wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (M9NDZ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDDFGSTASDLEEATCPMQANATFSIDWRVTLLDHWLDLYLGYMNRLHMLLSLAGRLHLLSRHILGTLGQDPIFMGVLQGSLLMLFLFLMHLLRLWSCGYAVERPLNPTPDVAKELSCDFNFVSEQEKRAAQEAATEALLEVEEKKRRKRFTKKRNCVSAGPILIALRHQSKRPKHHRHAALPFEPVTPGEIILDTYLPPRELPLTIRLPQLAEPVKEEEVEYIELKSEPRGTLSTTDEIYPDSSDSSLYVSDEEQEDASQYCRGGYHPVVIGDIFDNRFRVVRKLGWGHFSTVWLCRDLKDEKYVALKVVKSAPHYIETAADEIRLLEAIRDADPMDVKRERIVRLMNHFTVRGVNGMHTCLVFEALGCSLYKLIVKNNYQGLAIAQVRNIIRQVLEGLDYLHSKCSIIHTDIKPENILLVIDNAAAMNQQIDDEINSLRVKGVDFPDSYISSIEKQTKSRAKWPLIEPNGSTNTNTNTSNSTATNSNSSTPLAAVIMSTLDKEDTTTTTSSTLNSNTTSSLASKYSSLLGDSECNGGLGGSANINNRYRTEKKITAKQPTPNSTNSSCPSHNTATIAKSKINSNILSTCTSLTSTNEYCFTNTNTTTASTPSAPPSATPSSAPALASATPPSTCTPSFTQIAPSATAPATSTTCTTSAEFYDGDHKTTSTSTTTTSNAISSATTTTATTTTAIAKLNVHANAIPSQNQSQSSQNNTYTIQSLIDNSNVRVKIADLGNACYDYHHFTEDIQTRQYRSIEVLLGAPYNYTADIWSTACLAFELATGDYLFDPHAGESYSRDEDHLAHIVELLGSIPQSVIFRGKHGLKYFTSYGSLRNITKLKPWSLMNVLVEKYDWDPVEAKKFSDFLLPMLEYNPVIRASAAECLQHPWLEQEEFV
Protein: Mitochondrial substrate carrier family protein (F4II70)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- Mitochondrial substrate carrier family protein
- Phosphatidylinositol-3-phosphatase myotubularin-1
Sequence:
MVEEAQLDPKSKSIPNENLKFGERALSAGGAAFISAVIVNPLDVVKTRLQAQAAGVPYQGSCRLGCFDTNSTLVHDLRSNSAPGMCRITGSASVCSDNQYKGTLDVFYKIIRQEGFSRLWRGTNASLTLAIPTVGIYMPCYDYFRNIMEEFTTEKSPSLTVYVPLVAGTIARSLACISCYPVELARTRMQAFKGTQRNVKLPGVWKTLVDVVNPVKGSNNGYRMLWTGLGAQLARDVPFSAICWSILEPTRRSIQSAMGEEPRAGSIIGANFAAGFVAGAVAAAATCPLDVAKTRRQIEKNTDRAMTMTTRQTLAEIWRDGGMRGMFSGAGARVGRAGPSVAIVVSFYEVVKYGLHNFHQQ
Protein: Obg-like ATPase 1 (P91917)
Organism: Caenorhabditis elegans
Function: Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP. Plays a role in regulating starvation-induced thermotaxis responses in AFD thermosensory neurons.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03167}.
