wanglab/gogpt-training-data huggingface dataset:
Protein: Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta) (P02564)
Organism: Rattus norvegicus (Rat)
Function: Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle.
Subcellular location: Cytoplasm, myofibril {ECO:0000269|PubMed:26150528}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:26150528}. Note=Thick filaments of the myofibrils. {ECO:0000269|PubMed:26150528}.
Interaction partners:
- Myosin light chain 3
- Actin, alpha cardiac muscle 1
- Myosin-binding protein C, cardiac-type
- Myosin light chain 4
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin-6
- Myosin-4
- Troponin I, slow skeletal muscle
- Natriuretic peptides A
Sequence:
MADREMAAFGAGAPFLRKSEKERLEAQTRPFDLKKDVFVPDDKEEFVKAKIVSREGGKVTAETENGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAQVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFFSQGETTVASIDDSEEHMATDSAFDVLGFTPEEKNSIYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVAYAIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAHFSLIHYAGTVDYNILGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPVDKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLSRMEFKKLLERRDSLLIIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLDQDKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTRQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILVEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSTGKSIHELEKIRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKNNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKGLNEE
Protein: ETHE1 persulfide dioxygenase (M0QXB5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEAVLRVARRQLSQRGGSGAPILLRQMFEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIGEQLGTWTSGSERGGAGVLDSWV
Protein: Heat shock protein hsp-6 (Heat shock 70 kDa protein F, mitochondrial) (P11141)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion.
Interaction partners:
- Chaperonin homolog Hsp-60, mitochondrial
- GrpE protein homolog
- Probable mitochondrial import inner membrane translocase subunit tin-44
- DnaJ homolog dnj-10
- Mitochondrial import inner membrane translocase subunit TIM23
- COX5B-domain-containing protein
- Mitochondrial import inner membrane translocase subunit TIM14
- 10 kDa heat shock protein, mitochondrial
- NIF system FeS cluster assembly NifU N-terminal domain-containing protein
- Heat shock protein 110
Sequence:
MLSARSFLSSARTIARSSLMSARSLSDKPKGHVIGIDLGTTNSCVSIMEGKTPKVIENAEGVRTTPSTVAFTADGERLVGAPAKRQAVTNSANTLFATKRLIGRRYEDPEVQKDLKVVPYKIVKASNGDAWVEAQGKVYSPSQVGAFVLMKMKETAESYLGTTVNNAVVTVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKDAGDKIIAVYDLGGGTFDVSILEIQKGVFEVKSTNGDTFLGGEDFDHALVHHLVGEFKKEQGVDLTKDPQAMQRLREAAEKAKCELSSTTQTDINLPYITMDQSGPKHLNLKLTRAKFEQIVGDLIKRTIEPCRKALHDAEVKSSQIADVLLVGGMSRMPKVQATVQEIFGKVPSKAVNPDEAVAMGAAIQGAVLAGDVTDVLLLDVTPLSLGIETLGGIMTKLITRNTTIPTKKSQVFSTAADGQTQVQIKVFQGEREMATSNKLLGQFSLVGIPPAPRGVPQVEVTFDIDANGIVNVSARDRGTGKEQQIVIQSSGGLSKDQIENMIKEAEKNAAEDAKRKELVEVINQAEGIIHDTEAKMTEFADQLPKDECEALRTKIADTKKILDNKDNETPEAIKEACNTLQQQSLKLFEAAYKNMAAKNSGGDAQEAKTAEEPKKEQN
Protein: Insulin-like growth factor-binding protein 2 (IBP-2) (IGF-binding protein 2) (IGFBP-2) (P18065)
Organism: Homo sapiens (Human)
Function: Inhibits IGF-mediated growth and developmental rates. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted {ECO:0000269|PubMed:22869525, ECO:0000269|PubMed:34035374, ECO:0000269|PubMed:38796567}.
