wanglab/gogpt-training-data huggingface dataset:
Protein: Keratin-associated protein 3-1 (High sulfur keratin-associated protein 3.1) (Keratin-associated protein 3.1) (Q9BYR8)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 11-1
- Keratin-associated protein 9-3
- Keratin-associated protein 4-3
- Keratin-associated protein 9-4
- Keratin-associated protein 4-1
- Keratin, type I cuticular Ha3-II
- Keratin-associated protein 1-5
- Keratin-associated protein 1-1
- Keratin-associated protein 9-8
- Keratin-associated protein 3-2
Sequence:
MYCCALRSCSVPTGPATTFCSFDKSCRCGVCLPSTCPHEISLLQPICCDTCPPPCCKPDTYVPTCWLLNNCHPTPGLSGINLTTYVQPGCESPCEPRC
Protein: (2E,6E)-farnesyl diphosphate synthase (Dimethylallyltranstransferase) (Farnesyl diphosphate synthase) (Geranyltranstransferase) (A0A087X1D8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAWHSARCWCQAWTEEPRALCSSLRMNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDS
Protein: Small ribosomal subunit protein mS39 (28S ribosomal protein S39, mitochondrial) (MRP-S39) (Pentatricopeptide repeat domain-containing protein 3, mitochondrial) (Q2KI62)
Organism: Bos taurus (Bovine)
Function: Mitochondrial RNA-binding protein that has a role in mitochondrial translation.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS23
Sequence:
MASVASARWLRVSCGLCVPLTARRAGPCGRTPSSRFYSGSAAVPKDEGADIAGTEEVVIPKKKTWDKVAVLQALASTVHRDTTAAPYAFQDDPYLIPTSSVESHSFLLAKKSGENAAKFIINSYPKYFQKDIAEPHIPCLMPEYFEPQIEEISEAALQERIKLKKVKASVDIFDQLLQAGTTVSLETTNSLLDLLCYYGNQEPSTNYNFQQHEQTEELEEAEEGDNMKSKKKAGHQLGVTWRARNHAERIFALMPEKNAHSYCTMIRGMVKHRAHTQALSMYTELLNNRLRADVHTFNSLIEATALVVNAKFEEKWNNILDLLKQMVAQNVKPNLQTFNTILKCLRRFYAFGKLPALQTFREMKAIGIEPSLATYHHIIQLFYQHESPSKGSSLIIYDIMDEITGKTFSPKDPDDDMFFQSAMRVCSSLRDLELAYQVHGLLNTGDNRKFIGPDPRRNFYYSKFFSLLCLMEQIDVTLKWYKDLIPSVFFPHSQTLIDLLQALDVANRLEMIPQIWKDSKEYGHTFRSDLKEEILMLMARDQHPPELQAAFADCAADIKSTYESQDARQTASEWPANSLNYIAILFLRAGRTQEAWKMLGLFRKHNKIPRNELLNEFMDSAKASSSPAQAVEVVKLANSFSLPICEGLTQRLTADFTLSQEQKEALGDLTALTSDSESDSDSDTSKDK
Protein: Chitin elicitor-binding protein (CEBiP) (OsCEBiP) (Lysin motif-containing protein 1) (Os-LYP1) (Q8H8C7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Chitin elicitor-binding protein involved in the perception and transduction of chitin oligosaccharide elicitor signal for defense responses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16829581}; Single-pass membrane protein {ECO:0000269|PubMed:16829581}.
