wanglab/gogpt-training-data huggingface dataset:
Protein: Beta-1,4-galactosyltransferase galt-1 (EC 2.4.1.-) (O16374)
Organism: Caenorhabditis elegans
Function: Catalyzes the transfer of beta-galactose from UDP-galactose to position 4 of alpha-1,6-linked fucose at the reducing end GlcNAc in N-glycan cores. Involved in susceptibility to the nematotoxic C.cinerea galectin Cgl2, likely by contributing to the synthesis of core alpha-1,6-fucosylated N-glycans to which Cgl2 binds.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000303|PubMed:19858195}; Single-pass type II membrane protein {ECO:0000303|PubMed:19858195}. Note=Localizes to vesicles or organelles in coelomocytes. {ECO:0000269|PubMed:19858195}.
Interaction partners:
- Alpha-
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- Alpha-
- Alpha-
- GDP-mannose 4,6 dehydratase 1
- Galactoside 2-alpha-L-fucosyltransferase
- UAA transporter
Sequence:
MPRITASKIVLLIALSFCITVIYHFPIATRSSKEYDEYGNEYENVASIESDIKNVRRLLDEVPDPSQNRLQFLKLDEHAFAFSAYTDDRNGNMGYKYVRVLMFITSQDNFSCEINGRKSTDVSLYEFSENHKMKWQMFILNCKLPDGIDFNNVSSVKVIRSTTKQFVDVPIRYRIQDEKIITPDEYDYKMSICVPALFGNGYDAKRIVEFIELNTLQGIEKIYIYTNQKELDGSMKKTLKYYSDNHKITLIDYTLPFREDGVWYHGQLATVTDCLLRNTGITKYTFFNDFDEFFVPVIKSRTLFETISGLFEDPTIGSQRTALKYINAKIKSAPYSLKNIVSEKRIETRFTKCVVRPEMVFEQGIHHTSRVIQDNYKTVSHGGSLLRVYHYKDKKYCCEDESLLKKRHGDQLREKFDSVVGLLDL
Protein: Protein N-terminal glutamine amidohydrolase (EC 3.5.1.122) (Protein NH2-terminal glutamine deamidase) (N-terminal Gln amidase) (Nt(Q)-amidase) (WDYHV motif-containing protein 1) (Q80WB5)
Organism: Mus musculus (Mouse)
Function: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19560421}. Nucleus {ECO:0000269|PubMed:19560421}.
Interaction partners:
- Protein N-terminal asparagine amidohydrolase
- Arginyl-tRNA--protein transferase 1
- E3 ubiquitin-protein ligase UBR1
- E3 ubiquitin-protein ligase UBR2
- Coatomer subunit zeta-2
- TraB domain-containing protein
Sequence:
MEGDGPAATAPQYQPVCPTRDACVYNSCYCEENIWKLCEYIKTHNQYLLEECYAVFISNEKKMVPIWKQQARPENGPVIWDYHVVLLHVSREGQSFIYDLDTILPFPCPFDIYIEDALKSDDDIHLQFRRKFRVVRADSYLKHFASDRSHMKDSSGNWREPPPEYPCIETGDSKMNLNDFISMDPAVGWGAVYTLPEFVHRFSSKTYQA
Protein: GPI mannosyltransferase 3 (EC 2.4.1.-) (GPI mannosyltransferase III) (GPI-MT-III) (Phosphatidylinositol-glycan biosynthesis class B protein) (PIG-B) (Q92521)
Organism: Homo sapiens (Human)
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8861954}; Multi-pass membrane protein {ECO:0000269|PubMed:8861954}.