Interaction partners:
- Insulin-like growth factor 2
- Insulin-like growth factor 1
- Insulin
- Gamma-tubulin complex component 5
- Magnesium transporter NIPA2
- Magnesium transporter NIPA1
- Migration and invasion-inhibitory protein
- Cytoplasmic FMR1-interacting protein 1
- Insulin-like growth factor-binding protein 3
- Insulin-like growth factor 1 receptor
Sequence:
MLPRVGCPALPLPPPPLLPLLLLLLGASGGGGGARAEVLFRCPPCTPERLAACGPPPVAPPAAVAAVAGGARMPCAELVREPGCGCCSVCARLEGEACGVYTPRCGQGLRCYPHPGSELPLQALVMGEGTCEKRRDAEYGASPEQVADNGDDHSEGGLVENHVDSTMNMLGGGGSAGRKPLKSGMKELAVFREKVTEQHRQMGKGGKHHLGLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDERGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKLIQGAPTIRGDPECHLFYNEQQEARGVHTQRMQ
Protein: PR domain zinc finger protein 12 (EC 2.1.1.-) (PR domain-containing protein 12) (Q7T0V8)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR037163}.
Interaction partners:
Sequence:
MMGSVLPAEALVLKAGLKQPGLSLAELITSDILHSFLYGRWRNVLGEQLFEEKNNHISPKTAFTAEVLAQSFSGEVQKLSSLVLPSEVIIAQSSIPGEGLGIFSKTWIKAGTEMGPFTGRVISPEHVDLCKNNNLMWEVFNEDGTVRYFIDASQEDHRSWMTYIKCARNEQEQNLEVVQIGNSIFYKATETIPPDQELLVWYGNSLSSFLGIPGVPGMEEEQKKNKQEEFGIVDSTGPSLAGRMRCVICHRGFNSRSNLRSHMRIHTLDKPFVCRFCNRRFSQSSTLRNHVRLHTGERPYKCQVCQSAYSQLAGLRAHQKSARHRPPNGSLQTHSPTLPVPHPATLAHHIPTMVL
Protein: Type III effector protein gala6 (Q8XZN9)
Organism: Ralstonia nicotianae (strain ATCC BAA-1114 / GMI1000) (Ralstonia solanacearum)
Interaction partners:
- Type III effector protein awr1
- Type III effector protein popp2
Sequence:
MVSRIPTGNRGQGNGIEQSASSHATEATPWLGVNLPYGHWLPSSARSVVSRASSLLGGLANFRWGGRPASARPAPNIRSAAIAPAQQTLPPELWQQIATLAGARPRRAMREVSLELRNASRAVVTHLTISDPAMFRQLSLYPALKSVRFKGELTLEALKALPPELEHLEIGRCTGSAISAEGLAHLASMPLKSLNLNGIEIGVEGARTLAASKSLVSLSLIGCGIGDRAAQALVASRSIQCLDLSVNRIGRDGAQALAGAPLVSLNLHNNEIGNEGARVLATSRTLTSLDVSNNGVGNAGAEAFAGNTVLKQLSLAGGMISGDGAQALADNKSLTDLDLSNNRLGDAGAQALADSESFVSLKLGGNEIGADGAEALARNVVLQSLNLSYNPIGFWGVNALGRAKLRKLDLCACAIDSDGASALARNTSLASLYLGSNRIGDDGARALAKNSTLTLLNLSGNNIHAVGAQALASNDSLITLDLSRNGIGDDGTAALACHPRLTSLNLSRNQIGSTGAQQLAKSATLAELDLSENRIGPEGAEALARSTVLTTLNVSYNAIGEAGARALAESVSLTSLDARRNGIGEDGAKVLEANTRITGTPQNPNFLAEDVPRPDVRWRD
Protein: Ferredoxin--NADP reductase 1 (FNR 1) (Fd-NADP(+) reductase 1) (EC 1.18.1.2) (O31475)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Iron
- Ferredoxin
- Probable flavodoxin 1
- Probable flavodoxin 2
- Uncharacterized protein YkuO
- Iron
- Iron-uptake system-binding protein
Sequence:
MAENQEVYDVTIIGGGPIGLFTAFYCGMRELKTKVIEFLPKLGGKVSLFFPEKIIRDIGGIPGIAGKQLIEQLKEQAATFDPDIVLNQRVTGFERLDDGTIVLTGSEGKKHYTRTVILACGMGTLEVNEFDSEDAARYAGKNLHYGVEKLDAFKGKRVVISGGGDTAVDWANELEPIAASVTVVHRREEFGGMESSVTKMKQSSVRVLTPYRLEQLNGDEEGIKSVTVCHTESGQRKDIEIDELIINHGFKIDLGPMMEWGLEIEEGRVKADRHMRTNLPGVFVAGDAAFYESKLRLIAGGFTEGPTAVNSAKAYLDPKAENMAMYSTHHKKLVHK
Protein: Bone morphogenetic protein receptor type-1A (BMP type-1A receptor) (BMPR-1A) (EC 2.7.11.30) (Activin receptor-like kinase 3) (ALK-3) (BMP-2/BMP-4 receptor) (Serine/threonine-protein kinase receptor R5) (SKR5) (CD antigen CD292) (P36895)
Organism: Mus musculus (Mouse)
Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP2, BMP4, GDF5 and GDF6. Positively regulates chondrocyte differentiation through GDF5 interaction. Mediates induction of adipogenesis by GDF6.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P36898}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000269|PubMed:29415997}.
