wanglab/gogpt-training-data huggingface dataset:
Protein: Sphingosine kinase 2 (M0QXX5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPPPPPLAASTPLLHGEFGSYPARGPRFALTLTSQALHIQRLRPKPEARPRGGLVPLAEVSGCCTLRSRSPSDSAAYFCIYTYPRGRRGARRRATRTFRADGAATYEENRAEAQRWATALTCLLRGLPLPGD
Protein: 40S ribosomal protein S25 (Q8ILN8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 60S ribosomal protein L7a
- Small ribosomal subunit protein uS5
- 60S ribosomal protein L38
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL4
- 60S ribosomal protein L19
- 60S ribosomal protein L35, putative
- Large ribosomal subunit protein eL43
- 40S ribosomal protein S3
- 60S ribosomal protein L18a
Sequence:
MPPKERKTKEQIAAAAAASGRTKKKKWGKGKNKEKLNHAVFIDKSLHSKILECKNMKVITPSAIAEKYKVNLSVARAVINHLADKKLIAEVCVQSHSQKLYTKVA
Protein: Large ribosomal subunit protein bL12 (50S ribosomal protein L7/L12) (P9WHE3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 uL10
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL1
Sequence:
MAKLSTDELLDAFKEMTLLELSDFVKKFEETFEVTAAAPVAVAAAGAAPAGAAVEAAEEQSEFDVILEAAGDKKIGVIKVVREIVSGLGLKEAKDLVDGAPKPLLEKVAKEAADEAKAKLEAAGATVTVK
Protein: Alpha-mannosidase 2 (EC 3.2.1.114) (Golgi alpha-mannosidase II) (AMan II) (Man II) (Mannosidase alpha class 2A member 1) (Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase) (P28494)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:1885615, ECO:0000269|PubMed:2246269, ECO:0000269|PubMed:2748583}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-
- Alpha-mannosidase
- Golgin subfamily A member 2
- alpha-1,2-Mannosidase
Sequence:
MKLSRQFTVFGSAIFCVVIFSLYLMLDRGHLDYPRGPRQEGSFPQGQLSILQEKIDHLERLLAENNEIISNIRDSVINLSESVEDGPRGPAGNASQGSAHLHSAQLALQADPKDCLFASQSGNQHRDVQMLDVYDLIPFDNPDGGVWKQGFDIKYEADEWDREPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIDNPKKEAVKSLLQNGQLEIVTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSLQKTLEFFWRQNWDLGSTTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRYGCPWGVPPEAISPGNVQSRAQMLLDQYRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQYRNYEQLFSYMNSQPHLKVKIQFGTLSDYFDALEKSVAAEKKGGQSVFPALSGDFFTYADRDDHYWSGYFTSRPFYKRMDRIMESRLRTAEILYHLALKQAQKYKINKFLSSPHYTTLTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFQSLNSLEKIIGDSAFLLILKDKKLYQSDPSKAFLEMDTKQSSQDSLPKKNIIQLSAQEPRYLVVYNPFEQERHSVVSVRVNSATVKVLSDLGKAVEVQVSAVWKDMRTTSQAAYEVAFLAHLPPLGLKVYKILESQSSSSHLADYFLYNNDGQAESGIFHMKNMVDSGDAITIENSFLTLGFDRSGLMEKVRRKEDNKQQELKVQFLWYGTTNKRDKSGAYLFLPDGQGQPYVSLRTPFVRVTRGRIYSDVTCFLEHVTHKVRLYHIQGIEGQSMEVSNIVDIRSVHNREIVMRISSKINNQNRYYTDLNGYQIQPRRTMAKLPLQANVYPMSTMAYIQDAAHRLTLLSAQSLGASSMASGQIEVFMDRRLMQDDNRGLGQGVHDNKITANLFRILLEKRNGMNMEEDKKSPVSYPSLLSHMTSAFLNHPFLPMVLSGQLPSPAIELLSEFRLLQSSLPCDIHLVNLRTIQSKVGKGYSDEAALILHRKVFDCQLSSRAMGLPCSTTQGKMSIPKLFNNFAVESFIPSSLSLMHSPPDAQNTSEVSLSPMEISTSRIRLR
Protein: Elongation factor Ts, mitochondrial (EF-Ts) (EF-TsMt) (Q9HGL5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03135, ECO:0000269|PubMed:15695360}.