Interaction partners:
- GPI alpha-1,6-mannosyltransferase 2
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- GPI ethanolamine phosphate transferase 1
- GPI ethanolamine phosphate transferase, stabilizing subunit
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dol-P-Man:Man
- Dolichol-phosphate mannosyltransferase subunit 3
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
- GPI ethanolamine phosphate transferase 2, catalytic subunit
Sequence:
MRRPLSKCGMEPGGGDASLTLHGLQNRSHGKIKLRKRKSTLYFNTQEKSARRRGDLLGENIYLLLFTIALRILNCFLVQTSFVPDEYWQSLEVSHHMVFNYGYLTWEWTERLRSYTYPLIFASIYKILHLLGKDSVQLLIWIPRLAQALLSAVADVRLYSLMKQLENQEVARWVFFCQLCSWFTWYCCTRTLTNTMETVLTIIALFYYPLEGSKSMNSVKYSSLVALAFIIRPTAVILWTPLLFRHFCQEPRKLDLILHHFLPVGFVTLSLSLMIDRIFFGQWTLVQFNFLKFNVLQNWGTFYGSHPWHWYFSQGFPVILGTHLPFFIHGCYLAPKRYRILLVTVLWTLLVYSMLSHKEFRFIYPVLPFCMVFCGYSLTHLKTWKKPALSFLFLSNLFLALYTGLVHQRGTLDVMSHIQKVCYNNPNKSSASIFIMMPCHSTPYYSHVHCPLPMRFLQCPPDLTGKSHYLDEADVFYLNPLNWLHREFHDDASLPTHLITFSILEEEISAFLISSNYKRTAVFFHTHLPEGRIGSHIYVYERKLKGKFNMKMKF
Protein: Dmx-like 2 (A0A8I5ZMW1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MHLHQVLTGAVNPGDNCYSVGSVGEVPFTAYGSGCDIVILASDFECVQIIPGAKHGNIQVSCVECSNQHGRVAASYGNAVCIFEPLGINSHKRNSQLKCQWLKTGQFFLSSVTFNLAWDPQDNRLLTATDSIQLWAPPGSDILEEEEEVDNKVPPVLNDWKCIWQCKTSVSIHLMEWSPDGEYFATAGKDDCLLKVWYPMTGWKSSIIPQDPHEVKRRRASTQFSFVYLAHPRAVTGFSWRKTSKYMPRGSVCNVLLTSCHDGVCRLWAETLLPEDCLLGEQICETTTSSVASNLSSAGKHKDRIQHALETIHHLKNLRKGQRRSSVLVTHAELMPDKTATHEVHRHISHHANALCHFHIAASINPATDIPNVLVGTAFNIDDINGGFVVHWLNNKEFHFTSSTEIFMHQLRKLSEKQLDHESDDADREDDERSQEERERGLRMKLDHELSLDRESEAGTGSSEHEDGEREGSPRTHPRPSVSLPLPTVLLDRKIETLLTEWNKNPDMLFTIHPVDGTFLVWHVKYLDEYNPGIFRQVQVSFSSRIPVAFPSGDANSLSKNIMMYACVNATKDSYSTTSQPELMSVDSSHGSQPHYTSHSTDWNILAPTVMMVSKHIDGSLNQWAVTFADKSAFTTVLTVSHKFRYCGHRFHLNDLACHSVLPLLLTSSHHNALLTPEADCQWDTDSKLNRLIDPVKHTKGSSKQPLRNAATRTFHDPNAIYSELILWRVDPIGPLSYTGGVSELARINSLHTSAFSNVAWLPTLIPSYCLGTYCNSASACFVASDGKNLRLYQAVVDARKLLDELSDPEASKLIGEVFNIVSQQSTARPGCIIELDAITDQCGSNTQLLHVFQEDFIIGYKPHKEDMEKKEKETEIFFQPSQGYRPPPFSEKFFLVVIEKDGNNNSILHMWHLHLQSVQACLAKAAEGISSDSLLSVPGQKNMESSSETSSSVSSMPHSSSIANLQTASKLILSSRLVYSQPLDLPEAVEVIRATPSAGHLSSSSIYPVCLAPYLVVTTCSDNKVRFWKCCMETNSPCSSSGENETYHWRRWPLMNDEEKDNSSTVSIVGRPVAVSCSYTGRLAVAYKQPIHHNGFISKEFSMHVCIFECESTGGSEWVLEQTIHLDDLVKVGSVLDSRVSVDSNLFVYSKSDAFLSKDRYLIPNIKHLVHLDWVSKEDGSHILTVGVGANIFMYGRLSGIVNDQTNSKDGVAVITLPLGGSIKQGVKSRWVLLRSIDLVSSVDGTPSLPVSLSWVRDGILVVGMDCEMHVYAQWKHSVKFGDVEADSPVEQTIIQDHSAFKSSMLTRKSIAEGAAIPDDVFCSPTVVQDGGLFEAAHALSPTLPQYHPTQLLELMDLGKVRRAKAILSHLVKCIAGEVAIVRDPDAGEGTKRHLSRTISVSGSTAKDTVTIGKDGTRDYTEIDSIPPLPLHALLAADQDTSYRISEDSAKKPQSYEDHIESQPEDQYSELFQVQEITTDDIDLEPEKRENKSKVINLSQYGPAYFGQEHARVLSSHLMHSSLPGLTRLEQMFLVALADTVATTSTELDENRDKNYSGRDTLDECGLRYLLAMRLHTCLLTSLPPLYRVQLLHQGVSTCHFAWAFHSEAEEELINMIPAIQRGDPQWSELRAMGIGWWVRNVNTLRRCIEKVAKAAFQRNNDALDAALFYLSMKKKAVVWGLFRSQHDEKMTTFFSHNFNEDRWRKAALKNAFSLLGKQRFEQSAAFFLLAGSLKDAIEVCLEKMEDIQLAMVIARLFESEFETSSTYISILNQKILGCQKDGTGFNCKRLHPDPFLRSLAYWVMKDYTRALDTLLEQTPKEDDEQQVIIKSCNPVVFSFYNYLRTHPLLIRRNLASPEGTLATLGLKTEKNIADKINLIERKLFFTTANAHFKVGCPVLALEVLSKIPKVTKISSLNAKKDQLDFVSERMENGPSESKPVSSSDGGSGADWLAVTSSQFDWSQPIVTVDEEPLRLDWGEDHDGALEEDDGGGLVMKAADAKKAGQDQRASDPSALLTPQEEDCAEGDTEVDVIAEQLKFRACLKILMTELRTLATGYEVDGGKLRFQLYNWLEKEIAALHEICNHESVIKEYSSKAYSKVESELLDHEEMVDKPDIGSYERHQIERRRLQAKREHAERRKLWLQKNQDLLRVFLSYCSLHGAQGGGLASVRMELKFLLQESQQETTVKQLQSPLPLPTTLPLLSASIASTKTVIANPVLYLNNHIHDILYTIVQMRTPPQPSVEDVKVHTLHSLAASLSASIYQALCDSHSYSSQTDGNQFTGMAYQGLLLSDRRRLRTESIEEHATPNSAPAQWPGVSSLINLLSSAQDEDQPRLNVLLCEAVVAVYLSLLIHALATNSSNELFRLAAHPLNNRMWAAVFGGGVKLVVKPRRQSESIAAPPVASEDIDKHRRRFNMRMLVPGRPVKDATPPPVPAERPSYKEKFIPPELSMWDYFVAKPFLPLSDSGVIYDSDESVHSDDEEDDAFFSDTQIQEHQDPNSYSWALLHLTMVKLALHNIKNFFPIAGLEFSELPVTSPLGIAVIKNLENWEQILQEKMDHFEGPPPNYVNTYPTDLSVGAGPAILRNKAMLEPENTPFKSRDSSALPVKRLWHFLVKQEVLQETFIRYIFTKKRKQSEVEADLGYPGGKAKVIHKESDMIMAFSINKANCNEIVLASTHDVQELDVTSLLACQSYIWIGEEYDRESKSSDDIDYRGSTTTLYQPGAASHSSSQVHPPPSLPWLGSGQTSTGATVLMKRNLHNVKRMTSHPVHQYYLTGAQDGSVRMFEWTRPQQLVCFRQAGNARVTRLYFNSQGNKCGVADGEGFLSIWQVNQTASNPKPYMSWQCHSKATSDFAFITSSSLVATSGQSNDNRNVCLWDTLISPGNSLIHGFTCHDHGATVLQYAPKQQLLISGGRKGYICIFDIRQRQLMHTFQAHDSAIKALALDSCEEYFTTGSAEGNIKVWRLTGHGLIHSFKSEHAKQSIFRNIGAGVMQIEISQDNRLFSCGADGTLKTRVLPSAFNIPNRILDIL
Protein: AT5g04600/T32M21_200 (Putative RNA binding protein) (RNA-binding (RRM/RBD/RNP motifs) family protein) (Rna binding protein-like) (Q9LZ65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein WDR12 homolog
- At4g01560
- Nucleolar protein 16
- Pescadillo homolog
- Probable ribosome biogenesis protein RLP24
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Ribosome production factor 2 homolog
- Probable rRNA-processing protein EBP2 homolog
- Nucleolar complex-associated protein 3
