wanglab/gogpt-training-data huggingface dataset:
Protein: ATPase family AAA domain-containing protein At1g05910 (F4IAE9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- Histone H4
- Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial
- 26S proteasome regulatory subunit RPN13
- Proteasome subunit beta type-6
- Proteasome subunit beta type-4
- 26S proteasome non-ATPase regulatory subunit 3 homolog B
- 26S proteasome non-ATPase regulatory subunit 12 homolog A
Sequence:
MHPKRSSQGDGSVTKPVRTSDRLRRRPKLHGRSYLYYSSPNMLHNRKRNTKTRTAASQIAKMLHKGNRPARASNAAPIASDLRRSTRKRRISVNLEDYTDSSGAEDEDMMSPAYRTLRRRVHKNFSTSKSRKDMDAELAPRREGLRPRRSTTIANKRLKTESGADQDTSEEKDGQDETENGNELDDADDGENEVEAEDEGNGEDEGDGEDEGEEDGDDDEEGDEEQEGRKRYDLRNRAEVRRMPTGEINKQQQPRSPRRVLHQGMGTRVGRDGRRGGSRPHKRHRFTRTDDSDDSLLVDELDQGPAIPWARGGNRSGAPWLFGGLDTYGSSSLGLNVGASGWGHQSDGLAALTSGVQTAGPSSKGGADIQPLQINEDINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELKEELAATCVGYCGADLKALCTEAAIRAFREKYPQVYTSDDKYAIDVGLVNVEKSHFVEAMSAITPAAHRGSVVQSRPLSPVVLPCLHRHLLESMSLISDIFPSSATSSELTKLSILTFGSAIPLVYRPRLLLLGGEGVGLDHLGPAILHELEKFPIHSLGLPSLLSDPGAKTPEEALVHIFSEARRTTPSILYIPMFNNWWENAHEQLRAVFLTLLEELPSNLPILLLATSYGELSDMEEQSVFDNRSVYTVDKPSSEDRSLFFDRLIEAALSVISGLNGKPDGPQPLPELPKVPKEPTGPKPAEVKAKVEAEQHALRRLRMCLRDVCNRILYDKRFSAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDDYAGARIVSRAYELRDVVHGMLSQMDPALLTYCDKIAAEGGPSLIPDDLSGSILGLAPVVQMGTVTRTSARLRNVQPEVNLDRDYEGLKKPKKTTDAVSIDSAADKSQNQDSGQEMPSPDAANPQSAAPSPTDGDREDQSEPPSKEASAEDMSGDSCKGPAAKSDKEISSRTESVKGVFMERTDNYSIPQMERLYTRIMKGVLETLDKGLRDDDNNPKHSILRFLSEFAQHQANF
Protein: Protein hobbit (Bridge-like lipid transfer protein family member 2) (BLTP2) (Q9VZS7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Tube-forming lipid transport protein which binds to phosphatidylinositols and affects phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) distribution.
Subcellular location: Cell membrane {ECO:0000269|PubMed:34415038}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:34415038}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q06179}. Note=Localizes to endoplasmic reticulum-cell membrane and some endoplasmic reticulum-mitochondria contact sites. {ECO:0000269|PubMed:34415038}.
