wanglab/gogpt-training-data huggingface dataset:
Protein: Basic helix-loop-helix transcription factor scleraxis (Q64124)
Organism: Mus musculus (Mouse)
Function: Plays an early essential role in mesoderm formation, as well as a later role in formation of somite-derived chondrogenic lineages.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Tenomodulin
- Homeobox protein Mohawk
- Fibromodulin
- Transcription factor SOX-9
Sequence:
MSFAMLRSAPPPGRYLYPEVSPLSEDEDRGSESSGSDEKPCRVHAARCGLQGARRRAGGRRAAGSGPGPGGRPGREPRQRHTANARERDRTNSVNTAFTALRTLIPTEPADRKLSKIETLRLASSYISHLGNVLLVGEACGDGQPCHSGPAFFHSGRAGSPLPPPPPPPPLARDGGENTQPKQICTFCLSNQRKLSKDRDRKTAIRS
Protein: Amyloid-beta A4 precursor protein-binding family B member 3 (Protein Fe65-like 2) (Fe65L2) (O95704)
Organism: Homo sapiens (Human)
Function: May modulate the internalization of amyloid-beta precursor protein.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12153398}. Nucleus {ECO:0000269|PubMed:12153398}.; SUBCELLULAR LOCATION: [Isoform I-214]: Nucleus.; SUBCELLULAR LOCATION: [Isoform I-245]: Nucleus.
Interaction partners:
- Amyloid-beta precursor protein
- Amyloid beta precursor like protein 2
- Amyloid beta precursor like protein 1
- Rho-related BTB domain-containing protein 1
- COP9 signalosome complex subunit 4
Sequence:
MLGKDYMLAIILVNCDDDLWGDHSLEVEAGLPPGWRKIHDAAGTYYWHVPSGSTQWQRPTWELGDAEDPGTGTEGIWGLRPPKGRSFSSLESSLDRSNSLSWYGGESYIQSMEPGAKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRSRSQPPDGAWGEGQNMLMILKKDAMSLVNPLDHSLIHCQPLVHIRVWGVGSSKGRDRDFAFVASDKDSCMLKCHVFCCDVPAKAIASALHGLCAQILSERVEVSGDASCCSPDPISPEDLPRQVELLDAVSQAAQKYEALYMGTLPVTKAMGMDVLNEAIGTLTARGDRNAWVPTMLSVSDSLMTAHPIQAEASTEEEPLWQCPVRLVTFIGVGRDPHTFGLIADLGRQSFQCAAFWCQPHAGGLSEAVQAACMVQYQKCLVASAARGKAWGAQARARLRLKRTSSMDSPGGPLPLPLLKGGVGGAGATPRKRGVFSFLDAFRLKPSLLHMP
Protein: LP15255p (Q5BI69)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
QSANMVKLTLYGVNPSPPVRAVKLTLAALQLPYEFVNVNISGQEQLSEEYLKKNPEHTVPTLEDDGNYIWDSHAIIAYLVSKYADSDALYPRDLLQRAVVDQRLHFETGVVFANGIKAITKPLFFNGLNRIPKERYDAIVEIYDFVETFLAGHDYIAGDQLTIADFSLISSITSLVAFVEIDRLKYPRIIEWVRRLEKLPYYEEANAKGARELETILKSTNFTFAT
Protein: Isovaleryl-CoA dehydrogenase, mitochondrial (IVD) (EC 1.3.8.4) (Butyryl-CoA dehydrogenase) (EC 1.3.8.1) (P12007)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the leucine (Leu) catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of other saturated short-chain acyl-CoA thioesters as pentanoyl-CoA, hexenoyl-CoA and butenoyl-CoA.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:6401713}.
Interaction partners:
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Peroxisomal bifunctional enzyme
- Trifunctional enzyme subunit alpha, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Electron transfer flavoprotein subunit beta
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
Sequence:
MATAVRLLGRRVSSWRLRPLPSPLAVPQRAHSMLPVDDDINGLNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKNLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPDADVLVVYAKTDLTAVPASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGVILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRAFNADFR
Protein: Galactokinase (EC 2.7.1.6) (Galactose kinase) (P51570)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of a phosphate from ATP to alpha-D-galactose and participates in the first committed step in the catabolism of galactose.
