wanglab/gogpt-training-data huggingface dataset:
Protein: DNA adenine methylase (EC 2.1.1.72) (DNA-(N(6)-adenine)-methyltransferase) (Deoxyadenosyl-methyltransferase) (Orphan methyltransferase M.EcoT4Dam) (M.EcoT4Dam) (P04392)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: An alpha subtype methylase, recognizes the double-stranded sequence 5'-GATC-3' and methylates A-2. Also acts on 5-hydroxymethylcytosine (hmC)-containing DNA, the normal base in this virus. May prevent degradation of viral DNA by the host restriction-modification antiviral defense system (Probable).
Interaction partners:
Sequence:
MLGAIAYTGNKQSLLPELKSHFPKYNRFVDLFCGGLSVSLNVNGPVLANDIQEPIIEMYKRLINVSWDDVLKVIKQYKLSKTSKEEFLKLREDYNKTRDPLLLYVLHFHGFSNMIRINDKGNFTTPFGKRTINKNSEKQYNHFKQNCDKIIFSSLHFKDVKILDGDFVYVDPPYLITVADYNKFWSEDEEKDLLNLLDSLNDRGIKFGQSNVLEHHGKENTLLKEWSKKYNVKHLNKKYVFNIYHSKEKNGTDEVYIFN
Protein: Protein disulfide-isomerase A4 (EC 5.3.4.1) (Endoplasmic reticulum resident protein 72) (ER protein 72) (ERp-72) (ERp72) (P08003)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P13667}. Melanosome {ECO:0000250|UniProtKB:P13667}.
Interaction partners:
- Endoplasmin
- Hypoxia up-regulated protein 1
- Endoplasmic reticulum chaperone BiP
- Peptidyl-prolyl cis-trans isomerase B
- DnaJ homolog subfamily B member 11
- ERO1-like protein beta
- Stromal cell-derived factor 2-like protein 1
- ERO1-like protein alpha
- Protein disulfide-isomerase A6
- Calreticulin
Sequence:
MKLRKAWLLVLLLALTQLLAAASAGDAHEDTSDTENATEEEEEEDDDDLEVKEENGVWVLNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPPIAVAKIDATSASMLASKFDVSGYPTIKILKKGQAVDYDGSRTQEEIVAKVREVSQPDWTPPPEVTLSLTKDNFDDVVNNADIILVEFYAPWCGHCKKLAPEYEKAAKELSKRSPPIPLAKVDATEQTDLAKRFDVSGYPTLKIFRKGRPFDYNGPREKYGIVDYMIEQSGPPSKEILTLKQVQEFLKDGDDVVIIGLFQGDGDPAYLQYQDAANNLREDYKFHHTFSPEIAKFLKVSLGKLVLTHPEKFQSKYEPRFHVMDVQGSTEASAIKDYVVKHALPLVGHRKTSNDAKRYSKRPLVVVYYSVDFSFDYRAATQFWRNKVLEVAKDFPEYTFAIADEEDYATEVKDLGLSESGEDVNAAILDESGKKFAMEPEEFDSDTLREFVTAFKKGKLKPVIKSQPVPKNNKGPVKVVVGKTFDAIVMDPKKDVLIEFYAPWCGHCKQLEPIYTSLGKKYKGQKDLVIAKMDATANDITNDQYKVEGFPTIYFAPSGDKKNPIKFEGGNRDLEHLSKFIDEHATKRSRTKEEL
Protein: Autophagy-related protein 2 (Q9VZX7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Preautophagosomal structure membrane {ECO:0000256|ARBA:ARBA00004623}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004623}.