Interaction partners:
- Elongation factor Tu
- Putative ribosomal recycling factor
- rRNA biogenesis protein rrp5
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL9m
- Small ribosomal subunit protein uS3
- ATP synthase subunit 5, mitochondrial
Sequence:
MLFQRRLHFHQFFGKTRVTGSLSRQWYSKLPSKLADIKKLRSETNASMDLVKQSVEEAGVGNLELAREILKKKIVQRGGKLAEKSKNRTAKEGWIIQCISEDGRKAVMAEINCESDFVAQTTPFQDLARRIASTFLHYLPTNHSSYSVEATLKNEILKHQAYVSKNHEANEKDVSSNVSLEEEIVKMTSFTGEKVQVQRLHCMNARVPSTAIGIFSHGAKQSSPLQQLGRIGSMVQINSDLSTRKGLSNQIAKEIVAQDPSSTSELLSFRSLVDSEKTIKDVLGQSTILEWVRWERGGN
Protein: Appl1 (DCC-interacting protein 13-alpha) (B2XCL9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasmic vesicle, phagosome {ECO:0000256|ARBA:ARBA00004262}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004220}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPGIDKLPIEETLEDSPQTRSLLGVFEEDAAAISSYFSQLFKAMQRIYDAQNELSAATHLTSKLLKDYEKQRFPLGGDDEVMSSTLQQFAKVIDELSSCHAVLSTQLADAMMFPITQFQERDLREILILKEVFQLASDDHDAAVHRYSRLSKRKENEKVKNEVMEDVYTSRKKQHETTMHYFASLNMLQYKKKIALLEPLLGYMQAQISFFKLGSENLTQQWEDFLTNIGTSVQNVRREMDSDAEAMEQTIQDLKEASDPLYMPDPDPNRIPVNRNLTRKAGYLNTRNKTGLVSSSWERQYFFTQGGNLMSQSRGAVAGGLVMDIDNCSVMAVDCEDRRFCFQITAFDGKKAAVLQADSRKDCEEWIATINNISKRIYLSENPEEIAARVNQSALEAVTPSPSFQQRHESFRPNTQGKVKASRSGSQCSVGSESPALSSLSLDSLVAPDTPIQFDIISPVSEEHTSQTKSSAQGRTNPFGESGGSQSEESEDSILHQLFIVRFLGSMEVKATESSDVIYETMRQILAARAIHNIFRMTESHLLVTCECLKLIDPQTQVTRLRFPLSSVVLCASHQENKRLFGFVLQTAGGRADGQPVTVCYIFESNNDGEKICDSIGLAKQIALHSEMDRKASQKQRELDKAKEKQQEELHKQKQIEKDLEEQSRLIAASSRPNQPAADGQFLVLSNSQSEDSDVGEEGLKKGESEA
Protein: Zinc finger and BTB domain containing 16 protein (M5AK03)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
PSSVTSGLHVQPALVVSMDFSTYGGLLPQGFIQRELFSKLGELAVGMKAESRPLGEQCSVCGVELPDNEAVEQHRKLHSGMKTYGCELCGKRFLDSLRLRMHLLAHSAGAKAFVCDQCGAQFSKEDALETHRQTHTGTDMAVFCLLCGKRFQAQSALQQHMEVHAGVRSYICSECNRTFPSHTALKRHLRSHTGDHPYECEFCGSCFRDESTLKSHKCIHTGEKPYECNGCGKKF
Protein: Calcium uniporter protein C-terminal domain-containing protein (Q387B7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- EF-hand domain-containing protein
- EF-hand domain-containing protein
Sequence:
MWRPYTLFVVPMRFGSPLQLRSLFVSRMPGRFDAFLTRRFVSTATPGGQPICSDSHNSAACLTAEEFSNIVPMFLLGQALRQHTSNEENRAGAGEFVITREVFNRYCSESHVEDTDKALQLLCESGVVVSISDGAAVHLRPVQFLQMHNDAADASDAKVKTPFEDYIRAAQNRLADAEAEEMAMRVALQPAIDNAAKRRRLLWSGALCLMAVQLAVISRLTFVDLDWDIMEPVSYFLGSGTSILFLIYLLRNGRVKSYKEYEEKAAASRVRLHAPADFEWRKYDAVVRRVEVEKNMVEQMRKWFKHH
Protein: Indoleamine 2,3-dioxygenase 2 (IDO-2) (EC 1.13.11.-) (Indoleamine 2,3-dioxygenase-like protein 1) (Indoleamine-pyrrole 2,3-dioxygenase-like protein 1) (Q6ZQW0)
Organism: Homo sapiens (Human)
Function: Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. Involved in immune regulation. May not play a significant role in tryptophan-related tumoral resistance.