Sequence:
MGAKAKKALKKNMKKVAASASSSQLPLPQNPKPSADFLPLEGGPARKAPVTTPPLQNKATVLYIGRIPHGFYETEIEAFFSQFGTVKRVRVARNKKTGKSKHFGFIQFEDPEVAEIAAGAMNDYLLMEHMLKVHVIEPENVKPNLWRGFKCNFKPVDSVQIERRQLNKERTLEEHRKMLQKIVKKDQKRRKRIEAAGIEYECPELVGNTQPVPKRIKFSEED
Protein: Ribosome biogenesis protein SLX9 (P53251)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in ribosome biogenesis. Required for normal pre-rRNA processing in internal transcribed spacer 1 (ITS1). May be involved in the movements of the replication forks.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Casein kinase II subunit beta
- Casein kinase II subunit alpha
- Protein SQS1
- U3 small nucleolar RNA-associated protein 22
- U3 small nucleolar ribonucleoprotein protein IMP4
- U3 small nucleolar RNA-associated protein 18
- ATP-dependent RNA helicase HAS1
- Essential nuclear protein 1
- U3 small nucleolar RNA-associated protein 6
- KRR1 small subunit processome component
Sequence:
MVAKKRNTLRSKVSARNSQNFGPDVANNGILDESYDIESDPRAFLHQPKETKKEKLLNRQNTFLSNLKGKSTLNDGIAANFDGISKSSIRRRKRKLREELKPRMQDLLTSLEQEKDLRGIIENSSKDMNNDDDIDMDSKIRFVDTKEMNLKKIEPGSVRIKKNQPNIRNQKGAKALAANETARFNQVLTNQDFQKNPFGALREVIKLQKQ
Protein: MIP15702p (Paxillin, isoform H) (D3DMM0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MANYGDYDNLDALLADLQNSVPGQPQQPQPQYGTVQPKHQALQQQQFVDNTPGYGSLRGKAQPQVYQEHYSVETRSPTAGHDFNGSSTTPGYANQGSLPRQAAGASTGLSELDSLLQDLQKIDVPVNYSTPVSKYNTMNSYATVEERPSVDSLLKELDNAHIYAVPNGSAHKSPTPGRHVTITVRETKTEKLTGPDGPVGTVEEQIVQQKDSYTPNHAVPGQQVHQAYTSQATKELDDLMASLSDFKVSNGTNGIGNGSHPQQHSSTVQHQTVTDYARPNKGSQQAHLTQTIEETTIVEDSREDQLDSMLGNLQANMSRQGVNTVQKGCCNACEKPIVGQVITALGKTWHPEHFTCNHCSQELGTRNFFERDGFPYCEPDYHNLFSPRCAYCNGAILDKCVTALDKTWHTEHFFCAQCGQQFGEEGFHERDGKPYCRNDYFEMFAPKCNGCNRAIMENYISALNSQWHPDCFVCRDCRQPFQGGSFFDHEGLPYCETHYHAKRGSLCAGCSKPITGRCITAMFKKFHPEHFVCAFCLKQLNKGTFKEQKDKPYCHTCFDKIFG
Protein: Concanavalin V (ConV) (C0HJY1)
Organism: Canavalia cathartica (Jackbean) (Canavalia virosa)
Function: D-mannose/D-glucose-binding lectin which binds alpha-methyl-D-mannoside, D-mannose and D-glucose in that order. Also binds to serum fetuin and ovalbumin. Has hemagglutinating activity towards rabbit erythrocytes. Is not toxic towards larvae of the brine shrimp Artemia. Induces relaxation in rat endothelized aorta. Shows a transient edematogenic effect in rat.
