wanglab/gogpt-training-data huggingface dataset:
Protein: Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70) (P9WMJ9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Acts as a chaperone.
Subcellular location: Cytoplasm {ECO:0000305}. Secreted, capsule {ECO:0000269|PubMed:19470749}. Cell surface {ECO:0000269|PubMed:19470749}. Extracellular vesicle, bacterial extracellular vesicle {ECO:0000269|PubMed:21364279}. Note=Although thought of as a cytoplasmic chaperone this protein is routinely found extracellularly in the absence of cell lysis (PubMed:19470749). Present in extracytoplasmic vesicles (PubMed:21364279). {ECO:0000269|PubMed:19470749, ECO:0000269|PubMed:21364279}.
Interaction partners:
- Chaperone protein ClpB
- Protein GrpE
- Chaperone protein DnaJ 1
- Probable heat shock protein transcriptional repressor HspR
- Chaperonin GroEL 2
- Chaperone protein DnaJ 2
- Chaperone protein HtpG
- Co-chaperonin GroES
- Chaperonin GroEL 1
- Heat-inducible transcription repressor HrcA
Sequence:
MARAVGIDLGTTNSVVSVLEGGDPVVVANSEGSRTTPSIVAFARNGEVLVGQPAKNQAVTNVDRTVRSVKRHMGSDWSIEIDGKKYTAPEISARILMKLKRDAEAYLGEDITDAVITTPAYFNDAQRQATKDAGQIAGLNVLRIVNEPTAAALAYGLDKGEKEQRILVFDLGGGTFDVSLLEIGEGVVEVRATSGDNHLGGDDWDQRVVDWLVDKFKGTSGIDLTKDKMAMQRLREAAEKAKIELSSSQSTSINLPYITVDADKNPLFLDEQLTRAEFQRITQDLLDRTRKPFQSVIADTGISVSEIDHVVLVGGSTRMPAVTDLVKELTGGKEPNKGVNPDEVVAVGAALQAGVLKGEVKDVLLLDVTPLSLGIETKGGVMTRLIERNTTIPTKRSETFTTADDNQPSVQIQVYQGEREIAAHNKLLGSFELTGIPPAPRGIPQIEVTFDIDANGIVHVTAKDKGTGKENTIRIQEGSGLSKEDIDRMIKDAEAHAEEDRKRREEADVRNQAETLVYQTEKFVKEQREAEGGSKVPEDTLNKVDAAVAEAKAALGGSDISAIKSAMEKLGQESQALGQAIYEAAQAASQATGAAHPGGEPGGAHPGSADDVVDAEVVDDGREAK
Protein: SIN3 transcription regulator family member A (H3BQ76)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKRRLDDQESPVYAAQQRRIPGSTEAFPHQHRVLAPAPPVYEAVSETMQSATGIQYSVTPSYQVSAMPQSSGSHGPAIAAVHSSHHHPTAVQPHGGQVVQSHAHPAP
Protein: Temporin-LK1 (C3RT22)
Organism: Limnonectes kuhlii (Kuhl's Creek frog) (Rana kuhlii)
Function: Has antimicrobial activity against Gram-positive bacteria S.aureus ATCC 2592 (MIC=2.5 uM), S.aureus ATCC 43300 (MIC=2.5 uM) and B.subtilis (MIC=15.0 uM), against Gram-negative bacteria E.coli ML-35P (MIC=30.0 uM), P.aeruginosa PA01 (MIC=2.5 uM) and P.aeruginosa ATCC 27853 (MIC=2.5 uM) and against fungus C.albicans ATCC 2002 (MIC=5.0 uM).
Subcellular location: Secreted {ECO:0000255, ECO:0000269|PubMed:23054029}.
Interaction partners:
Sequence:
MFTMKKSLLLLFFLGAINLPLCQEERNAEEERRDGDDEGSVEVQKRFFPLLFGALSSMMPKLFGK
Protein: Neuroligin-4, Y-linked (Neuroligin Y) (Q8NFZ3)
Organism: Homo sapiens (Human)
Function: Putative neuronal cell surface protein involved in cell-cell-interactions.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Postsynaptic density membrane {ECO:0000250}.
