wanglab/gogpt-training-data huggingface dataset:
Protein: Lysine-specific demethylase 4C (EC 1.14.11.66) (JmjC domain-containing histone demethylation protein 3C) (Jumonji domain-containing protein 2C) ([histone H3]-trimethyl-L-lysine(9) demethylase 4C) (Q8VCD7)
Organism: Mus musculus (Mouse)
Function: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}.
Interaction partners:
- Lysine-specific histone demethylase 1A
- Lysine-specific demethylase 3A demethylase 3A)
- Histone-lysine N-methyltransferase SUV39H1
- Histone H3.2
- Histone H3.1
- Hypoxia-inducible factor 1-alpha
- Lysine-specific demethylase 6B demethylase 6B)
- Lysine-specific demethylase 6A
Sequence:
MEVVEVESPLNPSCKIMTFRPSMEEFREFNKYLAYMESKGAHRAGLAKVIPPKEWKPRQCYDDIDNLLIPAPIQQMVTGQSGLFTQYNIQKKAMTVKEFRQLANSSKYCTPRYLDYEDLERKYWKNLTFVAPIYGADINGSIYDEGVDEWNIARLNTVLDVVEEECGISIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAQGFFPSSSQGCDAFLRHKMTLISPSVLKKYGIPFDKITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATVRWIDYGKVAKLCTCRNDMVKISMDIFVKKFQPDRYQIWKQGKDIYTIDHTKPTPESTPEVKTWLQRKKKLRKPPKSLQGNKPLCKRPKPEEDEEFAEFSGEEGANPAMGPRHLKVTEKPEKALKLGKLEESSAKEALDTRIQVDQSLLNDTKLSGKGCISSSVTAEIPPEDNRASAVISPSQLKEGADCIPLSHGHQAGKESHLLKILKLESPKIPSPLPESNKVLTEGEENDEEGHGSNLEPGEIPEALSEERNGLNIPKIIEGQPKTTKSWRHPLGKPPARSPMTLVKQQVASDEELPEVLSIDEEVEETESWAKPLIHLWQTKSPNFMAEQEYNATVAKMEPNCAICTLLMPYYKPDSSKEENDSRWETAVNEVVQSGRKTKPIIPEMCFIYSEENVDYSPPNAFLEEDGTSLLISCAKCFVRVHASCYGVPSHEVCDGWLCARCKRNAWTAECCLCNLRGGALKQTKNNQWAHVICAVAVPEVRFTNVPERTQIDVDRIPLQRLKLKCIFCRHRVKKVSGACIQCSYGRCPASFHVTCAHAAGVLMEPDDWPYVVNITCFRHRVNSNAKSKTCEKAISVGQTVITKHRNTRYYSCRVIDVTSQTFYEVMFDDGSFSRDTFPEDIVSRNCVKLGPPAEGEVIQVKWPDGKLYGAKYLGSNVAYMYQVEFEDGSQIAMKREDIYTLDEELPKRVKARFSTASDMRFEDTFYGADVIQGERKRQRVLSSRLKNEYVDDPVYRTFLKSSFQKKCQKRQ
Protein: Ras-related protein M-Ras (EC 3.6.5.2) (Ras-related protein R-Ras3) (O14807)
Organism: Homo sapiens (Human)
Function: Serves as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Activates the MAP kinase pathway.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Leucine-rich repeat protein SHOC-2
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- RAF proto-oncogene serine/threonine-protein kinase
- Ral guanine nucleotide dissociation stimulator
- Rap guanine nucleotide exchange factor 5
- Rap guanine nucleotide exchange factor 2
- Son of sevenless homolog 1
- Afadin
- Ras association domain-containing protein 5
- Serine/threonine-protein kinase B-raf
Sequence:
MATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTAGQEEFSAMREQYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHDLVRVIRQQIPEKSQKKKKKTKWRGDRATGTHKLQCVIL
Protein: Probable WRKY transcription factor 54 (WRKY DNA-binding protein 54) (Q93WU8)
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). Together with WRKY70, negative regulator of developmental senescence, probably via the regulation of several senescence-associated markers genes. Positive regulator of EDS1-dependent defense against E.amylovora. In collaboration with WRKY70, prevents stomatal closure and, consequently, osmotic stress tolerance. Together with WRKY46 and WRKY70, promotes brassinosteroid (BR)-regulated plant growth but prevent drought response by modulating gene expression. Negative regulator of SA biosynthesis. Prevents defense response to the necrotrophic pathogens P.carotovorum and B.cinerea, but promotes defense against biotrophic/hemibiotrophic pathogens P.syringae pv. tomato (Pst) DC3000, probably by regulating negatively the jasmonic acid (JA)/ethylene (ET) and positively the salicylic acid (SA) signaling pathways.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223}.
