wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar protein sorting-associated protein 45 (H2KYN0)
Organism: Caenorhabditis elegans
Interaction partners:
- FYVE-type domain-containing protein
- t-SNARE coiled-coil homology domain-containing protein
- t-SNARE coiled-coil homology domain-containing protein
- Putative syntaxin 6
- Vacuolar protein sorting-associated protein 16 homolog
- small monomeric GTPase
- Vps8 domain-containing protein
- Vacuolar protein sorting-associated protein 18 homolog
- Endoplasmic reticulum-Golgi intermediate compartment protein 3
- Vacuolar protein sorting-associated protein 33B
Sequence:
MDLVQSSRKLIQDMIQLAGSQMKLLLMDGETTPTVSCAFAQSEVMQKEVYIFDRIENKTSSENIKNLKCVVFVRPTPKNIERLVKELQEPRFSQYYLYFTNTINKYDVKRLAEADKNETVREVQEVFLDGVPIRKDLFTLNLTHIFDSSFTLKEEAAERIKCGIIALLLQLKKAPAVRYQKSSPSCKKVADDVAQFIRRENGLFENSRADTTLLIIERSQDAVTPLLNQWTYEAMIHEMLTLTNNRCTCTDQNIVLSELHDEFFARNITANFGEIGQNIKTLISEFQEKKHINKNLESIQDMKKFVEDYPQFKKISGTVSKHVSLVGELSNLVQKHNLLGVSEVEQAIVSDGDHGKCINLVRGLLKNTKTREVDIIRLVLLYALRFENAPGNELNSLISQLRPQHPKIHQTVSTLLKYGGLSRRPADLFGGESTIDITKRFIKGLKGVENIYTQHSPYLKNMIESCQRGRLDNYPLLSNECDRMDNIIVFIVGGATYEEAAYVRSLNEKRMQGYGGPAVVLAGSSMLNTKSFLEEFANVDKNTGAVH
Protein: Protein PTST homolog 3, chloroplastic (PROTEIN TARGETING TO STARCH homolog 3) (F4KFB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in starch granule initiation in leaf chloroplasts.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:28684429}.
Interaction partners:
Sequence:
MATISQIPFSISFPCFEFRKPSFYYHQPQLFVSYLNSTKKHSFICFACSTKQTRVRKRVKSNEELRSEIMQFVALAGLPEGHVPSMKELSAHGRVDLANIVRRRGYKFIKELVANSGMEEDCNELVADSEDNNTNIETGGSRACLEDSSTDLSKEAEKQGSLSKDESSLAGVLSLENSFSNLGDSNHSGEITEKIFKIESVELNEIADIENSSSEASVFANHSQDLYDTSSCPDIEAGNVSMTEDEEVNDVDKDFSLTFDHYTSPTSNHYTSPDLNSIKHVDIATGSSYDLTSENTMTNVENFQNQQIDDIAANRSGSADDSLVESEDNDWMSGLSSCTSSIEEKTTRFIQNGYLDTVGADENDIPNESCPEESSETTKGGEYIGDSLGGPRIMSTPLNGSALALKEIIHATEVNSSDRNSDQRDGSVGLDTDPHHETRKRENQVEIDRLRFMLDQKELELSRLKEQIEKEKLSLSVLQRQAETEIQKAQMLISEKEVELQEAEESLSGLQEVVIEYCGDGNAVEVTGSFNGWQHRVGMELQASKSIGKQKCWSTLLWLYPGTYEIKFIVDGQWITDPQKDSVTRGHISNNILKVDSQ
Protein: GM14666p (Q8MR40)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPGRKARRKLIKKQQRKRRRQKHAKERDKLEEEAENQRLMQPEYQKWLQEQEEMQEFQRLADERERQLAEESWLRREATAQRQFQMDEAKKRQEQEEVERLQREQAKERAEREERQRKQREEETRKAAKAAAKFDAMMESMDVYLNNPRIEKPPSHLLRVMETHPEERACEFFSRTNCCRYGHACTFNHRRPMLGRILLIRHFFNHSMLQKRCTHKEYASAEEHLELTEQDLRHDYDEFFNDVVEELRKFGTIVNFRTVRNTLEHLRGHVFVEYTNERSALRAFTNLQGRYYASKRLNVEFSNLRTWRGAVCGT
Protein: Fasciculation and elongation protein zeta-1 (Zygin I) (Zygin-1) (P97577)
Organism: Rattus norvegicus (Rat)
Function: May be involved in axonal outgrowth as component of the network of molecules that regulate cellular morphology and axon guidance machinery. May participate in the transport of mitochondria and other cargos along microtubules.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell membrane. Note=Colocalizes with both, alpha- and gamma-tubulin (By similarity). Translocated from the plasma membrane to the cytoplasm by activation of the PKC zeta. {ECO:0000250}.
