wanglab/gogpt-training-data huggingface dataset:
Protein: Dynamin-type G domain-containing protein (Q57XN3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRQLGSAVLACGNFNTPLKSLRSITLPTTSSLKRLLRRSQLGANCSTNRMCFATTTTVMMLNKFGLKSSGDESASDGYNGIYRMESGSNKSGQHALEGVEEDLNSLKRRVQQRYSDELRFLSHDSNRQPMVIVLGNHSAGKSTMINRLLGIELQRSGVSPTDDGFTVIQSGEDDITEDGPTAVSDPRYSFQELRKFGIHFVNKFKVKTRKLPATSLLPPGLMIVDTPGMIDTPIHLNDRTSVEGQLRGYDLFAVTRWFASRCDLIILMFDPANPGTTGETLDVLTKSLAGVEHKLLIVLNKSDMYDKAADFARVYGVLCWNLSKVLQMKDIPHIYTTYFLPRGDEFDDTRDAAGFAAFNKSSSTEETAVGGRKTASGSPQKESTSIIARDELLRQRSEVVSEILQAPLRRYDNLITELEEGVKRVLLAGRVCTEIVSTYRKMKVVATLAPPAIFCVSGLLLAVGGFTEVAALLASATAIAAVFAALKTRKSLVDFENDVLTNIDVIFDRLYVRHEKTMDTQLRWKDTVKPEILEFLNSSSVAGRQSIASLPTLSKKSQDSIISILKNDIPQLRVRVANYKVKNFLRAGERQPLGNEVRVK
Protein: Hexokinase-6 (EC 2.7.1.1) (Hexokinase-2) (Q8LQ68)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Fructose and glucose phosphorylating enzyme. Functions as glucose sensor for plant growth and photosynthesis.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- phosphoglucomutase
- phosphoglucomutase
- Os08g0545200 protein
- Probable glucosamine 6-phosphate N-acetyltransferase 2
- Os05g0164100 protein
- mannose-6-phosphate isomerase
- Phosphomannomutase
- Mannose-6-phosphate isomerase
- Xylose isomerase
- Os01g0952600 protein
Sequence:
MGKGTVVGTAVVVCAAAAAAVGVAVVVSRRRRSKREAEEERRRRAAAVIEEVEQRFSTPTALLRGIADAMVEEMERGLRADPHAPLKMLISYVDNLPTGDEHGLFYALDLGGTNFRVIRVQLGGREKRVVSQQYEEVAIPPHLMVGTSMELFDFIAAELESFVKTEGEDFHLPEGRQRELGFTFSFPVHQTSISSGTLIKWTKGFSINGTVGEDVVAELSRAMERQGLDMKVTALVNDTVGTLAGGRYVDNDVAAAVILGTGTNAAYVEHANAIPKWTGLLPRSGNMVINMEWGNFKSERLPRSDYDNALDFESLNPGEQIYEKMISGMYLGEIVRRILLKLAHDASLFGDVVPTKLEQRFILRTPDMSAMHHDTSHDLKHLGAKLKDILGVADTSLEARYITLHVCDLVAERGARLAAAGIYGILKKLGRDRVPSDGSQKQRTVIALDGGLYEHYKKFRTCLEATLADLLGEEAASSVVVKLANDGSGIGAALLAASHSQYASVE
Protein: Sphingosine 1-phosphate receptor 2 (S1P receptor 2) (S1P2) (AGR16) (Endothelial differentiation G-protein coupled receptor 5) (G-protein coupled receptor H218) (Sphingosine 1-phosphate receptor Edg-5) (S1P receptor Edg-5) (P47752)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effects on most types of cells and tissues. Receptor for the chemokine-like protein FAM19A5. Mediates the inhibitory effect of FAM19A5 on vascular smooth muscle cell proliferation and migration.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O95136}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- RCG53912, isoform CRA_a.