Interaction partners:
- Bone morphogenetic protein 2
- Bone morphogenetic protein 4
- Bone morphogenetic protein 7
- Bone morphogenetic protein 6
- Bone morphogenetic protein receptor type-1B
- Bone morphogenetic protein receptor type-2
- Activin receptor type-1
- Growth/differentiation factor 5
- Activin receptor type-2B
- Mothers against decapentaplegic homolog 1
Sequence:
MTQLYTYIRLLGACLFIISHVQGQNLDSMLHGTGMKSDLDQKKPENGVTLAPEDTLPFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLTSGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQPTLPPVVIGPFFDGSIRWLVVLISMAVCIVAMIIFSSCFCYKHYCKSISSRGRYNRDLEQDEAFIPVGESLKDLIDQSQSSGSGSGLPLLVQRTIAKQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDIPLNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVESQDVKI
Protein: DNA fragmentation factor subunit beta (EC 3.-.-.-) (Caspase-activated deoxyribonuclease) (CAD) (Caspase-activated DNase) (Caspase-activated nuclease) (CPAN) (DNA fragmentation factor 40 kDa subunit) (DFF-40) (O76075)
Organism: Homo sapiens (Human)
Function: Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- DNA fragmentation factor subunit alpha
- Caspase-3
- Lipid transferase CIDEB
- Histone H1.0
- Apoptotic chromatin condensation inducer in the nucleus
- Lipid transferase CIDEA
- Deoxyribonuclease-2-alpha
- Histone H1.1
- Histone H1.3
- Histone H1.5
Sequence:
MLQKPKSVKLRALRSPRKFGVAGRSCQEVLRKGCLRFQLPERGSRLCLYEDGTELTEDYFPSVPDNAELVLLTLGQAWQGYVSDIRRFLSAFHEPQVGLIQAAQQLLCDEQAPQRQRLLADLLHNVSQNIAAETRAEDPPWFEGLESRFQSKSGYLRYSCESRIRSYLREVSSYPSTVGAEAQEEFLRVLGSMCQRLRSMQYNGSYFDRGAKGGSRLCTPEGWFSCQGPFDMDSCLSRHSINPYSNRESRILFSTWNLDHIIEKKRTIIPTLVEAIKEQDGREVDWEYFYGLLFTSENLKLVHIVCHKKTTHKLNCDPSRIYKPQTRLKRKQPVRKRQ
Protein: Minor capsid protein VP1 (EC 3.1.1.4) (Q3YPH4)
Organism: Primate bocaparvovirus 1 (strain Human bocavirus 1 type 1) (HBoV1) (Human bocavirus type 1)
Function: Capsid proteins self-assembles to form an icosahedral capsid with a T=1 symmetry, about 26 nm in diameter, and consisting of 60 copies of three size variants of the capsid proteins, VP1, and VP3, which differ by the presence of an N-terminal extension in the minor protein VP1 (Probable). The capsid has a channel at the 5-fold axis and there are densities extending the 5-fold axis into the interior of the capsid. The capsid encapsulates the genomic ssDNA (Probable). Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region. The additional N-terminal region of isoform Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (By similarity).