Interaction partners:
- Autophagy-related 18b, isoform A
- Autophagy-related 1, isoform B
- Autophagy-related 18a, isoform E
- Autophagy-related protein 9
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Cysteine protease
- Serine/threonine-protein kinase ULK3
- Ubiquitin-like-conjugating enzyme ATG3
- RB1-inducible coiled-coil protein 1
- Autophagy protein 5
Sequence:
MSWFNPWDGLKTKMCRYLLQRYLGQFFENNLNLEQLKVDLYNGKAVVEDIFLKVNAFNDLFEDQGWAFEVVSGHIGRLTVVVPWNALMTNDSSLEIHNLTITLRPVTRYQSGTTMLESMWSSVSSSMQMAEECMKQVDDDVPFLNHNNALIGLEKFAETIDNVLNRIRAKLTNTTLNIEYILPRSDRKLVLSFQASHVEYKNKTGYEMPMSTSQDTETEEDPNSSFNALPMIAKHNLVIEGLSLHTSEVLDVMDHQFGPTPYEQLCKIVELKGAQNIQINIKQTENIVGPKVSLELSLDDIYFMLTPRQIHLLIEFSKGFNCGGQQERPKKGRSLKSAPPSEYQMHSLQQPTRMTGILGQNADWCTGMSEADPSEYSVYGNPPRSGYARSRKMSESTNSMVTSCTNTLQQELGYTEKSGEILKFKVQISKIYGIALHQDILIQNTANIDSCSTVFDHASYLRYSDTASGFFLGTLLENHIPLQNQQYLLLRAAPIIVSGSQQRYFQELTSRTTLSATAVDLIEVLDNSKEHLLQFDRQRNCPDGYHIRPEIVLTQSSSFMFKQNHNRCSNKIECSLDECTAELDISIYDRLGALFGSSPFSGDSASSTPYPDDPNQTEFVVKSENLRLHLRFPVVDGRAANDPLKIPWWKKNVRRDFLAVEFRSLVVSSRSQISIVSDELDVFYCDADKQSAVHLLKCQQKMQPNKKIQIDVLQLKDTSDGQKKARKSPFSSKCTFGYTSHVEGLDGSVDKTDSLLPGETEEINEFCDSCTQSSKLKIFAFIPHVKVVLESKSMYELIYNRLNGDLFMWEPRSPHYDISPDNEVPESKDLYAEPQLEEFRRNLLLSTSAMESSIYFSMAEPTASAPPAPPVRNEAFSFELFVEQGTLILFSHLLDPETNQRSKECGKFQVNLKELRLFTVNGLDNDSTRSFFSIQLGEIDALHCGNTLQDLELAWSDLADEKLLPTIYNFASVHQQQDRKRMEVLSLVAEIKKQPEQRIKRMKMSFGICGAILQHHSCHSEHSWLNQLIDFMDVADFPIEEYEPFALVSELQLHVWNAGIDYRPKFFPQRAFLDLGYCTLSSNIISSMSGCTLRLLAEDCVLQLGLVKEESNDSLIPVLNLGLLNISFRLNAEGSGQPRVDLRSSIHDMHLKTCYDSAAALAQLIAYVANDRDLCPPEEPILNEDTKPAEPKPNEEHEMSDHTQNHVSKLMADAVIDVESSPNLRAMKSPGGREEGIEIFYFPDEPKEKRKSTSAKLQTKSLMVESPSVIGDILDFESNVILQSYYHQSQVQPQTSLGSQVQQELGSLGNASLEERDFDIIHDEEISRMDKFGVKQIYISEDPLQIVDNHFELPHEKVDLLRPPSNFPVAESTYTLCEMTFTWHLYGGRDFPDEPLKKSSSSATSGFGMSDTYKYGVSQAQEQDKQDKKGSKKGLLKQPKGSQRNLEVLVEMQLSKIRFSYETYPLTSMYSSRQVLLVSEIEIRDRLRSSDINKFLYHPTGNNLSHKPDENMVIVKALNVRPNPQKSSAEECSLRVSILPIKLNIDQDTLLFLEDFFSGMFRNSASAAGGTKTEGSSSSATDMPVMSVSKMPEELSDKLPDSEVKEMVERNLNVLIEENSLDVELEEDPATAPPVFFREVIFSPALPICFDYHGRRIELSRGPVTGLIMGLAQLQGSGINLREIVNRRGILGWNKLCEFLAKEWLKDIKRNQLPNILSGIGPTNAVLQLFQGIYDLFRLPIEQYNKDGRIIRGFQLGAQSFTARTALAALEITSRIIHLLQFTAETTFDMLSAGPSMKKRKGGRQGKRRRQGRPKDLREGVANAYTIVREGINESANTLIEAAITEHDQKGYSGAVGAVVRQIPQLVVCPAVLATQATTNILGGAKSSLIPEAKLEARDKWKQEIH
Protein: Ribosome production factor 2 homolog (Ribosome biogenesis protein RPF2 homolog) (Q8IJC0)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU367086}.