Interaction partners:
- Probable WRKY transcription factor 51
- High mobility group B protein 6
- Isochorismate synthase 1, chloroplastic
- Probable WRKY transcription factor 70
Sequence:
MDSNSNNTKSIKRKVVDQLVEGYEFATQLQLLLSHQHSNQYHIDETRLVSGSGSVSGGPDPVDELMSKILGSFHKTISVLDSFDPVAVSVPIAVEGSWNASCGDDSATPVSCNGGDSGESKKKRLGVGKGKRGCYTRKTRSHTRIVEAKSSEDRYAWRKYGQKEILNTTFPRSYFRCTHKPTQGCKATKQVQKQDQDSEMFQITYIGYHTCTANDQTHAKTEPFDQEIIMDSEKTLAASTAQNHVNAMVQEQENNTSSVTAIDAGMVKEEQNNNGDQSKDYYEGSSTGEDLSLVWQETMMFDDHQNHYYCGETSTTSHQFGFIDNDDQFSSFFDSYCADYERTSAM
Protein: Protein NSG2 (INSIG homolog 2) (P53898)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Stabilizes the HMG-CoA reductase HMG2 by preventing its HRD1-dependent degradation. Binds directly to the sterol-sensing domain (SSD)-containing transmembrane region of HMG2, promoting its folding to protect it from degradation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16270032}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16270032}.
Interaction partners:
- NPC intracellular sterol transporter 1-related protein 1
Sequence:
MANRGEPDPKKSTESICSLTKPQLYSLYDDDVVRSEDNEIYEELKRSVSIDSTKYSRDQTIDSTFYLAHKVGGSLPRNTVSSNNLERILSASSIHENFPSRTRQTRQNILHYLQAVLILSLSGFAYHELSRNLHDNHLLHPDFASRPLLLGVKLCNWLSNGVLPNWLGYGVEGLLFGSVVPILDNIFQTEVVKSSVHHDSLTSVIRSINAMLGVTFGIRKIQWNSSLQAAGAWGLLNIILWLFFDGSISMLMSCICIGVGCCISCYKDIIDGSQFLYFMDFYFLGSLMFGKLGRYLYSH
Protein: Synaptotagmin alpha, isoform A (Synaptotagmin alpha, isoform C) (Synaptotagmin alpha, isoform D) (Q9I7M6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDIVIREEDISLAQIGVYASVSFLVVSAVGAALYTTCSKRYRLNWFEQNLLESANEKDEDQQREALVAGAVGYNVDNVNEVPRGKYSSGNAGNLSPTSLKSEDNDPAFWVPASVTSTAAIQQQVSNTTEESAPPTSPTGSLKSNTLSYCSTTSVPIARSDKHVVLAMHPSRPRVSSMNAKLDHTKIDMTLYRSHSQPKTINPVSLNEVRGNLHVSLGYDPVGGLLNVRLLEAQNLQPRQFSGTADPYAKVRLLPDKKNFWQTRIHKRTLNPVFDEQFVFEVTAGVIDKRTVEILLYDFDAYSRHVCIGGSKLHLANLDLSEQLKLWTPLSSASAQDMKVDLGDIMVSLAYLPSAERLMVVLIKARNLRIVDDARNSSDPYVKVTLLGPGGKKIKKRKTGVQRGTLNPVYNEALAFDVAKETLKNCVLEFTVVHDGLLGSSEILGRTLIGNSPEVRTEEKIFFEEVFRAKNATAQWVPLQEPANNLATSAKSSKN
Protein: Regulator of sigma-E protease RseP (EC 3.4.24.-) (S2P endopeptidase) (Site-2 protease RseP) (S2P protease RseP) (Site-2-type intramembrane protease) (D0ZKX9)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Function: A site-2 regulated intramembrane protease that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLSILWNLAAFIIALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDRYGTEYVIALIPLGGYVKMLDERAEPVAPELRRHAFNNKTVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVIGEITPNSIAAQAQIAPGTELKAVDGIETPDWDAVRLQLVSKIGDQQTTVSVAPFGSDQRQDKTLDLRHWAFEPDKQDPVSSLGIRPRGPQIEPVLSEVQANSAASKAGLQAGDRIVKVDGQPLTQWMKFVTFVRDNPGKPLALEIERQGSALSLTLTPDTKSVNGKAEGFAGVVPKIIPLPEEYKTIRQYGPFSAILEATDKTWQLMKLTVSMLGKLITGDVKLNNLSGPISIAQGAGMSAEFGVIYYLMFLALISVNLGIINLFPLPVLDGGHLLFLAIEKLKGGPVSERVQDFSYRIGSILLVLLMGLALFNDFSRL