Interaction partners:
- Threonine--tRNA ligase, cytoplasmic
- Translation factor GUF1 homolog, mitochondrial
- Ribonucleoside-diphosphate reductase large subunit
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS9m
- Carbohydrate sulfotransferase chst-1
- Probable arginine--tRNA ligase, cytoplasmic
- Phenylalanine--tRNA ligase beta subunit
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein bL21m
Sequence:
MPPKKNVVEEKPALIGRLGTNLKVGILGLPNVGKSTFFNVLTKSEAQAENFPFCTIDPNESRVAVQDDRFDWLVNHYKPASKVPAFLNVTDIAGLVKGASEGQGLGNAFLSHVSACDALFHLCRAFDDDDVTHVEGEVDPVRDLEIISNELFAKDLQFIDGPLDKVEKLFTRANDKTKKIEYDTLVRVKKCLEEKKPVRQELWNEKEIEILNKHLFLTAKPIVYLVNLSEKDYIRKKNKWLPKIKAWIDTNDAGAVLIPFSGAFELKLLDMPEDERQKYLKEQGVTSNLDKIVHTGYKALQLEYFFTSGEDEVKAWTIQVGTPAPKAAGRIHTDFEKGFIMAEVMKVADLIELGDEAKCKAGGKYRQQGKTYIVQDGDVIFFKFNAGAGLQAKKK
Protein: Probable heme-iron transport system permease protein IsdF (Iron-regulated surface determinant protein F) (Staphylococcal iron-regulated protein G) (Q8Y586)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Lmo2182 protein
- High-affinity heme uptake system protein IsdE
- FhuC protein
- Lmo2429 protein
- Lmo2431 protein
- Lmo1073 protein
- Lmo0541 protein
- Sortase B
- Lmo1959 protein
- Hemin/hemoglobin-binding protein 1
Sequence:
MTIKQKSSFGAVIVLLIGTILWAVQAGSLSMSIPAFLSGIFSGGNEMVDVVIDLRFPRIIIALLAGAALSVSGLLLQAVMRNPLADAGVIGISAGAKFFSFVIILFLPELYFWLPLFSFIGGALACFLVFLFSYRSDFNPLRFIIIGIAINAVFTGLSDALSSQVALVSSQSASSAASLAMKKWSDVETLLIYVTIGLICALLLAKWCNVLGLENKMARGFGVPVNKTRIWLALIAVLLASITTAVVGVIAFVGLLVPHIARKLVGGNYQILVPFSILFGALLLLFADTIGRTLFQQMEIPASVIMLIIGGPFLIFLMRKGDFYGSKGR
Protein: Uncharacterized protein C622.15c (O94602)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MNEDETSILNKKMEKIEVEMAEFERLGAEREKEAVERIVQEENQNPEVPSNDDASTDIKSRKEGNMKVTAEEIGLETENFDELPVSNGFGVSRRETHYGNNRTYYKNSQGYRRKPKRDDYNNNRKNFYPPIQNSTYFINATGGIDSMPYFGLNNAPGNIYPFSMYKPLEADPQYLSVPSSMPSRREAGMAYGYQNYKRGGYTPNTQYFEEPLNNTSFPNSQGKEGKNSGYRKSSRILDIRVKFGNSSMKAINFQPKKKIVHVVHNPRLHQNKVLRVSIPGSQPALVTPKHKMNVPPMGMYPLPFSPLPSAAPPIPFSPNVSSHPHMAFLPATVPTHSAPPGFVPYDFPITNDKMYPSPSFQEEFPSTSKSPSATPGSSNAPVVDMHPSADSATYPTSIYPSNVRARDDSQQAYISANMTTGEMPSMTNVPAGNAPAAPGTMYTTPLPTANSPIAYQSYSVMPTYWSFPQNYDSTVPAVYPYMPPPFSGSDMNVMSNPAADTLRSYSPASQVSTPPFGFVYYYDPNQYYVPVSNESANATSQPLSNLDTGGSAPYDHI
Protein: Rho GTPase-activating protein 18 (Rho-type GTPase-activating protein 18) (Q8K0Q5)
Organism: Mus musculus (Mouse)
Function: Rho GTPase activating protein that suppresses F-actin polymerization by inhibiting Rho. Rho GTPase activating proteins act by converting Rho-type GTPases to an inactive GDP-bound state. Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts downstream of YAP1 and inhibits actin polymerization, which in turn reduces nuclear localization of YAP1. Regulates cell shape, spreading, and migration (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8N392}.