Interaction partners:
- Ribosome biogenesis regulatory protein
- Ribosome biogenesis protein NSA2 homolog
- 60S ribosomal subunit protein L24, putative
- 60S ribosomal protein L5, putative
- Nucleolar GTP-binding protein 2
- Pescadillo homolog
- Ribosome biogenesis protein MRT4, putative
- rRNA-processing protein EBP2, putative
- Nucleolar complex protein 2, putative
- Ribosome biogenesis protein BOP1 homolog
Sequence:
MDELNKEEIVDNINNEQAKTRKGHLILKKREGVYEESSKYCLFIGSNKRSLILKNFMYDIYSIYKPLTCYMPKAHSNLSNIIDKIDKLVDICVHNNCSFFFSVFSTKKKPSRFIIGRLYNNKILDYYVFSLISYIPLKLFPLSKEILYDTKPIVLIQGSYFEQNETNRYVKNILFDFFKHKNVDTFSKKSIQRLIVISAYQKNNEINADLGKKVEAGKENNDKNNDDDKNNDDNKNNDDDNKNNDDDNKNNDDDNKNNDDDKNNDDDKNNDDDKNNDDDNKNNDDDNKNNDDDKNNDDDKNNDDDKNNDDNKNNDDNNKNNNNDDDDDVTLNFTEDAMSTTKENVNDSFKNMDNIYNNLNTNKFNSYDKLKDKDKKNLYVISFNQYLITKEFFNINKENEQPPKLQEIGPRFEFTLEENYKTPEYNLFQEALRTVKKQEKTKIKNVHVDEFGHNIKKVYVQKQNFSKLHTKHTKFVKKNKFNT
Protein: Ankyrin-repeat and fibronectin type III domain containing 1 (F6RWQ6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
METSPNRRLPFKDRHFTCSKIIGRRFACFAQRLSYRRKQSQCDLLNESTGHLPATCSSAASKSLSWNYCSKMTQQMQNLHLSQSKKHSAPSSPNAAKRLYRNLSEKLKGSHSSFDEAYFRTRTDRLSLRKTSVNFQGNEAMFEAVEQQDLDAVQLLLYQYTPEELDLNTPNSEGLTPLDIAIMTNNVPIARILLRTGARESPHFVSLESRAMHLNTLVQEAQDRVSELSAQVENEGFTLDNTEKEKQLKAWEWRYRLYRRMKTGFEHARAPEVPANACLMVSSSTSLTVSFQEPLSVNAAVVTRYKVEWSMSKDFSPLAGEIIMDNLQTLRCTITGLTTGQQYFVQVSAYNMKGWGPAQTTTPVCASPSNWKDYDDREPRHKGQSEVLESLLQQVRALHQHYSCRESSKLQTTGRKQSVSRSLKHLFHSSNKFVKTLKRGLYIATIFYYKDNMLVTNEDQIPIVEIDDSHTSSITQDFLWFMKLSCMWEDIRWLRQSVPISMSSSTVLQTRQKMLAATAQLQNLLGTHNLGRLYYEPIKDRHGNILIVTIREVEMLYSFFNGKWMQISKLQSQRKSLSTPEEPTALDILLITIQDILSYHKRSHQRLSPGLYLGYLKLCSSVDQIKVLVTQKLPNILCHVKIRENHNISKEEWEWIQKLSGSESMESVDHNADCPMQLFFYELQMAVAALLKQINIPRHQARNFRLYTQEVLEIGHNVSFLLLLPASDDVCTAPGQNNPYTPHSGFLNLPLQMFELGIVACFT
Protein: Odorant receptor 67d (Q9VT92)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in detection and sensitivity to pheromones and signal transduction of the fatty-acid-derived male pheromone 11-cis vaccenyl acetate (cVA). Acts in concert with Snmp and lush to capture cVA molecules on the surface of Or67d expressing olfactory dendrites and facilitate their transfer to the odorant-receptor Orco complex. Necessary to mediate behavioral responses to cVA by regulating both male and female mating behavior. Activation of Or67d neurons by cVA inhibits courtship of other males, whereas in females their activation promotes receptivity to other males. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 65a
- Odorant receptor 88a
- General odorant-binding protein lush
- Odorant receptor 47b
- Odorant receptor coreceptor
- Odorant receptor 42b
- Odorant receptor 56a
- Odorant receptor 22a
- Putative odorant receptor 92a
- Odorant receptor 85a
Sequence:
MLKMAKVEPVERYCKVIRMIRFCVGFCGNDVADPNFRMWWLTYAVMAAIAFFFACTGYTIYVGVVINGDLTIILQALAMVGSAVQGLTKLLVTANNASHMREVQNTYEDIYREYGSKGDEYAKCLEKRIRITWTLLIGFMLVYIILLGLVITFPIFYLLILHQKVLVMQFLIPFLDHTTDGGHLILTAAHVILITFGGFGNYGGDMYLFLFVTHVPLIKDIFCVKLTEFNELVMKRNDFPKVRAMLCDLLVWHQLYTRMLQTTKKIYSIVLFVQLSTTCVGLLCTISCIFMKAWPAAPLYLLYAAITLYTFCGLGTLVENSNEDFLSVIYTNCLWYELPVKEEKLIIMMLAKAQNEVVLTAADMAPLSMNTALQLTKGIYSFSMMLMNYLG
Protein: Serine/threonine-protein kinase RUNKEL (Protein EMBRYO DEFECTIVE 3013) (Protein RUNKEL) (EC 2.7.11.1) (F4JY37)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein that regulates phragmoplast microtubule organization during cell plate expansion in cytokinesis during cell division, both somatic and syncytial. Required for endosperm cellularisation. In pollen development, involved in cellularisation during microsporogenesis by regulating radial microtubules (MT) organization in microspore mother cells. Seems to not have kinase activity.
Subcellular location: Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:19268593}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19268593}. Note=Also colocalizes with mitotic preprophase band. {ECO:0000269|PubMed:19268593}.
Interaction partners:
- Kinesin-like protein KIN-7A
- Uncharacterized protein At1g01500
- Mitotic checkpoint protein BUB3.2
- Pentatricopeptide repeat-containing protein At4g39530
- DNA replication complex GINS protein SLD5
- Phragmoplastin interacting protein 1
- At1g76620/F14G6_22
- Serine/threonine-protein kinase-like protein At1g28390
- Methionyl-tRNA formyltransferase, mitochondrial
- Titan9
Sequence:
MNQYHIYEAIGHGKCSTVYKGRKKKTIEYFACKSVDKSRKNKVLQEVRILHSLNHPNVLKFYAWYETSAHMWLVLEYCVGGDLRTLLQQDCKLPEESIYGLAYDLVIALQYLHSKGIIYCDLKPSNILLDENGHIKLCDFGLSRKLDDISKSPSTGKRGTPYYMAPELYEDGGIHSFASDLWALGCVLYECYTGRPPFVAREFTQLVKSIHSDPTPPLPGNASRSFVNLIESLLIKDPAQRIQWADLCGHAFWKSKINLVQLPTQPAFDDMIGINTKPCLSERNGDRPNKTPPKYREKDRKGGSKQNENSIQGSKGHETPIKGTPGGSKAQAKLPSRATEEKHGGRPAANRQVNILRLSRIAKANLQKENEKENYRRPLPNSNENCAEVKIDNTDMELDFDENNDDEGPDESEGTENTSCAQEERVMSHNENHRRQRVVSSNVPDENSSANETPTLGEARDCHEDQSEPMDMSAAPPSASPQLKTHRGRETSGVAVNHDSSKAPTSLTDVFWHISDLSVRPVMPSRKSDKEAVHSLSFETPQPSDFSKKGKQELEPLNNRIITVLSGSSSGLSEKQNLIRYLETLSTNADAANILTNGPIMLVLVKVLRLSKTPAFRVQIASLIGLLIRHSTSIEDDLANSGILDSLTNGLRDKHEKVRRFSMAALGELLFYISTQNEHKDFKPPESPSKETRSASGWQVSNALISLVSSVLRKGEDDLTQVYALRTIENICSQGAYWATRFSSQDLISNLCYIYKATGKQESMRQTAGSCLVRLARFNPPCIQTVVEKLSLKEIASSFVKGSAREQQVCLNLLNMAMIGSHTFTSFGRHLVTLTEEKNLFPSLLSIIEQGTEVLRGKALLFVAFLCKNSRRWLTNFFCNARFLPVVDRLAKEKDSYLQQCLEAFVNVIASIIPGMLDTITNDIQQLMTGRRHGPVSPLNSRAPVKTNAHLFPVVLHLLGSSSFKNKMVTPQVLRQLANLTKLVEASFQGRDDFRVTLLQVLECITGDAPLVTQNGEIIIREILPSLAAIYNGNKDGDARFLCLKIWFDSLTILLTECTEIEQQISEDLKSISNSHFLPLYPALIQDEDPIPAYAQKLLVMLVEFDYIKISNLLRHNTVSQCFEFLLGDLSSANVNNVKLCLALASAPEMESKLLSQLKVVRRIGNLLEFVNAKDMEDFLEPTLSLCRAFLLRSLGNKKGLSSNYTKEPTLLSEASFTFEVDPQECIRDIADFGSNIGLFLHFAGLDDDTSIAVADIASECVVLLLKAASREATTGFLTNLPKITPILDSWRRRKSTELHLLVLKRVLHCLGYACKQYLSQAMILSISGHDVSKINAIVSEMKNSDAAGLNSIASLVAMELQRLPR