Interaction partners:
Sequence:
ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFVFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
Protein: Protein Wnt-2 (INT-1-related protein) (IRP) (P21552)
Organism: Mus musculus (Mouse)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway. Functions as upstream regulator of FGF10 expression. Plays an important role in embryonic lung development. May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P09544}. Secreted {ECO:0000250|UniProtKB:P09544}.
Interaction partners:
- Low-density lipoprotein receptor-related protein 5
- Low-density lipoprotein receptor-related protein 6
- Frizzled-1
- Frizzled-2
- Wnt inhibitory factor 1
- Frizzled-4
- Protein-serine O-palmitoleoyltransferase porcupine
- Frizzled-5
- Frizzled-7
- Palmitoleoyl-protein carboxylesterase NOTUM
Sequence:
MNVPLGGIWLWLPLLLTWLTPEVSSSWWYMRATGGSSRVMCDNVPGLVSRQRQLCHRHPDVMRAIGLGVAEWTAECQHQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAISSAGVVFAITRACSQGELKSCSCDPKKKGSAKDSKGTFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKAVKRFLKQECKCHGVSGSCTLRTCWLAMADFRKTGDYLWRKYNGAIQVVMNQDGTGFTVANKRFKKPTKNDLVYFENSPDYCIRDREAGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHVTRMTKCECKFHWCCAVRCQDCLEALDVHTCKAPKSADWATPT
Protein: Slr1406 protein (P73592)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
Sequence:
MKVSKRFFQPCLVLGISLGLSLALVPDALALKTYYQLPISLAVEAAMEAVNTCQQDGYNVTATVVNREGLVQAVIRGDDATPHTIENSFYKAFTLITLGPITGQDSTGAIAQKMTPAPLPVGSVPLAPNPITGLSFSTGGSAIKVGDQLVAAIGVSGSPNGNLDQTCGLKGIEKIKSRLVP
Protein: Insulin-like growth factor-binding protein 3 (IBP-3) (IGF-binding protein 3) (IGFBP-3) (P17936)
Organism: Homo sapiens (Human)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R. Inhibits the positive effect of humanin on insulin sensitivity. Promotes testicular germ cell apoptosis.
Subcellular location: Secreted {ECO:0000269|PubMed:20353938}. Nucleus {ECO:0000269|PubMed:10874028, ECO:0000269|PubMed:19556345}.
Interaction partners:
- Insulin-like growth factor-binding protein complex acid labile subunit
- Insulin-like growth factor 2
- Insulin-like growth factor 1
- Insulin
- Epidermal growth factor receptor
- Insulin-like growth factor-binding protein 5
- Insulin-like growth factor-binding protein 3 receptor
- Fibronectin
- Insulin-like growth factor 1 receptor
- Retinoic acid receptor RXR-alpha
Sequence:
MQRARPTLWAAALTLLVLLRGPPVARAGASSAGLGPVVRCEPCDARALAQCAPPPAVCAELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVNASAVSRLRAYLLPAPPAPGNASESEEDRSAGSVESPSVSSTHRVSDPKFHPLHSKIIIIKKGHAKDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNHLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVHCYSMQSK
Protein: C-C chemokine receptor type 9 (C-C CKR-9) (CC-CKR-9) (CCR-9) (G-protein coupled receptor 28) (GPR-9-6) (CD antigen CDw199) (P51686)
Organism: Homo sapiens (Human)
Function: Receptor for chemokine SCYA25/TECK. Subsequently transduces a signal by increasing the intracellular calcium ions level.
Subcellular location: Cell membrane {ECO:0000305|PubMed:27926729}; Multi-pass membrane protein {ECO:0000305|PubMed:27926729}.