Interaction partners:
- LD33331p
Sequence:
MMLQLLLFCLALFIFVYWVLPTGISWYLVKRFRVKVRIGRISLPYLSLKNVHISKSGFSVQIEEVCLRSSFFTTEVTKLLSIYIRDIRINKDIHSRQDDSYDQDSYELRRTQTLAGKASEAKGVPDFRQTKVPASIITFAQFMAVHVNNISVVLMNNDFDPGWFIHATAKELHLDGSIVQNARVLLVNAALSEAQAKMLRHCSSRRQSLENLNKIRPCLGEVSFDMTLDASLFAQGPLSMDTLSLVINNAKSVIHGGLYEFLSEAKRRTSTGQPSRRSTQGLAPSKRSYDNDNYEKLAPIIPKNFNFSIKAATFSAVKENSQNDFSAKLQSFQISGKFNSKVTDEKTLLPSMLAKLGFHHLDIDTKYEKLLFVEQFTIDSVLEKDIFNLYVKLKTFQIIYNHSEIYDFVNNNFLARQRSSEAQPMQLIHKQKSLPDHLDLDTAVQSNLRANQRREGGVLEWIMQRIVVKGCAELFNVSLLMKLEDEHIAMSVSHTRFLLEQIEEKRSNLYENKFLNLLLNQRQWSMELMVETLWSNLGNSINDTNNLKKTHSPGSPFFLGVSLVKLCSYANTTKLDISVHTFRTEYSMQLAEFVVKSMECLRQYRGIKPKNMSGQSHARPNAGLTLSVQPSQSSTSLRVSVKVKDITAYFVNHHNVYSLLSFSELNLSRSQSLTTLKLEEFQMAIMRSMTASSLCLTDFSDVFATCKMIRLEHEQVEGTMGKLSIYIPGNMEATWNSNLHMHLLTLVRDMQDLKTELAIPASSVKKTTPKEGFIVELSAERSTIFEIKFSDRHSIQIFVESLFFSQKERCIIYAENVFVKIDDQHIFTVKELDLQSVPRLEVLTQERQNFPGFQLPSNKVWVTTIGSFKAIFPYDHDFYNAVNGECTSHFKWLKMVHNYKKKPFTVDSPLPCDLVIKIKEFLLEISDDPFEVKLRDNYVLLVDEYLESLKRKALFDKKIGELCSERLLLPSGTIEGLYANLVKKNSEIYIQRSKKIRESGPVRTRLLAWIMTDVNIMAMADTSIHGYNNVTRIMREIDHESPWPEEGLEFSTLWCRGVNISCTEWKFMLRDFPQPMFCVKSMRLYGNLCGAEQMGSKRAKRDVFIDVGEPFGTDVIQRSMPSLKFYHDFDCELESCSYAFGACWEPVMAQCNLSFEKISAPSKDPSPPLPFWDKLRLLLHGRLTLIAKQFTILLHASLDPYNTTEEMELTWNNCGIVLTNAKIMFKGELNVTVRTASRYDDCRLLHFPNLKLTIKLKWVCLANPNDHHAVMPCAPDKLPEYSSNQVHDSFRAFRSLNLNIWISFETKPKAGEDLEVDIPSLVLYGSTLRWFESLQLILSGVTRPTRRGPVFNNVRPRKKPLSRHYKKANLQMCLHKFQVLYWMSHALQKGFQLNGRRVSFSSEHSLTLNPIDDGLIHRPRADWSTIYMNCELNDAEIWLKSILTEKMDSSSENLASAADAFKIVRFYFLSVAKVSYGREALIPTTATSTEEDVKAQSTTPTHKLVVYDLKGAWTKSNRDVAFALFDSFMKSQKLKNNLSTEAVKSYRKEGPNSAVLKHKRSDSTITLSSTNNEVLPISNPNASMKKAPAQIHATAMLQQLIAEADHKFNVYSDDHSTQSRELQLQGLQACSAQDIIHENWSISLVNSQVLLKGCETSGYVIISAAKAEILQREHRPVWRERSLISKTTWKGLLECMQYYATVSAGDNNSLLEKEIMWLTVDNIQDKDETVINNLPDISHLVGSGRSVGGVVSETVGAFLSDNSGGAQPVQLQRIVSKCKCEFFYVSYGDAIDPNSITEVPPPPSEELQSPWEKQDDPVDAFTLMHHDLDVCTNSLQYAMILDIVNNLLLYVEPQRKQAAEKLTRMRFQLQLHSTEDQKRPIQQKQTVIRSLLMKIRSLEKDTHMISKERIEDGDSLELRQEYDHVQQMIRESKEELNTFSEDLDMMLLCYKETQLSQLSKISNVRSDESVTMVRTNEICFKRAQWRLTETDGQIGIADLVLSAFLYTKKSKSDDSVEHLLELGNIRMENLLPREIYRDVLLATEIQKDMPVDTHKRVLRIFCREKAPVGGISVKEHFEINVAPITIAITKKFYSTMLKFCFPDRDASETEVSDELDDNASTSSASTTNLQAKSSTSSSTKRSGKGKKGAKDSEFYVKIEKDDVEKMKERAEKNKLFIYIKIPEVPVRVSYKGNKEKNLEDITDYSLVIPTLEYHNVTWTWLDLLLAMKSVSRRVIFSQAIKQKLHIHQRQPILSAGERATPQEAEDKAVMLFGNRLLNENRNQKKGVFKFASSGKRSGND