Interaction partners:
- Neurexin-2
- Neurexin-1
- Disks large homolog 4
- Zinc finger Y-chromosomal protein
- Eukaryotic translation initiation factor 1A, Y-chromosomal
- Ubiquitin carboxyl-terminal hydrolase 9Y
- F-box-like/WD repeat-containing protein TBL1Y
- SH3 and multiple ankyrin repeat domains protein 3
- Putative serine/threonine-protein kinase PRKY
- Histone demethylase UTY demethylase UTY)
Sequence:
MLRPQGLLWLPLLFTSVCVMLNSNVLLWITALAIKFTLIDSQAQYPVVNTNYGKIQGLRTPLPSEILGPVEQYLGVPYASPPTGERRFQPPESPSSWTGIRNATQFSAVCPQHLDERFLLHDMLPIWFTTSLDTLMTYVQDQNEDCLYLNIYVPMEDDIHEQNSKKPVMVYIHGGSYMEGTGNMIDGSILASYGNVIVITINYRLGILGFLSTGDQAAKGNYGLLDQIQALRWIEENVGAFGGDPKRVTIFGSGAGASCVSLLTLSHYSEGLFQKAIIQSGTALSSWAVNYQPAKYTRILADKVGCNMLDTTDMVECLKNKNYKELIQQTITPATYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGLKFVDGIVDNEDGVTPNDFDFSVSNFVDNLYGYPEGKDTLRETIKFMYTDWADKENPETRRKTLVALFTDHQWVAPAVATADLHAQYGSPTYFYAFYHHCQSEMKPSWADSAHGDEVPYVFGIPMIGPTELFSCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVAWSKYNPKDQLYLHIGLKPRVRDHYRATKVAFWLELVPHLHNLNEIFQYVSTTTKVPPPDMTSFPYGTRRSPAKIWPTTKRPAITPANNPKHSKDPHKTGPEDTTVLIETKRDYSTELSVTIAVGASLLFLNILAFAALYYKKDKRRHETHRHPSPQRNTTNDITHIQNEEIMSLQMKQLEHDHECESLQAHDTLRLTCPPDYTLTLRRSPDDIPFMTPNTITMIPNTLMGMQPLHTFKTFSGGQNSTNLPHGHSTTRV
Protein: Protein Z-dependent protease inhibitor (PZ-dependent protease inhibitor) (PZI) (Serpin A10) (Q9UK55)
Organism: Homo sapiens (Human)
Function: Inhibits activity of the coagulation protease factor Xa in the presence of PROZ, calcium and phospholipids. Also inhibits factor XIa in the absence of cofactors.
Subcellular location: Secreted.
