wanglab/gogpt-training-data huggingface dataset:
Protein: Disease resistance protein (TIR-NBS-LRR class) family (F4JNB6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDHGIVRSCIIADELITAIREARISIVIFSENYASSTWCLNELVEIHKCHKDKDLDQMVIPVFYGVDPSHVRKQIGGFGDVFKKTCEDKPEDQKQRWVKALTDISNLAGEDLRNGPSEAAMVVKIANDVSNKLFPLPKGFGDLVGIEDHIEAIKLKLCLESKEARIMVGIWGQSGIGKSTIGRALFSQLSSQFHHRAFITYKSTSGSDVSGMKLSWEKELLSEILGQKDIKIEHFGVVEQRLKHKKVLILLDDVDNLEFLRTLVGKAEWFGSGSRIIVITQDRQLLKAHEIDLIYEVKLPSQGLALKMICQYAFGKYSPPDDFKELAFEVAKLAGNLPLGLSVLGSSLKRRSKEEWMEMLAELQNGLNRDIMKTLRVSYVRLDPKDQDIFHYIAWLFNGWKVKSIKDFLGDGVNVNIRLKTLDDKSLIRLTPNDTIEMHNLLQKLATEIDREESNGNPGKRRFLENAEEILDVFTDNTGTEKLLGIDFSTSSDSQIDKPFISIDENSFQGMLNLQFLNIHDHYWWQPRETRLRLPNGLVYLPRKLKWLRWENCPLKRLPSNFKAEYLVELRMENSALEKLWNGTQPLGSLKKMNLRNSNNLKEIPDLSLATNLEELDLCNCEVLESFPSPLNSESLKFLNLLLCPRLRNFPEIIMQSFIFTDEIEIEVADCLWNKNLPGLDYLDCLRRCNPSKFRPEHLKNLTVRGNNMLEKLWEGVQSLGKLKRVDLSECENMIEIPDLSKATNLEILDLSNCKSLVMLPSTIGNLQKLYTLNMEECTGLKVLPMDINLSSLHTVHLKGCSSLRFIPQISKSIAVLNLDDTAIEEVPCFENFSRLMELSMRGCKSLRRFPQISTSIQELNLADTAIEQVPCFIEKFSRLKVLNMSGCKMLKNISPNIFRLTRLMKVDFTDCGGVITALSDPVTTMEDQNNEKINKVEKRPKCDKDEDDEDEYEYEYDEDEDDEDEYGEIYFKFQNCFKLDRAARELILGSCFKTTMVLPGLLSKLDVNDVEFKFNGTRVKRCGIRLLNVSTSPDDSEGSSETESPDDSDGDSVTEYHQQSGEKCDDVETESSKKRMRMTLGNSEKYFNLPCGQIVTDTVPLGWGESSSVSFNPWLEGEALCVDSMITEQQDAQIHIANVDWEWELW
Protein: Probable steroid-binding protein 3 (AtMP3) (Membrane-associated progesterone-binding protein 2) (AtMAPR2) (Q9SK39)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305|PubMed:15608331}.
Interaction partners:
- Cytochrome B5 isoform C
- Cytochrome b5 isoform E
- Cytochrome B5 isoform D
- Cytochrome b5 isoform A
- Cytochrome b5 isoform B
- At4g10300
- Mitochondrial import receptor subunit TOM6 homolog
- Aluminum induced protein with YGL and LRDR motifs
- AT3g15450/MJK13_11
- Glycine--tRNA ligase, chloroplastic/mitochondrial 2
Sequence:
MEFTAEQLSQYNGTDESKPIYVAIKGRVFDVTTGKSFYGSGGDYSMFAGKDASRALGKMSKNEEDVSPSLEGLTEKEINTLNDWETKFEAKYPVVGRVVS
Protein: Rho-related protein racF2 (Q9GPS3)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- GTPase activating protein homolog 1
- Putative rho GDP-dissociation inhibitor 1
- Cofilin-1A
Sequence:
MQNIKCVVVGDGAVGKTCMLISYTTNGFPSEYLPTVFDNYCANLMLDGKPYSLGLWDTAGQEEYDRLRPLSYPQTDVFLICFSIISQSSFENVSTKWFKEVNHHAPGVPIVLVGTKQDIRNDNDSIKKLKERNIELVPYEKGLEKAKEINAIYLEASALTQRGVKNVFDQCIRSVIYPNKLNKKPKKKTCTIM
Protein: Fructose-1,6-bisphosphatase isozyme 2 (FBPase 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (Muscle FBPase) (Q9Z1N1)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate.