Subcellular location: [Isoform Minor capsid protein VP1]: Virion {ECO:0000269|PubMed:19244471}. Host nucleus {ECO:0000269|PubMed:20457462}. Host cytoplasm {ECO:0000269|PubMed:20457462}. Note=Slightly detected in the cytoplasm, mainly seen in the nucleus. {ECO:0000269|PubMed:20457462}.; SUBCELLULAR LOCATION: [Isoform Minor capsid protein VP2]: Virion {ECO:0000269|PubMed:19244471}.; SUBCELLULAR LOCATION: [Isoform Major capsid protein VP3]: Virion {ECO:0000269|PubMed:19244471, ECO:0000269|PubMed:28331084}. Host nucleus {ECO:0000269|PubMed:20457462}. Host cytoplasm {ECO:0000269|PubMed:20457462}. Note=Slightly detected in the cytoplasm, mainly seen in the nucleus. {ECO:0000269|PubMed:20457462}.
Interaction partners:
Sequence:
MPPIKRQPRGWVLPGYRYLGPFNPLDNGEPVNNADRAAQLHDHAYSELIKSGKNPYLYFNKADEKFIDDLKDDWSIGGIIGSSFFKIKRAVAPALGNKERAQKRHFYFANSNKGAKKTKKSEPKPGTSKMSDTDIQDQQPDTVDAPQNTSGGGTGSIGGGKGSGVGISTGGWVGGSHFSDKYVVTKNTRQFITTIQNGHLYKTEAIETTNQSGKSQRCVTTPWTYFNFNQYSCHFSPQDWQRLTNEYKRFRPKAMQVKIYNLQIKQILSNGADTTYNNDLTAGVHIFCDGEHAYPNASHPWDEDVMPDLPYKTWKLFQYGYIPIENELADLDGNAAGGNATEKALLYQMPFFLLENSDHQVLRTGESTEFTFNFDCEWVNNERAYIPPGLMFNPKVPTRRVQYIRQNGSTAASTGRIQPYSKPTSWMTGPGLLSAQRVGPQSSDTAPFMVCTNPEGTHINTGAAGFGSGFDPPNGCLAPTNLEYKLQWYQTPEGTGNNGNIIANPSLSMLRDQLLYKGNQTTYNLVGDIWMFPNQVWDRFPITRENPIWCKKPRADKHTIMDPFDGSIAMDHPPGTIFIKMAKIPVPTASNADSYLNIYCTGQVSCEIVWEVERYATKNWRPERRHTALGMSLGGESNYTPTYHVDPTGAYIQPTSYDQCMPVKTNINKVL
Protein: UBA-like domain-containing protein 1 (Q8TB05)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVNMDELKHQVMINQFVLTAGCAADQAKQLLQAAHWQFETALSAFFQETNIPYSHHHHQMMCTPANTPATPPNFPDALTMFSRLKASESFHSGGSGSPMAATATSPPPHFPHAATSSSAASSWPTAASPPGGPQHHQPQPPLWTPTPPSPASDWPPLAPQQATSEPRAHPAMEAER
Protein: Glycoprotein hormones alpha chain (Q9DG94)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU362129}.
