wanglab/gogpt-training-data huggingface dataset:
Protein: Protein ARV (Q582W1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368065}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368065}.
Interaction partners:
Sequence:
MLRCIQCNAAVYRIVQPENEVVEKCGTCGRRCDRYYEFSNCQKWISITLLEKPAWIHVLFNKKDIRATLFCTALLSRLIEAYVVRTSLVYGALRMLRSKGPVSNVSSVATLQLFRNVNPKIEPLMAYQDTLPNIFICACGEYLLCLLVTVIFALHSWRRGGSALWDVVLTWMTCVNLAYSAKLCFVVFLIWRIPIALVSLVDLISLLWAARGFSLVENRYPPLFTSVVVLICTAATRYLFRSVTQWSPQLLV
Protein: MPN domain-containing protein (EC 3.4.-.-) (Q8N594)
Organism: Homo sapiens (Human)
Function: Probable protease (By similarity). Acts as a sensor of N(6)-methyladenosine methylation on DNA (m6A): recognizes and binds m6A DNA, leading to its degradation.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 4
- Proteasome subunit beta type-2
- Ubiquitin-like protein FUBI
- Proteasome subunit alpha type-3
- 26S proteasome non-ATPase regulatory subunit 13
- Proteasomal ubiquitin receptor ADRM1
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-1
Sequence:
MAAPEPLSPAGGAGEEAPEEDEDEAEAEDPERPNAGAGGGRSGGGGSSVSGGGGGGGAGAGGCGGPGGALTRRAVTLRVLLKDALLEPGAGVLSIYYLGKKFLGDLQPDGRIMWQETGQTFNSPSAWATHCKKLVNPAKKSGCGWASVKYKGQKLDKYKATWLRLHQLHTPATAADESPASEGEEEELLMEEEEEDVLAGVSAEDKSRRPLGKSPSEPAHPEATTPGKRVDSKIRVPVRYCMLGSRDLARNPHTLVEVTSFAAINKFQPFNVAVSSNVLFLLDFHSHLTRSEVVGYLGGRWDVNSQMLTVLRAFPCRSRLGDAETAAAIEEEIYQSLFLRGLSLVGWYHSHPHSPALPSLQDIDAQMDYQLRLQGSSNGFQPCLALLCSPYYSGNPGPESKISPFWVMPPPEMLLVEFYKGSPDLVRLQEPWSQEHTYLDKLKISLASRTPKDQSLCHVLEQVCGVLKQGS
Protein: Myosin regulatory light chain 2, ventricular/cardiac muscle isoform (MLC-2) (MLC-2v) (Cardiac myosin light chain 2) (Myosin light chain 2, slow skeletal/ventricular muscle isoform) (MLC-2s/v) (Ventricular myosin light chain 2) (P10916)
Organism: Homo sapiens (Human)
Function: Contractile protein that plays a role in heart development and function. Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force (By similarity). During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly (By similarity).
Subcellular location: Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:P08733}.
Interaction partners:
- Myosin-7
- Myosin light chain 3
- Myosin-6
- Actin, alpha cardiac muscle 1
- Rho-associated protein kinase 2
- Myosin light chain kinase 3
- Myosin light chain kinase 2, skeletal/cardiac muscle
- Myosin light chain 4
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin-9
Sequence:
MAPKKAKKRAGGANSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD
Protein: Rho GTPase-activating protein 9 (Rho-type GTPase-activating protein 9) (Q9BRR9)
Organism: Homo sapiens (Human)
Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has a substantial GAP activity toward CDC42 and RAC1 and less toward RHOA. Has a role in regulating adhesion of hematopoietic cells to the extracellular matrix. Binds phosphoinositides, and has the highest affinity for phosphatidylinositol 3,4,5-trisphosphate, followed by phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate.