Interaction partners:
- Galactose mutarotase
- Galactose-1-phosphate uridylyltransferase
- UDP-glucose 4-epimerase
- UDP-glucose--hexose-1-phosphate uridylyltransferase
- Interleukin-11 receptor subunit alpha
- Thymidine kinase, cytosolic
- Thymidine kinase 2, mitochondrial
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
- Mevalonate kinase
- UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MAALRQPQVAELLAEARRAFREEFGAEPELAVSAPGRVNLIGEHTDYNQGLVLPMALELMTVLVGSPRKDGLVSLLTTSEGADEPQRLQFPLPTAQRSLEPGTPRWANYVKGVIQYYPAAPLPGFSAVVVSSVPLGGGLSSSASLEVATYTFLQQLCPDSGTIAARAQVCQQAEHSFAGMPCGIMDQFISLMGQKGHALLIDCRSLETSLVPLSDPKLAVLITNSNVRHSLASSEYPVRRRQCEEVARALGKESLREVQLEELEAARDLVSKEGFRRARHVVGEIRRTAQAAAALRRGDYRAFGRLMVESHRSLRDDYEVSCPELDQLVEAALAVPGVYGSRMTGGGFGGCTVTLLEASAAPHAMRHIQEHYGGTATFYLSQAADGAKVLCL
Protein: E3 ubiquitin-protein ligase HOS1 (EC 2.3.2.27) (Protein HIGH EXPRESSION OF OSMOTICALLY RESPONSIVE GENE 1) (RING finger protein HOS1) (RING-type E3 ubiquitin transferase HOS1) (Q84JU6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of the transcription factor ICE1. Acts as a negative regulator of cold signaling pathways. Probably involved in recruiting the NUP107-160 subcomplex of the nuclear pore complex to chromatin (Probable). Controls flowering time in response to ambient temperatures (16 and 23 degrees Celsius) and intermittent cold, probably via the regulation of FT and TSF levels.
Subcellular location: Nucleus {ECO:0000269|PubMed:11297514, ECO:0000269|PubMed:22960247}. Cytoplasm {ECO:0000269|PubMed:11297514, ECO:0000269|PubMed:22960247}. Note=Nuclear after cold treatment. Cytoplasmic when plant are grown or returned to normal growth temperatures. {ECO:0000269|PubMed:11297514, ECO:0000269|PubMed:22960247}.
Interaction partners:
- Transcription factor ICE1
- WD-40 repeat-containing protein MSI4
- Nuclear pore complex protein NUP160
- Histone deacetylase 6
- Phytochrome B
- E3 SUMO-protein ligase SIZ1
- Nuclear pore complex protein NUP96
- Serine/threonine-protein kinase SRK2E
- Transcription factor MYB15
- Dehydration-responsive element-binding protein 1B
Sequence:
MDTREINGFASAARSISLPTQPNYSSKPVQEALKHLASINLRELCNEAKVERCRATRDLASCGRFVNYVLNPCGHASLCTECCQRCDVCPICRSTLPKFGDRLRLRLYYECVEAGLISRTHEEASQDSDEDEHQLAADVHRLYSLFDVAMNNNLISVVCHYITNVCMDETAVSSDPVIAFLLDEVVVKDWVKRTFRSTLAELQEIYNLETKEMQAWLDKLLRCSKQVAGICSVLEVMESAFKGSVSPQLQDVQTLRENIGKTKQHLDIMVWCIRHGFLDDVRSRYSNFTSWNALVGERKSNAVKRAWPDAVDQSSDCSVQSASLFIEDALENLEREPEYSQEIGADLEVGRLQKDKRSFLRSKIEGTSGSYPFENLRTAADMLFLHGGSDLVVAKQAIFLYYLFDRHWTTPEKYWKHTIDDFAATFGITRHSLLESFVFYLLDDHSEEALQEACRILPEICGPETYPKVAQVLLERDNPETALMVLRWSGRDGVSELVSIGEAVTALRVRVECGLLSEAFTYQRTLCLKVKENNLKNGAVKHASDDLDIWSWTEWMEILVNEFCCLSIRRNLVDRIIELPWNPDEEKYLHRCLLDSATDDPSSAVGSLLVVFYLQRYRYIQAYQVDLRLQKIEEAFVSDNQIGEEVMFRMRSQSHWRKELVDRAIDILPVIQQQQVRSGQFSEMEDASEGAKKSDLPDAPDMITSSVPFATTNSVFLQSANNARAREPVANNGSPFQPGHMIGNASHDLSHGRLFTNANRGQKSEVRSVTKNLKFGEMSTPFKDLNRARGNSQLQGKRTEESSPEVNVDRYIENNMSSPYLRRITANNPVTVKSSSNHLNGSSQKPESTFFGTRMQPDKDNFVDLDDPMDMSSSLKDNNNNVLATESRNNSGGLRWRSDETSDDEDELTSFGSMPVKGRRRRRFAAR
Protein: Ubiquinol-cytochrome-c reductase complex assembly factor 3 (Assembly factor CBP4 homolog) (Q6UW78)
Organism: Homo sapiens (Human)
Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:25008109, ECO:0000269|PubMed:25605331}; Single-pass membrane protein {ECO:0000269|PubMed:25008109, ECO:0000269|PubMed:25605331}.
Interaction partners:
- Complex III assembly factor LYRM7
- Ubiquinol-cytochrome c reductase complex assembly factor 1
- Ubiquinol-cytochrome c reductase complex assembly factor 2
Sequence:
MDSLRKMLISVAMLGAGAGVGYALLVIVTPGERRKQEMLKEMPLQDPRSREEAARTQQLLLATLQEAATTQENVAWRKNWMVGGEGGAGGRSP
Protein: B-cell CLL/lymphoma 11A (Zinc finger protein), isoform CRA_b (BCL11A B-cell CLL/lymphoma 11A (Zinc finger protein) isoform 1) (D9YZW0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLRELAGNTSSPPLSPGRPSPMQRLLQPFQPGSKPPFLATPPLPPLQSAPPPSQPPVKSKSCEFCGKTFKFQSNLVVHRRSHTGEKPYKCNLCDHACTQASKLKRHMKTHMHKSSPMTVKSDDGLSTASSPEPGTSDLVGSASSALKSVVAKFKSENDPNLIPENGDEEEEEDDEEEEEEEEEEEEELTESERVDYGFGLSLEAARHHENSSRGAVVGVGDESRALPDVMQGMVLSSMQHFSEAFHQVLGEKHKRGHLAEAEGHRDTCDEDSVAGESDRIDDGTVNGRGCSPGESASGGLSKKLLLGSPSSLSPFSKRIKLEKEFDLPPAAMPNTENVYSQWLAGYAASRQLKDPFLSFGDSRQSPFASSSEHSSENGSLRFSTPPGELDGGISGRSGTGSGGSTPHISGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQVGKDVYKCEICKMPFSVYSTLEKHMKKWHSDRVLNNDIKTE
Protein: Keratin, type II cytoskeletal 4 (Cytokeratin-4) (CK-4) (Cytoskeletal 57 kDa keratin) (Keratin-4) (K4) (Type-II keratin Kb4) (P07744)
Organism: Mus musculus (Mouse)
Interaction partners:
- Keratin, type I cytoskeletal 13
- Small proline-rich protein 3
- Late cornified envelope 3A
- Keratinocyte differentiation-associated protein
Sequence:
MIARQSSVRGASRGFSSGSAIAGGVKRVAFSSGSMSGGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVGGYGAGFGAGGFGGGFGGSFNGRGGPGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKIRTAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSPKSLDPFFETYINALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECRMSGECKSAVSISVVGGSASIGGSGLGLGSGFCSGSGSGSGFGFGGGIYGGSGSKITSSATITKRSPR
Protein: Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2 (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase 2) (NDST-2) (Mndns) (N-heparan sulfate sulfotransferase 2) (N-HSST 2) [Includes: Heparan sulfate N-deacetylase 2 (EC 3.-.-.-); Heparan sulfate N-sulfotransferase 2 (EC 2.8.2.-)] (P52850)
Organism: Mus musculus (Mouse)
Function: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
- Exostosin-1
- Exostosin-2
- D-glucuronyl C5-epimerase
- Heparan-sulfate 6-O-sulfotransferase 1
- Heparan-sulfate 6-O-sulfotransferase 2
Sequence:
MLQLWKVVRPARQLELHRLILLLIGFSLVSMGFLAYYVSTSPKAKEPLPLPLGDCSSSGAAGPGPARPPVPPRPQRPPETTRTEPVVLVFVESAYSQLGQEIVAILESSRFRYSTELAPGRGDMPTLTDHTHGRYVLVIYENLLKYVNLDAWSRELLDRYCVEYGVGIIGFFRAREHSLLSAQLKGFPLFLHSNLGLRDYQVNPSAPLLHLTRPSRLEPGPLPGDDWTIFQSNHSTYEPVLIASHRPAELSMPGPVLRRARLPTVVQDLGLHDGIQRVLFGHGLSFWLHKLVFVDAVAYLTGKRLCLDLDRYILVDIDDIFVGKEGTRMKVADVEALLTTQNKLRTLVPNFTFNLGFSGKFYHTGTEEEDAGDDMLLKHRREFWWFPHMWSHMQPHLFHNRSVLADQMRLNKQFALEHGIPTDLGYAVAPHHSGVYPIHSQLYEAWKSVWGIQVTSTEEYPHLRPARYRRGFIHNGIMVLPRQTCGLFTHTIFYNEYPGGSRELDRSIRGGELFLTVLLNPISVFMTHLSNYGNDRLGLYTFESLVRFLQCWTRLRLQTLPPVPLAQKYFELFPQERSPLWQNPCDDKRHKDIWSKEKTCDRLPKFLIVGPQKTGTTAIHFFLSLHPAVTSSFPSPSTFEEIQFFNGPNYHKGIDWYMDFFPVPSNASTDFLFEKSATYFDSEVVPRRGAALLPRAKIITVLINPADRAYSWYQHQRAHGDPIALNYTFYQVISASSQAPLLLRSLQNRCLVPGYYSTHLQRWLTYYPSGQLLIMDGQELRVNPAASMEIIQKFLGITPFLNYTRTLRFDEDKGFWCQGLEGGKTRCLGRSKGRRYPDMDMESRLFLTDFFRNHNLELSKLLSRLGQPAPLWLREELQHSSVG
Protein: Serum amyloid A protein (B0M1H2)
Organism: Acinonyx jubatus (Cheetah)
Interaction partners:
Sequence:
MKLFTGLIFCSLVLGVSSEWYSFLGEAAQGAWDMWRAYSDMREANYIGADKYFHARGNYDAAQRGPGGAWAAKVISDARENSQRVTDFFRHGSSGHGAEDSKADQAANEWGRSGKDPNHFRPAGLPDKY
Protein: Argonaute protein hrde-1 (Heritable RNAi deficient 1) (Nuclear Argonaute HRDE-1) (Q09249)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:37083324}. Nucleus {ECO:0000269|PubMed:22810588}. Note=Shuttles to and from the nucleus to the peri-nuclear region of the cytoplasm called nuage (PubMed:37083324). Co-localizes with mut-16, probably to subdomains of the nuage known as Mutator foci (PubMed:37083324). {ECO:0000269|PubMed:37083324}.