Protein: Chaperonin GroEL (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin-60) (Cpn60) (Q5ZXP3)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
Interaction partners:
- Co-chaperonin GroES
- Chaperone protein DnaK
- Protein GrpE
- Chaperone protein HtpG
- Chaperone protein DnaJ
- ATP-dependent protease ATPase subunit HslU
- Curved DNA binding protein DnaJ
- RNA polymerase sigma factor RpoH
- Lon protease
- ATP-dependent protease subunit HslV
Sequence:
MAKELRFGDDARLQMLAGVNALADAVQVTMGPRGRNVVLEKSYGAPTVTKDGVSVAKEIEFEHRFMNMGAQMVKEVASKTSDTAGDGTTTATVLARSILVEGHKAVAAGMNPMDLKRGIDKAVLAVTKKLQAMSKPCKDSKAIAQVGTISANSDEAIGAIIAEAMEKVGKEGVITVEDGNGLENELSVVEGMQFDRGYISPYFINNQQNMSCELEHPFILLVDKKVSSIREMLSVLEGVAKSGRPLLIIAEDVEGEALATLVVNNMRGIVKVCAVKAPGFGDRRKAMLQDIAILTKGQVISEEIGKSLEGATLEDLGSAKRIVVTKENTTIIDGEGKATEINARITQIRAQMEETTSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGIVAGGGVALIRAQKALDSLKGDNDDQNMGINILRRAIESPMRQIVTNAGYEASVVVNKVAEHKDNYGFNAATGEYGDMVEMGILDPTKVTRMALQNAASVASLMLTTECMVADLPKKEEGVGAGDMGGMGGMGGMGGMM
Protein: tRNA N(3)-cytidine methyltransferase METTL6 (EC 2.1.1.-) (Methyltransferase-like protein 6) (Q8BVH9)
Organism: Mus musculus (Mouse)
Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Ser), including tRNA(Ser)(UGA) and tRNA(Ser)(GCU). Interaction with SARS1/SerRS is required for N(3)-methylcytidine methylation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8TCB7}. Nucleus {ECO:0000250|UniProtKB:Q8TCB7}.
Interaction partners:
- 18S rRNA aminocarboxypropyltransferase
- Serine--tRNA ligase, mitochondrial
- tRNA methyltransferase 10 homolog B
- Serine--tRNA ligase, cytoplasmic
Sequence:
MASFQRKGLQARILSTEEEEKLKRDQALVSAFKQQKLEKEAQKNWDLFYKRNSTNFFKDRHWTTREFEELRSCREYEGQKLTLLEAGCGVGNCLFPLLEEDLNLFAYACDFSPRAVDYVKQHPLYNAERCKVFQCDLTRDDLLDHVPPESVDAVTLIFVLSAVHPEKMRLVLLNVYKVLKPGRSVLFRDYGLNDHAMLRFKAGSKLGENFYVRQDGTRSYFFTDEFLAQLFVDAGYEEVVNEYVFRETVNKKEGLCVPRVFLQSKFRKPPKDPAPTSDSASL
Protein: Trafficking protein particle complex subunit (Q9VA95)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|RuleBase:RU366065}. Golgi apparatus, cis-Golgi network {ECO:0000256|RuleBase:RU366065}.