Interaction partners:
- Vitamin K-dependent protein Z
- Coagulation factor X
- Fibrinogen alpha chain
- Plasminogen
Sequence:
MKVVPSLLLSVLLAQVWLVPGLAPSPQSPETPAPQNQTSRVVQAPKEEEEDEQEASEEKASEEEKAWLMASRQQLAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSLFKGLRETLSRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRNLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPTLL
Protein: Core gene UL18 family protein (ORF26) (Putative minor capsid protein) (C7E599)
Organism: Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Interaction partners:
Sequence:
MALDKSIVVNFTSRLFADELAALQSKIGSVLPLGDCHRLQNIQALGLGCVCSRETSPDYIQIMQYLSKCTLAVLEEVRPDSLRLTRMDPSDNLQIKNVYAPFFQWDSNTQLAVLPPFFSRKDSTIVLESNGFDLVFPMVVPQQLGHAILQQLLVYHIYSKISAGAPDDVNMAELDLYTTNVSFMGRTYRLDVDNTDPRTALRVLDDLSMYLCILSALVPRGCLRLLTALVRHDRHPLTEVFEGVVPDEVTRIDLDQLSVPDDITRMRVMFSYLQSLSSIFNLGPRLHVYAYSAETLAASCWYSPR
Protein: Myopalladin (D4A7X7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MQDDSIEASTSISQLLRESYLAETRHRGDNERSRAEPSSNPFHFSSPGAAEGGGPEDLPDLSAFLSQEELDESVNLARLAINHDPLERVDESQTRKRLSSDQKPSFEPAFLQDSSRGLASSKDSPPETKRPQYSSETQSKKVFLNKAADFIEELSSLFKAHSSKRIRPRACKNHKSKTESPNKVVQENSPTFSDLTERRERTSVPIPIPADSRDNELNHAIEQREAKRREAELAAVEAAAGDSTPGSSPSSLYYEEPLGQPPRFTQKLRSREVPEGSRVQLDCIVVGIPPPQVRWYCEGKELENSPDIHIVQAGNLHSLTIAEAFEEDTGRYSCFASNIYGTDSTSAEIYIEGVSSSDSEGDPNKEEMNRIQKPNEVSSPPTTSATIPPTVQAQPRVSTIQQCQSPTNYLQGLNGKPIIAAPVFTKMLQNLSASEGQLVVFECRVKGAPSPKVEWYREGTLIEDSPDFRILQKKEICTLVIAEVFAEDSGCFTCTASNKYGTVSSIAQLAVRGNEDISDNETLHSDNSTTNPAATEQQPSPPNPQPPPEEQPPKPKLEGVLVNHNEPRSSSRIGLRVHFNLPEDDKDTEASSGCGMANTSQTRPDSFPERFNGQEARISEPSSPVKEPPPVLAKPKLDSTQLQQLHNQVLLEQLQLHNTSPSSPKESPFNTSILNSAPPTVTISSKQVKSPAPQTFNLARPKHFFPASSTSTATVSPSSSPVFTLSNTPQTIQRTVSKESLLMTHPSTQGRSPGGLSIQNEPAPPSPAEPAVPTVSYSITSGNQFQPHCVSPTPVSPTGRIQNPVAFLSSVLPSLPSIPPTNAMGLPKSAPSVPPQGLMKKTTKTPQAVSDDYIRETKNSVILDLGKKVNFSDVRSHQQEYKISSFEQRLMNEIEFRLERTPVDESDDEIQHDEIPTGKCIAPIFDKRLKHFRVTEGSPVTFTCKIVGIPVPKVYWFKDGKQISKRNEHCKMRRDGDGTCSLHIESTHGDDDGNYTIMAANPQGRISCSGHLMVQGFPIRNRLSPAGQSHRGRSRMQERDKEPLQERFFRPHFLQAPGDMVAHEGRLCRLDCKVSGLPPPELTWLLNGQPVLPDASHKMLVRETGVHSLLIDPLTQRDAGTYTCVATNKTGQNSFSLELTVVAKEVKKAPVILEKLQNSGVPEGHPVRLEGRVIGMPPPVFYWKKDNETIPFTRERISMHQDTTGYVCLLIQPAKKSDAGWYTLSAKNEAGIVSCTARLDIYAQWHQQIPTPISIRPSGSRYGSLTSKGLDIFSAFSSMESTMMYSCTSRSVVESDEL
Protein: CMP-sialic acid transporter 1 (CMP-SA-Tr 1) (CMP-Sia-Tr 1) (Q8LGE9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Sugar transporter involved in the transport of CMP-sialic acid from the cytoplasm into the Golgi.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- F-box protein At5g41720
- Protein kinase family protein
- Ubiquitin-conjugating enzyme E2 8
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Kinesin-like protein KIN-14F
Sequence:
MAATPWYFVAVLLTILTSSQGILTTLSQSDGGYKYDYATVPFLAEVFKLIISGLFLWREMRTSSSTTSRITTDWKSVRLFVIPSLIYLIHNNVQFATLTYVDTSTYQIMGNLKIVTTGILFRLFLKRKLSKLQWMAIGLLAVGTTTSQVKGCGEASCDSLFTAPIQGYLLGILSAGLSALAGIYTEFLMKRNNDTLYWQNLQLYTFGSLFNVARLIADDFRHGFEKGPWWQRIFDGYSITTWLVVLNLGSTGLLVSWLMKYADNIVKVYSTSMAMLLTMVASIYLFSFKPTLQLFLGIVICIMSLHMYFAPPHTLVDLPVTNEAHAKTLKQVVVEEKTDS
Protein: Dolichol phosphate-mannose biosynthesis regulatory protein (Q545R7)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU365084}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU365084}.