Interaction partners:
Sequence:
MNWLSSSSGVVLTAYHPSGKDQVAGDSHVKGGDEATSSRRYGQYTINQEGSTKVPERPPFDRSSSQDSLDESMEAYWTELENIKRSNENRQEGQEAIVVKEPDEGELEEEWLKEAGLSNLFGESIDDPQESILFLSTLTRTQAAAVQKRVETVSQTLRKKNKQHHIRDVRDIFAQQREAQEKPPDDSDLRSVRTNENKGQGKDDQPSSGAVDSKEQISRVPEDTPASETDINLEVSFAEQAVNQKEFSKERTQKISSNDSLPSFRLPKDKTGTTRIGDLAPQDMKKVCSLSLIELTALYDVLGLEFKQQKAVKIKTRDSGLFGIPLTILLEQDQRKVPGTRIPLIFQKLISRIEEGSLETEGLLRIPGAAMRIKNLCQELEAKFYEGTFNWESVKQHDAASLLKLFLRELPQPLLSMEYLKAFQAVQNLPTRKEQLQALNLLVILLPDANRDTLKALLEFLQRVIDNKEKNKMTAGNVAMVMAPNLFMCHTLGLKSSEQREFEMAAGTANVMHLLIRYQKILWTIPKFIVIQVRKQNIENQKKERKAMKKLLKKMAYDREKHEKQDKTANGADVPQGVIRVQAPHLSKVSMAIQLTEELKASDVLARFLSQESGVAQTLKKGEVFLYEIGGNIGERCLDDDTHMKDLYQLNPNAEWVIKSKPV
Protein: Zinc finger protein 467 (Endothelial cell-derived zinc finger protein) (EZI) (Q8JZL0)
Organism: Mus musculus (Mouse)
Function: Transcription factor that promotes adipocyte differentiation and suppresses osteoblast differentiation in the bone marrow. Enhances the osteoclast-supporting ability of stromal cells. Binds with STAT3 the consensus sequence 5'-CTTCTGGGAAGA-3' of the acute phase response element (APRE). Transactivates several promoters including FOS, OSM and PPARG. Recruits a histone deacetylase complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:12426389}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma
Sequence:
MRETLEALNSLGFSVGQPEMAPQSEPRDGFSNAQEKMSSRGESTLHSCSGHETPGQKEGIHTEQAEAPCMGSQASTPQKAEPAGSVPGEEWMIRKVKVEDEDQEAEEEVEWPQHLSFLPSPFPTPDLGQLAVTYKLEPGTPGALGGIALSGWAPIPEKPYGCEECERRFRDQLTLRLHQRLHRGEGPCACPDCGRSFTQRAHMLLHQRSHRGERPFPCSECDKRFSKKAHLTRHLRTHTGERPYPCAECGKRFSQKIHLGSHQKTHTGERPFPCTECEKRFRKKTHLIRHQRIHTGERPYQCTQCTRSFTHKQHLVRHQRVHDAASRTRSSPDIPVAPHSPTASLTPSPPGPKPFACSHCGQSFGWKKNLATHQSLHLTEGRPFGCDECALGTNVDPAAEPSACTPHAPDCGPGSGPAAPQRTTSSERSFFCPDCGRGFAHGQHLARHRRVHTGERPFACAQCGRRFGSRPNLVAHSRAHSGARPFACAQCGRRFSRKSHLGRHQAVHTGSRPHACAVCARCFSSKTNLVRHQAIHTGSRPFSCPQCAKSFSRKTHLVRHQRIHGDAALPAPASNLSAPAWSNPSEVVPPPIFF
Protein: tRNA-splicing endonuclease subunit SEN2 (EC 4.6.1.16) (Splicing endonuclease protein 2) (tRNA-intron endonuclease SEN2) (P16658)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. This subunit may anchor the endonuclease complex to the nuclear membrane. Probably carries the active site for 5'-splice site cleavage.
Subcellular location: Nucleus {ECO:0000269|PubMed:12925762}. Endomembrane system {ECO:0000269|PubMed:12925762}; Peripheral membrane protein {ECO:0000269|PubMed:12925762}. Mitochondrion outer membrane {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}; Peripheral membrane protein {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}; Cytoplasmic side {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}. Note=The tRNA splicing endonuclease complex is predominantly associated with the outer membrane of mitochondria, suggesting that tRNA splicing mainly takes place on the mitochondrial surface.