Interaction partners:
- Tryptophan 2,3-dioxygenase
- Kynureninase
- Kynurenine formamidase
- Tryptophan 5-hydroxylase 1
- Tryptophan 5-hydroxylase 2
- Cytochrome P450 1A2
- Indolethylamine N-methyltransferase
- Amine oxidase [flavin-containing] A
- Cytochrome P450 1A1
- Amine oxidase [flavin-containing] B
Sequence:
MEPHRPNVKTAVPLSLESYHISEEYGFLLPDSLKELPDHYRPWMEIANKLPQLIDAHQLQAHVDKMPLLSCQFLKGHREQRLAHLVLSFLTMGYVWQEGEAQPAEVLPRNLALPFVEVSRNLGLPPILVHSDLVLTNWTKKDPDGFLEIGNLETIISFPGGESLHGFILVTALVEKEAVPGIKALVQATNAILQPNQEALLQALQRLRLSIQDITKTLGQMHDYVDPDIFYAGIRIFLSGWKDNPAMPAGLMYEGVSQEPLKYSGGSAAQSTVLHAFDEFLGIRHSKESGDFLYRMRDYMPPSHKAFIEDIHSAPSLRDYILSSGQDHLLTAYNQCVQALAELRSYHITMVTKYLITAAAKAKHGKPNHLPGPPQALKDRGTGGTAVMSFLKSVRDKTLESILHPRG
Protein: Uncharacterized protein (Q4GZ98)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein L22p/L17e
- AB hydrolase-1 domain-containing protein
- Uncharacterized protein
- Ribosomal protein L11, putative
- Uncharacterized protein
- Uncharacterized protein
- Rhodanese domain-containing protein
- Large ribosomal subunit protein uL3m
Sequence:
MGYTRERTNRHFFVARANAFFSRLPIARVQRSLAMEAVREGRMRPWKYTKEQILGAPVTCNFEYNPRPVRLIGTVMDAHTEETSIKGGLKVYARNEETNMMLWIPPGNPKLRHEVTSTKGSFQHYLDERDKWDEAWITGRARMK
Protein: Endoribonuclease (E5QCG0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEKEEYLPPRRPIIRNIPPSITHKTSDGEYLLLGYHDRPMMTMATIIPTRYPVPGPHKAIGSTIERPPPQLLGPVEPQKHEDTSFILLLLNNHPIPFYATLVTMFALLLTVIWQCGRQWDQQKSTSRMDSFEIVNNPGESRSAQTSKQSNRGSFGWANRKIEIPEGWMAVGSKLMYSPSDILGTGCEGTVVYRGTFDGREVAVKRVVSEFVKFAHREADLLRESDTHPHVIRYFCMESDSQFRYLALELCIASLNDYVEQKEVQQNVTIALRDIMKQATDGLAHLHASKIVHRDMKPQNVLITMASQRGEMRAVISDFGLCKRVQPGKNSISRGIASGLAGTDGWIAPEVLISASTSYPVDIFSLGCIFYYVLTSGTHPFGKSLHRQANIVNGEYTLNKLADLDDWSLADDLISSMLNVEPLHRLTADAVLNHPFFWTSEKRLAYFSDVSDRVEKEEDNSPVVRRIETDARIVVCGGWREKICDALKEDLRKFRTYKSFSVRDLLRAMRNKKHHYRELPEDVRQSLGDIPDQFLHYFTSRFPRLLLHVYKATEYCSGEAVFKRYYSDDVRARMYPIVEEEERVRKKIKEEMANEVWARAPKPVEQRTPLKLDKRNIKKKSNPNTD
Protein: BCL2-interacting killer (Bcl-2-interacting killer) (Bik) (Q5RGV6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Noxa
Sequence:
MVEETRQQKNATTLQAGPAEVDHSNLYAFNMRVTQTIGRQLAQIGDEMDNKWRQEPPVPWQNLNFGIYPYVLSRRVFSGRILANLWGSKIMPIFRTSWLLPQLQNGCQEARKWAAWVSNLHVSDWSRSTTYTLASALLLVTVSIFLVNWNEYEG
Protein: Profilin (Q6FR43)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Actin
- Cofilin