Interaction partners:
- Kinesin-1 heavy chain
- Disrupted in schizophrenia 1 homolog
- Synaptotagmin-1
- Kinesin heavy chain isoform 5A
- Short coiled-coil protein
Sequence:
MEAPLVSLDEEFEDIRPCCTEDPEEKPQSLYGTSPHHLEDPSLSELENFSSEIISFKSMEDLVNEFDEKLNVCFRNYNAKTENLAPVKNQLQIQEEEETLRDEEVWDALTDNYIPSLSEDWRDPNIEALNGNSSDTEIHEKEEEDEFIEKSENDSGINEEPLLTADQVIEEIEEMMQNSPDPEEEVEVLEEEDGGEISSQADSVLLQEMQALTQTFNNNWSYEGLRHMSGSELTELLDQVEGAIRDFSEELVHQLARRDELEFEKEVKNSFITVLIEVQNKQKEQRELMKKRRKEKGLSLQSSRIEKGNQMPLKRFSMEGISNILQSGIRQTFGSSGADRQYLNTVIPYEKKSSPPSVEDLQMLTNILFAMKEDNEKVPTLLTDYILKVLCPT
Protein: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2) (PDC-E2) (PDCE2) (Q19749)
Organism: Caenorhabditis elegans
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Probable pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Probable citrate synthase, mitochondrial
- Probable ATP-citrate synthase
- 2-oxoglutarate dehydrogenase, mitochondrial
- ATP-citrate synthase
- Bifunctional glyoxylate cycle protein
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MSKFPVPLRTIGGLRPSTTAAISAANIGFTQSSRALSTGAAAKSSGLVGQVARQYPNAAAFSIKQVRLYSSGNLPKHNRVALPALSPTMELGTVVSWQKKEGDQLSEGDLLCEIETDKATMGFETPEEGYLAKILIQEGSKDVPIGKLLCIIVDNEADVAAFKDFKDDGASSGGSAPAAEKAPEPAKPAASSQPSPPAQMYQAPSVPKSAPIPHSSSGRVSASPFAKKLAAENGLDLSGVSGSGPGGRILASDLSQAPAKGATSTTTQAVSGQDYTDIPLSNMRKTIAKRLTESKSTIPHYYLTSEIQLDTLLQVREKLNGLLAKGTSGQATKISINDFIIKASALACQRVPEANSYWMDSFIRENHHVDVSVAVSTPAGLITPIIFNAHAKGLATIASEIVELAQRAREGKLQPHEFQGGTFTVSNLGMFGSVSDFTAIINPPQSCILAIGGASDKLVPDEAEGYKKIKTMKVTLSCDHRTVDGAVGAVWLRHFKEFLEKPHTMLL
Protein: Fimbrial assembly protein PilQ (P34750)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Essential for the formation of pili. Involved in the biogenesis of type 4 fimbriae probably by serving as a 'porthole' allowing passage of the fimbrae through the outer membrane.
Subcellular location: Cell outer membrane {ECO:0000305}.