Interaction partners:
- C-C motif chemokine 25
- Mucosal addressin cell adhesion molecule 1
- C-C motif chemokine 21
- C-C motif chemokine 19
- C-C motif chemokine 3
- Atypical chemokine receptor 4
- Stromal cell-derived factor 1
- C-C motif chemokine 27
- Guanine nucleotide-binding protein G
- C-C motif chemokine 5
Sequence:
MTPTDFTSPIPNMADDYGSESTSSMEDYVNFNFTDFYCEKNNVRQFASHFLPPLYWLVFIVGALGNSLVILVYWYCTRVKTMTDMFLLNLAIADLLFLVTLPFWAIAAADQWKFQTFMCKVVNSMYKMNFYSCVLLIMCISVDRYIAIAQAMRAHTWREKRLLYSKMVCFTIWVLAAALCIPEILYSQIKEESGIAICTMVYPSDESTKLKSAVLTLKVILGFFLPFVVMACCYTIIIHTLIQAKKSSKHKALKVTITVLTVFVLSQFPYNCILLVQTIDAYAMFISNCAVSTNIDICFQVTQTIAFFHSCLNPVLYVFVGERFRRDLVKTLKNLGCISQAQWVSFTRREGSLKLSSMLLETTSGALSL
Protein: 1-deoxy-D-xylulose-5-phosphate synthase (EC 2.2.1.7) (O50408)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1
- Thiazole synthase
- Type B diterpene cyclase
- Tuberculosinyl adenosine transferase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 1-deoxy-D-xylulose-5-phosphate synthase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- Geranylgeranyl diphosphate synthase
Sequence:
MFDTGHQTYPHKLLTGRGKDFATLRQADGLSGYPNRHESPHDWVENSHASVSLAWVDGIAKALALQGQCDRRVIAVIGDGALTGGVAWEGLNNLGAATRPVIVVLNDNGRSYDPTAGALAAHLEELRVGTPRGPNLFENMGFTYIGPVDGHNIPDTCAVLRKAAAAARPVVVHAVTSKGRGYPPAEADERDHMHACGVVDIATGLASTPSQRSWTDVFEDEIARIADDRSDVVGLTAAMRLPTGLGALSRRYPHRVFDSGIAEQHLLASAAGLAAAGTHPVVAVYSTFLHRAFDQLLFDIGLHRLPVTLVLDRAGVTGPDGPSHHGLWDLALLACVPGFQIACPRDAPRLRQQLRTAIATAAPTAVRFPKGAPGEPITAEHTIGGLDVLHTPPPHWRPDVLLVAVGAMSRPCMDAARCLSEEQIGVTVVDPQWVWPISPALTELAGRHRITVCVEDAIADVGIGAHLSHHIGRTHPRTRTYTLGLPPAYIPHASRDHILSSHGLTGPAIRIRCKSLLNALHEVPGPEDHPDSGDSY
Protein: F-box protein MAX2 (F-box/LRR-repeat protein 7) (Protein KARRIKIN INSENSITIVE 1) (Protein MORE AXILLARY BRANCHING 2) (Protein ORESARA 9) (Q9SIM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes the senescence. Is necessary for responses to strigolactones and karrikins. Contributes to the selective repression of axillary shoots and moderates the branching by regulating negatively the auxin transport in primary stems, in an AXR1-independent manner. Required for the progression of leaf senescence mediated by methyl jasmonate. Required at each node to suppress axillary bud growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:17346265}.
Interaction partners:
- Probable esterase KAI2
- Protein SUPPRESSOR OF MAX2 1
- Strigolactone esterase D14
- Carotenoid cleavage dioxygenase 8, chloroplastic
- Carotenoid cleavage dioxygenase 7, chloroplastic
- Cytochrome P450 711A1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2
- Protein SMAX1-LIKE 2
- Protein SMAX1-LIKE 6
- Protein SMAX1-LIKE 7
Sequence:
MASTTLSDLPDVILSTISSLVSDSRARNSLSLVSHKFLALERSTRSHLTIRGNARDLSLVPDCFRSISHLDLSFLSPWGHTLLASLPIDHQNLLALRLKFCFPFVESLNVYTRSPSSLELLLPQWPRIRHIKLLRWHQRASQIPTGGDFVPIFEHCGGFLESLDLSNFYHWTEDLPPVLLRYADVAARLTRLDLLTASFTEGYKSSEIVSITKSCPNLKTFRVACTFDPRYFEFVGDETLSAVATSSPKLTLLHMVDTASLANPRAIPGTEAGDSAVTAGTLIEVFSGLPNLEELVLDVGKDVKHSGVALEALNSKCKKLRVLKLGQFQGVCSATEWRRLDGVALCGGLQSLSIKNSGDLTDMGLVAIGRGCCKLTTFEIQGCENVTVDGLRTMVSLRSKTLTDVRISCCKNLDTAASLKAIEPICDRIKRLHIDCVWSGSEDEEVEGRVETSEADHEEEDDGYERSQKRCKYSFEEEHCSTSDVNGFCSEDRVWEKLEYLSLWINVGEFLTPLPMTGLDDCPNLEEIRIKIEGDCRGKRRPAEPEFGLSCLALYPKLSKMQLDCGDTIGFALTAPPMQMDLSLWERFFLTGIGSLSLSELDYWPPQDRDVNQRSLSLPGAGLLQECLTLRKLFIHGTAHEHFMNFLLRIPNLRDVQLRADYYPAPENDMSTEMRVGSCSRFEDQLNSRNIID