Subcellular location: Cell junction. Cytoplasm. Nucleus. Cytoplasm, myofibril, sarcomere, Z line. Note=In neonatal cardiomyocytes, distributed throughout the cytosol, accumulating in the intercalated disks which occur at the Z line of cardiomyocytes and connect adjacent cells, and also located in the nucleus; dissociates from the Z line following an increase in cytosolic Ca(2+) concentration. In muscle precursor cells, localizes predominantly to the nucleus and to a lesser extent to the cytoplasm at the proliferative phase, while mainly localizing to the cytoplasm at the differentiation phase. Colocalizes with ALDOA and alpha-actinin on both sides of the Z line of skeletal muscle; dissociates rapidly from the Z line following an increase in cytosolic Ca(2+) concentration.
Interaction partners:
- Glucose-6-phosphate isomerase
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
- Transaldolase
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4
- ATP-dependent 6-phosphofructokinase, platelet type
- ATP-dependent 6-phosphofructokinase, liver type
- ATP-dependent 6-phosphofructokinase, muscle type
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
- Transketolase
Sequence:
MTDRSPFETDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEGYAKYFDAATAEYVQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPESIHQRVPLILGSPEDVQEYLSCVQRNQAGR
Protein: Neurabin-1 isoform 1 (H9FWV3)
Organism: Macaca mulatta (Rhesus macaque)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MLKTESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKSDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPNENAAVIAKTRGKGGHSSPQRRMKPKEFLEKTDGSVVKLESSVSERISRFDTMYDGPSYSKFTETRKMFERSVHESGQNNRYSPKKEKAGGSEPQDEWGGSKSNRGSTDSLDSLSSRTEAVSPTVSQLSAVFENTDSPSAIISEKAENNEYSVTGHYPLNLPSVTVTNLDTFGHLKDSNSWSPSNKQGVDTEDAHKSNITLVPEVASKSTSLASIPGEEIQQSKEPEDSTSNQQTPDSIDKDGPEEPCAESKAMPKSEIPSPQSQLLEDAETNLLESEAAKQQRKELAGGDFTSPDASASSCGKEVPEDSNSFDSSHVYMHSDYNVYRVRSRYNSDWGETGTEQDEEEDSDENNYYQPDMEYSEIVGLPEEEEIPANRKIKFSSAPIKVFNTYSNEDYDRRNDEVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVGADAGLEKLGIFVKTVTEGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGNVRFVIGREKPGQVSEVAQLISQTLEQERRQRELLEQHYAQYDADDDETGEYATDEEEDEVGPVLPGSDMAIEVFELPENEDMFSPSDLDTSKLSHKFKELQIKHAVTEAEIQKLKTKLQAAENEKVRWELEKTQLQQNIEENKERMLKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIKRQEAERKKIEDLEKAHLVEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRTSLGEVSKGDTMENLDVKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPSRTRLYDSVSSTDGEDSLERKPSNSFYNHMHITKLLPPKGLRTSPESDSGVPPLTPVDSNVPFSSDQIAEFQEEPLDPEVGPLSSMWGDTSLFSTSKSDHDMEESPCHHQTSNKKILQEKDDAKDPKSLRASSSLAVQGGKIKQKFVDLGAPLRRNSNKGKKWKEKEASRFSAGSRIFRGRLENWTPKPRSAAQTSTRSPCMPFSWFNDSRKGSYSFRNLPAPTSSLQPSPETLISDKKGSKNFTFNDDFSPSSTSSADLSGLGAEPKTPGLSQSLALSSDEILDDGQSPKHSQCQNRAVQEWSVQQVSHWLMSLNLEQYVSEFSAQNITGEQLLQLDGNKLKALGMTASQDRAVVKKKLKEMKMSLEKARKAQEKMEKQREKLRRKEQEQMQRKSKKTEKMTSTAADGAGEQ
Protein: Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (TGF-beta receptor-interacting protein 1) (TRIP-1) (eIF-3-beta) (eIF3 p36) (Q9QZD9)
Organism: Mus musculus (Mouse)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit E
Sequence:
MKPILLQGHERSITQIKYNREGDLLFTVAKDPIVNVWYSVNGERLGTYMGHTGAVWCVDADWDTKHVLTGSADNSCRLWDCETGKQLALLKTNSAVRTCGFDFGGNIIMFSTDKQMGYQCFVSFFDLRDPSQIDSNEPYMKIPCNDSKITSAVWGPLGECVIAGHESGELNQYSAKSGEVLVNVKEHSRQINDIQLSRDMTMFVTASKDNTAKLFDSTTLEHQKTFRTERPVNSAALSPNYDHVVLGGGQEAMDVTTTSTRIGKFEARFFHLAFEEEFGRVKGHFGPINSVAFHPDGKSYSSGGEDGYVRIHYFDPQYFEFEFEA
Protein: Sodium-dependent proline transporter (Solute carrier family 6 member 7) (Q99884)
Organism: Homo sapiens (Human)
Function: Brain specific sodium (and chloride)-dependent proline transporter. Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals (Probable).
Subcellular location: Synaptic cell membrane {ECO:0000269|PubMed:7651355}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hairy and enhancer of split-related protein HELT
- Prothymosin alpha
Sequence:
MKKLQGAHLRKPVTPDLLMTPSDQGDVDLDVDFAAHRGNWTGKLDFLLSCIGYCVGLGNVWRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGAAMLLIVGLVAIYYNMIIAYVLFYLFASLTSDLPWEHCGNWWNTELCLEHRVSKDGNGALPLNLTCTVSPSEEYWSRYVLHIQGSQGIGSPGEIRWNLCLCLLLAWVIVFLCILKGVKSSGKVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLGVGFGGLLTFASYNTFHQNIYRDTFIVTLGNAITSILAGFAIFSVLGYMSQELGVPVDQVAKAGPGLAFVVYPQAMTMLPLSPFWSFLFFFMLLTLGLDSQFAFLETIVTAVTDEFPYYLRPKKAVFSGLICVAMYLMGLILTTDGGMYWLVLLDDYSASFGLMVVVITTCLAVTRVYGIQRFCRDIHMMLGFKPGLYFRACWLFLSPATLLALMVYSIVKYQPSEYGSYRFPPWAELLGILMGLLSCLMIPAGMLVAVLREEGSLWERLQQASRPAMDWGPSLEENRTGMYVATLAGSQSPKPLMVHMRKYGGITSFENTAIEVDREIAEEEESMM
Protein: EP3-2 procyclin (Q581G0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MAPRSLYLLAVLLFSANLFAGVGFAAAAEGPEDKGLTKGGKGKGGKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPGAATLKSVALPFAIAAVGLVAAF