Interaction partners:
- Type IV pilus inner membrane component PilM
- Type IV pilus inner membrane component PilP
- Type IV pilus inner membrane component PilN
- Type IV pilus inner membrane component PilO
- LysM domain-containing protein
- Type IV pilus assembly protein PilF
- Type IV pilus biogenesis factor PilY1
- Type IV pilus non-core minor pilin PilE
- Type IV pilus retractation ATPase PilT
- Type IV pilus ATPase PilU
Sequence:
MNSGLSRLGIALLAAMFAPALLAADLEKLDVAALPGDRVELKLQFDEPVAAPRGYTIEQPARIALDLPGVQNKLGTKNRELSVGNTRSVTVVEAKDRTRLIINLTALSSYTTRVEGNNLFVVVGNSPAGASVASAAPVKASPAPASYAQPIKPKPYVPAGRAIRNIDFQRGEKGEGNVVIDLSDPTLSPDIQEQGGKIRLDFAKTQLPDALRVRLDVKDFATPVQFVNASAQSDRTSITIEPSGLYDYLVYQTDNRLTVSIKPMTTEDAERRKKDNFAYTGEKLSLNFQDIDVRSVLQLIADFTDLNLVASDTVQGNITLRLQNVPWDQALDLVLKTKGLDKRKLGNVLLVAPADEIAARERQELEAQKQIAELAPLRRELIQVNYAKAADIAKLFQSVTSDGGQEGKEGGRGSITVDDRTNSIIAYQPQERLDELRRIVSQLDIPVRQVMIEARIVEANVGYDKSLGVRWGGAYHKGNWSGYGKDGNIGIKDEDGMNCGPIAGSCTFPTTGTSKSPSPFVDLGAKDATSGIGIGFITDNIILDLQLSAMEKTGNGEIVSQPKVVTSDKETAKILKGSEVPYQEASSSGATSTSFKEAALSLEVTPQITPDNRIIVEVKVTKDAPDYQNMLNGVPPINKNEVNAKILVNDGETIVIGGVFSNEQSKSVEKVPFLGELPYLGRLFRRDTVTDRKNELLVFLTPRIMNNQAIAIGR
Protein: cDNA FLJ52330, highly similar to Cystinosin (B4DML6)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MNWRRKSVIGLSFDFVALNLTGFVAYSVFNIGLLWVPYIKEQFLLKYPNGVNPVNSNDVFFSLHAVVLTLIIIVQCCLYERGGQRVSWPAIGFLVLAWLFAFVTMIVAAVGVITWLQFLFCFSYIKLAVTLVKYFPQAYMNFYYKSTEGWSIGNVLLDFTGGSFSLLQMFLQSYNNDQWTLIFGDPTKFGLGVFSIVFDVVFFIQHFCLYRKRPGYDQLN
Protein: DREV methyltransferase, putative (Q584Q2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIPSQLKSMTTFTNEGRVKPPMSYRANIDVLPQHIVTKYFILEKDKETTDWLKEAANVSALRILIANLLRHFVSLTTANGIVGRGGMFVVSTEQAANLLLGRTIAQQWTRYRDTMEPPFETLLDVGAGDGGVTSRLQPLFKRVTATEFSIPMRWRLWRRGYEVLPYQDPFTNKDGSRRYYDVISCLNVLDRADRPLDLLASMRDSLGPEGILLLAVVLPWCPFVEDGSIKRRPSQMMPMDGGECCKGATFEQSLQCLMDNVLVPFGFQLERWCKLPYLCEGNMIAEYAVLHDAVMVLTRKGDSGTATAEKDTDGSTIHT
Protein: RE58362p (Q8IGN4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
CSWPQNVDMLKFCSLRRSKEPAIVAPKVAKSSSLRLKDVPLNDAQLLQVLHAQRERGPLILALSSAKNSVQTCRKCGTPYENRQVVENGTTARPSYKSNGYVSEPEPNYDSDYSTVRYRTQNPHRVQSVSSAVNVRNLNQDEKLYGTMPNPIKSAQNSYKNQPGRIENYTTGHSSVSEKEKKEWWDEVMDIFNGNLEQSKLSPLYTEGNLSRALAKESGYTSDSNLVFRKKEVPVSSPLSPVEQKQAYKSLQAGGEPPLLGFRKPAPEKPRDLDPNAPPIPPQPPVKGLSSYDFPYSTDTVDGSDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: Cytosolic purine 5'-nucleotidase (EC 3.1.3.5) (Cytosolic nucleoside phosphotransferase 5'N) (EC 2.7.1.77) (Q54XC1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside. Through these activities regulates the purine nucleoside/nucleotide pools within the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49902}.