Interaction partners:
- tRNA-splicing endonuclease subunit SEN34
- tRNA-splicing endonuclease subunit SEN54
- tRNA-splicing endonuclease subunit SEN15
- Protein BZZ1
- tRNA ligase
- RNases MRP/P 32.9 kDa subunit
- Ribonuclease P protein subunit RPR2
- Ribonucleases P/MRP protein subunit POP1
- Ribonucleases P/MRP protein subunit POP6
- Ribonucleases P/MRP protein subunit POP3
Sequence:
MSKGRVNQKRYKYPLPIHPVDDLPELILHNPLSWLYWAYRYYKSTNALNDKVHVDFIGDTTLHITVQDDKQMLYLWNNGFFGTGQFSRSEPTWKARTEARLGLNDTPLHNRGGTKSNTETEMTLEKVTQQRRLQRLEFKKERAKLERELLELRKKGGHIDEENILLEKQRESLRKFKLKQTEDVGIVAQQQDISESNLRDEDNNLLDENGDLLPLESLELMPVEAMFLTFALPVLDISPACLAGKLFQFDAKYKDIHSFVRSYVIYHHYRSHGWCVRSGIKFGCDYLLYKRGPPFQHAEFCVMGLDHDVSKDYTWYSSIARVVGGAKKTFVLCYVERLISEQEAIALWKSNNFTKLFNSFQVGEVLYKRWVPGRNRD
Protein: Transcription factor SFL2 (Q5AK51)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor that plays a role of activator of filamentous growth and which is involved in invasive growth at a high temperature. Required for human oral epithelium colonization and damage. Promotes filamentous growth in EFG1- and FLO8-dependent manners. Antagonizes functions of SFL1.
Subcellular location: Nucleus {ECO:0000269|PubMed:21205158}. Note=Localizes to the nucleus in both yeast and hyphal cells.
Interaction partners:
Sequence:
MSKKNPGDPRVKKNAFVHKLYTMLHDPALSHLIWWTNRNGEQNTFALCPGKEFADCLTQYFKHGNVASFVRQLHMYGFHKVSDPLPITYPPNGNNNNNNNNKEVPPVWEFKHSSGRFKRGDETSLVYIKRRSSSNHTSGSTIYAEPIYNPLLTNPYNQPQFMYQDYSMGPPVEVQQFYNYQNQPLMYYQQPPGQVPPPPPPSLPPHQQPEMALQYHQYNNYQQPPPAPPAPPPQPGNVLFGYQQVAPPQQPGSTVQQIPANAPPTLDQTQPLSYTPQLEYQQQQYPQPPLPPPPPQLQLQTSPGIPKVNDNLSRPSPNEQHLQFRKIWPDENNEANSKPRNPSLMFDPLLRVNSEGSPKTQPNHSVSLLNNEVRSESSTSSSSTTVTSTALPPPSAIDRSVSLVGGSPFDLSSRMNNQQSFNRTPSISTPPTQNGRLPKISSPLIPSNTESQSPTMVTGTDNDVGVTSKGSTSIISVSKKPSVFSNSLQERLRPSMFEYHPIGNNLSKDVLTIPKISTNSNSGSRTTSQSSMSSASALSSKKSSLSSISSTHGNLSILNSTNYRSTSVGGSGSGPFSTSTSTSTTSPTLSSLLHHPQHEPQNSTIANGTSIRSSISSSQSISSPPLTTTTTTTTTDQRQLSNSPISRQQQQQPNNNTNKKVSVTSLLLPSHSQSQGYAQPLYKSSVIAEEENSTTSSGGGYRSKSDDDTDNMNK
Protein: Calmodulin regulator protein PCP4 (Brain-specific polypeptide PEP-19) (Purkinje cell protein 4) (P63055)
Organism: Rattus norvegicus (Rat)
Function: Functions as a modulator of calcium-binding by calmodulin. Thereby, regulates calmodulin activity and the different processes it controls. For instance, may play a role in neuronal differentiation through activation of calmodulin-dependent kinase signaling pathways.