Interaction partners:
- Glycoprotein hormone subunit beta domain-containing protein
- Glycoprotein hormones alpha chain
- Glycoprotein hormone subunit beta domain-containing protein
- Thyrotropin subunit beta
- Thyrotropin subunit beta
- Thyrotropin receptor
- G-protein coupled receptors family 1 profile domain-containing protein
- Uncharacterized protein
- G-protein coupled receptors family 1 profile domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
Sequence:
MCLLKSTGLFLILSALLVIADSYPNSDKTNMGCEECTLKPNTIFPNIMQCTGCCFSRAYPTPLRSKQTMLVPKNITSEATCCVAKEGERVTTKDGFPVTNHTECHCSTCYYHKS
Protein: Jabba, isoform F (A0A0B4JCT7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAQETKTVATAKDQNQRDHIDEEEVIELHESRSFYDRVREQAERFASTRVGQFVIERADKALAMIEDTAKWSLPQDKSSAPLERPLPWAPFLMLIVLLRLTRIWLSVGALMIGNGPISPTDMVYFIQTRRRKLRAIRVHGLKVMRRRQQEVSYGSGKGMTQKLNQWFSRAMCRPGVQQDSSSRRVFVRHSEQGLSNFVVKRPREEDCNADADLTIDQMLAKYANENSEDDSDFVPNEEEEEEESSSSSGESESESGSSEGISSGEVDEVVSQKSAGAVVENGVHKAEEKENDKGKLNITTTSNGNNDKEQADVAAAQPDEEWKSSPGHMSAAVMNTRLYNNTAAAVTTDPDPEPDTQPEPEFPSEPTSQSQPSTEETDDDAEDSCSSSGSNQTGITVYQADETQPDTQAEQILEIAATLTDSHLSNYPTVDTLTPATSSEDIFYSPIGSPTCFNTSLGTQALLKRASIQSVLAHSTPTTEMRDQPIEEANNSVPQTPETEKTQPQTPKEVHNQNQQQNQQQRQRNHPHQRYRGRNRR
Protein: GPI mannosyltransferase 4 (EC 2.4.1.-) (GPI mannosyltransferase IV) (GPI-MT-IV) (Phosphatidylinositol-glycan biosynthesis class Z protein) (PIG-Z) (SMP3 homolog) (hSMP3) (Q86VD9)
Organism: Homo sapiens (Human)
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to some trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is facultative and only scarcely detected, suggesting that it only exists in some tissues.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15208306}; Multi-pass membrane protein {ECO:0000269|PubMed:15208306}.
Interaction partners:
- GPI alpha-1,6-mannosyltransferase 2
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
- GPI ethanolamine phosphate transferase 2, catalytic subunit
- Glucosaminyl-phosphatidylinositol-acyltransferase PIGW
- GPI-anchor transamidase
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
Sequence:
MQICGSSVASVAAGTSFQVLGPVCWQQLDLKMAVRVLWGGLSLLRVLWCLLPQTGYVHPDEFFQSPEVMAEDILGVQAARPWEFYPSSSCRSVLFPLLISGSTFWLLRLWEELGPWPGLVSGYALLVGPRLLLTALSFALDGAVYHLAPPMGADRWNALALLSGSYVTLVFYTRTFSNTIEGLLFTWLLVLVSSHVTWGPTRKEPAPGPRWRSWLLGGIVAAGFFNRPTFLAFAVVPLYLWGTRGATNPGLKSLTREALVLLPGAALTAAVFVATDSWYFSSPATSRNLVLTPVNFLHYNLNPQNLARHGTHARLTHLAVNGFLLFGVLHAQALQAAWQRLQVGLQASAQMGLLRALGARSLLSSPRSYLLLLYFMPLALLSAFSHQEARFLIPLLVPLVLLCSPQTQPVPWKGTVVLFNALGALLFGCLHQGGLVPGLEYLEQVVHAPVLPSTPTHYTLLFTHTYMPPRHLLHLPGLGAPVEVVDMGGTEDWALCQTLKSFTRQPACQVAGGPWLCRLFVVTPGTTRRAVEKCSFPFKNETLLFPHLTLEDPPALSSLLSGAWRDHLSLHIVELGEET
Protein: Sigma factor binding protein 1, chloroplastic (AtsibI) (Sigma factor binding protein I) (SigA binding protein) (VQ motif-containing protein 23) (AtVQ23) (Q9LDH1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to plant defense. May regulate chloroplast metabolism upon infection with pathogens such as Pseudomonas syringae. Functions as activator of WRKY33 in plant defense against necrotrophic pathogens by stimulating the DNA-binding activity of WRKY33.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:11943170}. Nucleus {ECO:0000269|PubMed:21990940}. Note=Can localize to both chloroplast and nucleus. {ECO:0000305}.