Protein: Superoxide dismutase [Mn] 2, mitochondrial (EC 1.15.1.1) (P41977)
Organism: Caenorhabditis elegans
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17894411}.
Interaction partners:
- Superoxide dismutase
- Extracellular superoxide dismutase
- Superoxide dismutase
- Forkhead box protein O
- Catalase-2
- Large ribosomal subunit protein bL17m
- Peroxisomal catalase 1
- Superoxide dismutase 1, mitochondrial
- Insulin-like receptor
- Glutathione S-transferase 4
Sequence:
MLQSTARTASKLVQPVAGVLAVRSKHTLPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQIEEKLHEAVSKGNLKEAIALQPALKFNGGGHINHSIFWTNLAKDGGEPSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKILKIATCANQDPLEGMVPLFGIDVWEHAYYLQYKNVRPDYVHAIWKIANWKNISERFANARQ
Protein: tRNA (32-2'-O)-methyltransferase regulator TRM732 (Q03496)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required together with TRM7 for the methylation of the 2'-O-ribose of cytidine at position 32 of the tRNA anticodon loop of tRNA(Phe) and tRNA(Leu(UAA)).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- Multifunctional methyltransferase subunit TRM112
- tRNA
Sequence:
MTTDVQFSSQEIELFRVKEFLIANNPAKINNENKDAVLTQIEHDFRYLIQYIKDGLPNLNESTRLIFPDTFSICLLRSHQIIASKKIDSQEFLSAVKEQLLTEANANIIFEYVLDFWADGGAPLMNALRDLFSKLLNLLKITYPMSTLKDVLFNWMNEILEVPSTLRVQYYLIDALSSDFDLYYIIEKKPHFIDNSFSLMNSDLLANSVGKCIVSLLLNIYEKHFKKNESFVQEWIQLWKSCALKYIHDKQYTKSINLYIMIPLFKNMPNSAFTLFLECMSNKDPSLLLSLLKIGQELGIEEEPFCDNKYTTVDSVNKLIEQDEYKLQVFEILTFSTKKSKPIRPFVFKTIKQYLYVFFVDTELERRNYFCSSMKHFIFRTRDCAYSLARDARKLKKAEKFPDEQREKLAQVEEARAFLVWLCNFIKYNLAPGTLYQANVTSLKLMHILIKSGVDKSTPQKFLDNQNKREYPFSIPILQDVTFLRLLIDLLVSNYADVRELSKEMLFIMISADESRGLFLDTLDANALKWTATSLLSDYEKGDAGATVYEFIFTVMGSQRSFIDQTIDILAQMVQNLQNDSIGCAENSIGPHFAALSLILNKFNSEENHQDTSKIISKLINLVLKSWEATRNVVCHDSAHGILPEKYANCGVPDQVIISHAFRAIKEASYLLETILKKYPLTRDQLDSIGDLFIVQLSTIRHSGAFQAVLPGLKAFCIRCQLEFPAILEELLSKSVKSLKSKTQHITRRSGGLPFLVTTVLSAEVTKGRPLLQKTFENLLLVARLPIPPHQDEFDLPQVNAINCINAIFVEPKLSVHCTSFVSEALELALLNFDCDIWALRNCSIMLFTSLQNRIFGKVGRSVSAKLFFTKYSGLRQLLLNILNSSIAQYSGSERKSYQIESIFLVLNVLLRLRPTAGYTGLKEFNVSVYECLSNENWKIRDMASRVLHMLSENFEEEIRKLLDLASIAKQNQLHGHLLALQQLVPQYLSGTRDMELIQRILEKKRMLLLENKCFITKKAYLKLTCCILETCDIPDSILKDYISTLRNTFIAENNEYVVDGSKQLYLAQILDMLLKYEDSIYLDDICLLGLYSPFYEAQLSTLQYMNTNFHWETTRNSEFLEQLQLLLRVPDLLPMAKALVVKILSRKKNTLSLTTCTDLLKTNNSEDTKLAAVSSLSAKLSSQTFHQVWNLLQGFFADSCSKDFRLASLECLTAYPESCKNSRILLQLYNFLWDDDSEIREKASFYLNKNFIQTADWEYNRNTSVTALIFTKKFVDVFTSSEVVEELCLQLFQYLNEYDMFAAEESAKNCLFTIEKDNQFINELQKAMHILNMIKLTGRDISKCYKDQIHHLKSALLEHFNTEDFKDSPLGWCSNAEIFSRITLLKELIQHYSPSDYENFINVLTKHSVHPLIISYSQL
Protein: Malignant T-cell-amplified sequence 1 (MCT-1) (Multiple copies T-cell malignancies) (Q9ULC4)
Organism: Homo sapiens (Human)