Interaction partners:
- Calmodulin-like protein 4
- Calmodulin-1
- Calmodulin-like protein 3
Sequence:
MSERQSAGATNGKDKTSGDNDGQKKVQEEFDIDMDAPETERAAVAIQSQFRKFQKKKAGSQS
Protein: Alpha-S1-casein (B5B3R8)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKDDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSGKTTMPLW
Protein: Calreticulin (P29413)
Organism: Drosophila melanogaster (Fruit fly)
Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
- Heat shock protein 83
- Protein disulfide-isomerase
- Hypoxia up-regulated protein 1
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase A6 homolog
- UDP-glucose:glycoprotein glucosyltransferase
- Protein disulfide-isomerase
- X-box-binding protein 1
- Inositol 1,4,5-trisphosphate receptor
- Calnexin 14D
Sequence:
MMWCKTVIVLLATVGFISAEVYLKENFDNENWEDTWIYSKHPGKEFGKFVLTPGTFYNDAEADKGIQTSQDARFYAASRKFDGFSNEDKPLVVQFSVKHEQNIDCGGGYVKLFDCSLDQTDMHGESPYEIMFGPDICGPGTKKVHVIFSYKGKNHLISKDIRCKDDVYTHFYTLIVRPDNTYEVLIDNEKVESGNLEDDWDFLAPKKIKDPTATKPEDWDDRATIPDPDDKKPEDWDKPEHIPDPDATKPEDWDDEMDGEWEPPMIDNPEFKGEWQPKQLDNPNYKGAWEHPEIANPEYVPDDKLYLRKEICTLGFDLWQVKSGTIFDNVLITDDVELAAKAAAEVKNTQAGEKKMKEAQDEVQRKKDEEEAKKASDKDDEDEDDDDEEKDDESKQDKDQSEHDEL
Protein: Alpha-soluble NSF attachment protein (SNAP-alpha) (N-ethylmaleimide-sensitive factor attachment protein alpha) (Q9DB05)
Organism: Mus musculus (Mouse)
Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. Together with GNA12 promotes CDH5 localization to plasma membrane.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P54920}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54920}.
Interaction partners:
- Syntaxin-1A
- Synaptosomal-associated protein 25
- Vesicle-associated membrane protein 2
- Vesicle-associated membrane protein 8
- Syntaxin-4
- Syntaxin-5
- Vesicle-fusing ATPase
- Syntaxin-3
- Synaptosomal-associated protein 23
- Vesicle-associated membrane protein 3
Sequence:
MDNSGKQAEAMALLAEAERKVKNSQSFFSGLFGGSSKIEEACEIYARAANMFKMAKNWSAAGNAFCQAAQLHLQLQSKHDAATCFVDAGNAFKKADPQEAINCLMRAIEIYTDMGRFTIAAKHHISIAEIYETELVDVEKAIAHYEQSADYYKGEESNSSANKCLLKVAGYAAQLEQYQKAIDIYEQVGTSAMDSPLLKYSAKDYFFKAALCHFCIDMLNAKLAVQKYEELFPAFSDSRECKLMKKLLEAHEEQNVDSYTEAVKEYDSISRLDQWLTTMLLRIKKTIQGDEEDLR
Protein: CCCTC-binding factor like (V9GYX4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAATEISVLSEQFTKIKELELMPEKGLKEEEKDGVCREKDHRSPSELEAERTSGAFQDSVLEEEVELVLAPSEESEKYILTLQTVHFTSEAVELQDMSLLSIQQQEGVQVVVQQPGPGLLWLEEGPRQSLQQCVAISIQQELYSPQEMEVLQFHALEENVMVASEDSKLAVSLAETTGLIKLEEEQEKNQLLAERTKEQLFFVETMSGDERSDEIVLTVSNSNVEEQEDQPTAGQADAEKAKSTKNQRKTKGAKGTFHCDVCMFTSSRMSSFNRHMKTHTSEKPHLCHLCLKTFRTVTLLRNHVNTHTGTRPYKCNDCNMAFVTSGELVRHRRYKHTHEKPFKCSMCKYASVEVKPFLDLKLHGILVEAAVQVTPSVTNSRICYKQAFYYSYKIYAGNNMHSLL
Protein: GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (EC 2.4.1.131) (Alpha-1,2-mannosyltransferase ALG11) (Asparagine-linked glycosylation protein 11) (Glycolipid 2-alpha-mannosyltransferase) (P53954)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11278778, ECO:0000269|PubMed:19929855}; Single-pass membrane protein {ECO:0000269|PubMed:19929855}.