Interaction partners:
- Probable WRKY transcription factor 33
- VQ motif-containing protein 22
- Protein MKS1
- VQ motif-containing protein 9
- Calmodulin-binding protein 25
- VQ motif-containing protein 29
- Protein HAIKU1
- VQ motif-containing protein 20
- VQ motif-containing protein 4
- VQ motif-containing protein 8, chloroplastic
Sequence:
MESSSSTFLTTTSLDKKKPSPVSRKSPKQKKKTTSTNKPIKVRYISNPMRVQTCASKFRELVQELTGQDAVDLQPEPIYSPSSDDHNLSPPAENLAPRVLHQEPFGERDSDCYEPLNAEDMFLPDQMSAGFSGFFSNGFYNVNDFGSIDSM
Protein: C-type lectin domain family 14 member A (Epidermal growth factor receptor 5) (EGFR-5) (Q86T13)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- mRNA-capping enzyme
- Multimerin-2
- mRNA cap guanine-N
- Liver carboxylesterase 1
Sequence:
MRPAFALCLLWQALWPGPGGGEHPTADRAGCSASGACYSLHHATMKRQAAEEACILRGGALSTVRAGAELRAVLALLRAGPGPGGGSKDLLFWVALERRRSHCTLENEPLRGFSWLSSDPGGLESDTLQWVEEPQRSCTARRCAVLQATGGVEPAGWKEMRCHLRANGYLCKYQFEVLCPAPRPGAASNLSYRAPFQLHSAALDFSPPGTEVSALCRGQLPISVTCIADEIGARWDKLSGDVLCPCPGRYLRAGKCAELPNCLDDLGGFACECATGFELGKDGRSCVTSGEGQPTLGGTGVPTRRPPATATSPVPQRTWPIRVDEKLGETPLVPEQDNSVTSIPEIPRWGSQSTMSTLQMSLQAESKATITPSGSVISKFNSTTSSATPQAFDSSSAVVFIFVSTAVVVLVILTMTVLGLVKLCFHESPSSQPRKESMGPPGLESDPEPAALGSSSAHCTNNGVKVGDCDLRDRAEGALLAESPLGSSDA
Protein: Zinc finger protein 622 (F4JS04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPGLTCNACNMEFKDEEERNLHYKSDWHRYNLKRKVAGVPGVTEALFEARQSALAQEKNKSNEAPMLYTCAICAKGYRSSKAHEQHLQSRSHVLRVSQGTSINGEEDIAIIRQLPRRVQHRGSIDDDSEDEWVEVDSDEELAAEEASDSLSKLNVNESGSAEDMDDDGDADKYELDPTCCLMCDKKHKTLESCMLHMHKHHGFFIPDIEYLKDPEGLLTYLGLKVKRDFMCLYCNELCRPFSSLEAVRKHMEAKSHCKLHYGDGDDEEDAELEEFYDYSSSSYVDEAGKQIVVSGETDNTVELVGGSELLITEKSENTTTSKTLGSREFMRYYRQKPRPTSQDSNQIIASLSSRYKSLGLKTVPSKEETLRMKVRKEMSKRGETMRTKIGVKSNVIRNLPNNVPY
Protein: Na(+)-translocating NADH-quinone reductase subunit C (Na(+)-NQR subunit C) (Na(+)-translocating NQR subunit C) (EC 7.2.1.1) (NQR complex subunit C) (NQR-1 subunit C) (Q56582)
Organism: Vibrio alginolyticus
Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00427, ECO:0000305}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00427}.
Interaction partners:
- Na
- Na
- Na
- Na
- Na
- NADH:ubiquinone reductase
- FAD:protein FMN transferase
- 
- NADP-dependent oxidoreductase
- Electron transport complex subunit RsxG
Sequence:
MASNNDSIKKTLGVVIGLSLVCSIIVSTAAVGLRDKQKANAVLDKQSKIVEVAGIDANGKKVPELFAEYIEPRLVDLETGNFTEGNASTYDQREASKDAERSIALTPEEDVADIRRRANTAVVYLVKDQDEVQKVILPMHGKGLWSMMYAFVAVETDGNTVSAITYYEQGETPGLGGEVENPSWRDQFIGKKLYNEDHQPAIKVVKGGAPQGSEHGVDGLSGATLTSNGVQHTFDFWLGDKGFGPFLAKVRDGELN
Protein: Alpha-ionylideneethane synthase aba3 (EC 4.2.3.-) (Abscisic acid biosynthesis cluster protein 3) (Sesquiterpene synthase aba3) (A0A384JQC9)
Organism: Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Function: Alpha-ionylideneethane synthase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene. The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom.