Function: Anti-oncogene that plays a role in cell cycle regulation; decreases cell doubling time and anchorage-dependent growth; shortens the duration of G1 transit time and G1/S transition. When constitutively expressed, increases CDK4 and CDK6 kinases activity and CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK complex formation. Involved in translation initiation; promotes recruitment of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role as translation enhancer; recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, subsequently altering the mRNA translation profile; up-regulates protein levels of BCL2L2, TFDP1, MRE11, CCND1 and E2F1, while mRNA levels remains constant. Hyperactivates DNA damage signaling pathway; increased gamma-irradiation-induced phosphorylation of histone H2AX, and induces damage foci formation. Increases the overall number of chromosomal abnormalities such as larger chromosomes formation and multiple chromosomal fusions when overexpressed in gamma-irradiated cells. May play a role in promoting lymphoid tumor development: lymphoid cell lines overexpressing MCTS1 exhibit increased growth rates and display increased protection against apoptosis. May contribute to the pathogenesis and progression of breast cancer via promotion of angiogenesis through the decline of inhibitory THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in the process of proteasome degradation to down-regulate Tumor suppressor p53/TP53 in breast cancer cell; Positively regulates phosphorylation of MAPK1 and MAPK3. Involved in translation initiation; promotes aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11709712, ECO:0000269|PubMed:16982740}. Note=Nuclear relocalization after DNA damage.
Interaction partners:
- Density-regulated protein
- Cullin-4B
- Obg-like ATPase 1
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS8
Sequence:
MFKKFDEKENVSNCIQLKTSVIKGIKNQLIEQFPGIEPWLNQIMPKKDPVKIVRCHEHIEILTVNGELLFFRQREGPFYPTLRLLHKYPFILPHQQVDKGAIKFVLSGANIMCPGLTSPGAKLYPAAVDTIVAIMAEGKQHALCVGVMKMSAEDIEKVNKGIGIENIHYLNDGLWHMKTYK
Protein: Probable WRKY transcription factor 60 (WRKY DNA-binding protein 60) (Q9SK33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223}.
Interaction partners:
- Probable WRKY transcription factor 40
- WRKY transcription factor 18
- Magnesium-chelatase subunit ChlH, chloroplastic
- Ethylene-responsive transcription factor ABI4
- Protein ABSCISIC ACID-INSENSITIVE 5
Sequence:
MDYDPNTNPFDLHFSGKLPKREVSASASKVVEKKWLVKDEKRNMLQDEINRVNSENKKLTEMLARVCEKYYALNNLMEELQSRKSPESVNFQNKQLTGKRKQELDEFVSSPIGLSLGPIENITNDKATVSTAYFAAEKSDTSLTVKDGYQWRKYGQKITRDNPSPRAYFRCSFSPSCLVKKKVQRSAEDPSFLVATYEGTHNHTGPHASVSRTVKLDLVQGGLEPVEEKKERGTIQEVLVQQMASSLTKDPKFTAALATAISGRLIEHSRT
Protein: Sucrose synthase 4 (AtSUS4) (EC 2.4.1.13) (Sucrose-UDP glucosyltransferase 4) (Q9LXL5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways.