Interaction partners:
- 3',5'-cyclic-AMP phosphodiesterase 4
- Probable adenosine deaminase
- Inosine-5'-monophosphate dehydrogenase
- AMP deaminase
- cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A
- Adenosine deaminase 2
- Deoxyadenosine kinase
- Hypoxanthine-guanine phosphoribosyltransferase
- Nicotinamide-nucleotide adenylyltransferase
- Adenylosuccinate lyase
Sequence:
MAENNNNNNNNNNNNVSTPPHQKPHLTTGLRTSSSGLLMDKRRQDEEKFSAEQVAMGKKSPTKLFSAYSLNDLSNPPTDEELNNYKDLPASSLPPIHKREKLRRVFVNRDIKLDRIEFFGFDMDYTLAVYNSPDFEELAYDMVLDKLIDIGYPKSIRKLKYDPNFPTRGLFLDRELGNLLKIDSFGNIIICVHGRTTLSKNRTAEFYPSMRVSSDEIARNRFYLLNTLFTLPEACLYADLVDHLERESGLRLTEEVADEQQQMNSPPLSSLGSESVRIDESNHQPEGDLSFSNLFQDVRTACDLVHNDGSLKTRVLDDLPRYIRKTPDMPVFFDRLRQNKNKVFLLTNSEFYYTNKVMSYMMNGYNPNYQSWRDYFDVIIVGADKPRFFSEGTTIREVDTETGNLRITNVKDRFEQGKVYHGGSLSLFQKLTGAKGSRVLYIGDHIFADIIKSKKTHGWRNLLVVPELQHELEVMNQQKDTTIHLMNLEFIRAEIYRGLDSESTTPPDIEVLHQHLKNTNDKLNFAYNKYFGSLFKNGSKSTFFSMQVQRYADLYTSDYLNLLNYPLFYHFCANSLPLPHESSSFSSFDTSN
Protein: Zydeco, isoform G (A0A021WZA4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKYINCTQPAIDDFPRDLFSEAQRQSGAVVLHVIASLYLFVALAVVCDEYFVPAVEKICAALNMSNDVAGATFMAAATSAPELFVNVIGTFITEGDIGVGTIVGSAVFNILAVAACCGIGAGMTIPLDWWPLTRDSIAYGVTVAILICVMHDERVEWYEALILVSLYAVYLAVMYFDKTFQKCAKELVENRICQNMANIQLNGGLNKEQAKATSTSGAGTTAISITTSTMTTTLSTTHSAGGGGGAVGLCSGPGAIVQMAPLDDAEAESHVAVAAADEGRKEEGYSLLSYPKDKSCFAQFTWLIIWPIHLLFRIAIPDCKKAKNNKIFPLTFIMCIVWIGSLSYVVAWMITIIGDTLKIPDSVMGITFLAAGTSVPEAVSSVIVAKRGHGSMGICNSIGSNTFDILLCLGVPWLIKAVFFPIQPGQNYVAINSAGLEYSAITLLSTLFLLYLTFSTNKFKLDKKVGTACLVMYLVFMVFASLIELNVFFRVNLPTCGRS
Protein: E3 ubiquitin-protein ligase RAD18 (EC 2.3.2.27) (Postreplication repair protein RAD18) (mRAD18Sc) (RING-type E3 ubiquitin transferase RAD18) (Q9QXK2)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NS91}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NS91}. Note=Associates with chromatin. Colocalizes with SLF1 in the nucleus and to centrosomes. Relocalizes with SLF1 to nuclear foci in response to DNA damage. Accumulates with the SLF1-SLF2 and SMC5-SMC6 complexes at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner. {ECO:0000250|UniProtKB:Q9NS91}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 B
- Proliferating cell nuclear antigen
- Helicase-like transcription factor
- Ubiquitin-conjugating enzyme E2 A
- DNA repair protein RAD51 homolog 1
- E3 ubiquitin-protein ligase SHPRH