- Candida glabrata strain CBS138 chromosome J complete sequence
- Adenylyl cyclase-associated protein
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Protein transport protein SEC22
- Coronin
- F-actin-capping protein subunit beta
- Actin-related protein 3
Sequence:
MSWQAYTDNLLATGKVDKAVIYSKAGDAVWATSGGLSLQANEISEIVQGFDNPTGLQSNGLHIQGQKFMLLRADDRSIYGRHDAEGVVCVRTKQTVLIAHYPPTVQAGEATKIVEQLADYLISVQY
Protein: Probable LRR receptor-like serine/threonine-protein kinase RFK1 (EC 2.7.11.1) (Receptor-like kinase in flowers 1) (Q9FXF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- At2g17975
- Protein FIP1
- Zinc finger
- T1N15.19
- Probable disease resistance protein RDL6
- Major latex protein-like
- AT4g14060/dl3070w
Sequence:
MISLYQILAEKKKKKKNDLNIFAFSVFAIICFKFYSVNAIKLPQQEVDALQQIATTLGSKFWKFDAENCKIEMVGLTETPPPTAKQEIECECSPTNDTDCHVVKFAFKDHNLPGTLPQIVKLPYLREIDLAYNYINGTLPREWASSNLTFISLLVNRLSGEIPKEFGNSSLTYLDLESNAFSGTIPQELGNLVHLKKLLLSSNKLTGTLPASLARLQNMTDFRINDLQLSGTIPSYIQNWKQLERLEMIASGLTGPIPSVISVLSNLVNLRISDIRGPVQPFPSLKNVTGLTKIILKNCNISGQIPTYLSHLKELETLDLSFNKLVGGIPSFAQAENLRFIILAGNMLEGDAPDELLRDGITVDLSYNNLKWQSPESRACRPNMNLNLNLFQSTSTKKSSKFLPCIKDFKCPRYSSCLHVNCGGSDMYVKEKKTKELYEGDGNVEGGAAKYFLKPDANWGFSSTGDFMDDNNFQNTRFTMFVPASNQSDLYKSARIAPVSLTYFHACLENGNYTINLDFAEIRFTNDENYNRLGRRLFDIYIQEKLVAKDFNIMDEAKGAQTPIIKPLTAYVTNHFLTIRLSWAGKGTTRIPTRGVYGPIISAISIVSDSKPCERPKTGMSPGAYIAIGIGAPCLIIFILGFLWICGCLPRCGRQRKDPYEEELPSGTFTLRQIKFATDDFNPTNKIGEGGFGAVFKGVLADGRVVAVKQLSSKSRQGNREFLNEIGAISCLQHPNLVKLHGFCVERAQLLLAYEYMENNSLSSALFSPKHKQIPMDWPTRFKICCGIAKGLAFLHEESPLKFVHRDIKATNILLDKDLTPKISDFGLARLDEEEKTHISTKVAGTIGYMAPEYALWGYLTFKADVYSFGVLVLEIVAGITNSNFMGAGDSVCLLEFANECVESGHLMQVVDERLRPEVDRKEAEAVIKVALVCSSASPTDRPLMSEVVAMLEGLYPVPESTPGVSRNAGDIRFKAFKDLRRGMENNSKTQCSVKSYPSSSSTSSGAGQAVQERKKEESRP
Protein: Beta-2-syntrophin (59 kDa dystrophin-associated protein A1 basic component 2) (Syntrophin-3) (SNT3) (Syntrophin-like) (SNTL) (Q61235)
Organism: Mus musculus (Mouse)
Function: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:9214383}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:9214383}; Peripheral membrane protein {ECO:0000269|PubMed:9214383}. Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9214383}. Note=Membrane-associated. In insulinoma cell line, it is enriched in secretory granules (By similarity). In muscle, it is exclusively localized at the neuromuscular junction. {ECO:0000250}.