Interaction partners:
Sequence:
MQQVITQTLVDDRFIQISDSKKSEGLATDSTKRQSQEQPIHDKDPIKAATAAMAATPLVKEHQDTWYYPPDIANDLQSINLPAELKGEIFACAWEYTRCVIPNYTNWNRYVAFMRIIIMGIIAEFRGEMVDVTASNNLLGYDLDATLAALFEGTPGHKEMAREYKTFLLITADKASERRDGELFRRYVNALAQSPRHWFRMRDCDALARFTIASALACNDLDDIWFTEDQFEILTEIGDTLYDAVAFYKHRAEGETNSTFAYMPEDLRIKAYSECREILWALDAAWARNPKLANVINFVRFFGGPIHMMMRRYRFVEENLTIGKSETDKVVDQTRKNFKLWNRVDANKRSVLNTQRYKALIARSEELMFPGLAEFLEMGGDGICDKCKYRESYGAELSHQFGGVELCSECRLSWRKYLECFVERATKVFPELKTHFEVPV
Protein: Ribosomal protein L18 (H0YHA7)
Organism: Homo sapiens (Human)
Subcellular location: Rough endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004427}.
Interaction partners:
Sequence:
XVKLYRFLARRTNSTFNQVVLKRLFMSRTNRPPLSLSRMIRKMKLPGRENKTAVVVGTITDDVRVQEVPKLKPCPLHQVCALRVTSRARSRILRAGGKILTFDQLALDSPKGCGTVLLSGPRKGREVYRHFGKAPGTPHSHTKPYVRSKGRKFERARGRRASRGYKN
Protein: Murein DD-endopeptidase MepH (EC 3.4.-.-) (Murein hydrolase MepH) (P76190)
Organism: Escherichia coli (strain K12)
Function: A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant.
Interaction partners:
- Murein DD-endopeptidase MepM
- D-alanyl-D-alanine endopeptidase
- D-alanyl-D-alanine carboxypeptidase DacB
- D-alanyl-D-alanine-carboxypeptidase/endopeptidase AmpH
- Lipoprotein NlpI
- Penicillin-binding protein 1A
Sequence:
MARINRISITLCALLFTTLPLTPMAHASKQARESSATTHITKKADKKKSTATTKKTQKTAKKAASKSTTKSKTASSVKKSSITASKNAKTRSKHAVNKTASASFTEKCTKRKGYKSHCVKVKNAASGTLADAHKAKVQKATKVAMNKLMQQIGKPYRWGGSSPRTGFDCSGLVYYAYKDLVKIRIPRTANEMYHLRDAAPIERSELKNGDLVFFRTQGRGTADHVGVYVGNGKFIQSPRTGQEIQITSLSEDYWQRHYVGARRVMTPKTLR
Protein: Hydrogenase 3 maturation protease (EC 3.4.23.51) (HycI protease) (P0AEV9)
Organism: Escherichia coli (strain K12)
Function: Protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3.
Interaction partners:
- Formate hydrogenlyase subunit 5
- Formate hydrogenlyase maturation protein HycH
- Formate hydrogenlyase subunit 4
- Formate hydrogenlyase subunit 6
- Formate hydrogenlyase subunit 7
- Formate hydrogenlyase subunit 2
- Formate hydrogenlyase subunit 3
- Carbamoyltransferase HypF
- Hydrogenase-4 component G
- Hydrogenase-4 component H
Sequence:
MTDVLLCVGNSMMGDDGAGPLLAEKCAAAPKGNWVVIDGGSAPENDIVAIRELRPTRLLIVDATDMGLNPGEIRIIDPDDIAEMFMMTTHNMPLNYLIDQLKEDIGEVIFLGIQPDIVGFYYPMTQPIKDAVETVYQRLEGWEGNGGFAQLAVEEE