Interaction partners:
Sequence:
MATGTDQAVGFGLVAVSLIIFTYYTTWVILLPFIDSQHVIHKYFLPRAYAVLLPLAAGLLLLLFVGLFITYVMLKSQKITKKAQ
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (O01712)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADEKAKESFRERQAQELEVIKSIFGCDVEDLRPQANPSLWKPTDIRIQLTPLRDSSNGLETYVCTKLHVTCPSKYPKLPPKISLEESKGMSDQLLEALRNQLQAQSQELRGEVMIYELAQTVQAFLLEHNKPPKGSFYDQMLQDKQKRDQELQDIQRQRESLQRQTLIDEVERRKEMFKTEAKRRGEPRRSMSESNPRHPSSSESSENSSPYYRGHIYPSKCLDHRNTETLYFHKMGRQIQRGCCVGHSQRGCIAYTGIDMHCGQLLYITEWNIKYSQLEQPCIGGGKCHWSSESKCMGSHRVDEVMASIEKQVSSLSQLQHKNLVSYECVLCIKRKEGLLVYLVQDFLLGTSVFSISSSLGWCMDGARMVARGVLDALVFLHNKGVSHSHLLDTTVFMDNTGNVRVSDFSLVPNLLELLSGAGQSSSCGDLPALGALVESLMPTNSYEMRDFVDKCNSDRTLSASELLEHPFLRFYVDNGQQQVMPLPQQQHPNTVQRTGSAMPYQIPTLALSQSRLRTEFEVLMYLGKGAFGDVLKVRNILDNREYAIKRIPLPARSRQLYKKMTREVELLSRLNHENVVRYFNSWIESVDDADAAEMDKLLGGEWSQSQQDLSVKPAKSPQLGPTLEEDEDEEDSSSSMWNGYIPNMEDSDSDGIEFVDSNGKVAVYDDEEQEDSTRGKTNSPRPLMQVMYIQMEFCEKCTLRTAIDDNLFNDTDRLWRLFREIAEGLAHIHQQGIIHRDLKPVNIFLDSHDQIKIGDFGLATTSFLALQAHDAAPAPVNQITSAEDGTGTGKVGTTLYVAPELTGNASKSVYNQKVDMYTLGIILFEMCQPPFDTSMERAQTIMALRNVSINIPDAMLKDPKYEKTVKMLQWLLNHDPAQRPTAEELLISDLVPPAQLEANELQEMLRHALANPQSKAYKNLVARCLQQESDEVLEHTYHLGSSRAMKSWNSAIIIDDIVSLNPVIEFVKAKVVNLFRKHGAIEVDSPLLSPLSARNSTANANANAVHLMTHSGCVVVLPCDLRTQFARHVTMNSVNLIRRYCVDRVYREERVFNFHPKQSYDCSFDIIAPTTGSHLVDAELLSLAFEITSELPRLREKNLAIRMNHTNLLRAILIFCNVPKAQYGALFEGTMDFIESRISRFQFHSSITGIMEKSRTSAQTLMDMLLANFLLTGSRSTVDDSALKSLMRGKGEAASLARGALRELETVVGLAYSLGVKCPIHIWAGLPISFDRASNGGIVWQMTADLKPNRSGHPSVLAIGERYDSMLHEFQKQAQKFNPAMPARGVLSGAGLTFSLDKLVAAVGVEYAKDCRAIDVGICVCGTRPPLKDVTYIMRLLWSVGIRCGIVEAASELGDEAQDLARLGALHVILVAENGSLRVRSFERERFQERHLTRTELVEFIQKMLRSDGLNGTTVDNFSQLSALGSGDNRSSGGKERERGENGLSTSASNATIKNNYSQLPNLQVTFLTHDKPTANYKRRLENQVAQQMSSTLSQFLKKETFVVLVVELPPAVVNAIVGAINPREIRKRETEPEINYVIERFSKYKRYISEINEEVVDYLSDAKTPIVALYSISDSYYRVII
Protein: Four-jointed box protein 1 (Four-jointed protein x1) (Four-jointed protein homolog) (Q8BQB4)
Organism: Mus musculus (Mouse)
Function: Acts as an inhibitor of dendrite extension and branching.