Protein: Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 (Atrophin-1-interacting protein 3) (AIP-3) (BAI1-associated protein 1) (BAP-1) (Membrane-associated guanylate kinase inverted 1) (MAGI-1) (Trinucleotide repeat-containing gene 19 protein) (WW domain-containing protein 3) (WWP3) (Q96QZ7)
Organism: Homo sapiens (Human)
Function: May play a role as scaffolding protein at cell-cell junctions. May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface (By similarity).
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:11969287}. Cell membrane {ECO:0000269|PubMed:11969287}; Peripheral membrane protein {ECO:0000269|PubMed:11969287}. Note=Localizes to epithelial cells tight junctions.
Interaction partners:
- Synaptopodin
- Immunoglobulin superfamily member 5
- Alpha-actinin-4
- Rap guanine nucleotide exchange factor 2
- Catenin beta-1
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
- Partitioning defective 3 homolog
- Cell division control protein 42 homolog
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
Sequence:
MSKVIQKKNHWTSRVHECTVKRGPQGELGVTVLGGAEHGEFPYVGAVAAVEAAGLPGGGEGPRLGEGELLLEVQGVRVSGLPRYDVLGVIDSCKEAVTFKAVRQGGRLNKDLRHFLNQRFQKGSPDHELQQTIRDNLYRHAVPCTTRSPREGEVPGVDYNFLTVKEFLDLEQSGTLLEVGTYEGNYYGTPKPPSQPVSGKVITTDALHSLQSGSKQSTPKRTKSYNDMQNAGIVHAENEEEDDVPEMNSSFTADSGEQEEHTLQETALPPVNSSIIAAPITDPSQKFPQYLPLSAEDNLGPLPENWEMAYTENGEVYFIDHNTKTTSWLDPRCLNKQQKPLEECEDDEGVHTEELDSELELPAGWEKIEDPVYGIYYVDHINRKTQYENPVLEAKRKKQLEQQQQQQQQQQQQQQQQQQQQTEEWTEDHSALVPPVIPNHPPSNPEPAREVPLQGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDGKMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLPFDPDDPNTSLVTSVAILDKEPIIVNGQETYDSPASHSSKTGKVNGMKDARPSSPADVASNSSHGYPNDTVSLASSIATQPELITVHIVKGPMGFGFTIADSPGGGGQRVKQIVDSPRCRGLKEGDLIVEVNKKNVQALTHNQVVDMLVECPKGSEVTLLVQRGGLPVPKKSPKSQPLERKDSQNSSQHSVSSHRSLHTASPSHSTQVLPEFPPAEAQAPDQTDSSGQKKPDPFKIWAQSRSMYENRPMSPSPASGLSKGEREREINSTNFGECPIPDYQEQDIFLWRKETGFGFRILGGNEPGEPIYIGHIVPLGAADTDGRLRSGDELICVDGTPVIGKSHQLVVQLMQQAAKQGHVNLTVRRKVVFAVPKTENEVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSGGGGGSGVVSTVVQPYDVEIRRGENEGFGFVIVSSVSRPEAGTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNATLLTNAEKIATITTTHTPSQQGTQETRNTTKPKQESQFEFKAPQATQEQDFYTVELERGAKGFGFSLRGGREYNMDLYVLRLAEDGPAERCGKMRIGDEILEINGETTKNMKHSRAIELIKNGGRRVRLFLKRGDGSVPEYDPSSDRHGPATGPQGVPEVRAGPDRRQHPSLESSYPPDLHKSSPHGEKRAHARDPKGSREYSRQPNEHHTWNGTSRKPDSGACRPKDRAPEGRRDAQAERAAAANGPKRRSPEKRREGTRSADNTLERREKHEKRRDVSPERRRERSPTRRRDGSPSRRRRSLERLLEQRRSPERRRGGSPERRAKSTDRRRARSPERRRERSLDKRNREDRASHREREEANLKQDAGRSSRHPPEQRRRPYKECSTDLSI
Protein: Peptidoglycan D,D-transpeptidase PbpA (EC 3.4.16.4) (Penicillin-binding protein A) (PBPA) (P9WKD1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall (Probable). Required for the regulation of cell length. Plays critical roles for the survival of the pathogen inside the host. Required for both bacterial survival and formation of granuloma structures in a guinea pig infection model.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Peptidoglycan glycosyltransferase RodA
- Serine/threonine-protein kinase PknB
- Serine/threonine-protein kinase PknA
- Serine/threonine protein phosphatase PstP
- Cell division protein FtsQ
- FHA domain-containing protein FhaB
- Penicillin-binding protein PbpB
- Probable peptidoglycan glycosyltransferase FtsW
- Cell wall synthesis protein Wag31
- PASTA domain-containing protein
Sequence:
MNASLRRISVTVMALIVLLLLNATMTQVFTADGLRADPRNQRVLLDEYSRQRGQITAGGQLLAYSVATDGRFRFLRVYPNPEVYAPVTGFYSLRYSSTALERAEDPILNGSDRRLFGRRLADFFTGRDPRGGNVDTTINPRIQQAGWDAMQQGCYGPCKGAVVALEPSTGKILALVSSPSYDPNLLASHNPEVQAQAWQRLGDNPASPLTNRAISETYPPGSTFKVITTAAALAAGATETEQLTAAPTIPLPGSTAQLENYGGAPCGDEPTVSLREAFVKSCNTAFVQLGIRTGADALRSMARAFGLDSPPRPTPLQVAESTVGPIPDSAALGMTSIGQKDVALTPLANAEIAATIANGGITMRPYLVGSLKGPDLANISTTVGYQQRRAVSPQVAAKLTELMVGAEKVAQQKGAIPGVQIASKTGTAEHGTDPRHTPPHAWYIAFAPAQAPKVAVAVLVENGADRLSATGGALAAPIGRAVIEAALQGEP
Protein: E3 SUMO-protein ligase NSE2 (E3 SUMO-protein transferase NSE2) (Non-structural maintenance of chromosomes element 2 homolog) (Q8I8I0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSDFVSDFSDGGKIKKLLEQSVEQSVEHAVNVVHMKIKHQSLNKAMNQVKNSSATMEEFEEVWKERSKAVEQKRINVKNLHEFKNFVKAVESAAGQAGAEVNDQANGTAYDEDLIMEDSGSEVFSFYDPWSKALIKNPIRNKMCGHIYDRDSVMPIIMDRIGIRCPVLGCANLCYIQPDHLVQDANVQQKIQQSMSNAIVDVTASEEDEE
Protein: ATPase inhibitor A, mitochondrial (ATP synthase F1 subunit epsilon A) (Inhibitor of F(1)F(o)-ATPase A) (IF(1) A) (IF1 A) (Protein pinotage) (A3KNL5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing fech to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- ATP synthase subunit alpha
- ATP synthase subunit gamma.