Interaction partners:
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dol-P-Man:Man
- UDP-N-acetylglucosamine transferase subunit ALG13
- Alpha-1,3/1,6-mannosyltransferase ALG2
- Man
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- UDP-N-acetylglucosamine transferase subunit ALG14
- Dol-P-Man:Man
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
Sequence:
MGSAWTNYNFEEVKSHFGFKKYVVSSLVLVYGLIKVLTWIFRQWVYSSLNPFSKKSSLLNRAVASCGEKNVKVFGFFHPYCNAGGGGEKVLWKAVDITLRKDAKNVIVIYSGDFVNGENVTPENILNNVKAKFDYDLDSDRIFFISLKLRYLVDSSTWKHFTLIGQAIGSMILAFESIIQCPPDIWIDTMGYPFSYPIIARFLRRIPIVTYTHYPIMSKDMLNKLFKMPKKGIKVYGKILYWKVFMLIYQSIGSKIDIVITNSTWTNNHIKQIWQSNTCKIIYPPCSTEKLVDWKQKFGTAKGERLNQAIVLAQFRPEKRHKLIIESFATFLKNLPDSVSPIKLIMAGSTRSKQDENYVKSLQDWSENVLKIPKHLISFEKNLPFDKIEILLNKSTFGVNAMWNEHFGIAVVEYMASGLIPIVHASAGPLLDIVTPWDANGNIGKAPPQWELQKKYFAKLEDDGETTGFFFKEPSDPDYNTTKDPLRYPNLSDLFLQITKLDYDCLRVMGARNQQYSLYKFSDLKFDKDWENFVLNPICKLLEEEERG
Protein: Pantothenate kinase 3 (hPanK3) (EC 2.7.1.33) (Pantothenic acid kinase 3) (Q9H999)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of pantothenate to generate 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23152917, ECO:0000305}.
Interaction partners:
- Phosphopantothenate--cysteine ligase
- Phosphopantothenoylcysteine decarboxylase
- Bifunctional coenzyme A synthase
- Pantothenate kinase 2, mitochondrial
- Pantetheinase
- Pantetheine hydrolase VNN2
- Pantothenate kinase 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Dynein regulatory complex subunit 4
Sequence:
MKIKDAKKPSFPWFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDLPTFIQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERCQKMPFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVRDIYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSMKLLAYALDYWSKGQLKALFLEHEGYFGAVGALLGLPNFS
Protein: Toxin Rv2653c (P9WJ13)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin Rv2654c.
Interaction partners:
- Antitoxin Rv2654c
- Uncharacterized protein Rv2658c
- Uncharacterized protein Rv2656c
Sequence:
MTHKRTKRQPAIAAGLNAPRRNRVGRQHGWPADVPSAEQRRAQRQRDLEAIRRAYAEMVATSHEIDDDTAELALLSMHLDDEQRRLEAGMKLGWHPYHFPDEPDSKQ
Protein: Exosome complex component RRP43 (Exosome component 8) (Opa-interacting protein 2) (OIP-2) (Ribosomal RNA-processing protein 43) (p9) (Q96B26)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC8 binds to ARE-containing RNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17545563}. Nucleus {ECO:0000269|PubMed:17545563}. Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Exosome complex component 10
- Exosome complex component RRP45
- Exosome complex exonuclease RRP44
- Nuclear nucleic acid-binding protein C1D
- M-phase phosphoprotein 6
- Exosome complex component CSL4
- Exosome complex component RRP4
- Exosome complex component RRP40
- DIS3-like exonuclease 1
- Exosome complex component RRP41
Sequence:
MAAGFKTVEPLEYYRRFLKENCRPDGRELGEFRTTTVNIGSISTADGSALVKLGNTTVICGVKAEFAAPSTDAPDKGYVVPNVDLPPLCSSRFRSGPPGEEAQVASQFIADVIENSQIIQKEDLCISPGKLVWVLYCDLICLDYDGNILDACTFALLAALKNVQLPEVTINEETALAEVNLKKKSYLNIRTHPVATSFAVFDDTLLIVDPTGEEEHLATGTLTIVMDEEGKLCCLHKPGGSGLTGAKLQDCMSRAVTRHKEVKKLMDEVIKSMKPK
Protein: Heat shock 70-related protein 5 (Q54MR6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May function in protein folding and assembly, and disassembly of protein complexes.