Subcellular location: Secreted {ECO:0000269|PubMed:16145673}.
Interaction partners:
- Protocadherin Fat 4
- Protocadherin-16
- Golgi-associated kinase 1A
- FAT atypical cadherin 1
- Glycosaminoglycan xylosylkinase
- Protocadherin Fat 3
Sequence:
MGRKMRGAAAAAGLWLLALSSLLTLWGGLLPPRTELPASRPPEDRLPPHPIQSGGPAPEPRFPLPPPLVWDARGGSLKTFRALLTLAAGADNPPRRHQDDRGRHEPSGLSWPEERRAVHGGVFWSRGLEEQVPRGFSEAQAAAWLEVARGARVVALDRGGCGRSSNRLARFADGTRACVRYGINPEQIQGEALSYYLARLLGLQRHVPPLALARVEARGAQWVQVQEELRTAHWTEGSVVSLTRWLPNLTDVVVPEPWRSEDGRLRPLRDAGGELTNLSQAELVDLVQWTDLILFDYLTANFDRLVSNLFSLQWDPRVMHRATSNLHRGPGGALVFLDNEAGLVHGYRVAGMWDKYNEPLLQSVCVFRERTARRVLELHRGQDAAARLLRLYSRHEPRFPELAELSEPHAQLLQRRLDFLAKHILHCKAKYGRRPGDLITLRGREGLGYE
Protein: Three-finger toxin Tschuditoxin-I (C0HLK3)
Organism: Micrurus tschudii (Desert coral snake)
Function: Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site (By similarity). Binds to and inhibits the endogenous nicotinic acetylcholine receptors (nAChR) (By similarity). This neurotoxin is lethal to mice by intraperitoneal or intravenous injection.
Subcellular location: Secreted {ECO:0000269|PubMed:31211957}.
Interaction partners:
Sequence:
MICYNQQSSEPPTTKTCSEGQCYKKTWSDHRGTIIERGCACPNVKPGVKISCCSSDK
Protein: Uncharacterized protein (Q381M0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIHAVVMALFHNKISRVTLGSTPQGAVSLPVAQWLKPMLESNTSLTTVTLHTQYIPPESLKVVLLGASRCRGLQYLRLVGGISVLQSKVLMSALAHFTLSYRPSRPSTDARCRVPNGEEYSHAQRVAQPSPSGAPERENGRFALKACEAQRANDMDMCCNPIYQRLCSPALLNARAAGPPSPCIRQHNGVHVVLDVQHMDDVVAAFLVRGLERAERVIGLDVHVSSVSQTASRAAARLLSRTESIIKLNAERLGHLLARCPSPVPQKKSSRRHAENAVRLGTSPHSPLCRPNAGADGGPPRPPTANPQSLPTRRYSPPRLLPEHPCEPHSPPPRPLGAGAPHRLFSTPSVTFTADGDCAEEESDDNTLTGGEGRGEGDKEEYEEIREANKECESAPPNNRVSPNTDIVACPFQKLEQKKVEVWGSRSTVPGSPSPCYKPHAPLHQPPSHQGQLVQHMRHMRNYVKDINSVVVRYQVGSRETVQRMVTAMQQLEEQLTQSVTEKLTDMLVTISEVERPET
Protein: Ubiquitin-conjugating enzyme E2 G1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme G1) (E217K) (UBC7) (Ubiquitin carrier protein G1) (Ubiquitin-protein ligase G1) [Cleaved into: Ubiquitin-conjugating enzyme E2 G1, N-terminally processed] (P62254)
Organism: Mus musculus (Mouse)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4.