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
- Probable glucose-1-phosphate adenylyltransferase large subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
- alpha-D-xyloside xylohydrolase
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- Probable fructokinase-1
Sequence:
MANAERVITRVHSQRERLDATLVAQKNEVFALLSRVEAKGKGILQHHQIIAEFEAMPLETQKKLKGGAFFEFLRSAQEAIVLPPFVALAVRPRPGVWEYVRVNLHDLVVEELQASEYLQFKEELVDGIKNGNFTLELDFEPFNAAFPRPTLNKYIGDGVEFLNRHLSAKLFHDKESLHPLLKFLRLHSHEGKTLMLNNRIQNLNTLQHNLRKAEEYLMELKPETLYSEFEHKFQEIGLERGWGDTAERVLNMIRLLLDLLEAPDPCTLENFLGRIPMVFNVVILSPHGYFAQDNVLGYPDTGGQVVYILDQVRALETEMLQRIKQQGLNITPRILIITRLLPDAAGTTCGQRLEKVYGSQYCDILRVPFRTEKGIVRKWISRFEVWPYLETFTEDVAAEISKELQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKLDEKYHFSCQFTADLIAMNHTDFIITSTFQEIAGSKDTVGQYESHRSFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFAYTEEKRRLTAFHLEIEELLYSDVENEEHLCVLKDKKKPIIFTMARLDRVKNLSGLVEWYGKNTRLRELVNLVVVGGDRRKESQDNEEKAEMKKMYELIEEYKLNGQFRWISSQMNRVRNGELYRYICDTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDKAAESLADFFTKCKHDPSHWDQISLGGLERIQEKYTWQIYSQRLLTLTGVYGFWKHVSNLDRLESRRYLEMFYALKYRPLAQAVPLAHEE
Protein: Extracellular xylan exo-alpha-(1->2)-glucuronosidase (EC 3.2.1.131) (Alpha-glucuronidase) (B3PC73)
Organism: Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Function: Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. It catalyzes the cleavage of the alpha-1,2-glycosidic bond at the non-reducing end of 4-O-methyl-D-glucuronic acid (4-O-MeGlcA) side chain of short xylooligosaccharides and releases 4-O-methylglucuronic acid. It can also hydrolyze small soluble oligosaccharides such as dobiouronic acid, aldotriouronic acid, aldotetraouronic acid, and aldopentaouronic acid.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:12169619}.
Interaction partners:
- Beta-xylanase
- Gylcosyl hydrolase 115 C-terminal domain-containing protein
- Beta-xylosidase/alpha-L-arabinfuranosidase, putative, gly43G
- Beta-xylosidase/alpha-L-arabinfuranosidase, putative, gly43F
- Endo-1,4-beta-xylanase A
- Beta-xylanase
- Endo-1,4-beta-xylanase B
- Sialic acid-specific 9-O-acetylesterase
Sequence:
MSTFARLFLCLVFFASLQPAMAQTEDGYDMWLRYQPIADQTLLKTYQKQIRHLHVAGDSPTINAAAAELQRGLSGLLNKPIVARDEKLKDYSLVIGTPDNSPLIASLNLGERLQALGAEGYLLEQTRINKRHVVIVAANSDVGVLYGSFHLLRLIQTQHALEKLSLSSAPRLQHRVVNHWDNLNRVVERGYAGLSLWDWGSLPNYLAPRYTDYARINASLGINGTVINNVNADPRVLSDQFLQKIAALADAFRPYGIKMYLSINFNSPRAFGDVDTADPLDPRVQQWWKTRAQKIYSYIPDFGGFLVKADSEGQPGPQGYGRDHAEGANMLAAALKPFGGVVFWRAFVYHPDIEDRFRGAYDEFMPLDGKFADNVILQIKNGPIDFQPREPFSALFAGMSRTNMMMEFQITQEYFGFATHLAYQGPLFEESLKTETHARGEGSTIGNILEGKVFKTRHTGMAGVINPGTDRNWTGHPFVQSSWYAFGRMAWDHQISAATAADEWLRMTFSNQPAFIEPVKQMMLVSREAGVNYRSPLGLTHLYSQGDHYGPAPWTDDLPRADWTAVYYHRASKTGIGFNRTKTGSNALAQYPEPIAKAWGDLNSVPEDLILWFHHLSWDHRMQSGRNLWQELVHKYYQGVEQVRAMQRTWDQQEAYVDAARFAQVKALLQVQEREAVRWRNSCVLYFQSVAGRPIPANYEQPEHDLEYYKMLARTTYVPEPWHPASSSRVLK