- Ubiquitin-conjugating enzyme E2 N
- DNA polymerase eta
- Fanconi anemia group M protein homolog
- DNA repair protein RAD51 homolog 3
Sequence:
MEVLAEPRWPPGLAVMKTIDDLLRCGICFEYFNIAVIIPQCSHNYCSLCIRKFLSYKTQCPTCCVAVTEPDLRNNRLLDELVKSMNFARTHLLQFALESPPISPVSSTSKKVVVKVHNADAAQHPVKQANRLMDKFLIRETGDCVFELLGKENERKFSPQKELSTSAEIKETSLLGKPVLGLSDANGPVTPSTSTMKLDTKVSCPVCGVSIPENHINKHLDSCLSREEKKESLRSSAHKRKPLPKTVYNLLSDRDLKKKLKQYGLSVQGNKQQLIKRHQEFVHMYNAQCDALHPKSAAEIVQEIESMEKTRMRLEASKLNENVMVFTKNQTEKEIEEVHSEYRKKHQNAFQLLVDQAKKGYKKTGRVSQAAAMRTDEPAETLPSMRTDEPAETLPSMRTDEPAETLPLMRADEPAETLPSECIAQEDNVSFSDTVSVTNHFPQPQLDSPGPSEPERPDDSSSCTDILFSSDSDSCNRNDQNREVSPQQTRRTRASECVEIEPRNKRNKN
Protein: DNA helicase IV (EC 5.6.2.4) (75 kDa helicase) (DNA 3'-5' helicase IV) (P15038)
Organism: Escherichia coli (strain K12)
Function: Helicase IV catalyzes the unwinding of duplex DNA in the 3' to 5' direction with respect to the bound single strand in a reaction that is dependent upon the hydrolysis of ATP.
Interaction partners:
- HTH-type transcriptional activator AaeR
- ATP-dependent DNA helicase RecQ
- Cell division protein FtsN
- Inner membrane protein YccF
- Outer membrane porin C
- Outer membrane porin PhoE
- Elongation factor Tu 1
- Outer membrane porin F
- Universal stress protein A
- Cell division topological specificity factor
Sequence:
MELKATTLGKRLAQHPYDRAVILNAGIKVSGDRHEYLIPFNQLLAIHCKRGLVWGELEFVLPDEKVVRLHGTEWGETQRFYHHLDAHWRRWSGEMSEIASGVLRQQLDLIATRTGENKWLTREQTSGVQQQIRQALSALPLPVNRLEEFDNCREAWRKCQAWLKDIESARLQHNQAYTEAMLTEYADFFRQVESSPLNPAQARAVVNGEHSLLVLAGAGSGKTSVLVARAGWLLARGEASPEQILLLAFGRKAAEEMDERIRERLHTEDITARTFHALALHIIQQGSKKVPIVSKLENDTAARHELFIAEWRKQCSEKKAQAKGWRQWLTEEMQWSVPEGNFWDDEKLQRRLASRLDRWVSLMRMHGGAQAEMIASAPEEIRDLFSKRIKLMAPLLKAWKGALKAENAVDFSGLIHQAIVILEKGRFISPWKHILVDEFQDISPQRAALLAALRKQNSQTTLFAVGDDWQAIYRFSGAQMSLTTAFHENFGEGERCDLDTTYRFNSRIGEVANRFIQQNPGQLKKPLNSLTNGDKKAVTLLDESQLDALLDKLSGYAKPEERILILARYHHMRPASLEKAATRWPKLQIDFMTIHASKGQQADYVIIVGLQEGSDGFPAAARESIMEEALLPPVEDFPDAEERRLMYVALTRARHRVWALFNKENPSPFVEILKNLDVPVARKP
Protein: Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296) (Cap methyltransferase 2) (Cap2 2'O-ribose methyltransferase 2) (HMTr2) (MTr2) (FtsJ methyltransferase domain-containing protein 1) (Protein adrift homolog) (Q8IYT2)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N(7) methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:21310715}. Cytoplasm {ECO:0000269|PubMed:21310715}.