Interaction partners:
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-conjugating enzyme E2 G2
- Polyubiquitin-B
- Ubiquitin-like modifier-activating enzyme 6
- Ubiquitin-conjugating enzyme E2 variant 2
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-conjugating enzyme E2 variant 1
- Ubiquitin-like modifier-activating enzyme 7
Sequence:
MTELQSALLLRRQLAELNKNPVEGFSAGLIDDNDLYRWEVLIIGPPDTLYEGGVFKAHLTFPKDYPLRPPKMKFITEIWHPNVDKNGDVCISILHEPGEDKYGYEKPEERWLPIHTVETIMISVISMLADPNGDSPANVDAAKEWREDRNGEFKRKVARCVRKSQETAFE
Protein: SHOCT domain-containing protein (Q9BKP3)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSAYPDASPYITSSWPWWWLLLPLLAALLLTLLCCCIPWCLKRRYRSSKEHSRLVTNGQHAPLLEEQKAGMNENMRQLETRLDKMRGAVDGRARGDFEDGYMKGYKDANKLGSAHAARRRLDDDYGTRDDRFHEGYVKGLKDAGMTGMTTSMHNLAQRTGGGYSAGFAQGYKDGNSGIFGDRVTPSLISRLDEQYAGQEDFKQGYVDGFKEGASSRVGERSRFEDSRKLQQSLTELTERLTSLEKTKGDEIHSTKIYHVYNQQPEGATMSSTGAQLAQELEEIGSTSRRSTLRRHYTPGDYLKQDAEEGYNSLSRNRRSLSASALAANREDKSGKWAEQLIDLVSEPLDTTIARINNYTSSSNDRGQGDVVEEKYHRSYKEEHSSR
Protein: Pentatricopeptide repeat-containing protein MRL1, chloroplastic (Protein MATURATION OF RBCL 1) (AtMRL1) (Q0WLC6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulator of the large subunit (LS) of RuBisCO. Involved either in the processing or in the stabilization of the processed transcript, probably by acting as a barrier to the 5'>3' degradation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18431481}.
Interaction partners:
- Ribulose bisphosphate carboxylase large chain
- Protein high chlorophyll fluorescent 107
- Polyribonucleotide nucleotidyltransferase 1, chloroplastic
- Photosystem II reaction center protein H
- Protein MULTIPLE CHLOROPLAST DIVISION SITE 1
- Cytochrome b6
- Ribonuclease J
- Protein HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 244
- Large ribosomal subunit protein eL30z
- Uncharacterized aarF domain-containing protein kinase At5g05200, chloroplastic
Sequence:
MEVTSTTFISTTRSSKYLTLTSYSPVILPASTLRRDFLGCCHSLRPSPHLRTRAGKRNSRRSSIRSPRLVVRASIDSGLILIVVAVTAFSAIAFAYCQSTFRKRKSSDEVATVHGGKNSAENRREIHGDIHEGNPVEINVGFRKVEEESVNLLEEEKAHQIHEVAVMDYDSVSAEDSQFAVASVTTVATAHTLIDESFSSSIVNGSVALESATFGVKTPEKQVGNSEDQKGLEHDFSQAVVGIHSIASPQVVDDTRALEYEYNGLLQKPLEYSIFAESKREEIHTFYGSNHSSAKSSRLPSLKAVSPAVTSATNSLFLDHKNNGVIDTQFPGQSSGQATGDVQEENLVAHSNGGVSHIRKDVKGDWKFPSDGKHVGHQIDESMPQFPARNFELHNSNGRSPETSDAYNRLLRDGRIKDCISLLEDLDQRDLLDMDKIYHASFFKACKKQRAVKEAFRFTKLILNPTMSTFNMLMSVCASSQDIEGARGVLRLVQESGMTADCKLYTTLISSCAKSGKVDAMFEVFHQMSNSGVEANLHTFGALIDGCARAGQVAKAFGAYGILRSKNVKPDRVVFNALISACGQSGAVDRAFDVLAEMKAETHPIDPDHISIGALMKACCNAGQVERAKEVYQMIHKYGIRGTPEVYTIAVNSCSKSGDWDFACSIYKDMKEKDVTPDEVFFSALIDVAGHAKMLDEAFGILQDAKSQGIRLGTISYSSLMGACCNAKDWKKALELYEKIKSIKLRPTISTMNALITALCEGNQLPKAMEYLDEIKTLGLKPNTITYSMLMLASERKDDFEVSFKLLSQAKGDGVSPNLIMCRCITSLCKRRFEKACAGGEPVVSFKSGRPQIENKWTSMALMVYRETISGGTVPTTEVVSQVLGCLQLPHDAALRDRLISTLGINISSQKQHNIFPLVDGFGEYDPRAFSLLEEATSLGVLPSVSFNKIPLFFDTTELPKNVAEVYLLTIFKGLKHRLAAGAKIPHINLIISIQEKEIRTPEGEKTIDLTGRVGQEIGALLRRLDIPYHRKDSRLRINGVSLKNWFQPKLDSPFSGGKPGDLRSSQVPLGNQISRQQRSIRLGNLSLE