Interaction partners:
- SET domain-containing protein
- Intron-binding protein aquarius
- DEAD-box ATP-dependent RNA helicase rde-12
- DRBM domain-containing protein
- Piwi-like protein 1
- Piwi domain-containing protein
- Nuclear exosome regulator NRDE2
- Dynein regulatory complex subunit 7
- Nuclear RNAi defective-3 protein
- Histone-lysine N-methyltransferase set-25
Sequence:
MADLLDKIMGSSSSNRIPKRDNRMNQDKDEPTSKRSAPMFSTPKSTTPIGRDSFATMDTMNVQMNMFPVDIKDMPHKIQRFQVDVIVCSSNGKQINANLGVLAAKGDVNSHNRRLAQYYIMRTVHDKLLVKFSGKSHHFLAYDCAATLYLPEGVYTGDDQEEVTLTIDDFPKEEWKFVSKLSRRKDDSYLVVLKPAGFVYTQGEVAQEEANRMELTRIIEIVTSQKLNNEDYLQFGNATFPRLSPPHSEPDAISEIRSGFAKVSRLSQNGGGKAFMTVDTKISPFYKDTSVIKFSSNKLSEMKGGGGGRGGYGRSDSRDSRGGYRGGRSDSRDFRGVYGNRGGNDRYRDESRGRRDMYDSRRDSGSSNGADYSPSDAAELEHAFGERGNTKRCIEEALKGLDVECTHLKGNLIRVSSIAENNAENTSFMMKDDKGEREVTVAEYFLLQYNIKLKYPRLPLVVSKRFKHESFFPMELLRIAPGQRIKVNKMSPTVQSAMTGRNASMPQHHVKLVQDILRDNLKLEQNKYMDAFGIKLMSTEPIQMTAKLLPPAQIKFKGQTYMPDMSRPAFRTQDKFVEPARIRKIGIVVFDNCIQMRQAEDFCDKLSNFCRDNGITVEKDSRDWSIRELNSSDSVAIQNLMKKWLDDRVDILVGIAREKKPDVHDILKYFEESIGLQTIQLCQQTVDKMMGGQGGRQTIDNVMRKFNLKCGGTNFFVEIPNAVRGKAVCSNNETLRKKLLEHVQFIGFEISHGASRTLFDRSRSQMDGEPSVVGVSYSLTNSTQLGGFTYLQTQKEYKLQKLDEFFPKCVRSYKEHSKTLPTRIVIYRVGAGEGNFNRVKEEVEEMRRTFDKIQPGYRPHLVVIIAQRASHARVFPSCISGNRATDQNIPSGTCVENVLTSYGYDEFILSSQTPLIGTVRPCKYTILVNDAKWSKNELMHLTYFRAFGHQVSYQPPSVPDVLYAAENLAKRGRNNYKIHQRYVNLQAVENRIIKDHSELINEDMREELAAAIVDEMSVAMNGMTIPKRNFWA
Protein: ADP-ribose glycohydrolase MACROD2 (MACRO domain-containing protein 2) (O-acetyl-ADP-ribose deacetylase MACROD2) (EC 3.5.1.-) ([Protein ADP-ribosylaspartate] hydrolase MACROD2) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD2) (EC 3.2.2.-) (Q3UYG8)
Organism: Mus musculus (Mouse)
Function: Removes ADP-ribose from aspartate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:A1Z1Q3}. Note=Recruited to DNA lesions, probably via mono-APD-ribosylated proteins. {ECO:0000250|UniProtKB:A1Z1Q3}.