- ATP synthase subunit beta
- ETS variant transcription factor 7.
- ATP synthase F1 subunit delta.
- ATP synthase subunit d
- Borealin
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk-membrane subunit b.
Sequence:
MARLLLRRGFFSSHIRMSSDQLGELGTGAGKGGGGGGSVRAAGGSFGRREAAEEERYFRQKEREQLAALKNHHEEEIDHHKKEIERLQREIDRHKGKIRKLKHDD
Protein: Macrophage mannose receptor 1 (MMR) (C-type lectin domain family 13 member D) (C-type lectin domain family 13 member D-like) (Human mannose receptor) (hMR) (Macrophage mannose receptor 1-like protein 1) (CD antigen CD206) (P22897)
Organism: Homo sapiens (Human)
Function: Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:20035344}; Single-pass type I membrane protein {ECO:0000269|PubMed:20035344}. Cell membrane {ECO:0000269|PubMed:20035344}; Single-pass type I membrane protein {ECO:0000269|PubMed:20035344}.
Interaction partners:
- WD repeat and HMG-box DNA-binding protein 1
- Protein MCM10 homolog
- Cell division control protein 45 homolog
- Integrin alpha-M
- Scavenger receptor cysteine-rich type 1 protein M130
- C-type mannose receptor 2
- TIMELESS-interacting protein
- Secretory phospholipase A2 receptor
- Arginase-1
- Macrosialin
Sequence:
MRLPLLLVFASVIPGAVLLLDTRQFLIYNEDHKRCVDAVSPSAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQKWECKNDTLLGIKGEDLFFNYGNRQEKNIMLYKGSGLWSRWKIYGTTDNLCSRGYEAMYTLLGNANGATCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDTDKLFGYCPLKFEGSESLWNKDPLTSVSYQINSKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSGLWIGLNSLSFNSGWQWSDRSPFRYLNWLPGSPSAEPGKSCVSLNPGKNAKWENLECVQKLGYICKKGNTTLNSFVIPSESDVPTHCPSQWWPYAGHCYKIHRDEKKIQRDALTTCRKEGGDLTSIHTIEELDFIISQLGYEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLRGEPSHENNRQEDCVVMKGKDGYWADRGCEWPLGYICKMKSRSQGPEIVEVEKGCRKGWKKHHFYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRPEKYFWTGLSDIQTKGTFQWTIEEEVRFTHWNSDMPGRKPGCVAMRTGIAGGLWDVLKCDEKAKFVCKHWAEGVTHPPKPTTTPEPKCPEDWGASSRTSLCFKLYAKGKHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHKLFWLGLTYGSPSEGFTWSDGSPVSYENWAYGEPNNYQNVEYCGELKGDPTMSWNDINCEHLNNWICQIQKGQTPKPEPTPAPQDNPPVTEDGWVIYKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDAQSAYFIGLLISLDKKFAWMDGSKVDYVSWATGEPNFANEDENCVTMYSNSGFWNDINCGYPNAFICQRHNSSINATTVMPTMPSVPSGCKEGWNFYSNKCFKIFGFMEEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSAWTGLNDVNSEHTFLWTDGRGVHYTNWGKGYPGGRRSSLSYEDADCVVIIGGASNEAGKWMDDTCDSKRGYICQTRSDPSLTNPPATIQTDGFVKYGKSSYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQMETSNERVWIALNSNLTDNQYTWTDKWRVRYTNWAADEPKLKSACVYLDLDGYWKTAHCNESFYFLCKRSDEIPATEPPQLPGRCPESDHTAWIPFHGHCYYIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLKSKTNFWIGLFRNVEGTWLWINNSPVSFVNWNTGDPSGERNDCVALHASSGFWSNIHCSSYKGYICKRPKIIDAKPTHELLTTKADTRKMDPSKPSSNVAGVVIIVILLILTGAGLAAYFFYKKRRVHLPQEGAFENTLYFNSQSSPGTSDMKDLVGNIEQNEHSVI
Protein: Phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) (EC 3.1.4.50) (Glycoprotein phospholipase D) (Glycosyl-phosphatidylinositol-specific phospholipase D) (GPI-PLD) (GPI-specific phospholipase D) (Q8R2H5)
Organism: Rattus norvegicus (Rat)
Function: This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane.