- Sphingosine kinase 1
- Reticulon-4
- Apolipoprotein M
Sequence:
MGGLYSEYLNPEKVQEHYNYTKETLDMQETPSRKVASAFIIILCCAIVVENLLVLIAVARNSKFHSAMYLFLGNLAASDLLAGVAFVANTLLSGPVTLSLTPLQWFAREGSAFITLSASVFSLLAIAIERQVAIAKVKLYGSDKSCRMLMLIGASWLISLILGGLPILGWNCLDHLEACSTVLPLYAKHYVLCVVTIFSVILLAIVALYVRIYFVVRSSHADVAGPQTLALLKTVTIVLGVFIICWLPAFSILLLDSTCPVRACPVLYKAHYFFAFATLNSLLNPVIYTWRSRDLRREVLRPLLCWRQGKGATGRRGGNPGHRLLPLRSSSSLERGLHMPTSPTFLEGNTVV
Protein: Transcription factor NF-E2 45 kDa subunit (Leucine zipper protein NF-E2) (Nuclear factor, erythroid-derived 2 45 kDa subunit) (p45 NF-E2) (Q07279)
Organism: Mus musculus (Mouse)
Function: Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron.
Subcellular location: Nucleus, PML body. Cytoplasm {ECO:0000250}. Note=The sumoylated form locates to the nuclear bodies PML oncogenic domains (PODs). Translocated to the cytoplasm through interaction with ITCH (By similarity). {ECO:0000250}.
Interaction partners:
- Transcription factor MafG
- Transcription factor MafK
- Transcription factor Maf
- Transcription factor MafF
- Erythroid transcription factor
- Kelch-like ECH-associated protein 1
Sequence:
MPPCPPQQNRNRLSQLPVGELGEMELTWQEIMSITELQGLNVPSETSFEPQAPTPYPGPLPPPTYCPCSIHPDAGFSLPPPSYELPASTPHVPELPYSYGNVAIPVSKPLTLSGLLNEPLPDHLALLDIGLPVGQPKPQEDPESDSGLSLNYSDAESLELEGMEAGRRRSEYVDMYPVEYPYSLMPNSLAHPNYTLPPTETPLALESSSGPVRAKPAVRGEAGSRDERRALAMKIPFPTDKIVNLPVDDFNELLAQYPLTESQLALVRDIRRRGKNKVAAQNCRKRKLETIVQLERELERLSSERERLLRARGEADRTLEVMRQQLAELYHDIFQHLRDESGNSYSPEEYVLQQAADGAIFLVPRGTKMEATD
Protein: Coagulation factor VIII (D3ZEB1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- von Willebrand factor
- Vitamin K-dependent protein C
- Coagulation factor IX
- Prothrombin
- Coagulation factor X
- Coagulation factor XI
- Vitamin K-dependent protein S
- Antithrombin-III
- Platelet glycoprotein Ib alpha chain
- Protein-tyrosine sulfotransferase 1
Sequence:
MRAARGLCFFLSLCALCSCATRKYYLGAVELPWDYVSGGASGAQRSDSRFPPGTPAPSAHVVHTKTVFVEYMDRFFHTAKPRPLWMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGMSFWKASEGAAYDDHSSPAEKDDDKVLPGESHTYAWQVLGESGPMASDPPCLTYAYLSHVDLVRDLNSGLVGALLVCKEGRLSADRTRMPPHFVLLFAVFDEGRSWHAATRDPASTEAQPTVHTVNGYTNRTLPGLTGCRGTSVYWHVMAVGTTPDIHSILLEGHTFSVRSHRQASLEISPMTLLTAQTWLMDLGRFLLFCHISSHRHGGMEAYVQVDNCPEAPQGQGKRDEDTEDYDDLDSEMDVFTWDPDAAPFVQVRSAAKRHPKTWVHYIAAEEGDWDYAPAAATLEDGSLRNRYLGRGPGRIGSKYKKVRFVAYTDGTFHTREATPREAGLLGPLLYGEVGDSLLIVFKNRASRAYNIHPHGIRDVGAVHAGRLPRGVKHVKDLPIRPGETFKYRWTLTAEDGPARSDARCVTRYYASAVDPERDLASGLIGPLLICCKESVDQRGNQMMSDERNVILFSVFDENRSWYISENMRRFLPDEAHVQLQDPEFEASNLMHSINGYVFDSLELRVCLHEVAAWHVLSVGAQTDFLSVFFSGHTFRHRAVYADTLTVFPHSGVTVFMSMDNPGVWVLGCHNPDFRESGMTALLKVSSCDEGVSDYYGETYEGVLAPLANDNAVDPRSFSQNSNHLHSRKKKSNTPMRFPLSHPTQHGSFWSDSQGDVHDAVHRAHSPAAAHSNEGPAEAAQLEPKPHPGEKMALPPSWLRAKRSLVTTMEAKRKKLDLQVQVSGLPDDRTTAVVAPDDPMAACKKAGSSGFPDESSPAALGKKMYPRIRPHGPLSIIEGNRDSNSSDSTLMYRLGSPPGDATSWTENRRGLGEKRSHRVAFLARGNTLLSDVDEKSHAPGPTSVGNSTAAVQDTILEICSEILEVTPPIHDRILSDKSATYLRPHRTPDRITSTERKDIRHKKDGDLVPQDADDTSAPFSEAPFLSESTDWLKEANGDNSAKPEQEPSPEQLVYLMYIKCMENQSFSSEKNKMIAGQGGFTKNTGLEDTVFPRKTSVFLTTVAKRQESGRHNQENIPQAVTEKEAPIEEKGALPQVHIATGSKNFPRDMFVLGTGQNINLHEETYVPVHKNVPWTRNPTDTRQIPMVHFFKKRKEEETNSGGLVNKTRETVRNYPSQKNSVARRREQASGRIKASARWLPDVNRSIQSLLKQIDHRKERKKFIIESRSADSSGTKSPTQTNHSPSHVVKMSAFPPRDIRRIESRDSSQVWVSSYAYDFETGSSRIRESSPFLNETETDNPSLAVPPRERFVRRGRFASPEKVNTHSAPCDKPENVVSSEPVSPGEAVTVALPPHVSTQEEEPLPAGSSCERRGHVDLFLEISLQRTRGPVERSRGRRSGGDTEGHTENPGKTPSPLPQMPKDQRGSEAGYPKICRWRDGTVLPPRPHNLSLGAKKKPNLPRREATRVEQGEAPSLVSPEPLVLRRRPREASTLLPGGEMREDDGDGVTAEYDDDDDVMAEYDDDAVTVDTPEDFDIYGEEAGQGPRGFQQKTRHYFIAAVEELWDYGVRVSPGALGDRAWSGDAARFRKVVFREFTDGSFTQRVHRGELDAHLGLLGPYIRAEVEDNIVVTFRNQASRPYSFYSSLVSYPEADGGAAPRSNFVRPNETKTYFWRVRPHMAPTDGEFDCKAWAYFSDVDLERDLHSGLIGPLLVCHASTLHPSHARPLAVQEFALLFAVFDETKSWYCAENLDRKCRPPRGTPAGDPAWREEYRFHAVNGYVADALLGLVMAEGRRTRWHLLSMGDPGHAQSVHFSAHSVTVRDGGEHRTAVCNLYPGVFTTVEMLPSRAGIWRVESLVGEHLQAGMSALFLVYSTRCQVPLGMASGYIRDSQITASGYHGLWTPQLARLHNAGSVNAWSAKEPFAWIKVDLLAPMILHGIETQGARHRLSSLYVSQFIIMYSLDGKQWLSYRGNSTGSLMVFFGNVDASTVRHNRFDPPIVARYIRVHPTHASIRTALRMELLGCDLNSCSAPLGMESGWISDTQVTASSHLSTTFSAWPPALARLHLRGGANAWRPQVNDPTQWLQVDLQRTVKVTGVVTQGARSLLTAMFVKKFLVSTSQDGRHWTHVLQDGKVKVFQGNRDASTPMVNSLHPPRFTRYLRIHPQVWERQIALRLEILGCEAQQLD
Protein: Solute carrier family 5 member 4 (D3ZIS0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9ET37}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPAMGTALPRAMASTASVSTSTGSSELSSLSDNINNPADISVIVIYFVVVMAVGVWAMVKTNRSTVGGFFLAGRSMTWWPMGASLFASNIGSGHFVGLAGTGAATGIAVTAFESHSFALLLVLGWFFVPIYIKAGVMTMPEYLRKRFGGKRLQIYLSVLSLFICVILTISADIFSGAIFIKLALGLDLYLAIFILLAITAVFTITGGLASVIYTDTLQAIIMLVGSFILMIYAFVEVGGYESFTEKYMNAIPSVVEGDNLTISPKCYTPQPDSFHIFRDAVTGDIPWPGTAFGMPITALWYWCINQVIVQRCLCGKNMSHVKAACIVCGYLKLLPIFFMVMPGMISRILYTDMVACVVPSECVKQCGVDVGCTNYAYPMLVLKLMPMGLRGLMLSVMLASLMSSLTSIFNSASTLFTMDLYTKIRKKASERELLIAGRLFVSVLIVTSILWVPIVEVSQGGQLIHYTEAISSYLGPPIAAVFLVAIFCKRVNEQGAFWGLMVGLVLGLIRMIAEFSYGTGSCLAPSSCPKVICGVHYLYYAIILFFVSILVILGVSYLTKPIPDVHLYRLCWSLRNSEEERIDLDAEDREENEADARTEEDQTEKPRGCLKKTYDLCCGLQRAEPKLTKEEEEALKKKLTDTSEKPFWRTVVNVNVIVLLAVAAFFYGYFA
Protein: Protein translocase subunit SecY (P9WGN3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01465}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01465}.