Interaction partners:
- Trafficking protein particle complex subunit 2-like protein
- FI18195p1
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Probable trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 10
- Trafficking protein particle complex subunit 11
- Protein brunelleschi
Sequence:
MTIFNLYIFDKFGTLLHYAEWNRTKKSGITREEEAKLTYGMLFSIKSFVSKISPHDPKEGFLYYKTNRYALHYLETPSGLKFVLNTDTTAINVKELLQQLYAKVWVEFVVRDPLWTPGTVVTSELFQSKLDEFVRQSPIFGIRNI
Protein: Rab proteins geranylgeranyltransferase component A (Q6RFG0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MAAEDLPSQFDVVILGTGLTESVIAAACSRVGQSVLHLDRRNYYAGNWASFTFNGLLSWIEEYKNQQELQITESEQEWRSLIEDGEEAVPLNSVDSSISNLEVFCYASEEEEQEEETKDLLTCPNAETVSEETNSDSTETQDTVTSDDVTESNVKVQNEENEDSAPKEQLHASDISEHSQSVEEKQPNRSPADPPAELQKKITYQKLLKEGRRFNIDLVSKLMYSRGALVDLLIKSNVSRYAEFKNIGRILTCRNGKVEQVPCSRADVFASKQLTVVEKRMLMKFLTFCLDFEQHPEEYQDYSEKPFSEFLKNKKLTENLQDFVLLSIAMVTQQTLTEEGLKATQHFLRCLGRYGNTPFLFPLYGLGEIPQCFCRMCAVFGGIYCLRHSVQCLVVDKESNKVKAVIDTRGQKIGCSHFVVEDSYIREEQRESIDYRQISRAVLITDRSVLPSESDQQISLVTVPPVESSGPAVRMVELCSSSMTCMPGTCLVHLTCSSSGTAQQDLAPVVSQLFHIPTTPGEDPSEGTGEISKPAVLWVMYFNMRDTSAMDSSCYSLPSNVHVCTGPDAGLGSDYSIKLAESVFHCLLPDEEFCPPAPNPEDIIYDGDAPQAEGRGFDESNDTEANKSQAEEEGTTNETNPENSEAAEMDSVAQETTLDTNPPSEE
Protein: aspartate transaminase (EC 2.6.1.1) (Q7K221)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSIYADVPKGPAIEVFALTQAFKDDSNPNKVNLSVGAYRTDAGVPWVLPVVRKTEISIASDEQVNHEYLPVTGLETFTNAATELVLGADSPAIKENRAFGVQTISGTGALRVAADFLHTQLNRNVVYYSNPTWENHHKIFCDAGFTTVKSYRYWDQNKRELDFKNMLADLNDAPPGAVIILHACAHNPTGIDPTQEQWTELADLMEKKKLFPLFDSAYQGFASGDPDRDAWAARYFVQRGFELFICQSFAKNFGLYCERTGNLAVVQKNGATKAAVHSQLTLLIRGQYSNPPAYGARIVSKVLNTPELRKEWMASIQAMSSRIREMRTALRDKLVALGTPGTWDHIVNQIGMFSYTGLNESHVRVLIDQYHIYLLKTGRISMSGLNKGNVEYVAKAIHAAVTGSGESASCPCENKL
Protein: Formamidase (G5EB67)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Glutamine synthetase
- CN hydrolase domain-containing protein
- Nitrilase
- Cyanide hydratase
- Glutamine synthetase
- NADP-specific glutamate dehydrogenase
- NAD-specific glutamate dehydrogenase
- Nitrite reductase [NAD
- Formate dehydrogenase
- Cupin type-1 domain-containing protein
Sequence:
MGTKAIRTAVKVDLNKPAREQKGLHNRWHPDIPSYGTIANNEVVKIECLDWTGGQIKNDDSADDIKNVDLTQIHYLSGPFDIETAEPGDVLLVEIQDVQPFEDQPWGFTGVFARENGGGFLDEIYPEPAKAIWDFEGIFCSSRHIPHVRFAGLIHPGILGCAPSAEVLAEWNRREGELIAANTLGRDVAKPPEPSNVHAGSADGELAAKIGREGARTIPGRPEHGGNCDIKNLSRGSKVYLPVHVPGAKFSVGDLHFSQGDGEISFCGAIEMAGVITLKFTVIKDGMAKMAMKSPIFHPGPVEPQFGPGRYLTFEGFSVDEKGKQHYLDATVAYRQTCLRVIEYLRRYGYNDYQIYLLLSCAPVQGHIAGLVDIPNACTTLGVPMDIFDFDIRPEADAVKLDMGSCAFASK
Protein: Protein 4.1 (Band 4.1) (Erythrocyte membrane protein band 4.1) (D4A6Q4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTEKSLAAEAENSQHQKEEGEGATNSGQQESQLEEASQAAAAEGSNQGEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLLSSFLKRPKSQVSEEEGREVESEREKGEGEQKETELGTSLDEDVILKAPIAAPEPELKTDPSLDLHSLSSIETQPAQEEHREDPDSETKEGEGIEECSGTEVKEDPESRAEREPETSQKPIRRHRNMHCKVSLLDDTVYECVVETWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTVQSELGDYDPELHGVDYVSDFKLAPNQTRELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEHYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTLPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAAESTDRSPRPTSAPAIAQSQVMEGPGAPAKKAPKEAVKVEEKRGEEPAEPEPEPTEAWKDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQVPTGDGPPLVKTQTVTISDTANAVKSEIPTKDVPIVHTETKTITYEAAQTEDSNGDLDPGVLLTAQTITSETTSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEISEE
Protein: Translocated intimin receptor Tir (Secreted effector protein Tir) (B7UM99)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Function: Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion. In strain E2348/69, acts mainly via the host adaptor proteins NCK1 and NCK2. Once clustered and phosphorylated at Tyr-474, Tir binds to NCK proteins, which in turn bind and activate host WASL/N-WASP, leading to actin polymerization. Can also trigger an inefficient, NCK-independent pedestal formation. This pathway involves phosphorylation of Tyr-454 and probably a putative host adaptor. Acts also via direct binding to the host cytoskeletal protein alpha-actinin in a NCK- and phosphotyrosine-independent manner. This interaction may stabilize the pedestal, but is not essential for its formation.
Subcellular location: Secreted. Host cell membrane; Multi-pass membrane protein. Note=Secreted via the type III secretion system (T3SS). Released into the host cytoplasm via T3SS and then independently inserts into the plasma membrane from a cytoplasmic location. In host cells, localizes to the tip of the actin pedestal.
Interaction partners:
Sequence:
MPIGNLGNNVNGNHLIPPAPPLPSQTDGAARGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAATSETCLLGGFEVLHDKGPLDILNTQIGPSAFRVEVQADGTHAAIGEKNGLEVSVTLSPQEWSSLQSIDTEGKNRFVFTGGRGGSGHPMVTVASDIAEARTKILAKLDPDNHGGRQPKDVDTRSVGVGSASGIDDGVVSETHTSTTNSSVRSDPKFWVSVGAIAAGLAGLAATGIAQALALTPEPDDPTTTDPDQAANAAESATKDQLTQEAFKNPENQKVNIDANGNAIPSGELKDDIVEQIAQQAKEAGEVARQQAVESNAQAQQRYEDQHARRQEELQLSSGIGYGLSSALIVAGGIGAGVTTALHRRNQPAEQTTTTTTHTVVQQQTGGNTPAQGGTDATRAEDASLNRRDSQGSVASTHWSDSSSEVVNPYAEVGGARNSLSAHQPEEHIYDEVAADPGYSVIQNFSGSGPVTGRLIGTPGQGIQSTYALLANSGGLRLGMGGLTSGGESAVSSVNAAPTPGPVRFV
Protein: High-affinity lysophosphatidic acid receptor homolog (O43898)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MACNSTSLEAYTYLLLNTSNASDSGSTQLPAPLRISLAIVMLLMTVVGFLGNTVVCIIVYQRPAMRSAINLLLATLAFSDIMLSLCCMPFTAVTLITVRWHFGDHFCRLSATLYWFFVLEGVAILLIISVDRFLIIVQRQDKLNPRRAKVIIAVSWVLSWVLSFCIAGPSLTGWTLVEVPARAPQCVLGYTELPADRAYVVTLVVAVFFAPFGVMLCAYMCILNTVRKNAVRVHNQSDSLDLRQLTRAGLRRLQRQQQVSVDLSFKTKAFTTILILFVGFSLCWLPHSVYSLLSVFSQRFYCGSSFYATSTCVLWLSYLKSVFNPIVYCWRIKKFREACIELLPQTFQILPKVPERIRRRIQPSTVYCCNENQSAV
Protein: PX domain-containing protein LEC1 (Lipid-droplet ergosterol cortex protein 1) (Q06839)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:36354737}; Peripheral membrane protein {ECO:0000269|PubMed:36354737}. Lipid droplet {ECO:0000269|PubMed:36354737}. Note=Associated with endoplasmic reticulum-lipid droplet contact sites. {ECO:0000269|PubMed:36354737}.