Protein: Calcium-binding protein 7 (CaBP7) (Calneuron II) (Calneuron-2) (Q91ZM8)
Organism: Mus musculus (Mouse)
Function: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MPFHPVTAALMYRGIYTVPNLLSEQRPVDIPEDELEEIREAFKVFDRDGNGFISKQELGTAMRSLGYMPNEVELEVIIQRLDMDGDGQVDFEEFVTLLGPKLSTSGIPEKFHGTDFDTVFWKCDMQKLTVDELKRLLYDTFCEHLSMKDIENIIMTEEESHLGTAEECPVDVETCSNQQIRQTCVRKSLICAFAIAFIISVMLIAANQVLRSGMK
Protein: Smooth protein (Smooth, isoform A) (Smooth, isoform E) (Q7JMZ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYNGASNGSGASGAGGGGATIVVTEGPQNKKIRTGVQQPGENDVHMHARSTPQQNQQQALMNKSNDDLRRKRPETTRPNHILLFTIINPFYPITVDVLHKICHPHGQVLRIVIFKKNGVQAMVEFDNLDAATRARENLNGADIYAGCCTLKIDYAKPEKLNVYKNEPDTSWDYTLSTEPPLLGPGAAFPPFGAPEYHTTTPENWKGAAIHPTGLMKEPAGVVPGRNAPVAFTPQGQAQGAVMMVYGLDHDTSNTDKLFNLVCLYGNVARIKFLKTKEGTAMVQMGDAVAVERCVQHLNNIPVGTGGKIQIAFSKQNFLSEVINPFLLPDHSPSFKEYTGSKNNRFLSPAQASKNRIQPPSKILHFFNTPPGLTEDQLIGIFNIKDVPATSVRLFPLKTERSSSGLIEFSNISQAVLAIMKCNHLPIEGKGTKFPFIMKLCFSSSKSMNGAWNNAASEGMIEKENEVDTKVDIYN
Protein: Tubulin alpha-3C chain (EC 3.6.5.-) (Alpha-tubulin 2) (Alpha-tubulin 3C) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-3C chain] (P0DPH7)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-2A chain
- Tubulin beta chain
- Tubulin beta-4B chain
- Tubulin beta-6 chain
- Tubulin beta-4A chain
- Tubulin beta-1 chain
- Tubulin beta-8 chain
- Tubulin beta-2B chain
- Tubulin beta-3 chain
- Cell division control protein 42 homolog
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY
Protein: Probable polyketide synthase Pks17 (O06585)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable polyketide synthase Pks8
- Probable fatty acid synthase Fas
- Probable polyketide synthase Pks9
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks15
- Polyketide synthetase MbtC
- Polyketide synthase Pks13
- Phenyloxazoline synthase MbtB
- NADH-quinone oxidoreductase subunit C
- Probable polyketide synthase Pks7
- NADH-quinone oxidoreductase subunit I
Sequence:
MEAGPQRIAQMLAELVELFKTEALHRLPVKSWDVRHAREAYRFLSQARHVGKVVLTMPDAWAAGTVLITGGTGMAGSAVARHLVSRYGVRQVVLASRAGEHTESVAALVDELGSAGARVQVVSCDVADRDAVAGLVASQPDLTAVFHAAGVLDDAVITGLTPERVDKVLRAKVDGAWNLHELTRHLDVSAFVLFSSMAGIVGAPGQANYAAANAFLDGLAAYRRSRGLAALSVAWGLWEQASAMTEHLGERDRVRMSRVGLAPLPTNQAMGFLDAALLADRPVVVAARLDRAALAGAELPALFSQLVAGPIRRIIDGADEVSGSGLASRLHGLTPEQRHRELTELVCSNAAIVLGHSGTEIDAHKAFQDLGFDSLTAVELRNRLKTATGLTLPPTLIFDYPTAAELAEHLDIQLANAPAVTVDQPNPSTRFNEVTRELQALLDQPNWNPDDKTRLIKRLQAILTDCTAPPASSGPSTTHDDEDITTATESQLFAILDDELGP
Protein: Disease resistance protein L6 (2' cyclic ADP-D-ribose synthase) (2'cADPR synthase L6) (EC 3.2.2.-) (NAD(+) hydrolase L6) (EC 3.2.2.6) (NADP(+) hydrolase L6) (EC 3.2.2.-) (Q40253)
Organism: Linum usitatissimum (Flax) (Linum humile)
Function: TIR-NB-LRR receptor-like protein that confers resistance to the flax rust phytopathogenic fungus (M.lini). Acts as a NAD(+) hydrolase (NADase): in response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death. Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules.