Interaction partners:
- Protein translocase subunit SecE
- Probable protein-export membrane protein SecG
- Protein translocase subunit SecA 1
- Protein translocase subunit SecA 2
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL5
- Membrane protein insertase YidC
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL22
Sequence:
MLSAFISSLRTVDLRRKILFTLGIVILYRVGAALPSPGVNFPNVQQCIKEASAGEAGQIYSLINLFSGGALLKLTVFAVGVMPYITASIIVQLLTVVIPRFEELRKEGQAGQSKMTQYTRYLAIALAILQATSIVALAANGGLLQGCSLDIIADQSIFTLVVIVLVMTGGAALVMWMGELITERGIGNGMSLLIFVGIAARIPAEGQSILESRGGVVFTAVCAAALIIIVGVVFVEQGQRRIPVQYAKRMVGRRMYGGTSTYLPLKVNQAGVIPVIFASSLIYIPHLITQLIRSGSGVVGNSWWDKFVGTYLSDPSNLVYIGIYFGLIIFFTYFYVSITFNPDERADEMKKFGGFIPGIRPGRPTADYLRYVLSRITLPGSIYLGVIAVLPNLFLQIGAGGTVQNLPFGGTAVLIMIGVGLDTVKQIESQLMQRNYEGFLK
Protein: Protein real-time (Q9VMD6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15700158}.
Interaction partners:
- Protein preli-like
Sequence:
MVQKFQSPVRVYKYPFELVMKAYERRFPTCPQMPIVLDCEVIKDESLEDGAKRNTSRRCKLAVDAPYIFKKLIGVDHVYFLQHNFLDLANRTLSIEAVNESFSSRIEIFERCRYYAHPDNSEWTCFDQSATLDIKNFFGFEHSMEKMGMKQYTQTTLKGKEIIEFFIGQLREEGITHVERWTSPSDATKSPTLDQASDQQHSILLDGDFIARSLGQLSPMQESKLLELRKMLDGVDDLERVPSYQTILRFLAARDWHVSQAYAMLCDSLRWRREHRIDALLAEYSKPAVVVEHFPGGWHHLDKDGRPVYILRLGHMDVKGLLKSLGMDGLLRLALHICEEGIQKINESAERLEKPVLNWSLLVDLEGLSMRHLWRPGIKALLNIIETVERNYPETMGRVLVVRAPRVFPIAWTIVSAFIDEHTRSKFLFYGPDCAHMKDGLAQYLDEEIVPDFLGGPCKTMIHEGGLVPKTLYKMNSLEDHDDEVTAELPTTAAAQALVPGKRLSANQQHDHRNLYKSVDLKAGFAHELLIRNEDPKSVLTWDFDVMRNDLHFTLYRVTQELPEKNDSAVSYFDLQDFVEGVNYFREEPTLICRHKESVQGSHVMHHNDSYLMHWFSPSGAQLNVFYEVLSSANYKGSMTSLQSAFSSNSSAASSVQSR
Protein: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC 2.1.1.14) (Cobalamin-independent methionine synthase) (Methionine synthase, vitamin-B12 independent isozyme) (Q8CWX6)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Interaction partners:
- Hcy-binding domain-containing protein
- homocysteine desulfhydrase
- S-adenosylmethionine synthase
- S-ribosylhomocysteine lyase
- O-acetylhomoserine sulfhydrylase
- S-methylmethionine:homocysteine methyltransferase
- Methionine--tRNA ligase
- cysteine-S-conjugate beta-lyase
- GAF domain-containing protein
- Cysteine synthase
Sequence:
MTKVSSLGYPRLGENREWKKLIEAYWAGKVSKNDLFAGAKELRLDFLKKQLNAGLDLIPVGDFSLYDHILDLSVQFNIIPKRFAKEPIDIDLYFAIARGNKENVASSMKKWFNTNYHYIVPEWSKQRPKLNNNRLLDLYLEAREVVGDKAKPVITGPITYVALSTGVEDFTAAVKSLLPLYKQVFTELVKAGASYIQVDEPIFVTDEGKDYLQAAKAVYAYFAKEVPDAKFIFQTYFEGLIDSQVLSQLPVDAFGLDFVYGLEENLEAIKTGAFKGKEIFAGVIDGRNIWSSDFVKTSALLETIEEQSAALTIQPSCSLLHVPVTTKNETDLDPVLRNGLAFADEKLTEVKRLAEHLDGREDPAYDLHIAHFDALQAADFRNVKLEDLSRVATKRPSDFAKRRDIQQEKLHLPLLPTTTIGSFPQSREIRRTRLAWKRGDISDAEYKQFIQAEIERWIRIQEDLDLDVLVHGEFERVDMVEFFGQKLAGFTTTKFGWVQSYGSRAVKPPIIYGDVQHLEPITVEETVYAQSLTDRPVKGMLTGPITITNWSFERTDIPRDQLFNQIGLAIKDEIKLLENAGIAIIQVDEAALREGLPLRKSKQKAYLDDAVHAFHIATSSVKDETQIHTHMCYSKFDEIIDAIRALDADVISIETSRSHGDIIESFETAVYPLGIGLGVYDIHSPRVPTKEEVVANIERPLRQLSPTQFWVNPDCGLKTRQEPETIAALKVLVAATKEVRQKLGN
Protein: Bomanin Short 3 (Bomanin-3) (Immune-induced peptide 3) (DIM-3) (DIM3) (Q9V8G0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Secreted immune-induced peptide induced by Toll signaling. Has a role in resistance bacterial and fungal infections. The strength of antimicrobial activity appears to correlate with the overall level of expression. Has no activity against the fungus C.glabrata in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:29920489, ECO:0000269|PubMed:9736738}.
Interaction partners:
- Daisho1
- Bomanin Short 2
- Bomanin Short 1
- Bomanin Tailed 2
- Bomanin Bicipital 1
- Bomanin bicipital 2, isoform A
- Dorsal-related immunity factor Dif
- Embryonic polarity protein dorsal
- GNBP-like 3
- demerged
Sequence:
MKFLSLAFVLGLLALANATPLNPGNVIINGDCRVCNVRA
Protein: NAC transcription factor 25 (AtNAC025) (Q8GY42)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor of the NAC family. May be associated with anther development and pollen production (Probable). Required for normal seed development and morphology.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 7b
- Expansin-A2
Sequence:
MENMGDSSIGPGHPHLPPGFRFHPTDEELVVHYLKKKADSVPLPVSIIAEIDLYKFDPWELPSKASFGEHEWYFFSPRDRKYPNGVRPNRAATSGYWKATGTDKPIFTCNSHKVGVKKALVFYGGKPPKGIKTDWIMHEYRLTDGNLSTAAKPPDLTTTRKNSLRLDDWVLCRIYKKNSSQRPTMERVLLREDLMEGMLSKSSANSSSTSVLDNNDNNNNNNEEHFFDGMVVSSDKRSLCGQYRMGHEASGSSSFGSFLSSKRFHHTGDLNNDNYNVSFVSMLSEIPQSSGFHANGVMDTTSSLADHGVLRQAFQLPNMNWHS
Protein: Large ribosomal subunit protein bL12 (50S ribosomal protein L7/L12) (O51351)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Interaction partners:
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein bL25
- Large ribosomal subunit protein bL36
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein bL33
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein bL17
Sequence:
MALNKEDILTWLEGAKTMEVVDLVTAIEEKFGVTAAVAAGVGGAVSVGSADSEEQTEFDVILMSFGDSKINVIKEVRAITGLGLGEAKALVEAAPKAIKEGLSKSDAEELKKKLEAVGAKVEVK