Interaction partners:
- mRNA-capping enzyme
- mRNA cap guanine-N
- Small nuclear ribonucleoprotein F
Sequence:
MSKCRKTPVQQLASPASFSPDILADIFELFAKNFSYGKPLNNEWQLPDPSEIFTCDHTELNAFLDLKNSLNEVKNLLSDKKLDEWHEHTAFTNKAGKIISHVRKSVNAELCTQAWCKFHEILCSFPLIPQEAFQNGKLNSLHLCEAPGAFIASLNHYLKSHRFPCHWSWVANTLNPYHEANDDLMMIMDDRLIANTLHWWYFGPDNTGDIMTLKFLTGLQNFISSMATVHLVTADGSFDCQGNPGEQEALVSSLHYCEVVTALTTLGNGGSFVLKMFTMFEHCSINLMYLLNCCFDQVHVFKPATSKAGNSEVYVVCLHYKGREAIHPLLSKMTLNFGTEMKRKALFPHHVIPDSFLKRHEECCVFFHKYQLETISENIRLFECMGKAEQEKLNNLRDCAIQYFMQKFQLKHLSRNNWLVKKSSIGCSTNTKWFGQRNKYFKTYNERKMLEALSWKDKVAKGYFNSWAEEHGVYHPGQSSILEGTASNLECHLWHILEGKKLPKVKCSPFCNGEILKTLNEAIEKSLGGAFNLDSKFRPKQQYSCSCHVFSEELIFSELCSLTECLQDEQVVVPSNQIKCLLVGFSTLRNIKMHIPLEVRLLESAELTTFSCSLLHDGDPTYQRLFLDCLLHSLRELHTGDVMILPVLSCFTRFMAGLIFVLHSCFRFITFVCPTSSDPLRTCAVLLCVGYQDLPNPVFRYLQSVNELLSTLLNSDSPQQVLQFVPMEVLLKGALLDFLWDLNAAIAKRHLHFIIQREREEIINSLQLQN
Protein: Carbohydrate sulfotransferase 1 (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 1) (GST-1) (Keratan sulfate Gal-6 sulfotransferase) (KS6ST) (KSGal6ST) (KSST) (EC 2.8.2.21) (O43916)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of internal galactose (Gal) residues of keratan. Cooperates with B4GALT4 and B3GNT7 glycosyltransferases and CHST6 sulfotransferase to construct and elongate disulfated disaccharide unit [->3(6-sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer. Has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. Involved in biosynthesis of phosphacan, a major keratan sulfate proteoglycan in the developing brain (By similarity). Involved in biosynthesis of 6-sulfoGalbeta-containing O-linked glycans in high endothelial venules of lymph nodes. May act in a synergistic manner with CHST4 to generate sialyl 6',6-disulfo Lewis X motif, a recognition determinant for immune cell receptors implicated in leukocyte trafficking. Catalyzes sulfation of N-acetyllactosamine (LacNAc) oligosaccharides with highest efficiency for sialylated LacNAc structures.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Lumican
- Keratocan
- Sulfotransferase 1C3
- Sulfotransferase 1C4
- Sulfotransferase 1B1
Sequence:
MQCSWKAVLLLALASIAIQYTAIRTFTAKSFHTCPGLAEAGLAERLCEESPTFAYNLSRKTHILILATTRSGSSFVGQLFNQHLDVFYLFEPLYHVQNTLIPRFTQGKSPADRRVMLGASRDLLRSLYDCDLYFLENYIKPPPVNHTTDRIFRRGASRVLCSRPVCDPPGPADLVLEEGDCVRKCGLLNLTVAAEACRERSHVAIKTVRVPEVNDLRALVEDPRLNLKVIQLVRDPRGILASRSETFRDTYRLWRLWYGTGRKPYNLDVTQLTTVCEDFSNSVSTGLMRPPWLKGKYMLVRYEDLARNPMKKTEEIYGFLGIPLDSHVARWIQNNTRGDPTLGKHKYGTVRNSAATAEKWRFRLSYDIVAFAQNACQQVLAQLGYKIAASEEELKNPSVSLVEERDFRPFS