Interaction partners:
- Pleckstrin
- Carabin
- Cell division control protein 42 homolog
- Pleckstrin-2
- Ras-related C3 botulinum toxin substrate 2
Sequence:
MLSSRWWPSSWGILGLGPRSPPRGSQLCALYAFTYTGADGQQVSLAEGDRFLLLRKTNSDWWLARRLEAPSTSRPIFVPAAYMIEESIPSQSPTTVIPGQLLWTPGPKLFHGSLEELSQALPSRAQASSEQPPPLPRKMCRSVSTDNLSPSLLKPFQEGPSGRSLSQEDLPSEASASTAGPQPLMSEPPVYCNLVDLRRCPRSPPPGPACPLLQRLDAWEQHLDPNSGRCFYINSLTGCKSWKPPRRSRSETNPGSMEGTQTLKRNNDVLQPQAKGFRSDTGTPEPLDPQGSLSLSQRTSQLDPPALQAPRPLPQLLDDPHEVEKSGLLNMTKIAQGGRKLRKNWGPSWVVLTGNSLVFYREPPPTAPSSGWGPAGSRPESSVDLRGAALAHGRHLSSRRNVLHIRTIPGHEFLLQSDHETELRAWHRALRTVIERLVRWVEARREAPTGRDQGSGDRENPLELRLSGSGPAELSAGEDEEEESELVSKPLLRLSSRRSSIRGPEGTEQNRVRNKLKRLIAKRPPLQSLQERGLLRDQVFGCQLESLCQREGDTVPSFLRLCIAAVDKRGLDVDGIYRVSGNLAVVQKLRFLVDRERAVTSDGRYVFPEQPGQEGRLDLDSTEWDDIHVVTGALKLFLRELPQPLVPPLLLPHFRAALALSESEQCLSQIQELIGSMPKPNHDTLRYLLEHLCRVIAHSDKNRMTPHNLGIVFGPTLFRPEQETSDPAAHALYPGQLVQLMLTNFTSLFP
Protein: AT4g31460/F3L17_30 (Ribosomal L28 family) (Q9SV23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAFRGKEMMKKLVKKVGAENITPELKEKLKACVPDTKVVMGRAKRGLYAGRHIQYGNRVSEDGGNKSRRCWKPNVQEKRLFSYIFDSHIKVKVTTHALRCIDKAGGIDEYLLKTPYQKMDTEMGLYWKTKVEARYAELGQMEVAFFNPEDEAKLEQGFKDLNIAKKDARREARRTFRKKGGGNKGDEEASIEGGGGSESHQEDDNGWLEAKA
Protein: Biotin carboxyl carrier protein of acetyl-CoA carboxylase (A0A0H2UNJ7)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MNLNDIKDLMTQFDQSSLREFSYKNGTDELQFSKNEARPVPEVATQVAPAPVLATPSPVAPTSAPAETVAEEVPAPAEASVATEGNLVESPLVGVVYLAAGPDKPAFVTVGDSVKKGQTLVIIEAMKVMNEIPAPKDGVVTEILVSNEEMVEFGKGLVRIK
Protein: Forked, isoform B (Forked, isoform D) (Q9VX60)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, stereocilium {ECO:0000256|ARBA:ARBA00004645}.
Interaction partners:
Sequence:
MHSHQLDSYLGGVGSMMNLGGMGQVGQMYHPGSVSGSERPNGGALALHYAAARGCLDCVQLLVAASVDICANTQMDNDVTPVYLAAQEGHLEVLKFLVLEAGGSLYVRARDGMAPIHAASQMGCLDCLKWMVQDQGVDPNLRDGDGATPLHFAASRGHLSVVRWLLNHGAKLSLDKYGKSPINDAAENQQVECLNVLVQHGTSVDYNGKSSSQRHKSQQQLHQQHQQQQQQQQQQHLSSSCNSNSNSSKQTSRSNTIKSKSSSTLSSDVEPFYLHPPALAGGSGGSGMGLGMGMGMGMGMSMGLGISRKNSDALYSQQSRSSSEKLYNGSSSLGGNPGGNSSSGGGGVGGGGGSGGALLPNDGLYVNPMRNGGMYNTPSPNGSISGESFFLHDPQDIIYNRVRDLFVDSDCSSSVKQHGKSHAHQLLQSKAGNAMTIQADVHSSSSGAGSGSDESVSISSSFNSPKQQQQLRSQSFNRHGSSSNISASGNIKNNNYKAHKGKPSNQNGGGDHDYEDIYLVREESRKQHQQQQQHQLQQQQQLQHQATQQQQQQQQQQQQLQHKYNVGRSRSRDSGSHSRSASASSTRSTDIVLQYSNHHLNNKRNMNNNSNMNNSSSNIAQSSSSNNNNNSLLNRNKSHSIIGLHSSKYESSLKDNYSAKNVNLKNQLLNGGIKSDTYESVCPPEDVAERTKQTHKNSMIRNNLADASSNNNTSGSINNISNIGNMNGGNQSSRNLKRVSSAPPMQNLAVVNGPPPPPLPPPLRAPVQQQRNNLSVDQPNSMTGNNGIYKKNVFGPNQGPTNANGTGGAAPPPVPAPNPVATEAVDSDSGLEVVEEPSLRPSELVRGNHNRTMSTISANKKAKLLNAGSTNGSSIAASSDDSQSRYGGSVHAANGSAANGHFYGYSEGNKNQGSNGNGNGNGNGGGGNYHSHPNQPHYATGQPHQYTPSLYGGGSSAEDHYELTQQQQQIYGETHLPSGQRTGGPNLVNKQLVLPFVPPSFPNKSQDGVTHLIKPSEYLKSISIDKRSCPSSARSTDTEDYMQIQIAQQQSHPHQHQHHPHPHPHPHHPHQLHGMGEQPPLPPPPPPLPHGMLPPQPPMGPPMGVAGGQDATMSGKSHKPKKPHGSAPNSQDTATRKQHQPLSAISIQDLNSVQLRRTDTQKVPKPYQMPARSLSMQCLTSSTETYLKSDLIAELKISKDIPGIKKMKVEQQMASRMDSEHYMEITKQFSGNNYVDQIYLQIPERDQAGNAIPDWKRQMMAKKAAERAKKDFEERMAQEAESRRLSQIPQWKRDLLARREETENKLKAAIYTPKVEENNRVADTWRLKNRAMSIDNININLAGMEQHYQQIQFQQKQQQLQLGNKENHVDPKGADQDQEHGVGIGSGVGNANSGVIGGQELIDPSEGSQGRAEEEEDNIIPWRAQLRKTNSRLSLI
Protein: 3-alpha-mycarosylerythronolide B desosaminyl transferase (EC 2.4.1.278) (Desosaminyl transferase EryCIII) (Erythromycin biosynthesis protein CIII) (A4F7P3)
Organism: Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
Function: Catalyzes the conversion of alpha-L-mycarosylerythronolide B into erythromycin D in the erythromycin biosynthesis pathway.
Interaction partners:
- Cytochrome P450 family protein EryCII
- Erythromycin 3''-O-methyltransferase
- 6-deoxyerythronolide-B synthase
- Erythromycin C-12 hydroxylase
- TDP-desosamine-N-dimethyltransferase
- 6-deoxyerythronolide-B synthase
- 6-DEB TDP-mycarosyl glycosyltransferase
- TDP-4-keto-6-deoxyhexose 2,3-reductase
- dTDP-4-keto-6-deoxy-L-hexose 4-reductase
- NDP-4-keto-6-deoxy-glucose 2,3-dehydratase
Sequence:
MRVVFSSMASKSHLFGLVPLAWAFRAAGHEVRVVASPALTEDITAAGLTAVPVGTDVDLVDFMTHAGHDIIDYVRSLDFSERDPATLTWEHLLGMQTVLTPTFYALMSPDTLIEGMVSFCRKWRPDLVIWEPLTFAAPIAAAVTGTPHARLLWGPDITTRARQNFLGLLPDQPEEHREDPLAEWLTWTLEKYGGPAFDEEVVVGQWTIDPAPAAIRLDTGLKTVGMRYVDYNGPSVVPEWLHDEPERRRVCLTLGISSRENSIGQVSIEELLGAVGDVDAEIIATFDAQQLEGVANIPDNVRTVGFVPMHALLPTCAATVHHGGPGSWHTAAIHGVPQVILPDGWDTGVRAQRTQEFGAGIALPVPELTPDQLRESVKRVLDDPAHRAGAARMRDDMLAEPSPAEVVGICEELAAGRREPR
Protein: Pygopus homolog 1 (Zgc:172214 protein) (A8WG61)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTEQEKESFSLKRNRGGEAGLDVLAGPGLLLGSPDKKRRKSSTQAPPFSPLSEYAPPPNPSADHLIAANPFDDNYISPSLKPYFGHSHYPASNSYGSSRMPSPYGPTIQTQPQYFSQNPTGFSRTHRFNYSPNYVHAFCGGSNNNNNMHFGSVEHGDQIPLQNLNQRSPGFNPDANTTRNMSPNLNNFTQSNTKQDHSEAANKKYSHNVNCEENATQDNKTKGGPEKLNGVFHSNNEKKSPDYRRSALRMNKVKRRSTSSSSEPVFPCGICLNEVNDDQEAILCEASCQKWFHRVCTGMTETAYNLLTAETSAVWGCDTCMEDREVQMMKNSDGQS
Protein: COP9 signalosome complex subunit 5b (Signalosome subunit 5b) (EC 3.4.-.-) (Jun activation domain-binding homolog 2) (Q9FVU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex (By similarity). The CSN complex is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of PSIAA6 by regulating the activity of the Ubl ligase SCF-TIR complex. Not involved in CSN's deneddylation/derubylation activity. Essential for the structural integrity of the CSN holocomplex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9811788}. Nucleus {ECO:0000269|PubMed:9811788}.