Protein: (-)-alpha-pinene synthase 2, chloroplastic (EC 4.2.3.119) ((-)-beta-pinene synthase 2) (EC 4.2.3.120) (Terpene synthase TPS-Pin-2) (PgTPS-Pin-2) (F2XF96)
Organism: Picea glauca (White spruce) (Pinus glauca)
Function: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (1S,5S)-beta-pinene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MALVSIAPLASKSCLHKSLSSSAHELKTICRTIPTLGMSRRGKSATPSMSMSLTTTVSDDGVQRRMGDFHSNLWNDDFIQSLSTSYGEPSYRERAERLIGEVKKMFNSMSSEDGELINPHNDLIQRVWMVDSVERLGIERHFKNEIKSALDYVYSYWSEKGIGCGRESVVADLNSTALGLRTLRLHGYAVSADVLNLFKDQNGQFACSPSQTEEEIGSVLNLYRASLIAFPGEKVMEEAEIFSAKYLEEALQKISVSSLSQEIRDVLEYGWHTYLPRMEARNHIDVFGQDTQNSKSCINTEKLLELAKLEFNIFHSLQKRELEYLVRWWKDSGSPQMTFGRHRHVEYYTLASCIAFEPQHSGFRLGFAKTCHIITILDDMYDTFGTVDELELFTAAMKRWNPSAADCLPEYMKGMYMIVYDTVNEICQEAEKAQGRNTLDYARQAWDEYLDSYMQEAKWIVTGYLPTFAEYYENGKVSSGHRTAALQPILTMDIPFPPHILKEVDFPSKLNDLACAILRLRGDTRCYKADRARGEEASSISCYMKDNPGVTEEDALDHINAMISDVIRGLNWELLNPNSSVPISSKKHVFDISRAFHYGYKYRDGYSVANIETKSLVKRTVIDPVTL
Protein: Antitoxin ChpS (P08365)
Organism: Escherichia coli (strain K12)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. May be involved in the regulation of cell growth. It acts as a suppressor of the endoribonuclease (inhibitory function) of ChpB protein. Both ChpS and ChpB probably bind to the promoter region of the chpS-chpB operon to autoregulate their synthesis.
Interaction partners:
- Endoribonuclease toxin ChpB
- Endoribonuclease toxin MazF
- Antitoxin MazE
- Antitoxin DinJ
- Antitoxin YefM
- mRNA interferase toxin YafQ
- Antitoxin HicB
- Antitoxin YafN
- Toxin YoeB
- Antitoxin MqsA
Sequence:
MRITIKRWGNSAGMVIPNIVMKELNLQPGQSVEAQVSNNQLILTPISRRYSLDELLAQCDMNAAELSEQDVWGKSTPAGDEIW
Protein: Telomeric DNA-binding factor trf1 (Q6E434)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds the telomeric double-stranded TTACAGG repeat and regulates telomere length.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19074598}. Note=Enriched throughout the euchromatic hemisphere.
Interaction partners:
- Telomere length regulator taz1
- DNA-binding protein rap1
- Protection of telomeres protein tpz1
- Protection of telomeres protein poz1
- Coiled-coil quantitatively-enriched protein 1
- Trehalose-phosphatase
- Pre-mRNA-splicing factor cwf5