Interaction partners:
- DnaJ homolog subfamily A member 1 homolog
- Heat shock protein
- Heat shock cognate 90 kDa protein
- Cytochrome c oxidase subunit 4, mitochondrial
- Luminal-binding protein 1
- J domain-containing protein
- J domain-containing protein
- GrpE protein homolog, mitochondrial
- J domain-containing protein
- J domain-containing protein
Sequence:
MANNNIMGIDFGTHFACVGIFKNERIEICPNQQGNRTTPSVVSFVGDDKLVGDEAKAQMDRNPLNTIYDVKRLLGRKTTDELFDHEVKKLSFKVTTYEDNNEKIEFQVNYKSNVVTLTPIEIATSILEQIKHTAETFIGGESIKKAVISVPTDFTEKQRNDLKEAATAAGITVVRMIHEHSAVALAYGYDQVKECSETTNESKESNVMVFDLGGSGVSASMIRVRSKLFEMIGNVSDHTVSGEHFDHVLVQHFTQEFNRKYRCDLTDNARSKAKLKSACEKAKRNLSNMTQAALEIDSLYDGRDFFTNITRARFEDMASGLIKGSINAVSQLLEKCNMTKEQVDKVLLVGGASRIPSVQNQLLNFFDNRQDILERSMNQEEVVAHGTTIQATILAADKSNQSLTCNSSNISMGAPFSAKFTPVTIGIQDSNGNLIPIIPSSSLIPCKRTFTLNTSSENQDNLNMAVYQGSAPLAKDNQLVSRFIFKSSPNPIDVTFEIDNNNTLLIKSEQANYSIKF
Protein: Calreticulin (56 kDa protein) (Q9SLY8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Endoplasmin homolog
- Calnexin
- Os02g0710900 protein
- Protein disulfide isomerase-like 5-2
- Protein disulfide isomerase-like 1-1
- Heat shock 70 kDa protein BIP3
- Os06g0163300 protein
- Protein disulfide isomerase-like 1-2
- Os04g0521600 protein
- Protein disulfide isomerase-like 1-3
Sequence:
MAIRARSSSYAAAAVALALALASVAAVAGEVFFQEKFEDGWESRWVKSEWKKDENMAGEWNHTSGKWNGDPEDKGIQTSEDYRFYAISAEYPEFSNKDKTLVLQFSVKHEQKLDCGGGYVKLLGGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHTIFTKNDKNHLIKKDVPCETDQLSHVYTLIIHPDATYTILIDNVEKQSGSIYEHWDILPPKQIKDPEAKKPEDWDDKEYIPDPEDKKPEGYDDIPKEIPDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGPWKQKKIKNPNYQGKWKAPMIDNPDFKDDPYIYAFDSLKYIGIELWQVKSGTLFDNFLITDDPELAKTFAEETWGKHKDAEKAAFDEAEKKKEEEEAAKAGEDDDDLDDEDAEDEDKADEKADSDAEDGKDSDDEKHDEL
Protein: Transcription factor RSL3 (Basic helix-loop-helix protein 54) (AtbHLH54) (bHLH 54) (ROOT HAIR DEFECTIVE 6-LIKE 4) (Protein RHD SIX-LIKE 4) (Transcription factor EN 114) (Transcription factor bHLH54) (bHLH transcription factor bHLH054) (Q8LEG1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in the regulation of root hair elongation. Is sufficient to promote postmitotic cell growth in root-hair cells and is a direct transcriptional target of RHD6 and RSL1. Involved in the regulation of root hair elongation in response to low phosphate. Controls root hair cell growth by regulating the expression of genes encoding proteins involved in cell signaling, cell wall modification and secretion.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:20139979, ECO:0000269|PubMed:27251390}.
Interaction partners:
- Expansin-A7
- Protein ETHYLENE INSENSITIVE 3
- Respiratory burst oxidase homolog protein C
- Transcription factor WER
- Expansin-A18
- Homeobox-leucine zipper protein GLABRA 2
- Proline-rich receptor-like protein kinase PERK13
- Phosphatidylinositol/phosphatidylcholine transfer protein SFH1
- MYB-like transcription factor ETC1
- Auxin response factor 19
Sequence:
MDVFVDGELESLLGMFNFDQCSSSKEERPRDELLGLSSLYNGHLHQHQHHNNVLSSDHHAFLLPDMFPFGAMPGGNLPAMLDSWDQSHHLQETSSLKRKLLDVENLCKTNSNCDVTRQELAKSKKKQRVSSESNTVDESNTNWVDGQSLSNSSDDEKASVTSVKGKTRATKGTATDPQSLYARKRREKINERLKTLQNLVPNGTKVDISTMLEEAVHYVKFLQLQIKLLSSDDLWMYAPLAYNGLDMGFHHNLLSRLM