Interaction partners:
- ADP-ribosylhydrolase ARH3
- Poly
- Core histone macro-H2A.2
- ADP-ribose glycohydrolase OARD1
Sequence:
MYPSNKKKKVWREEKERLLKMTLEERRKEYIRDYVSLSTILSWKEEMKSKGQNDEENTQEAPQMKKSLSEKVSLYRGDITLLEVDAIVNAANASLLGGGGVDGCIHRAAGPCLLAECRNLNGCETGHAKITCGYDLPAKYVIHTVGPIARGHINGSHKEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLAKNHQEVDRIIFCVFLEVDFKIYKKKMNEFFPVDDNNEGTDADMKEDSEGPEPKGLSPPHKKSKAKKPESSKDSSEDESGPEEKQTAEEMEGQSQEAGGLRFLLRNLLGLIHRDGVNTTPVPSPASEDKAEVHKDEDSAKDDNTVKDSDMTNHSVCDQELPNGQENDSAKSEGKTEAESPSSSMETEDLSPNQEDAAIVEQPEVIPLIDDQEAQEGGEAQGKDAPAVFAESQGSSEAENTSGPDVDMNSQVDGVNEPTESLQEDLQ
Protein: IQ motif and Sec7 domain ArfGEF 1 (A0A2R8Y695)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLKFKAFCLDYWQFLCLQPLHGAYKSVEGEAPSSETGTSLDSPSAYPQGPLVPGSSLSPDHYEHTSVGAYGLYSGPPGQQQRTRRPKLQHSTSILRKQAEEEAIKRSRSLSESYELSSDLQDKQVEMLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSVTNDGSQLGALVSPECGDLSEPTTLKSPAPSSDFADAITELEDAFSRQVKSLAESIDDALNCRSLHTEEAPALDAARARDTEPQTALHGMDHRKLDEMTASYSDVTLYIDEEELSPPLPLSQAGDRPSSTESDLRLRAGGAAPDYWALAHKEDKADTDTSCRSTPSLERQEQRLRVEHLPLLTIEPPSDSSVDLSDRSERGSLKRQSAYERSLGGQQGSPKHGPHSGAPKSLPREEPELRPRPPRPLDSHLAINGSANRQSKSESDYSDGDNDSINSTSNSNDTINCSSESSSRDSLREQTLSKQTYHKEARNSWDSPAFSNDVIRKRHYRIGLNLFNKKPEKGVQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSTMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCICNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKMKLEDFIKNLRGVDDGEDIPREMLMGIYERIRKRELKTNEDHVSQVQKVEKLIVGKKPIGSLHPGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQ
Protein: 2-acylglycerol O-acyltransferase 1 (EC 2.3.1.22) (Acyl-CoA:monoacylglycerol acyltransferase 1) (MGAT1) (Diacylglycerol acyltransferase 2-like protein 1) (Monoacylglycerol O-acyltransferase 1) (Q91ZV4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA. Probably not involved in absorption of dietary fat in the small intestine.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:12077311}; Multi-pass membrane protein {ECO:0000305|PubMed:12077311}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Phosphatidate phosphatase LPIN1
- Phospholipid phosphatase 2
- Phosphatidate phosphatase LPIN2
- Patatin-like phospholipase domain-containing protein 2
- Monoglyceride lipase
- Phosphatidate phosphatase LPIN3
- 1-acylglycerol-3-phosphate O-acyltransferase Pnpla3
- Hepatic triacylglycerol lipase
- Phospholipid phosphatase 4
Sequence:
MMVEFAPLNTPLARCLQTAAVLQWVLSFLLLVQVCIGIMVMLVLYNYWFLYIPYLVWFYYDWRTPEQGGRRWNWVQSWPVWKYFKEYFPICLVKTQDLDPGHNYIFGFHPHGIFVPGAFGNFCTKYSDFKKLFPGFTSYLHVAKIWFCFPLFREYLMSNGPVSVSKESLSHVLSKDGGGNVSIIVLGGAKEALEAHPGTFTLCIRQRKGFVKMALTHGASLVPVFSFGENDLYKQINNPKGSWLRTIQDAMYDSMGVALPLIYARGIFQHYFGIMPYRKLIYTVVGRPIPVQQTLNPTSEQIEELHQTYLEELKKLFNEHKGKYGIPEHETLVFK
