSVINQNLNSSIAPYDQINFDPILRYNSNIKDKDRIQMGSRVLVPFPCECQPGDFLGHNFSYSVRQEDTYERVAISNYANLTTMESLQARNPFPATNIPLSATLNVLVNCSCGDESVSKDFGLFVTYPLRPEDSLSSIARSSGVSADILQRYNPGVNFNSGNGIVYVPGRDPNGAFPPFKSSKQDGVGAGVIAGIVIGVIVALLLILFIVYYAYRKNKSKGDSFSSSIPLSTKADHASSTSLQSGGLGGAGVSPGIAAISVDKSVEFSLEELAKATDNFNLSFKIGQGGFGAVYYAELRGEKAAIKKMDMEASKQFLAELKVLTRVHHVNLVRLIGYCVEGSLFLVYEYVENGNLGQHLHGSGREPLPWTKRVQIALDSARGLEYIHEHTVPVYVHRDIKSANILIDQKFRAKVADFGLTKLTEVGGSATRGAMGTFGYMAPETVYGEVSAKVDVYAFGVVLYELISAKGAVVKMTEAVGEFRGLVGVFEESFKETDKEEALRKIIDPRLGDSYPFDSVYKMAELGKACTQENAQLRPSMRYIVVALSTLFSSTGNWDVGNFQNEDLVSLMSGR
Protein: Protein CIMAP1D (CIMAP1 family member D) (Outer dense fiber protein 3-like protein 2) (Q3SX64)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGTLSCDSTPRLATAPLGRRVTEGQIPETGLRKSCGTATLENGSGPGLYVLPSTVGFINHDCTRVASPAYSLVRRPSEAPPQDTSPGPIYFLDPKVTRFGRSCTPAYSMQGRAKSRGPEVTPGPGAYSPEKVPPVRHRTPPAFTLGCRLPLKPLDTSAPAPNAYTMPPLWGSQIFTKPSSPSYTVVGRTPPARPPQDPAEIPGPGQYDSPDANTYRQRLPAFTMLGRPRAPRPLEETPGPGAHCPEQVTVNKARAPAFSMGIRHSKRASTMAATTPSRPAGHRLPGRCC