Interaction partners:
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 6a
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 6b
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 1
- COP9 signalosome complex-related / CSN complex-like protein
- NEDD8-like protein RUB3
Sequence:
MEGSSSTIARKTWELENSILTVDSPDSTSDNIFYYDDTSQTRFQQEKPWENDPHYFKRVKISALALLKMVVHARSGGTIEIMGLMQGKTDGDTIIVMDAFALPVEGTETRVNAQDDAYEYMVEYSQTNKLAGRLENVVGWYHSHPGYGCWLSGIDVSTQRLNQQHQEPFLAVVIDPTRTVSAGKVEIGAFRTYSKGYKPPDEPVSEYQTIPLNKIEDFGVHCKQYYSLDVTYFKSSLDSHLLDLLWNKYWVNTLSSSPLLGNGDYVAGQISDLAEKLEQAESHLVQSRFGGVVPSSLHKKKEDESQLTKITRDSAKITVEQVHGLMSQVIKDELFNSMRQSNNKSPTDSSDPDPMITY
Protein: Glutaredoxin-like protein (EC 1.11.1.15) (Q8IBZ7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- BolA-like protein, putative
- Anamorsin homolog
- Cysteine desulfuration protein SufE
Sequence:
MNKYIRAPNLIYICASLGIHSILFKKQKSPDNKNSYHIKDFIKLKNIIFLTSCEVTQDPKEGGGKKNYDRYHNELFNNKINQNKVHIDNNELVNYFDELYEQSKNENIITKGEGEEVEFNSSNLLLPFVEEHEHVKDKNDNDKCIKYEYVNDKCIKDEHGEFERVEENIKLSEDIINIIENILKKYNVVLFMKGTALNPYCKYSKQAIHILKLNKVKQIHTVNILDNQELRNALKIYSNWPTFPQLYVNQKFIGGIDKLQELHDQNKIKDII
Protein: Ecdysone receptor co-activator Taiman (Q9GS19)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSIAAAENAGLSPSDLPDHWASGTSNPSTSTSSSSSSSISASGSNNNKYNSGNISVCNLPRSSPAAATAAVTLSSAAGGIGSNLLSGLHHGLAPGTHPLQRATAASGGGAGAGGVAGASTAAALTLQQHQHQQQQQQQQQQAQHQHQHQHQQQTQQQQLAYQHQQLQQQIISHRSIQNKAAATAAAQTANLAAALQRSAAIMNAVASPISANSANSATSGRKIRRKTDSKVNLPQSQINKCNNEKRRREAENGYIEQLSEILTLNKRGDMTSTKPDKAAILNQVVRTYREICDKGQNRDISSTSTNNNNSTTTTNNNTNSNNNNNTSKPQATSTRCSRCATDNCSIHPVQQGEVSSTEPPLPEPSLLLGQVPEISAYFEALEHYISGVGWVLLQVNANGIIESCTQNIRDLIGYEKQELYHQPLYMYLYSGDHAKLEPIINTMYNNPNGGNSNSANNSGPGGSSAGTSAGVWGDLEELNNGNASQGSNSSGAGGLGGAGGAAAGKKRSISTKVRMLVKDTRTATQTSSNCEEKPLRQSGHQDKYEEVVLIAAPVKDDADASSSVLCLITRPEDESPLEINIQQHVQQQPIEQMTFKLDIHGKILTLDPTALREPFKQHLQTWVGRLWQDLCHPHDLSTLKSHLRDIQDSASANSPGAGAGTSVVSRPFRLRLGAPDVYVHVKANSRLFLNQTPGEGDFIMSVQTLLNSENDMNSSNTGAGSGGLGLGQLCAMAPSPSLASSLLSSLSMDGLHGGTGSGSSSSPAASGMLPTHLLGGLVGGGQQGGGGNSTQTTSVGGPLMSSAIINGTGLQQQQQQQQRSGASSSASSSANALVNAFTASPAPAEHSFYGSDTFEFDIAAHSSSFELDPSGGVGAWTDSRPNSRASVATPVSTPRPPSGHGFSPAVCASPATPYQLSSHSAASLPSPQSNASAGGGNYGGFNFHSFDSSDVKPEKDVQQQQNQQQSNNNSSSSNPLLGGGLPNGVGGMLLSQQQQQQQTPPQQQQQQQQQESSERLRHLLTKSQSMAGGLGGLGDDEKYFKPEGSEEEKHASGGFKMGGQPGGMGMFGPMGSMGRGVGNSSMLHKAGNSQNPMLLKLLNEKSEDDDGNGSGGGPGSMNNSRQSELMRQLKNPDGGSHGMHRNSASGNMSTEDLKAMLKIQSDPSLNRKRSLNEPDDDPSAKRSEDKPSKLCTQNKMLAKLLQNPPKIPKAPNPEQPLQVKTLPDITSSTVSSTLAAPGNLISAGSTGPKAAANRNRKQQQQQQQQQQQQQQQQVAGIPSQQQQQQPNDVYLSQQQQQQLQSPQLAFQHQQLATTATTSITTAASTSAAAAAAAAILGEGDSELSKLLDSVMEYYPDDTPIVTNAPSEASAINDIQKSLMLDVESAAFGNDLNQQLMMTQQQQHQQQQQQQQLLALQLAQQQQQQRQQHLQQPPAYPGMLNMQQQQHQQQQQQNQQHIMQRLEAMRNQGNQGFQRPPPMYPARGRGPMNAVATPGGVVLPAQQQLRNIRQQQQLAAAQQKERLLQQQQKQQLLVPENASEYWGNSNLQLIIKLIVSYILAGMNAGLNNIGSLLNTTGAPNVSLSRTNLPSDAQLSPNFAQTLMQQQLSPGRSAPYSPQPNQGYAPQFPQPGQRLSPQQQQQLSQQQQNNVQQQQLAYQQQQVGDGGRSNTPFGSNSGMQSPGMQNSPQQWGSGGGGGGGPGGPLPSGNAGRTLQQHNPMLIAQLQGVSPYNARQYQQNQRRGLNSPGAVGPGGNPAAQAALQRQNSFQGQGGGGATTPDGSGVGFGGPQSPYGTNVNVFQQQQLQRLQRQGSVPQATQHLPGSPRFGSSPGSSNNTDSSAAAGNQQQQQQQQQQQQQQHQQQQHQQLMNGLSMSPHPHPHPAMMGVGGMGSGGGNGIIGLGGGGGNYGATLGGYGQSQQANDFYGRAQTAGGGGSVAGGNANSEFVKQELRAVVSVRAQQAAAAATGGAGVGGGVAQRGQTPQSPLQQGSVIGGGGGIVGGFNSTNTMGNVTPTGSGNVSNSMLNTPPDPTLSFSF
Protein: RNA polymerase II subunit D (E9PB93)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLLEHRKQQNESAEDEQELSEVFMKTLNYTARFSRFKNRETIASVRSLLLQKKLHKFELACLANLCPETAEESKALIPSLEGRFEDEELQQILDDIQTKRSFQY
Protein: Osteocalcin-2 (OG2) (Bone Gla protein 2) (BGP2) (Gamma-carboxyglutamic acid-containing protein 2) (P86547)
Organism: Mus musculus (Mouse)
Function: Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium.
Subcellular location: Secreted {ECO:0000269|PubMed:17693256, ECO:0000269|PubMed:20655470, ECO:0000269|PubMed:20655471, ECO:0000269|PubMed:21333348, ECO:0000269|PubMed:24074871}.