Interaction partners:
- Utrophin
- Dystrophin
- Dystrobrevin alpha
- Dystroglycan 1
- Dystrobrevin beta
- Microtubule-associated serine/threonine-protein kinase 2
- Beta-1-syntrophin
- Alpha-1-syntrophin
- Gamma-2-syntrophin
- Gamma-1-syntrophin
Sequence:
MAVWTRATKAGLVELLLRERWVRVVAELSGESLSLTGDAAAVEPEPPAAAFNGLPNGGGGESLPGSPNRGLGPPSPPAPPRGPAGEASASPPVRRVRVVKQEAGGLGISIKGGRENRMPILISKIFPGLAADQSRALRLGDAILSVNGTDLRQATHDQAVQALKRAGKEVLLEVKFIREVTPYIKKPSLVSDLPWEGASPQSPSFSGSEDSGSPKHQNTTKDRKVIPLKMCFAARNLSMPDLENRLIELHSPDSRNTLILRCKDTATAHSWFVAIHTNIMALLPQVLAELNAMLGATSTAGGSKEVKHIAWLAEQAKLDGGRQQWRPVLMAVTEKDLLLYDCMPWTRDAWASPCHSYPLVATRLVHSGSGCRSPSLGSDLTFATRTGSRQGIEMHLFRVETHRDLSTWTRILVQGCHAAAELIKEVSLGCTLSGQEVRFTVHYEHGFTITRDNGGASSILYRYPFERLKMSADDGIRNLYLDFGGPEGELTMDLHSCPKPIVFVLHTFLSAKVTRMGLLV
Protein: BAG family molecular chaperone regulator 1 (BAG-1) (Bcl-2-associated athanogene 1) (Q60739)
Organism: Mus musculus (Mouse)
Function: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli (By similarity).
Subcellular location: [Isoform 1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
Interaction partners:
- Heat shock 70 kDa protein 1B
- Heat shock cognate 71 kDa protein
- Apoptosis regulator Bcl-2
- DnaJ homolog subfamily B member 1
- BAG family molecular chaperone regulator 2
- Hsp70-binding protein 1
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 4L
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 4
Sequence:
MAGRSAARRPRGDREPLGPRLRAPRPAREPRQSESRAERGLPPSQRSSVRSAASGHDRSTRGAPAGACKPRVKKKVRPRSSQSEKVGSSSRELTRSKKVTRSKNVTGTQVEEVTKIEEATQTEEVTVAEEVTQTDNMAKTEEMVQTEEMETPRLSVIVTHSNERYDLLVTPQQGNSEPVVQDLAQLVEEATGVPLPFQKLIFKGKSLKEMETPLSALGMQNGCRVMLIGEKSNPEEEVELKKLKDLEVSAEKIANHLQELNKELSGIQQGFLAKELQAEALCKLDRKVKATIEQFMKILEEIDTMVLPEQFKDSRLKRKNLVKKVQVFLAECDTVEQYICQETERLQSTNLALAE
Protein: Isopentenyl-diphosphate delta-isomerase (EC 5.3.3.2) (Isopentenyl pyrophosphate isomerase) (IPP isomerase) (P15496)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Isopentenyl-diphosphate delta-isomerase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway. IDI1 catalyzes the 1,3-allylic rearrangement of isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Diphosphomevalonate decarboxylase
- Farnesyl pyrophosphate synthase
- Geranylgeranyl pyrophosphate synthase BTS1
- Hydroxymethylglutaryl-CoA synthase
- Mevalonate kinase
- Phosphomevalonate kinase
- Squalene synthase ERG9
- Lanosterol synthase ERG7
- Acetyl-CoA acetyltransferase
- Squalene epoxidase ERG1
Sequence:
MTADNNSMPHGAVSSYAKLVQNQTPEDILEEFPEIIPLQQRPNTRSSETSNDESGETCFSGHDEEQIKLMNENCIVLDWDDNAIGAGTKKVCHLMENIEKGLLHRAFSVFIFNEQGELLLQQRATEKITFPDLWTNTCCSHPLCIDDELGLKGKLDDKIKGAITAAVRKLDHELGIPEDETKTRGKFHFLNRIHYMAPSNEPWGEHEIDYILFYKINAKENLTVNPNVNEVRDFKWVSPNDLKTMFADPSYKFTPWFKIICENYLFNWWEQLDDLSEVENDRQIHRML