Interaction partners:
Sequence:
MSYLREVATAVALLLPFILLNKFWRPNSKDSIVNDDDDSTSEVDAISDSTNPSGSFPSVEYEVFLSFRGPDTREQFTDFLYQSLRRYKIHTFRDDDELLKGKEIGPNLLRAIDQSKIYVPIISSGYADSKWCLMELAEIVRRQEEDPRRIILPIFYMVDPSDVRHQTGCYKKAFRKHANKFDGQTIQNWKDALKKVGDLKGWHIGKNDKQGAIADKVSADIWSHISKENLILETDELVGIDDHITAVLEKLSLDSENVTMVGLYGMGGIGKTTTAKAVYNKISSCFDCCCFIDNIRETQEKDGVVVLQKKLVSEILRIDSGSVGFNNDSGGRKTIKERVSRFKILVVLDDVDEKFKFEDMLGSPKDFISQSRFIITSRSMRVLGTLNENQCKLYEVGSMSKPRSLELFSKHAFKKNTPPSYYETLANDVVDTTAGLPLTLKVIGSLLFKQEIAVWEDTLEQLRRTLNLDEVYDRLKISYDALNPEAKEIFLDIACFFIGQNKEEPYYMWTDCNFYPASNIIFLIQRCMIQVGDDDEFKMHDQLRDMGREIVRREDVLPWKRSRIWSAEEGIDLLLNKKGSSKVKAISIPWGVKYEFKSECFLNLSELRYLHAREAMLTGDFNNLLPNLKWLELPFYKHGEDDPPLTNYTMKNLIIVILEHSHITADDWGGWRHMMKMAERLKVVRLASNYSLYGRRVRLSDCWRFPKSIEVLSMTAIEMDEVDIGELKKLKTLVLKFCPIQKISGGTFGMLKGLRELCLEFNWGTNLREVVADIGQLSSLKVLKTTGAKEVEINEFPLGLKELSTSSRIPNLSQLLDLEVLKVYDCKDGFDMPPASPSEDESSVWWKVSKLKSLQLEKTRINVNVVDDASSGGHLPRYLLPTSLTYLKIYQCTEPTWLPGIENLENLTSLEVNDIFQTLGGDLDGLQGLRSLEILRIRKVNGLARIKGLKDLLCSSTCKLRKFYITECPDLIELLPCELGGQTVVVPSMAELTIRDCPRLEVGPMIRSLPKFPMLKKLDLAVANITKEEDLDAIGSLEELVSLELELDDTSSGIERIVSSSKLQKLTTLVVKVPSLREIEGLEELKSLQDLYLEGCTSLGRLPLEKLKELDIGGCPDLTELVQTVVAVPSLRGLTIRDCPRLEVGPMIQSLPKFPMLNELTLSMVNITKEDELEVLGSLEELDSLELTLDDTCSSIERISFLSKLQKLTTLIVEVPSLREIEGLAELKSLRILYLEGCTSLERLWPDQQQLGSLKNLNVLDIQGCKSLSVDHLSALKTTLPPRARITWPDQPYR