Interaction partners:
- Osteopontin
- Osteocalcin
- SPARC
- Runt-related transcription factor 2
- Vitamin K-dependent gamma-carboxylase
- Integrin-binding sialoprotein
- Tumor necrosis factor ligand superfamily member 11
- Osteocalcin-related protein
- Parathyroid hormone
- G-protein coupled receptor family C group 6 member A
Sequence:
MRTLSLLTLLALAALCLSDLTDAKPSGPESDKAFMSKQEGNKVVNRLRRYLGASVPSPDPLEPTREQCELNPACDELSDQYGLKTAYKRIYGITI
Protein: Trans-golgi network protein 2 (A0A5F9UY30)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRFVVALVLLNVAAAGAVPLLATESVKQEEAGVRPSAGNVSTHPSLSQRPGGSTKSHPEPQTPKDSPSKSSAEAQTPEDTPNKSGAEAKTQKDSSNKSGAEAKTQKGSTSKSGSEAQTTKDSTSKSHPELQTPKDSTGKSGAEAQTPEDSPNRSGAEAKTQKDSPSKSGSEAQTTKDVPNKSGADGQTPKDGSSKSGAEDQTPKDVPNKSGAEKQTPKDGSNKSGAEEQGPIDGPSKSGAEEQTSKDSPNKVVPEQPSRKDHSKPISNPSDNKELPKADTNQLADKGKLSPHAFKTESGEETDLISPPQEEVKSSEPTEDVEPKEAEDDDTGPEEGSPPKEEKEKMSGSASSENREGTLSDSTGSEKDDLYPNGSGNGSAESSHFFAYLVTAAILVAVLYIAHHNKRKIIAFVLEGKRSKVTRRPKASDYQRLDQKIFFPLSPNRMVYSSGKR
Protein: 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase (HMP-P synthase) (Hydroxymethylpyrimidine phosphate synthase) (EC 2.-.-.-) (Thiamine biosynthesis protein 5) (Thiamine pyrimidine synthase) (C4YMW2)
Organism: Candida albicans (strain WO-1) (Yeast)
Function: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.
Interaction partners:
Sequence:
MSTNKITFLLNWEAAPYHIPVYLANIKGYFKDENLDIAILEPSNPSDVTELVGSGKVDMGLKAMVHTLAAKARGFPVTSIGSLLDEPFTGICYLEGSGITSDFQSLKGKRIGYVGEFGKIQVDELTKHYGMTPDDYVAVRCGMNVAKYILEGTIDCGIGIECIQQVELEEALKEQGKDSNDAKMLRIDKLAELGCCCFCTILYIANDKFIAENPQAVKKFLKAIKRATDYMLAHPREAWAEYGNFKPTMQTDLNTKKFQRCYAYFSESLYNVHRDWRKVNNYGKRLDILPENYVPNYTNEYLSWPEPKEVDDPEKAQDLMLKHQEECKTCGGYKRLVLA
Protein: DNA-directed RNA polymerase I subunit rpa49 (RNA polymerase I subunit A49) (DNA-directed RNA polymerase I 49 kDa polypeptide) (O14086)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase I subunit rpa1
- DNA-directed RNA polymerase I subunit rpa43
- DNA-directed RNA polymerase I subunit RPA12
- Probable DNA-directed RNA polymerase I subunit RPA2
- RNA polymerase I-specific transcription initiation factor rrn3
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MAGDELKGKKRKYRDSHSGDEKSVKILPLSESSLPPLVTTISGFYPPENTRFQLLKKSNQSNRDASLIGRTERVQFEAKNQSTATVEANYCLAVADKTGRVKKIVPAKYLNTFERNILALQEKDKFLKKKHGTVSGTVMEQRANLGLAFGTRKSQKAIMEESANRVKAETLGDVKDQLVSNVQKATEALPTQEDIAAAQAQDRPIPPVNVGAESIEDAYKLEDIIPKEEFSAIYIKPLLENPDERNWAKLLPYRHSLFINERFQRLLSIEEVDQKRARILYYISLLQAFLFSRRSVGNRETLRKKLADPPEILIDGLIKRFTQTTGIGSVQVSSREVDKIICYILVLCLIVDNYSTDVLTLANDLNVKTMKANELFRTVGCRIMAYTETQRMALGLNKTDAKNHKRAVLKIPLEFPKPRRGRARN
Protein: Protein arginine N-methyltransferase 6 (EC 2.1.1.319) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 6) (Histone-arginine N-methyltransferase PRMT6) (Q96LA8)
Organism: Homo sapiens (Human)
Function: Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53. Repression of TP53 blocks cellular senescence (By similarity). Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Promotes fasting-induced transcriptional activation of the gluconeogenic program through methylation of the CRTC2 transcription coactivator (By similarity). May play a role in innate immunity against HIV-1 in case of infection by methylating and impairing the function of various HIV-1 proteins such as Tat, Rev and Nucleocapsid protein p7 (NC). Methylates GPS2, protecting GPS2 from ubiquitination and degradation (By similarity). Methylates SIRT7, inhibiting SIRT7 histone deacetylase activity and promoting mitochondria biogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11724789}.