Protein: Valine--pyruvate aminotransferase (EC 2.6.1.66) (Alanine--valine transaminase) (Transaminase C) (P09053)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of alanine.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Branched-chain-amino-acid aminotransferase
- Glutamate-pyruvate aminotransferase AlaA
- 2-isopropylmalate synthase
- Dihydroxy-acid dehydratase
- Periplasmic alpha-amylase
- Glutamate-pyruvate aminotransferase AlaC
- Aromatic-amino-acid aminotransferase
Sequence:
MTFSLFGDKFTRHSGITLLMEDLNDGLRTPGAIMLGGGNPAQIPEMQDYFQTLLTDMLESGKATDALCNYDGPQGKTELLTLLAGMLREKLGWDIEPQNIALTNGSQSAFFYLFNLFAGRRADGRVKKVLFPLAPEYIGYADAGLEEDLFVSARPNIELLPEGQFKYHVDFEHLHIGEETGMICVSRPTNPTGNVITDEELLKLDALANQHGIPLVIDNAYGVPFPGIIFSEARPLWNPNIVLCMSLSKLGLPGSRCGIIIANEKIITAITNMNGIISLAPGGIGPAMMCEMIKRNDLLRLSETVIKPFYYQRVQETIAIIRRYLPENRCLIHKPEGAIFLWLWFKDLPITTKQLYQRLKARGVLMVPGHNFFPGLDKPWPHTHQCMRMNYVPEPEKIEAGVKILAEEIERAWAESH
Protein: QM-like protein (Q967R7)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MARRPARCYRFCKNKPYPKSRFCRGVPDPRIRTFDIGKRRAPVDEFPVCVHVVSRELEQISSEALEAARIQANKYMVKRANKECFHMRIRAHPFHVLRINKMLSCAGADRLQTGMRQSYGKPNGTCARVRIGQILLSMRTKDTYVPQALESLRRAKMKFPGRQIIVISKYWGFTNILRNEYEELRDAGKLQQRGLHVKLITPKGKITPYNIMA
Protein: Putative GMC-type oxidoreductase R135 (EC 1.-.-.-) (Q5UPL2)
Organism: Acanthamoeba polyphaga mimivirus (APMV)
Subcellular location: Virion {ECO:0000269|PubMed:16971431}. Host membrane {ECO:0000269|PubMed:16971431}; Single-pass membrane protein {ECO:0000269|PubMed:16971431}.
Interaction partners:
Sequence:
MKNKECCKCYNPCEKICVNYSTTDVAFERPNPCKPIPCKPTPIPCDPCHNTKDNLTGDIVIIGAGAAGSLLAHYLARFSNMKIILLEAGHSHFNDPVVTDPMGFFGKYNPPNENISMSQNPSYSWQGAQEPNTGAYGNRPIIAHGMGFGGSTMINRLNLVVGGRTVFDNDWPVGWKYDDVKNYFRRVLVDINPVRDNTKASITSVALDALRIIAEQQIASGEPVDFLLNKATGNVPNVEKTTPDAVPLNLNDYEGVNSVVAFSSFYMGVNQLSDGNYIRKYAGNTYLNRNYVDENGRGIGKFSGLRVVSDAVVDRIIFKGNRAVGVNYIDREGIMHYVKVNKEVVVTSGAFYTPTILQRSGIGDFTYLSSIGVKNLVYNNPLVGTGLKNHYSPVTITRVHGEPSEVSRFLSNMAANPTNMGFKGLAELGFHRLDPNKPANANTVTYRKYQLMMTAGVGIPAEQQYLSGLSPSSNNLFTLIADDIRFAPEGYIKIGTPNIPRDVPKIFFNTFVTYTPTSAPADQQWPIAQKTLAPLISALLGYDIIYQTLMSMNQTARDSGFQVSLEMVYPLNDLIYKLHNGLATYGANWWHYFVPTLVGDDTPAGREFADTLSKLSYYPRVGAHLDSHQGCSCSIGRTVDSNLKVIGTQNVRVADLSAAAFPPGGNTWATASMIGARAVDLILGFPYLRDLPVNDVPILNVN
Protein: ADP-ribosylation factor-binding protein GGA3 (Golgi-localized, gamma ear-containing, ARF-binding protein 3) (A0A0G2JV04)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR receptor ADRA2B to the cell surface. Involved in BACE1 transport and sorting as well as regulation of BACE1 protein levels. Regulates retrograde transport of BACE1 from endosomes to the trans-Golgi network via interaction through the VHS motif and dependent of BACE1 phosphorylation. Modulates BACE1 protein levels independently of the interaction between VHS domain and DXXLL motif through recognition of ubiquitination (By similarity). Key player in a novel DXXLL-mediated endosomal sorting machinery to the recycling pathway that targets NTRK1 to the plasma membrane.