Protein: RNA polymerase III subunit E (A0A0C4DH01)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTYDDIPHLSAKIKPKQQKVELEMAIDTLNPNYCRSKGEQIALNVDGACADETSTYSSKLMDKQTFCSSQTTSNTSRYAAALYRQGELHLTPLHGILQLRPSFSYLDKADAKHREREAANEAGDSSQDEAEDDVKQITVRFSRPESEQARQRRVQSYEFLQKKHAEEPWVHLHYYGLRDSRSEHERQYLLCPGSSGVENTELVKSPSEYLMMLMPPSQEEEKDKPVAPSNVLSMAQLRTLPLADQIKILMKNVKVMPFANLMSLLGPSIDSVAVLRGIQKVAMLVQGNWVVKSDILYPKDSSSPHSGVPAEVLCRGRDFVMWKFTQSRWVVRKEVATVTKLCAEDVKDFLEHMAVVRINKGWEFILPYDGEFIKKHPDVVQRQHMLWTGIQAKLEKVYNLVKETMPKKPDAQSGPAGLVCGDQRIQVAKTKAQQNHALLERELQRRKEQLRVPAVPPGVRIKEEPVSEEGEEDEEQEAEEEPMDTSPSGLHSKLANGLPLGRAAGTDSFNGHPPQGCASTPVARELKAFVEATFQRQFVLTLSELKRLFNLHLASLPPGHTLFSGISDRMLQDTVLAAGCKQILVPFPPQTAASPDEQKVFALWESGDMSDQHRQVLLEIFSKNYRVRRNMIQSRLTQECGEDLSKQEVDKVLKDCCVSYGGMWYLKGTVQS
Protein: Synaptotagmin-like protein 5 (Q80T23)
Organism: Mus musculus (Mouse)
Function: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids (By similarity).
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Ras-related protein Rab-27A
- Ras-related protein Rab-27B
- Ras-related protein Rab-3A
Sequence:
MSKNSEFINLSFLLDHEKEMILGVLKRDEYLKKVEDKRIRKLKNELLEAKRRSGKTHQEASRVCVHCHKTLGLIFDRGDPCQACSLRVCSECRVTGLDGSWKCTVCAKVAQLRIISGEWFLEEKAKRFKQVNVLGTDVVRQSILRRSPGSEETQNQEQAQQCVDKSDTLSSVRQKTTHDGPKKKGFLLSKFRSATRGEIRTPKPESGRSYSLDLDSQNLQSFKSASGSDRGSTTSSDLIDQEAGRRTSKSSYSNGGIPVTQRSPVPSAHSVTSINSREHGFENSMALATIENTCEELTKSHRRNTSGTPSIAVSGTSLSSERSRSEVDLSESFAEDLEDTSSIRSRSVPGALDKDLNSLEDTEDGVDLVSSRFSANTHSLASGLSTNSQAGSDRKRSYLNVPDADSDTTSLNSMMSVYSETGDYGNVKVTGEILLHISYCYKTGGLYIFVKSCRNLATGDEKKQRTDAYVKSYLLPDKSRNNKRKTKIRTGTNPEFNETLKYTISHTQLETRTLQLSVWHYDRFGRNSFLGEVEIAFDSWNFENPCDEWFVLQPKVELAPDISLQYKGELTIVLRYIPPEENLIFPAGQRQEKKIFKRGKKKESSSISGGILEVFIKKAKNLTAVKSGGTSDSFVKGYLLPDDNKATKHKTAVVKKSVNPEWNHTFIFSGLYPQDIKNACLELTIWDKEAFSSNVFLGGVRLNSGSGMSYGKTVDWMDSHGEEQRLWQKMADNPGTSVEGVLMLRSSMAKCRL
Protein: Pastrel, isoform E (Pastrel, isoform G) (Q8IQ82)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MANRLGNHEVTRTAREVQQNFAESLGYAEEIIWDLLSHEQHDVLRGKLCQLIRDSPEPKTATETEKDRKIRLKVNADNERARQIIFDSVWQQRKYTNRQSLTAIIYVMVVTDETDVNRAEDARVFSVHPVFRARRCVVGSSGTSSVSSNCCNLFIDELGRVYQNWEMYVTTNELPAGVMVAPEKGIYRLVRDQVRLDKYTTPAGTTNRKVLGYLDTGSAVGGFFAACVPIAALLTLPVSAPLMGAAGVVGLASAGYAASRSGSKLFDRSQHEQSINVTDREARGHWLGVAGGTVGLAAAGATTVLTTATNAGREVGAITQLTVNSMNISSIVVSGTGVANGVLDLILKAKDGDEIVAMDVLQLSASLVLLTHSVYNFKLASTIINETSNANIADYRKNLSNRQRRTFDKAAKETVRMQGNTRGKLDIIRNVNEISPQEFNDLFKINKNLNQEGVRYSFAPDGKGFLLNGDVQTTGAELRASVQHNQGGNVLGKVSQPIPGSHAGSGRLQLGGVNQVSRLIGPLPTSHPRQEPSTYAAGVFALELSSVLVGGVVFVLEKYGKIIFEHVINAESFESLINIMANKLDPKVFDHIMLLTRAFMDTMLEDLTSVLKFFISTESVLYRILLYILRNFEDVQLSVIADHTCEIVEAVRVYFMSLNPNAFPGLLQKCPKCIGHFSVCPL