Interaction partners:
- Uncharacterized protein YKR078W
- Eisosome protein SEG2
- Vacuolar import and degradation protein 27
Sequence:
MITQDTPALNPTEEHYLKRELLRCQLDYEIGKLNDQFALRKFGYPFSPNDPTAPQPISNNDSSPVLGGKGHFSVNYPMLSYVLQEFISTFPLLSTNLLVDEKFWQSKVQVFFEHFMSLGFSESYDREEASKRKKVSKKLSKVILLLFNSGVGSFQEQAYYNEDKFVLQSGQARKRSNIEKFAMPTRENLENLLTNESVFINGWDVNIISVFNKNSRKCTESVDNDKSSKSTPTSSPKSHAIKSFASTSKWMKNAFNNTINSTINSMPESSASLFSKLSLGVPSTKSKQSRKHHYFLIKIKKQDDDDQDNSNEENSNLDHHAGYFYVTRTYSDFKKLSHDLKSEFPGKKCPRLPHRNKKVTSMITKTEVLHNGQTKSAAREKIVNTFDTDLQSASESDNSSFLQTTNELSATETVLTEKETETLRKNILNEIKEEDNIDEDEYEEEGEGEESDFDEYKDASDSKINTLVGEKMRTSLRQYLRTLCKDAEVSQSSSIRRFFLSGPNLDIKDINPKIADDIRNRALIDVSNLENQIRFQQMALEKSLKLQDSMKDFKTSLLKDEKYLMSLLVEIKDNTKVEDLSPLLQDFVEWCKIYISSMIYQMFLGNDNSYELYTQIRRLHKLMPYTVMGQIMKFTNPIAIMRGMIELFMAQPFGGHSLLQTMFSTILTDDLKTQKVAIKELERKIAEMDPGASVVTKCLKDFVFNNDTKDEHDTKLFTMDAVNAESESMNMPVPLIVLMKSAAANLIPDEVVAGLIESYSSWKLQKEDTDALNVTSEDQSGIYFTHVKDLWQLYIKEHDKQLMRQLWQDPELTQMLKAIVTMIYEPMVKIFKVARMDVALKNFEKFMSDLIRLVDDVINGQLGVSTQFDVVEEIHNLVTKHQDAFFEFIHDVYLNDSEGIFEGFITWITTIVKFLQKSKFGGPSERIDFNKLICRDDIDIDVKLLKVQVNNVLNKKIGARKIYKKLLDLKVKQGTKQNNKHAAGILQKNWSDINSLVMPSSSGSFGLGDGDLVDLDLDTGDYDFLHKENEVELEKQYKDLLNLVVDESEIDKLRSQVFAQELKNYLEAQIAKK
Protein: Ras-related protein Rab-7b (Q8VEA8)
Organism: Mus musculus (Mouse)
Function: Controls vesicular trafficking from endosomes to the trans-Golgi network (TGN). Acts as a negative regulator of TLR9 signaling and can suppress TLR9-triggered TNFA, IL6, and IFNB production in macrophages by promoting TLR9 lysosomal degradation. Also negatively regulates TLR4 signaling in macrophages by promoting lysosomal degradation of TLR4. Promotes megakaryocytic differentiation by increasing NF-kappa-B-dependent IL6 production and subsequently enhancing the association of STAT3 with GATA1. Not involved in the regulation of the EGF- and EGFR degradation pathway.