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NZ52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZ52}. Endosome membrane {ECO:0000250|UniProtKB:Q9NZ52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZ52}. Early endosome membrane {ECO:0000269|PubMed:26446845}; Peripheral membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000269|PubMed:26446845}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- ADP-ribosylation factor 6
- Rab GTPase-binding effector protein 1
- Cation-independent mannose-6-phosphate receptor
- Cation-dependent mannose-6-phosphate receptor
- ADP-ribosylation factor 1
- Polyubiquitin-C
- Clathrin heavy chain 1
- Adapter molecule crk
- Ubiquitin-ribosomal protein eL40 fusion protein
- Beta-secretase 1
Sequence:
MAEAEGESLESWLNKATNPSNRQEDWEYIIGFCDQINKELEGPQIAVRLLAHKIQSPQEWEAVQALTVLEACMKNCGRRLHNEVGKFRFLNELIKVVSPKYLGDRVSEKVKAKVIELLFSWTLALPEEAKIKDAYHMLKRQGIVQSDPPIPMDRTLIPSPPPRPKNPVFDDEEKSKLLAKLLRSKNPDDLQEANQLIKSMVKEDEARIQKVTKRLHTLEEVNNNVKLLHEMLLHYSQEFSSEADKELMKELFDRCENKRRTLFKLASETEDNDNSLGDILQASDNLSRVINSYKTIIEGQIINGEVTTSTVPDSEGNSHCGNQGALIDLAELDTPSSSSPVLAPAPAPPTSGIPILPPPPQTSGPPRSRSSSQAEAPSGPDSTNNALSLLDEELLCLGLSDPAPTAPKESAGNSPWHLFQNEPSSDLDFFSPRLVSAASCPSEGSLLPPPVSTSSLSQAPLPAAFPAPVVPASAVTHSTGSFTFSSGPAPALVPKAEPEGPEYPSSSISHRLDALDQLLEEAKVTSGLVKPVSCFSPGPTASPLLPASTPARPLLPFSTGPGSPLFQSPAFQSQGSPQKGPELSLASVHVPLESIKPSSALPVTAYDKNGFRILFHFAKECPPGRPDVLVVVVSMLNTAPLPVKSIVLQAAVPKSMKVKLQPPSGTELSPFSPIQPPAAITQVMLLANPMKEKVRLRYKLTFALGEQLSTELGEVDQFPPVEQWGNL
Protein: Vesicle transport through interaction with t-SNAREs homolog 1A (Vesicle transport v-SNARE protein Vti1-like 2) (Vti1-rp2) (Q96AJ9)
Organism: Homo sapiens (Human)
Function: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. Involved in vesicular transport from the late endosomes to the trans-Golgi network. Along with VAMP7, involved in an non-conventional RAB1-dependent traffic route to the cell surface used by KCNIP1 and KCND2. May be involved in increased cytokine secretion associated with cellular senescence.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:19138172}. Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- Syntaxin-5
- Syntaxin-16
- Syntaxin-10
- Syntaxin-12
- Vesicle-associated membrane protein 4
- Syntaxin-6
- Vesicle-associated membrane protein 3
- Synaptobrevin homolog YKT6
- Syntaxin-8
- Syntaxin-7
Sequence:
MSSDFEGYEQDFAVLTAEITSKIARVPRLPPDEKKQMVANVEKQLEEAKELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDDGNSSENQRAHLLDNTERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARERLRETDANLGKSSRILTGMLRRIIQNRILLVILGIIVVITILMAITFSVRRH