Protein: Gliomedin (Cancer-related gene liver 2 protein) (CRG-L2) [Cleaved into: Gliomedin shedded ectodomain] (Q8BMF8)
Organism: Mus musculus (Mouse)
Function: Ligand for NRCAM and NFASC/neurofascin that plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Mediates interaction between Schwann cell microvilli and axons via its interactions with NRCAM and NFASC. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with NRCAM, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17293346}; Single-pass type II membrane protein {ECO:0000305|PubMed:17293346}. Cell projection, axon {ECO:0000269|PubMed:17293346, ECO:0000269|PubMed:20188654}. Note=Localizes to the nodes of Ranvier (PubMed:17293346, PubMed:20188654). Detected at immature heminodes (By similarity). {ECO:0000250|UniProtKB:Q80WL1, ECO:0000269|PubMed:17293346, ECO:0000269|PubMed:20188654}.; SUBCELLULAR LOCATION: [Gliomedin shedded ectodomain]: Secreted {ECO:0000269|PubMed:17293346}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q80WL1}. Note=Proteolytic processing gives rise to a soluble extracellular domain that is secreted (PubMed:17293346). The gliomedin shedded ectodomain localizes to the nodes of Ranvier (By similarity). {ECO:0000250|UniProtKB:Q80WL1, ECO:0000269|PubMed:17293346}.
Interaction partners:
- Neurofascin
- Neuronal cell adhesion molecule
- Contactin-associated protein 1
- Ankyrin-3
Sequence:
MTRAAERGQGATGWGLRGALVAIALLSALNAAGTVFVLCQWRGLSAALRALEAQRGREQREDSALRAFLAELSRAPGRVPEPSQDPMSAARNKRSHNGEPASHIRAESQDMMMMMTYSMVPIRVMIDLCNSTQGICLTGPPGPPGPPGAGGLPGHNGSDGQPGLQGPKGEKGAIGKRGKMGLPGATGNPGEKGEKGDAGELGLPGNEGPPGQKGDKGDKGDVSNDVLLTGAKGDQGPPGPPGPPGPPGPPGSRRSKGPRPPNVFNSQCPGETCVIPNDDTLVGRADEKANERHSPQTESMITSIGNPAQVLKVRETFGTWMRESANKSDDRIWVTEHFSGIMVKEFKDLPALLNSSFTLLHLPHYFHGCGHAVYNNSLYYHKGGSNTIVRFEFGKETPQTLKLENALYFDRKYLFANSKTYFNIAVDEKGIWIIYASSVDGSSILVAQLDERTFSVTQHINTTYPKSKAGNAFIARGILYVTDTKDTRVTFAFDLLGGKQINANFDFRMSQSVLAMLSYNMRDQHLYSWEDGHLMLYPVQFLSAASSQR
Protein: Membrane steroid-binding protein 2 (AtMP2) (Membrane-associated progesterone-binding protein 3) (AtMAPR3) (Q9M2Z4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250}.
Interaction partners:
- Calcium ion-binding protein
- ADP-ribosylation factor C1
Sequence:
MVQQIWETLKETITAYTGLSPAAFFTVLALAFAVYQVVSGFFVSPEVHRPRSLEVQPQSEPLPPPVQLGEITEEELKLYDGSDSKKPLLMAIKGQIYDVSQSRMFYGPGGPYALFAGKDASRALAKMSFEDQDLTGDISGLGAFELEALQDWEYKFMSKYVKVGTIQKKDGEGKESSEPSEAKTASAEGLSTNTGEEASAITHDETSRSTGEKIAETTEKKDVATDDDDAAKE