Subcellular location: Late endosome {ECO:0000269|PubMed:19587007}. Lysosome {ECO:0000269|PubMed:17395780, ECO:0000269|PubMed:19587007}. Golgi apparatus {ECO:0000250|UniProtKB:Q96AH8}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q96AH8}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q96AH8}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:Q96AH8}.
Interaction partners:
- Rab-interacting lysosomal protein
- TBC1 domain family member 15
- TBC1 domain family member 17
- Ras-related protein Rab-7a
- FYVE and coiled-coil domain-containing protein 1
- Cytoplasmic dynein 1 heavy chain 1
- Cytoplasmic dynein 1 light intermediate chain 2
- Cytoplasmic dynein 1 light intermediate chain 1
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 2 heavy chain 1
Sequence:
MNPRKKVDLKLIIVGALGVGKTSLLHQYVHKTFFEEYQTTLGASILSKIIILDDTTLKLQIWDTGGQERFRSMVSTFYKGSDGCILAFDVTDPESFEALDIWRDDVLAKIIPMEQSYPMVVLGNKIDLEDRKVSQEVVHGWCKEKDMPYFEVSAKNDINVVQAFEVLASRALLRYQGTAENHLIDSIKLSPGQPKSRCC
Protein: Alanine--glyoxylate aminotransferase 2, mitochondrial (AGT 2) (EC 2.6.1.44) ((R)-3-amino-2-methylpropionate--pyruvate transaminase) (EC 2.6.1.40) (Beta-ALAAT II) (Beta-alanine-pyruvate aminotransferase) (EC 2.6.1.18) (D-3-aminoisobutyrate-pyruvate aminotransferase) (D-AIBAT) (D-beta-aminoisobutyrate-pyruvate aminotransferase) (Q9BYV1)
Organism: Homo sapiens (Human)
Function: Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:20018850, ECO:0000269|PubMed:24586340, ECO:0000269|PubMed:31818439}.
Interaction partners:
- Alanine--glyoxylate aminotransferase
- Glycine dehydrogenase
- D-amino-acid oxidase
- Cysteine sulfinic acid decarboxylase
- Acidic amino acid decarboxylase GADL1
- Glycine amidinotransferase, mitochondrial
- 4-trimethylaminobutyraldehyde dehydrogenase
- Peroxisomal sarcosine oxidase
- Aldehyde dehydrogenase, mitochondrial
- Alpha-aminoadipic semialdehyde dehydrogenase
Sequence:
MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQSLGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCHPKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLMARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSHCRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPKGFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAAVITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAKLRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQTFRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK
Protein: Conserved domain protein (Q726V4)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Conserved domain protein
- Capsule polysaccharide biosynthesis protein
Sequence:
MEIRDMSTNDDIRLLLCDPATLGEMTADGVHGRFALAGCVHNPDMFGAVEAAPGLYLLPETGWREGAALCVGEARPVGDDAGLGTTVSATQKGALRHRLEGAPCWKGKGYLLFFDTANDYRIIFPRPTREKLAEHYRAFESSPSLRNFNFEYHAFVLCRAIGRETLDGLDVLDVASGNGSFLSVLRGKGAHVTGFEPSESECREAAKSGLELINAPFTPAMLPEGRQYDVVIAGNIFEHVPDPVPFMERIRARLKPGGWLFFQIPNDFNAIQMKYLERSGSDAWFVAPPDHLNYWDVPQARRFVDAQGFDVVHEEAQFPIEMFLLMGMDYRKQPELGRQAHLMRCAFEDSFADDMGTLSRFYASLIGGGFGRDYVAVLRKRP
Protein: Activin receptor type-1 (EC 2.7.11.30) (Activin receptor type I) (Type I TGF B receptor) (Q90ZK6)
Organism: Gallus gallus (Chicken)
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 activin (By similarity).