Protein: Putative small GTPase superfamily, P-loop containing nucleoside triphosphate hydrolase (ROP small G protein) (Rho-like GTP-binding protein) (B2MVQ1)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Interaction partners:
- Guanine nucleotide exchange factor, putative
- Dol-P-Glc:Glc
- TIME FOR coffee-like protein, putative
- LSD1-type zinc finger protein
- Transmembrane protein, putative
- Myosin heavy chain-like protein
- Actin-related protein 2
- Kinesin-like calmodulin-binding protein
- Kinesin-like calmodulin-binding protein
- RING-type E3 ubiquitin transferase
Sequence:
MASTASRFIKCVTVGDGAVGKTCMLICYTSNKFPTDYIPTVFDNFSANVVVEGITVNLGLWDTAGQEDYNRLRPLSYRGADVFVLAFSLVSRASYENVFKKWIPELQHFAPGVPVVLVGTKLDLREDRHYLADHPGMVPVTTEQGEELRKQIGATYYIECSSKTQQNVKGVFDAAIRMVIKPPQKQHEKRKKARRGCFLNVLCGRSIVRHK
Protein: Glutathione S-transferase U15 (AtGSTU15) (EC 2.5.1.18) (GST class-tau member 15) (Q9LQ48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase F4
- Glutathione S-transferase F11
- Glutathione S-transferase F13
- Glutathione S-transferase F14
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase DHAR2
- Cytochrome c oxidase subunit 5b-2, mitochondrial
- Glutathione S-transferase DHAR3, chloroplastic
- Glutathione synthetase, chloroplastic
Sequence:
MGEREEVKLLGTWYSPVVIRAKIALRLKSVDYDYVEEDLFGSKSELLLKSNPIFKKVPVLIHNTKPVCVSLNIVEYIDETWNSSGSSILPSHPYDRALARFWSVFVDDKWLPTLMAAVVAKSEEAKAKGMEEVEEGLLQLEAAFIALSKGKSFFGGETIGFIDICLGSFLVLLKAREKLKNEKILDELKTPSLYRWANQFLSNEMVKNVVPDIDKVAKFIEEFEDRAQYIRCF
Protein: Nup98 (A1YK27)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
Sequence:
KLSSEADATRATNPAAQQAVLDLTSNQYKISTSNNPAPMKVKTLGSTLNRKSLFDGLEEFDASVEGFNLKPSAKRLVIKPKVKSVEGGNPSSSIGSAPNTPQSRPKGATPNKERESFSGAIPSEPLPPAGNSPGATNGRESQDNGRRESWLHPNNLEKVRQHNIQTGMDQGSPHNSTLNELVPRKPLDTYRPSSTVRLSVSTIPENPFEDQSSTIARRETFTSQQANESVLSNRSNEAEDSAANRSRLAIEAAAAEAADDESHPTGIVLRRVGYYTIPSLDDLRSYLAEDGSCVVPNFTVGREGYGNVFFGKEMDVAGLNLDEIVHFRNKEIIIYPDDENKPPIGQGLNRDAQVTLDQVWPLDKTKHEAIKDPQRLLEMDWEGKLRRVCDKNDTRFIEYRPETGSWVFRVKHF
Protein: Beta-ketodecanoyl-[acyl-carrier-protein] synthase (EC 2.3.1.207) (Q9HYV7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the condensation of octanoyl-CoA, obtained from exogenously supplied fatty acids via beta-oxidation, with malonyl-[acyl-carrier protein], forming 3-oxodecanoyl-[acyl-carrier protein], an intermediate of the fatty acid elongation cycle that can then be extended to supply all of the cellular fatty acid needs. The enzyme thereby shunts fatty acid degradation intermediates from the beta-oxidation pathway into de novo fatty acid biosynthesis.