Subcellular location: Secreted. Note=Associated with the High-Density Lipoproteins (HDL). {ECO:0000250}.
Interaction partners:
- Glucosaminyl-phosphatidylinositol-acyltransferase PIGW
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Apolipoprotein A-II
Sequence:
MSVGRLWSGLLLLLLFFCSRSSSCGLSTHVEIGHRALQFLQLQDGRINYKELLLEHQDAYQAGTVFPDAFYPSICKQGKFHEVSESTHWTPFLNASIHYIRENYPLPWEKDTEKLVAFLFGVTSHMVADVSWHSLGIEQGFLRTMGAIDFYDSYSEAHSAGDFGGDVLSQFEFNFNYLSRRWYVPIQDLLRIYDNLYGRKVITKNVIVDCTYLQFLEMHGEMLAVSKLYSTYSTKSPFLVEQFQDYFLGGLDDMAFWSTNIYRLTSFMLENGTSDCNLPENPLFISCDGRKNHTLSSSKVQKNDFHRNLTMFISKDIRKNLNYTERGVFYSTGSWAPESVTFMYQTLERNLRMMFTGNSQTALKHVSSPSASYTLSVPYARLGWVMASADLNQDGHGDLVVGAPGYSHPGRFQIGRVYIIYGNDLGLPPIDLDLDKEAHGVLEGFQPSGRFGSALAVLDFNKDGLPDLAVGAPSVGSGQLTYNGSVYVYYGSQQGRLSSSPNITISCKDTYCNLGWALLAADADGDGQHDLVISSPFAPGGGKQRGIVAAFYSHPRRNDKESLTLDEADWKVNGEEDFSWFGYSLHGVTVANRSLLLIGSPTWKNISRMARSSHQKNQEKKSLGRVYGYFPPNRQREITISGDKAMGKLGTSLSSGYVRVNGTLTQVLLVGAPTHDDVSKMAFLTMTLHHGGATRMYELAPEKTQPALFSTFSGDRRFSRFGSVLHLTDLDDDGLDEIIMAAPLRITDVTSGLLGEEDGRVYIYNGMHTTLGDVTGKCKSWMTPCPEEKAQYVLISPEASSRFGSSLVSVRSKERNQVVVAAGRSSWGARLSGALHVYSFSSD
Protein: 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC 1.14.15.18) (25-OHD-1 alpha-hydroxylase) (25-hydroxyvitamin D(3) 1-alpha-hydroxylase) (VD3 1A hydroxylase) (Calcidiol 1-monooxygenase) (Cytochrome P450 subfamily XXVIIB polypeptide 1) (Cytochrome P450C1 alpha) (Cytochrome P450VD1-alpha) (Cytochrome p450 27B1) (O35132)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)(2)D3), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). Is also active with 25-hydroxy-24-oxo-vitamin D3. Plays an important role in normal bone growth, calcium metabolism, and tissue differentiation.
Subcellular location: Mitochondrion membrane.