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Bone morphogenetic protein 6.
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein 4
- Bone morphogenetic protein 7.
- Mothers against decapentaplegic homolog 5
- Mothers against decapentaplegic homolog.
- Mothers against decapentaplegic homolog
- Activin receptor type-2A
- Mothers against decapentaplegic homolog
- Bone morphogenetic protein 2
Sequence:
MALPVLLLLLALPSRSVQDEELKLNECVCEGMSCGNGDRCQGQQCFASLSINDGAKVYQKGCFQVYEQGKMTCKTPPSPDQAVECCQGYLCNMNITAKLPSSKGQTLQGEAAGYSMETLIIVILAPVVVLVIFSVVAVLIIRRIQKNHMERLNSRDAEYGTIEGLIASNVGDSTLADLLDHSCTSGSGSGLPFLVQRTVARQITLVECVGKGRYGEVWRGQWQGENVAVKIFSSRDEKSWFRETELYNTVLLRHENILGFIASDMTSRNSSTQLWLITHYHEMGSLYDYLQLTTLDTVSCLRIVLSIASGLAHLHIEIFGTQGKPAISHRDLKSKNILVKKNGQCCIADLGLAVMHSQSTNQLDVGNNPRVGTKRYMAPEVLDETIQADCFDSYKRVDIWAFGLVLWEVARRMVSNGIVEDYKPPFYDLVPNDPSFEDMRKVVCVDQQRPNIPNRWFSDPTLTSLAKLMKECWYQNPSARLTALRIKKTLTKIDNSLDKLKADC
Protein: NADH dehydrogenase (ubiquinone) complex I, assembly factor 6 homolog (dNDUFAF6) (Protein severe impairment of CI with lengthened youth) (Q9VYS5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (Complex I) at early stages. Interacts with cytosolic Hsp90 to chaperone the Complex I subunit ND-42 in the cytoplasm.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:23509070}. Cytoplasm, cytosol {ECO:0000269|PubMed:23509070}.
Interaction partners:
- GM10285p
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- Arginine-hydroxylase NDUFAF5, mitochondrial
- Hydroxymethylglutaryl-CoA synthase
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Mitochondrial ribonuclease P catalytic subunit
- RE26969p)
- Fatty acid hydroxylase domain-containing protein
- G1/S-specific cyclin-E
- rRNA biogenesis protein RRP5
Sequence:
MRRLVRNWNCRLLFNAKSGQEIVSHAGIHQEAKTNAIPREKKVIEADKNGYGAKHCMSLVEKYDYENYLCTLLLPRELRRAAFALRAFNVEVSRSVSGHQIEPQIAKMRLKFWHDSIDKCFEPDSQRSYVEDQPVLRELKHTVGSRKLNKVYLRRLVTARERPPTHAFESIRELEEYTEQTFSSLLLLLLEVGGVRDLNADHAASHLGKAQGIATLLRSIPLAGRQQAPCIPLEVLVLHGVSQERIIRSKSDDKGVEDCIFDVASAANTHLKLARQLHDKVPPQVRKIFLSAVATDAYLERLRRANFLLTHKSCVGRDTLLPARLFWKSLLNRF
Protein: Palustrin-2AJ1 (G3ETQ3)
Organism: Amolops jingdongensis (Chinese torrent frog)
Function: Displays broad-spectrum antibacterial activity against a range of Gram-positive and Gram-negative bacteria. Has low hemolytic activity, low cytotoxicity and low antioxidant activity.
Subcellular location: Secreted {ECO:0000269|PubMed:21816202}.
Interaction partners:
Sequence:
MFTLKKPLLVLLFLGTVSLSLCEQERAADDDEGEVIEEEVKRGFMDTAKNVAKNVAVTLIDKLRCKVTGGC