Protein: Glycerol-3-phosphate acyltransferase 4 (EC 2.3.1.15) (1-acylglycerol-3-phosphate O-acyltransferase 6) (1-AGP acyltransferase 6) (1-AGPAT 6) (Acyl-CoA:glycerol-3-phosphate acyltransferase 4) (Lysophosphatidic acid acyltransferase zeta) (LPAAT-zeta) (Testis spermatogenesis apoptosis-related protein 7) (TSARG7) (Q86UL3)
Organism: Homo sapiens (Human)
Function: Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) by incorporating an acyl moiety at the sn-1 position of the glycerol backbone. Active against both saturated and unsaturated long-chain fatty acyl-CoAs. Protects cells against lipotoxicity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18238778}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase 1-like protein
- Glycerol kinase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- Glycerol kinase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Acylglycerol kinase, mitochondrial
Sequence:
MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKSLLKIFAWATLRMERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCRKGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRIALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRNGGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHLVAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAFWNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLLWDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS
Protein: phosphorylase kinase (EC 2.7.11.19) (Q9VYV7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAKDEEDDLLPDKDAAKGFYAKYEPKEILGRGISSTVRRCIEKETGKEFAAKIIDLGATTESGETNPYHMLEATRQEISILRQVMGHPYIIDLQDVFESDAFVFLVFELCPKGELFDYLTSVVTLSEKKTRTIMRQIFEGVEYIHAKSIVHRDLKPENILLDENHNVKITDFGFAKAVARGREITNLCGTPGYLAPETLKCNMFEGSPGYSQEVDIWACGVIMFTLLVGCPPFWHRKQMVMLRNIMEGKYSFTSPEWADISEDPKDLIRKCLVVDPSQRITVKEVLRHPFFNQMVLMGDRRHPAPPIAPAQTNSRHLLQPEASSYRFGQLNSSCAGAPNYLYCAPQSSYSSNRMRDGALDDAGASAASATCHVMSPSNASNSYATNTTANTSNSALASASSHKTLTAMVYYQQQPQQHQTQQQQQQYQQQQTTQLPVQLQLPNPLLQTGGDGKQSVYAPPTVQLRKQSRFNARKKFQFAILVIRAIIRIRRLRFTAEPLHVEEAIRDPYRVKVMRKVIDGCACRVYGHWVKKGEGQDRAALFENTPRTELHALYINNLSR
Protein: FRIGIDA-like protein 3 (Q67ZB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transducin family protein / WD-40 repeat family protein
- Protein C2-DOMAIN ABA-RELATED 7
- Formin-like protein 13
- Protein MEI2-like 1
- Formin-like protein 14
Sequence:
MEDTRSVASLMDSTSSKIQQLQKAFAELESQRAVTLNLKWKELEEHFHGLERSLKRRFHELEDQEKEYETKTRKAQELLEKKKAAVEAKEKAALERLQKKRDAAMFTINSALDKYNNAPVSKPSVGERWPQNAVEDSSNVFAADSITDDNPDGIVQDVQISPVMGNYEVKAYPQLLKLCGDMDSTGLHKFVSDNRKNLASLKEEIPMAFRAAANPASLVLDSLEGFYPMEAPTADGKKDANLLGMRRTCIMLMECLSILLSGLDRNCLAVVLSQNVKHRAKTIAEGWNPLLESLDMDACNGNSLEAHAFLQLLATFAIVADFKEDELLKLIPMVSRRRQAAELCRSLGLAEKMPGVIEVLVNSGKQIDAVNLAFAFELTEQFSPVSLLKSYLIEARRSSPQGRPGNASPAVQDEFNERELIGLKTVIKCIEEHSLEEQYPVEPLHKRILQLEKAKADKKRATEPMKPQPKRPRGAQPRVTDNNNNINNNKTGYGRVIPERYPQYVYDNRPFLSGPIMAAQPPPPPPPQTYTFNPAPAHGNFYANCYQYQAPPPPPYFH
Protein: Runt-related transcription factor 2 (Acute myeloid leukemia 3 protein) (Core-binding factor subunit alpha-1) (CBF-alpha-1) (Oncogene AML-3) (Osteoblast-specific transcription factor 2) (OSF-2) (Polyomavirus enhancer-binding protein 2 alpha A subunit) (PEA2-alpha A) (PEBP2-alpha A) (SL3-3 enhancer factor 1 alpha A subunit) (SL3/AKV core-binding factor alpha A subunit) (Q13950)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Inhibits KAT6B-dependent transcriptional activation.
Subcellular location: Nucleus {ECO:0000269|PubMed:28505335, ECO:0000269|PubMed:28738062}. Cytoplasm {ECO:0000250|UniProtKB:Q08775}.
Interaction partners:
- Core-binding factor subunit beta
- Histone deacetylase 4
- Osteocalcin
- Homeobox protein MSX-2
- Homeobox protein DLX-5
- E3 ubiquitin-protein ligase SMURF1
- Protein c-Fos
- Bone morphogenetic protein 2
- Transcription factor SOX-9
- Transcription factor Sp7
Sequence:
MASNSLFSTVTPCQQNFFWDPSTSRRFSPPSSSLQPGKMSDVSPVVAAQQQQQQQQQQQQQQQQQQQQQQQEAAAAAAAAAAAAAAAAAVPRLRPPHDNRTMVEIIADHPAELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGEVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKVTVDGPREPRRHRQKLDDSKPSLFSDRLSDLGRIPHPSMRVGVPPQNPRPSLNSAPSPFNPQGQSQITDPRQAQSSPPWSYDQSYPSYLSQMTSPSIHSTTPLSSTRGTGLPAITDVPRRISDDDTATSDFCLWPSTLSKKSQAGASELGPFSDPRQFPSISSLTESRFSNPRMHYPATFTYTPPVTSGMSLGMSATTHYHTYLPPPYPGSSQSQSGPFQTSSTPYLYYGTSSGSYQFPMVPGGDRSPSRMLPPCTTTSNGSTLLNPNLPNQNDGVDADGSHSSSPTVLNSSGRMDESVWRPY
Protein: GTP cyclohydrolase 1 feedback regulatory protein (GFRP) (GTP cyclohydrolase I feedback regulatory protein) (p35) (P30047)
Organism: Homo sapiens (Human)
Function: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine.
Subcellular location: Nucleus {ECO:0000269|PubMed:16778797}. Nucleus membrane {ECO:0000269|PubMed:16778797}. Cytoplasm, cytosol {ECO:0000269|PubMed:16778797}.
Interaction partners:
- GTP cyclohydrolase 1
- 6-pyruvoyl tetrahydrobiopterin synthase
- Sepiapterin reductase
Sequence:
MPYLLISTQIRMEVGPTMVGDEQSDPELMQHLGASKRRALGNNFYEYYVDDPPRIVLDKLERRGFRVLSMTGVGQTLVWCLHKE