Interaction partners:
- Vitamin D 25-hydroxylase
- 1,25-dihydroxyvitamin D
- Vitamin D3 receptor
- Fibroblast growth factor 23
- Parathyroid hormone
- Vitamin D-binding protein
- Retinoic acid receptor RXR-alpha
- Sodium-dependent phosphate transport protein 2A
- Sodium-dependent phosphate transport protein 2C
- Klotho
Sequence:
MTQAVKLASRVFHRVQLPSQLGSDSVLRSLSDIPGPSTPSFLAELFCKGGLSRLHELQVHGAARYGPIWSGSFGTLRTVYVADPALVEQLLRQESHCPERCSFSSWSEHRRRHQRACGLLTADGEEWQRLRSLLAPLLLRPQAAAGYAGTLDSVVSDLVRRLRRQRGRGSGLPDLVLDVAGEFYKFGLEGIGAVLLGSRLGCLEAEVPPDTETFIEAVGSVFVSTLLTMAMPSWLHRLIPGPWARLCRDWDQMFAFAQKHVEQREGEAAVRNQGKPEEDLPTGHHLTHFLFREKVSVQSIVGNVTELLLAGVDTVSNTLSWALYELSRHPEVQSALHSEITGAVNPGSYAHLQATALSQLPLLKAVIKEVLRLYPVVPGNSRVPDRDICVGNYVIPQDTLVSLCHYATSRDPAQFREPNSFNPARWLGEGPAPHPFASLPFGFGKRSCIGRRLAELELQMALAQILTHFEVLPEPGALPVKPMTRTVLVPERSIHLQFVDR
Protein: Kinesin-related protein 6 (Kinesin family member 6) (Kinesin-13) (Q6S004)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Aurora kinase
- Kinesin-related protein 13
Sequence:
MDFENDQLYNWLQLANLESFYPNFIKKNVSCDSFLSFTMQDYGNVGITSLQDRKKLFHLLQQLKKQTPPISNTSSPVINSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSSGLRQPTSTSSLLSNNNLMSTQTQQSSSSSSSSSLSSKSNSNSDFMQKAQQLLKQRELERQQYAKQQQQQQSTQTKYQSSLKDFDITSSNKNNNLDDFFEDDNLYSQQQQQQQQQQQQQDFEFEEEEEEEDQQQQYDEEEEEEEEYEEDFYKEDLGEIDDGNVLDISDDEPDPNSSCIIVEGSPDEEDDDVEYIPQNESLVNGFGSMKIQQQQQQQFQPLQQQQQQQQQQQQQFYQQQIQQQQQQQQQQQQQQVQQQQQQFNNFNYSGLNEEQIKYYQQQAQYQQQVQQAQQAAIQQAQQAAALAQASQQQLQQQEQQRQQASNFFLDMNEYGQRIRVCVRKRPLNKKEIAKSEKDIIEVLPKKDLIVNEPKTKLDLSKFIEKHKFTFDGVFDESANNYQVYLHTAYPLVDSIFHKGKATCFAYGQTGSGKTHTQMGQQGDGLYALAARDIFHRLETYFKDQLQVCISFFEIYGGKLFDLLNERKKLACRENELQNVVIVGLSEKHVTSPQELMNCIIDGNKIRSTGSTGVNSDSSRSHAILQISLKNIKTNKLHGKFSFIDLAGSERGSDTYDNDKQTRKEGADINKSLLALKECIRALDQSSKHTPFRQSTLTQVLKDSFVGNSRTVMIANISPNQSSSEHTLNTLRYADRVKELGTSESNSNKKPVATYNIPAPLPPPDHLKQNFNDPILIPSTTTTTTTTATAINSQQPIIQQTSQPVSKIKQPVKQQQESQIPQTPQQQQQQQPPQQQPQQQQYNIPQTPQQTQQQFNIPQTPKQQQPIQTQPPMSPPKIDFVNYHRNHVDQFADILKKELISINQFESSKGSIPLENYINNIEQFLDSKQLLINHLRGIIQQHQQQPIQQQQQQQQPIQQQQQSTPQPSQLQTPQQRERARSQLQPPKPSIYSSRN
Protein: Retinoblastoma-binding protein homolog 5 (Q09309)
Organism: Caenorhabditis elegans
Function: Required for di- and trimethylation at 'Lys-4' of histone H3. Regulates left/right asymmetry of ASE sensory neurons, via its role as a component of the SET2 complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:21698137}.