Interaction partners:
- Histone H4
- Histone H3.2
- Protein arginine N-methyltransferase 5
- Histone deacetylase 1
- Histone H3.3
- Histone H3.1
- WD repeat-containing protein 5
- Methyl-CpG-binding protein 2
- Histone-lysine N-methyltransferase SETD1A
- High mobility group protein HMG-I/HMG-Y
Sequence:
MSQPKKRKLESGGGGEGGEGTEEEDGAEREAALERPRRTKRERDQLYYECYSDVSVHEEMIADRVRTDAYRLGILRNWAALRGKTVLDVGAGTGILSIFCAQAGARRVYAVEASAIWQQAREVVRFNGLEDRVHVLPGPVETVELPEQVDAIVSEWMGYGLLHESMLSSVLHARTKWLKEGGLLLPASAELFIAPISDQMLEWRLGFWSQVKQHYGVDMSCLEGFATRCLMGHSEIVVQGLSGEDVLARPQRFAQLELSRAGLEQELEAGVGGRFRCSCYGSAPMHGFAIWFQVTFPGGESEKPLVLSTSPFHPATHWKQALLYLNEPVQVEQDTDVSGEITLLPSRDNPRRLRVLLRYKVGDQEEKTKDFAMED
Protein: Chromatin structure-remodeling complex subunit RSC4 (RSC complex subunit RSC4) (Remodel the structure of chromatin complex subunit 4) (Q02206)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton.
Subcellular location: Nucleus {ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:14562095}. Note=Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.
Interaction partners:
- Actin-related protein 7
- Chromatin structure-remodeling complex subunit RSC9
- Chromatin structure-remodeling complex subunit RSC2
- Chromatin structure-remodeling complex protein RSC6
- Chromatin structure-remodeling complex protein RSC8
- Chromatin structure-remodeling complex subunit SFH1
- High temperature lethal protein 1
- Chromatin structure-remodeling complex protein RSC58
- Nuclear protein STH1/NPS1
- Chromatin structure-remodeling complex subunit RSC7
Sequence:
MVVKKRKLATEAGGSDERPKYLPGKHPKNQEKTPHVDYNAPLNPKSELFLDDWHIPKFNRFISFTLDVLIDKYKDIFKDFIKLPSRKFHPQYYYKIQQPMSINEIKSRDYEYEDGPSNFLLDVELLTKNCQAYNEYDSLIVKNSMQVVMLIEFEVLKAKNLKRNYLINSEVKAKLLHYLNKLVDATEKKINQALLGASSPKNLDDKVKLSEPFMELVDKDELPEYYEIVHSPMALSIVKQNLEIGQYSKIYDFIIDMLLVFQNAHIFNDPSALIYKDATTLTNYFNYLIQKEFFPELQDLNERGEINLEFDKFEFENYLAIGGGGPAAAGALAISALDNDIEPESNREDLIDQADYDFNHFEGLGNGYNRSLLTEDYLLNPNNFKKLIAKPETVQSEVKNERSTTSDIEKTNSLESEHLKIPKYNVIKSMQKEMQSLSEQHTMEYKPYKLIQQIYIFSSKNLYSQATKPLLGSRPSCNQNWVEYIFNGNELSQNENAFSFMLQPMQTFLTLQSHLTSSLKDTETLLTINKEPVKSRTSNVNSNLSQPQQQENDVIGNDTKQDIENLTIGGGNNNDIVGNDNDKRNNITEIFDIRLSEGLNHLMFRCEDKISHETEFMNFWINVLP
Protein: Evasin P1096 (A0A0K8RKE4)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokine CXCL8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MELNAFTILHIAVFIAVGYYANTHTTVTGSVEGKPNNPNEDIEVSYCRMNCTVENGVSSACSGDCVCVHRDNEPNGICVEITYFGDFGDPSQDPSIDEAAPRESVSKRRSNGES