- Telomerase reverse transcriptase
- DNA-binding protein reb1
- Telomere elongation protein est1
Sequence:
MSKRSLDPSDDFKGQKRLAIDPESTALEQDRQMLQQLSEQNSELEPQNVAPNAEIPLGFDLSGIQFNMTPDFYLRMNQGMDYAFNQPNPIATPQQLLRTSLIPTLGNLSNIILSILGKPVQEASAIVTNPASEMGMAFTKVMNMFRMVKDIYTEESFIYSSAIGMRTPSQRSTTRRANLAIFLAAVYGALQIGFFHLNENFLEVFAPDESNILTNQGTLYMELKTQAYISAMAQAERPKGDILNDLFPSDMAHRFLIRRNAKLDDKLTYVEKQIIEKCTARKERLANFSPQEALNEVYPWGKFLSEIACYIHNNYSSISAIPIPANSFKRRSKKNGLRFKAGEAESSPSESGSDLTDSLAFGIPSSTFDGSSETQNVSSVVLYDQVRHMTNNNLNNKRTRRVANRRSWTKEEEEALLDGLDLVKGPRWSQILELYGPGGKKSEVLKYRNQVQLKDKARNMKLFFLKSGQVVPAALQCVTGDLRRD
Protein: Oxidation resistance protein 1 (Q38BQ8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MSGRGGSRAQSPCVTPSRCFLTNPFKISPAQTPKTTYLMRILGESIRRSSNVVATVAATVVLLEDDGFSTNSEFLMKWWRMLERCLGELAGVVNSCEENIREKDMRVLLALSHGFALAAQLSSLERRFLACLHRFAEVCEGAETVGAGEKLSGALSDITSLLKGEETILVAIRRQEANYIEKAIALQEEVFRVGEEGEPFFGKVEEPETRRTYLGSLWHALTAPFDDSEEVNNEQLVAADGGDWSQLISTFGSGGGASVCNWDDSMLLNSIVECAFASAEQQHTLLSERNFAVALFLFSTKCNVLEELVEVCFQLRLGNGGLFGFEKLMYTDVSSQRERTVDWLSTILSPLREDVLHLELCDGNPKPPYFVAVVFLTLLWNTTYCMWKRGCIREAYEWLRVVDLGQLRRMAKAEDERGMKREISPESGVNSEAEDVGNVQEELKYTGSLSWDYIVHRAAGCPGPDRAKQVHRHSEVDFRHDRSGQLMWFVHHISCLRNACALALLCSTPHDVMYIISKFHHSRRWQWRQCVYLHESAKDAGANLSAEFGVVDSKFEVLSLTNFIVENYLARRSVRMYHFRSPPSPRKATSSDTTIEGSVVHVCDELICSMSYGRFSGVKEMEEAMFSELFGACCEGEIGEETGGEATTEGDDGSQRRLNWLEVHVAKVAVAFARDFRGNIYFQNAWVGTERGARSEKHSGGGAEEASWSSVLPLVKGLHGSAAHPPMPTDAGGGNQPINACSQGTTHHEFEKEPQGLLRHVSCMVPVRMTPPRVEHQAENERCTLWLPSRKGVGLLLLPEETDVNGEYDSFGEVALRLLVIACRYCDSMKLLPLHSRFSHHAVPEAGRVDAENNDHLSGWDSCHALLPSVVHELNVGLSLITDELRSSAGGDVLSVWHQQRDSSISRFRLNHLVSVTLHGLCSDALTSIELQMREESSVISARCTISQAVGAVQESDQGELTVIDSCSTPRDLLLDSSTRKSNELFMPSPTSPFHLGDKRQSSSAFAPDLSFDFSAFNSETLYATKQLVRELTEREEKWRRATEDDSLPPNTEECGISVLPWGARKLLHDRLPLMWQFAPWRLIYGTRFHGYSYSNMINACQREVNNAKRDGKQPKMILLLELDMSAVCLEDVVTEEGNEKKGGFVIGVCMSHPLSLDNRRFYGGSTTFVFQIRIPPSPQEPAIRTFHATGRNEKFINCTPQRIAIGGGGGCSLFLSNSISSGSTAACVTFDSPPLTHWRDPSLPSLSAGPSTSDSVSSFDIRTVEVIVVGE
Protein: CXADR-like membrane protein (Adipocyte adhesion molecule) (Coxsackie- and adenovirus receptor-like membrane protein) (CAR-like membrane protein) (Q8K1G0)
Organism: Rattus norvegicus (Rat)
Function: May be involved in the cell-cell adhesion. May play a role in adipocyte differentiation and development of obesity. Is required for normal small intestine development (By similarity).