Protein: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (BPG-independent PGAM) (Phosphoglyceromutase) (iPGM) (EC 5.4.2.12) (P75167)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Interaction partners:
- Enolase
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Transketolase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Deoxyribose-phosphate aldolase
- Phosphoenolpyruvate-protein phosphotransferase
- L-lactate dehydrogenase
Sequence:
MHKKVLLAILDGYGISNKQHGNAVYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLSLINQNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQVKMVLHLFGDGRDVAPCTMKSDLEAFMVFLKDYHNVIIGTLGGRYYGMDRDQRWDREEIAYNAILGNSKASFTDPVAYVQSAYDQKVTDEFLYPAVNGNVDKEQFALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKAGRKYNLFFVTMMNYEGIKPSAVVFPPETIPNTFGEVIAHNKLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQINQFDLTVLNFANPDMVGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMIDSNNNPVTKHTVNKVPFVCTDTNIDLQQDSASLANIAPTILAYLGLKQPAEMTANSLLISKK
Protein: UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.15) (GlcNAc-1-P transferase) (G1PT) (GPT) (N-acetylglucosamine-1-phosphate transferase) (P42867)
Organism: Mus musculus (Mouse)
Function: Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P23338}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H3H5}.
Interaction partners:
- UDP-N-acetylglucosamine transferase subunit ALG14
- UDP-N-acetylglucosamine transferase subunit ALG13
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichol kinase
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichyldiphosphatase 1
- UDP-N-acetylglucosamine transferase subunit ALG13
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
- Glutamine--fructose-6-phosphate aminotransferase 1
Sequence:
MWAFPELPLPLPLLVNLIGSLLGFVATVTLIPAFRSHFIAARLCGQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLNCFVEEQCKAFPHHEFVALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPKPFRWILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELEGDYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQVFNFLYSLPQLFHIIPCPRHRMPRLNAKTGKLEMSYSKFKTKNLSFLGTFILKVAENLRLVTVHQGESEDGAFTECNNMTLINLLLKVFGPIHERNLTLLLLLLQVLSSAATFSIRYQLVRLFYDV
Protein: Baramicin A1 [Cleaved into: Immune-induced peptide 24 (DIM-24) (DIM24) (IM24); Immune-induced peptide 10 (DIM-10) (DIM10) (IM10); Immune-induced peptide 12 (DIM-12) (DIM12) (IM12); Immune-induced peptide 13 (DIM-13) (DIM13) (IM13); Immune-induced peptide 22 (DIM-22) (DIM22) (IM22); Immune-induced peptide 5 (DIM-5) (DIM5) (IM5); Immune-induced peptide 6 (DIM-6) (DIM6) (IM6); Immune-induced peptide 8 (DIM-8) (DIM8) (IM8)] (C0HLZ9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Secreted immune-induced peptides induced by Toll signaling. Has a significant role in resistance to infection by the entomopathogenic fungus B.bassiana R444 and weak antifungal activity against M.rileyi PHP1705. In adult males, activity appears to be important for neuromuscular processes that mediate correct wing posture upon Toll activation.