Protein: Ribosomal L1 domain containing 1 (J3QSV6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEDSASASLSSAAATGTSTSTPAAPTARKQLDKEQVRKAVDALLTHCKSRKNNYGLLLNENESLFLMVVLWKIPSKELRVRLTLPHSIRSDSEDICLFTKDEPNSTPEKTEQFYRKLLNKHGIKTVSQIISLQTLKKEYKSYEAKLRLLSSFDFFLTDARIRRLLPSLIGRHFYQRKKVPVSVNLLSKNLSREINDCIGGTVLNISKSGSCSAIRIGHVGMQIEHIIENIVAVTKGLSEKLPEWESVKLLFVKTEKSAALPIFSSFVSNWDEATKRSLLNKKKKEARRKRRERNFEKQKERKKKRQQARKTASVLSKDDVAPESGDTTVKKPESKKEQTPEHGKKKRGRGKAQVKATNESEDEIPQLVPIGKKTPANEKVEIQKHATGKKSPAKSPNPSTPRGKKRKALPASETPKAAESETPGKSPEKK
Protein: At3g12480/MQC3.32 (Nuclear factor Y, subunit C11) (Q9LHG0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- AT5g08190/T22D6_130
- TATA-binding protein-associated factor BTAF1
- TATA-box-binding protein 1
- TATA-box-binding protein 2
- Protein Dr1 homolog
- Nuclear transcription factor Y subunit B-3
- Protein MIZU-KUSSEI 1
- At5g23100
- Monothiol glutaredoxin-S17
- Nuclear transcription factor Y subunit B-7
Sequence:
MRKKLDTRFPAARIKKIMQADEDVGKIALAVPVLVSKSLELFLQDLCDRTYEITLERGAKTVSSLHLKHCVERYNVFDFLREVVSKVPDYGHSQGQGHGDVTMDDRSISKRRKPISDEVNDSDEEYKKSKTQEIGSAKTSGRGGRGRGRGRGRGGRAAKAAEREGLNREMEVEAANSGQPPPEDNVKMHASESSPQEDEKKGIDGTAASNEDTKQHLQSPKEGIDFDLNAESLDLNETKLAPATGTTTTTTAATDSEEYSGWPMMDISKMDPAQLASLGKRIDEDEEDYDEEG
Protein: Interleukin-8 (IL-8) (C-X-C motif chemokine 8) (Chemokine (C-X-C motif) ligand 8) (Neutrophil attractant/activation protein 1) (NAP-1) (Permeability factor 1) (PF1) (rPF1) (P19874)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Chemotactic factor that mediates inflammatory response by attracting neutrophils, basophils, and T-cells to clear pathogens and protect the host from infection. Also plays an important role in neutrophil activation. Released in response to an inflammatory stimulus, exerts its effect by binding to the G-protein-coupled receptors CXCR1 and CXCR2, primarily found in neutrophils, monocytes and endothelial cells. G-protein heterotrimer (alpha, beta, gamma subunits) constitutively binds to CXCR1/CXCR2 receptor and activation by IL8 leads to beta and gamma subunits release from Galpha (GNAI2 in neutrophils) and activation of several downstream signaling pathways including PI3K and MAPK pathways.
Subcellular location: Secreted.
Interaction partners:
- C-X-C chemokine receptor type 1
- C-X-C chemokine receptor type 2
- Permeability factor 2
- Chemokine interleukin-8-like domain-containing protein
- Interleukin-1 beta
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor Jun
- Tumor necrosis factor
- C-X-C chemokine receptor type 4
- Interleukin-6
Sequence:
MNSKLAVALLATFLLSLTLCEAAVLTRIGTELRCQCIKTHSTPFHPKFIKELRVIESGPHCANSEIIVKLVDGRELCLDPKEKWVQKVVQIFLKRAEQQES