Interaction partners:
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Probable sigma-70 factor, ECF subfamily
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Malonyl CoA-acyl carrier protein transacylase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- Biotin carboxylase
- Aspartate aminotransferase
- Enoyl-[acyl-carrier-protein] reductase
Sequence:
MESFNTFVRQYNDQHAEAIAKGELEALAESSSAFIEKASGIKSRFVMNKEGILDPQRMVPYLPERSNDEWSILCEMAVAAAREALQRAGRSAADIDGVIVACSNLQRAYPAIAVEVQAALGIQGYGYDMNVACSSATFGIQAATTAIQTGQARAILMVNPEICTGHLNFRDRDSHFIFGDACTAVIVERADLAVSKHQFDIVSTRLLTQFSNNIRNNFGFLNRADESGIGKRDKLFVQEGRKVFKDVCPMVAELIGEHLAANEIQVAEVKRFWLHQANLNMNLLITRKLLGRDAEAHEAPVILDSYANTSSAGSVIALHKHQDDLPSGAIGVLSSFGAGYSIGSVILRKH
Protein: Adenylate cyclase type 7 (EC 4.6.1.1) (ATP pyrophosphate-lyase 7) (Adenylate cyclase type VII) (Adenylyl cyclase 7) (P51829)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of cAMP in response to activation of G protein-coupled receptors (Probable). Functions in signaling cascades activated namely by thrombin and sphingosine 1-phosphate and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G alpha protein with GNA13. Also, during inflammation, mediates zymosan-induced increase intracellular cAMP, leading to protein kinase A pathway activation in order to modulate innate immune responses through heterotrimeric G proteins G(12/13). Functions in signaling cascades activated namely by dopamine and C5 alpha chain and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G protein with G beta:gamma complex (By similarity). Functions, through cAMP response regulation, to keep inflammation under control during bacterial infection by sensing the presence of serum factors, such as the bioactive lysophospholipid (LPA) that regulate LPS-induced TNF-alpha production. However, it is also required for the optimal functions of B and T cells during adaptive immune responses by regulating cAMP synthesis in both B and T cells.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase catalytic subunit beta
- Rap guanine nucleotide exchange factor 4
- cAMP-dependent protein kinase catalytic subunit alpha
- Guanine nucleotide-binding protein G
- Protein kinase C delta type
- Rap guanine nucleotide exchange factor 3
- Ectonucleoside triphosphate diphosphohydrolase 2
- Cannabinoid receptor 1
- Cancer-related nucleoside-triphosphatase homolog
Sequence:
MPAKGRYFLNEGDEGPDQAALYEKYRLTSLHGPLLLLLLLVAAATCIALISIAFSHEDLRRHQVVLGTAFLMLTLFVALYVLVYVECLVQRWLRALALLTWACLMVLGSVLMWDSLENEAHAWEQVPFFLFVVFVVYALLPLSRRAAIVAGVTSTVSHLLVFGAVTRAFQTSMSSTQLGLQLLANAVILLGGNFTGAFHKHQLQDASRDLFIYTVKCIQIRRKLRVEKRQQENLLLSVLPAHISMGMKLAIIERLKEGGDRHYMPDNNFHSLYVKRHQNVSILYADIVGFTRLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDICEAIKQVREATGVDISMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLNHLDKAYEVEDGHGEQRDPYLKEMNIRTYLVIDPRSQQPPPPSHHLSKPKGDATLKMRASVRVTRYLESWGAARPFAHLNHRESVSSSETPISNGRRQKAIPLRRHRAPDRSASPKGRLEDDCDDEMLSAIEGLSSTRPCCSKSDDFHTFGPIFLEKGFEREYRLVPIPRARYDFACASLVFVCILLVHLLVMPRMATLGVSFGLVACLLGLVLSFCFATEFSRCFPSRSTLQAISESVETQPLVRLVLVVLTVGSLLTVAIINMPLTLNPGPEQPGDNKTSPLAAQNRVGTPCELLPYYTCSCILGFIACSVFLRMSLELKAMLLTVALVAYLLLFNLSPCWHVSGNSTETNGTQRTRLLLSDAQSMPSHTLAPGARETAPSPSYLERDLKIMVNFYLILFYATLILLSRQIDYYCRLDCLWKKKFKKEHEEFETMENVNRLLLENVLPAHVAAHFIGDKAAEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKEGLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSAPSGHENQDLERKHVHIGVLVEFSMALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
Protein: Mitochondrial RNA binding protein (Q381A0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitochondrial RNA binding complex 1 subunit
- Mitochondrial RNA binding complex 1 subunit
- REH2-associated factor 2
Sequence:
MLLSTRARQGNALLLGVSYGGGVRTLSDTRGVGWSLKVSARLHVGMNVCSVSSVFLQSRSFYIFCTLCCFCSRHQPQSILPSFLLTTLVTALAPVLHRRVKLRVHIFCGVMSNPFEKVARGIAFKMRSKVHKQGYSNTVMAQQARRLSPTGLLAMERLTELTALQQRHQCTFDPALRSKATQILRTLPLLSIDEDPYFTHTQRALRLAAYFGAVDLPVTYALINQHTKNAFMLDAFSMASFFYTLAKLKHPQTKEIVGILLPRLREVAPELIAREAVHILRLLCSIQMADAQLVKVVTETVVATAADVPLRDARQCAFILSETFPEEAQRILGAVEHRLCDDIDMNADANEVKTTILDVCRVVSATCKGPRRLLNSVARRSMELLPQLTPLDVAFVLKAFHLSSYRHLRLLRVLSSSLAASFPTSNVTKEHGLAASIVVQSLAHFYLSGCEEVVVTLVNASVNVLEGLNLALTLLACVRLRCVSPGVDPAVDALCSGAPMRRYVHNAHSMQVTSRILYGLAHAGRCRSDEEVAIVLPLLKSVVRTPGALRDDCRGFLLDAVTALGADGECSNDALQEQVRKVYERLSQDGGK
Protein: Heat shock protein homolog SSE1 (Chaperone protein MSI3) (P32589)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Hsp70 nucleotide exchange factor FES1
- Heat shock protein SSA1
- Protein SIS1
- Heat shock protein STI1
- Mitochondrial protein import protein MAS5
- HSP70 co-chaperone SNL1
- ATP-dependent molecular chaperone HSP82
- Heat shock protein homolog SSE2
- ATP-dependent molecular chaperone HSC82
- Heat shock protein 104
Sequence:
MSTPFGLDLGNNNSVLAVARNRGIDIVVNEVSNRSTPSVVGFGPKNRYLGETGKNKQTSNIKNTVANLKRIIGLDYHHPDFEQESKHFTSKLVELDDKKTGAEVRFAGEKHVFSATQLAAMFIDKVKDTVKQDTKANITDVCIAVPPWYTEEQRYNIADAARIAGLNPVRIVNDVTAAGVSYGIFKTDLPEGEEKPRIVAFVDIGHSSYTCSIMAFKKGQLKVLGTACDKHFGGRDFDLAITEHFADEFKTKYKIDIRENPKAYNRILTAAEKLKKVLSANTNAPFSVESVMNDVDVSSQLSREELEELVKPLLERVTEPVTKALAQAKLSAEEVDFVEIIGGTTRIPTLKQSISEAFGKPLSTTLNQDEAIAKGAAFICAIHSPTLRVRPFKFEDIHPYSVSYSWDKQVEDEDHMEVFPAGSSFPSTKLITLNRTGDFSMAASYTDITQLPPNTPEQIANWEITGVQLPEGQDSVPVKLKLRCDPSGLHTIEEAYTIEDIEVEEPIPLPEDAPEDAEQEFKKVTKTVKKDDLTIVAHTFGLDAKKLNELIEKENEMLAQDKLVAETEDRKNTLEEYIYTLRGKLEEEYAPFASDAEKTKLQGMLNKAEEWLYDEGFDSIKAKYIAKYEELASLGNIIRGRYLAKEEEKKQAIRSKQEASQMAAMAEKLAAQRKAEAEKKEEKKDTEGDVDMD