Subcellular location: Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSLFFLWLVTYYVGTLGTHTEIKRVAEEKVTLPCHHQLGLPEKDTLDIEWLLTDNEGNQKVVITYSSRHVYNNLTEEQKGRVAFASNFLAGDASLQIEPLKPSDEGRYTCKVKNSGRYVWSHVILKVLVRPSKPKCELEGEPTEGSDLTLQCESASGTKPIVYYWQRIREKEGEDEHLPPKSRIDYNNPGRVLLQNLTMASSGLYQCTAGNEAGKESCVVRVTVQYVQSIGMVAGAVTGIVAGALLIFLLIWLLIRRKSKERYEEEDRPNEIREDAEAPRARLVKPSSSSSGSRSSRSGSSSTRSTGNSASRSQRTLSSEAAPQPGLATQAYSLIGPEVRGSEPKKAHHTTLTKAETTLSTMPSQSRAFQTV
Protein: Kinesin-like protein Klp68D (P46867)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plus-end directed microtubule motor that may be used for anterograde axonal transport and could conceivably move cargos in fly neurons different than those moved by kinesin heavy chain or other plus-end directed motors.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin associated protein 3, isoform G
- Kinesin-like protein
Sequence:
MSAKSRRPGTGSSQTPNECVQVVVRCRPMSNRERSERSPEVVNVYPNRGVVELQNVVDGNKEQRKVFTYDAAYDASATQTTLYHEVVFPLVSSVLEGFNGCIFAYGQTGTGKTFTMEGVRGNDELMGIIPRTFEQIWLHINRTENFQFLVDVSYLEIYMEELRDLLKPNSKHLEVRERGSGVYVPNLHAINCKSVEDMIKVMQVGNKNRTVGFTNMNEHSSRSHAIFMIKIEMCDTETNTIKVGKLNLIDLAGSERQSKTGASAERLKEASKINLALSSLGNVISALAESSPHVPYRDSKLTRLLQDSLGGNSKTIMIANIGPSNYNYNETLTTLRYASRAKSIQNQPIKNEDPQDAKLKEYQEEIERLKRLIGPQQQQRSEKQVTAKKQRVKKPKKETVTKEMSDSLQVSTIEQPVEDDSDPEGAESESDKENEAEVAKSNEELERERVENSKLAAKLAELEGQLVRGGKNLLDTYSERQIELEKKLVEIAERKKREIEIQQQLELQEETTLEIRERNVSLEQEVELKKRKLSKCYAKYLALQQELNDCKSDHNQDLRELEMAQNELVKELKRQLLIIDNFVPIEVKQRLYTQAKYDEEQEEWKFSSMSLPTPPGGDGKFSSKRPVSHPQRRRPTSEYALQEAKSNSPSSLRFKSENIVNYELEMPCRTTQEYRTPKVSASLQAVLAQAMQTGGDDIDIVDSHTNSLRSRLENIINANANGGAGPGAGVAVGSSIPNVRNIKSSRGLPSAASNLDSNRRPPTGRLPAKKPASAYPKARGLVNK
Protein: Pro-adrenomedullin [Cleaved into: Adrenomedullin (AM); Proadrenomedullin N-20 terminal peptide (ProAM N-terminal 20 peptide) (PAMP) (ProAM-N20)] (P43145)
Organism: Rattus norvegicus (Rat)
Function: AM and PAMP are potent hypotensive and vasodilatator agents.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P35318}.
Interaction partners:
- Receptor activity-modifying protein 2
- Receptor activity-modifying protein 3
- Calcitonin gene-related peptide type 1 receptor
- Receptor activity-modifying protein 1
- Islet amyloid polypeptide
- Calcitonin receptor
- Calcitonin gene-related peptide 2
- Protein ADM2
- Atypical chemokine receptor 3
- G-protein coupled receptor 182
Sequence:
MKLVSIALMLLGSLAVLGADTARLDTSSQFRKKWNKWALSRGKRELQASSSYPTGLVDEKTVPTQTLGLQDKQSTSSTPQASTQSTAHIRVKRYRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGYGRRRRRSLPEVLRARTVESSQEQTHSAPASPAHQDISRVSRL
Protein: Mediator of RNA polymerase II transcription subunit 1 (Mediator complex subunit 1) (Q12321)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 9
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 6
Sequence:
MVEGDSYVETLDSMIELFKDYKPGSITLENITRLCQTLGLESFTEELSNELSRLSTASKIIVIDVDYNKKQDRIQDVKLVLASNFDNFDYFNQRDGEHEKSNILLNSLTKYPDLKAFHNNLKFLYLLDAYSHIESDSTSHNNGSSDKSLDSSNASFNNQGKLDLFKYFTELSHYIRQCFQDNCCDFKVRTNLNDKFGIYILTQGINGKEVPLAKIYLEENKSDSQYRFYEYIYSQETKSWINESAENFSNGISLVMEIVANAKESNYTDLIWFPEDFISPELIIDKVTCSSNSSSSPPIIDLFSNNNYNSRIQLMNDFTTKLINIKKFDISNDNLDLISEILKWVQWSRIVLQNVFKLVSTPSSNSNSSELEPDYQAPFSTSTKDKNSSTSNTEPIPRSNRHGSVVEASRRRRSSTNKSKRPSITEAMMLKEEGLQQFNLHEILSEPAIEEENGDSIKEHSTTMDGANDLGFTASVSNQENAGTDIVMEDHGVLQGTSQNYGTATADDADIEMKDVSSKPSKPESSVLQLIVSEDHIILDTISECNLYDDVKCWSKFIEKFQDIVS
Protein: Lim3, isoform E (M9NCY1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MATIPKCGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDFFKRYGTKCSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRKLICKRDYEEAKAKGLYLDGSLDGDQPNKRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEKRLKKDAGRTRWSQYFRSMKGNCSPRTDKFLDKDELKVDYDSFSHHDLSNDSYSTVNLGLDEGASPHSIRGSYMHGSSSPSQYPPSSRSPPPVGQGHTFGSYPDNIVYTNIDQAVGSSLHASKAHHRLHSSNNVSDLSNDSSPDQGYPDFPPSPDSWLGDSGSTNTTSANNNANNNSSSSHNNNNSSGGGSGGVSVSTAPNPSAPGVHY
Protein: Beta-1,4-galactosyltransferase 1 (Beta-1,4-GalTase 1) (Beta4Gal-T1) (b4Gal-T1) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (Neolactotriaosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.275) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1) [Cleaved into: Processed beta-1,4-galactosyltransferase 1] (P15535)
Organism: Mus musculus (Mouse)
Function: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
Subcellular location: [Isoform Long]: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:18511602}; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Cell surface. Cell projection, filopodium {ECO:0000269|PubMed:18511602}. Note=Found in trans cisternae of Golgi. B4GALT1 cell surface expression is regulated by UBE2Q1 (PubMed:18511602). {ECO:0000269|PubMed:18511602}.; SUBCELLULAR LOCATION: [Isoform Short]: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:3149531}; Single-pass type II membrane protein {ECO:0000269|PubMed:3149531}. Note=Found in trans cisternae of Golgi. {ECO:0000269|PubMed:3149531}.; SUBCELLULAR LOCATION: [Processed beta-1,4-galactosyltransferase 1]: Secreted {ECO:0000250|UniProtKB:P15291}. Note=Soluble form found in body fluids. {ECO:0000250|UniProtKB:P15291}.
Interaction partners:
- Alpha-lactalbumin
- Beta-galactoside alpha-2,6-sialyltransferase 1
- Alpha-
- N-acetyllactosaminide alpha-1,3-galactosyltransferase
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
- CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
- Galactoside 2-alpha-L-fucosyltransferase Sec1
- Beta-1,3-galactosyltransferase 5
- Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase
- Type 2 lactosamine alpha-2,3-sialyltransferase
Sequence:
MRFREQFLGGSAAMPGATLQRACRLLVAVCALHLGVTLVYYLSGRDLSRLPQLVGVSSTLQGGTNGAAASKQPPGEQRPRGARPPPPLGVSPKPRPGLDSSPGAASGPGLKSNLSSLPVPTTTGLLSLPACPEESPLLVGPMLIDFNIAVDLELLAKKNPEIKTGGRYSPKDCVSPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGDTMFNRAKLLNIGFQEALKDYDYNCFVFSDVDLIPMDDRNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLAINGFPNNYWGWGGEDDDIFNRLVHKGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIAHTKETMRFDGLNSLTYKVLDVQRYPLYTQITVDIGTPR