Subcellular location: [Immune-induced peptide 24]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 6]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 12]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 10]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851, ECO:0000269|PubMed:9736738}.; SUBCELLULAR LOCATION: [Immune-induced peptide 5]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 8]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 13]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851, ECO:0000269|Ref.7}.; SUBCELLULAR LOCATION: [Immune-induced peptide 22]: Secreted {ECO:0000269|PubMed:34432851}.
Interaction partners:
Sequence:
MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY
Protein: ESCRT-I complex subunit vps23 (Suppressor of ste12 deletion protein 6) (Q7Z992)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association to the ESCRT-0 complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Endosome {ECO:0000269|PubMed:16823372}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Class E vacuolar protein-sorting machinery protein hse1
- Vacuolar protein sorting-associated protein 27
- Vacuolar-sorting protein dot2
- Vacuolar protein-sorting-associated protein 25
- Vacuolar-sorting protein snf7
- Vacuolar protein sorting-associated protein 28 homolog
- Vacuolar protein-sorting-associated protein 36
- Suppressor protein of bem1/bed5 double mutants
- Uncharacterized carboxypeptidase C24C9.08
- Vacuolar protein-sorting-associated protein 46
Sequence:
MSDHAINEHPSRILNTIEKIRFWKNGLAEELELLFRKQCEDTFTLQAINIEVDTQDENKIEEVRIYLSTPAFDKTILTSACITVRSYYPSQPPIVQLLDEKGGKHKYTSLLLQLWKNERSVFNIYRLVQALIKQDFEREHTSPPELPTKLVNTIEKLKVKEENEAPPVIPAKPFSSSSEQHFRKVPALPSKLPPKPLKITANSSLGQETNSNSSSFQSTLFSLNTAPFSATSQQLVHDSVSLRRPSSNIPAQKPIPPKPEQNEIIITKDTPSLKDKYSKPALLPQKPKVSKGQIVQQVSVFSTGKKIESQSLLNLIDTDIETPLKGSSELLYSEDFKPNVDPVKIQQILHKQNKIIEEKWISQIRISKNLEVKQRLLDQERHALETLAKNIENNRFILGKRRRKAREALQKLDNLKDLSVQELFIIPSERELKYYELKRKDEKLDEGIRALNQALHHESIMPASWLKGIKLLARQQFLIRDEMLQYS
Protein: NADH dehydrogenase subunit NI8M (Q380Z9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Complex 1 LYR protein domain-containing protein
- FAD-binding domain-containing protein
- Uncharacterized protein
- Sulfotransferase
- Flavoprotein monooxygenase, putative
- NADH dehydrogenase 1 beta subcomplex subunit 7
- SET domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MSWRARFTPCVASLTVWLNPKDPNCFGVRNWWRNNLPELQLLNPFCSFTIQELSFGEPHMYINYTPTDQRMIRLAGATEDECEDIMEACITYGMNHAIIERPRTDDGGDLINQPAITSFGYTESFMSKLEVSPPADIGQRTPEGVDDPGQKPRVYPRNVGFKIMP