Interaction partners:
- Dosage compensation protein dpy-30
- Set1/Ash2 histone methyltransferase complex subunit ash-2
- CXXC-type zinc finger protein 1
- PHD-type domain-containing protein
- JmjC domain-containing protein
- WD repeat-containing protein wdr-5.1
- Histone-lysine N-methyltransferase set-2
- PAX-interacting protein 1
- WD repeat-containing protein wdr-5.3
- WD_REPEATS_REGION domain-containing protein
Sequence:
MVEILDRTYGAQFPEELECHLDLQNASANCCKFNRWGSIVAVGCTDGRVLIYDFMTRNIARTFSAHCLPVSCLSWSRDGRKLLTSSADNSIAMFDVLAGTLLHRIRFNSMVTFAMFHPRNDNKAIVLQVNKQPTVEQFSPRIQTVLANDTPGSSDESASCVSYDRKGKYIIAGTGKGKLLIYNAETLKCVAWCKQNTVQQIRQIIVPMKSRFIITNTQDRVIRTYELEDLLHQRGQMVEAKYKVLDMVNKAAWKNVCTDSDGLYVCGASTKAHSLYIWESNTGSLIKILHGNKGEALLDVQWHPTRPIILSIAQGTVSMWTQAHVENWSAFAPEFQELEENEKYIEKENEFDMEDEDADEDMTSKSQDAEDDIIDVVNVRPEDYLASSDEEDCNIMKPARNLESGPLWYIPVPLDIENADNDQRLPDDIRNLDNLLNPAWVASAKGYELSPKSK
Protein: Mediator of RNA polymerase II transcription subunit 20 (Mediator complex subunit 20) (TRF-proximal protein homolog) (hTRFP) (Q9H944)
Organism: Homo sapiens (Human)
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. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 17
Sequence:
MGVTCVSQMPVAEGKSVQQTVELLTRKLEMLGAEKQGTFCVDCETYHTAASTLGSQGQTGKLMYVMHNSEYPLSCFALFENGPCLIADTNFDVLMVKLKGFFQSAKASKIETRGTRYQYCDFLVKVGTVTMGPSARGISVEVEYGPCVVASDCWSLLLEFLQSFLGSHTPGAPAVFGNRHDAVYGPADTMVQYMELFNKIRKQQQVPVAGIR
Protein: Uncharacterized protein YcaQ (P75843)
Organism: Escherichia coli (strain K12)
Interaction partners:
- 3-deoxy-manno-octulosonate cytidylyltransferase
- Uncharacterized protein YcbJ
- Tetraacyldisaccharide 4'-kinase
- Uncharacterized protein YcaI
Sequence:
MSLPHLSLADARNLHLAAQGLLNKPRRRASLEDIPATISRMSLLQIDTINIVARSPYLVLFSRLGNYPAQWLDESLARGELMEYWAHEACFMPRSDFRLIRHRMLAPEKMGWKYKDAWMQEHEAEIAQLIQHIHDKGPVRSADFEHPRKGASGWWEWKPHKRHLEGLFTAGKVMVIERRNFQRVYDLTHRVMPDWDDERDLVSQTEAEIIMLDNSARSLGIFREQWLADYYRLKRPALAAWREARAEQQQIIAVHVEKLGNLWLHDDLLPLLERALAGKLTATHSAVLSPFDPVVWDRKRAEQLFDFSYRLECYTPAPKRQYGYFVLPLLHRGQLVGRMDAKMHRQTGILEVISLWLQEGIKPTTTLQKGLRQAITDFANWQQATRVTLGCCPQGLFTDCRTGWEIDPVA