Interaction partners:
- Chitin elicitor receptor kinase 1
- Receptor-like cytoplasmic kinase 185
Sequence:
MASLTAALATPAAAALLLLVLLAAPASAANFTCAVASGTTCKSAILYTSPNATTYGNLVARFNTTTLPDLLGANGLPDGTLSSAPVAANSTVKIPFRCRCNGDVGQSDRLPIYVVQPQDGLDAIARNVFNAFVTYQEIAAANNIPDPNKINVSQTLWIPLPCSCDKEEGSNVMHLAYSVGKGENTSAIAAKYGVTESTLLTRNKIDDPTKLQMGQILDVPLPVCRSSISDTSADHNLMLLPDGTYGFTAGNCIRCSCSSTTYQLNCTAVQNKGCPSVPLCNGTLKLGETNGTGCGSTTCAYSGYSNSSSLIIQTSLATNQTTACQRGGSGRSQFARSMWSMSVISFHMVLIIICFL
Protein: Non-specific serine/threonine protein kinase (H2KYA7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPVGNSGSRSGRLARISQSNIRPFGSNGGGATNSYGPGTHPMSGAEPCSPTKKEKHRFEITKKLGSGTYGKVSLAYDHKFDREVAVKLIKKSAIESKADLVRIRREIRIMSALNHPNIIQIYEVFENKDKIILVMEYSSGGELYDYVSRCGSLPEAEARRIFRQITSAVLYCHKHRVAHRDLKLENILLDQNNNAKIADFGLSNYFADKNLLTTFCGSPLYASPEIINGTPYKGPEVDCWSLGILLYTLVYGSMPFDGRDFNRMVRQIKRGAYFEPETPSTASMLIRNMLRVNPERRATIFDIASHWWLNLEENMPVIQELPENQIIDHTPLTEREETMIVQDLADEQDVFMEFGHLSSETRRKIEDFRIRRKEAEEFNDNSPVKPPKARKTDELTGKISKEQPEEMKSAEKSLRGVKEEKEKPKVVDPNDPLERLRQIENRLGQNKKDKEAAKTSARVETVKLKEVKKEKSPEQQPEDPKTARGTSKPADSRAPSFVPVKDRPETSEPERPRTRPHLTASAYRIETDSLNMLMNQVLEQMEKGPVNLNIIARIKAHPLYDTRPMVKELLESIIAAQPEPVQKQTSKVVEQQTFSRQNTLTRKKKEDPLEEEIPEVPSPSRKMKERPWHSVEVGFDPDEEPEHDRMQESIASNATEVTVQDTSFEDDSSDEEERKKTPVASTPKTPVLIVEKQESSTNAEDEESDEGDDYSDAEMEELADEVDKKGPSDSKLAPVVENLEANPPPDPSSSPQFLDAFDRGLIKRQSKGKYQAKEILQTYPNNKLDARGIDVELRRKLRMEKVKADLLKQPKDGDKPRNSYVGSVPPRSPPPIVVKSDGEELDDEEEEEEDEEEIEETDSEEGSDFENFKPKRPIIAAVRRDDGAVVPVIHQTTRPAVVSPNSQNPRYQVASPKTSTVIQATPEKVPVAGTSAKYLVTVAELKLKPTDKKEEAQLKEQLKDSEINSERKVTKGAAPSTISQDSDGKDTFESASAYIRRKNRERRQRNRTIGTAEEALRALERPSVDPYDDRAFSPLSTDPFYSHHSSGSAAPSALGYVRPRYHDDSYRTHRDSDYRPMSPTSRYTAAVTRDDRGKSTSYDPHETTRPSYDRGYITSSNASPSYTRKFEHEQPTLNSWANDRKFEVYKTRAERDAERNTYHPTGTTGASSYRPSSYYTSASDRPVTGLRRPEESYTSSTNYGRYDGRSTTPSNDQYAISTALAENQASSMNNRFRPTARRVASAMTDADRRNYHRSRSMDRNKVDYEYGSNLLNRLTTPDSHGDYSYVNYHDSSNGRSNITLEKDGQPRSILKNKQSADIEPRVESSYEPSNGVRSVASVGPHSRNIDSTSSALDNPKKKRSLLSFNRRKTSEVRMGADGKLVTNGYDSTPSSRDFKRPSSPIDRIKSLFRKNESSGTGHSDYYNSSRNYTSSNPVSTTREPYVAQYRKYPGSTSRDTSSALNRYSYTPGLTDQRRHWYDDPNIY
Protein: Pupal cuticle protein Edg-91 (Ecdysone-dependent protein 91) (P27781)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the pupal cuticle.
Interaction partners:
Sequence:
MALVRVSCMLALLLIAGQGQAAPVKTEGSTLGLLGGGFGGSVGLSAGIGVGGGLYSGFGGGGYPGGYASGYPGGYGGGYSGYNGYGGSGFGGGYYPGGGYSGFGHRPHHHGGYYPGGGSYHNQGGSYGGHYSQSQYSNGYYGGGGYGGGGYGGNGFFGK
Protein: Neuroendocrine protein 7B2 (Secretogranin V) (Secretogranin-5) (Secretory granule endocrine protein I) [Cleaved into: N-terminal peptide; C-terminal peptide] (P01165)
Organism: Sus scrofa (Pig)
Function: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:6514132}. Note=Neuroendocrine and endocrine secretory granules. {ECO:0000269|PubMed:6514132}.
Interaction partners:
- Rho GTPase activating protein 11A.
- Neuroendocrine convertase 2
- Proprotein convertase subtilisin/kexin type 7.
- Secretogranin-2
- Secretogranin-1
- Proprotein convertase subtilisin/kexin type 4
- Membrane-bound transcription factor site-1 protease
Sequence:
MVSTMLSGLVLWLTFGWTPALAYSPRTPDRVSETDIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNTPKDFSEDQGYPDPPNPCPIGKTDDGCLENTPDTAEFSREFQLHQHLFDPEHDYPGLGKWNKKLLYEKMKGGQRRKRRSVNPYLQGQRLDNVVAKKSVPHFSDEDKDPE
Protein: Acireductone dioxygenase 4 (Acireductone dioxygenase (Fe(2+)-requiring) 4) (ARD' 4) (Fe-ARD 4) (EC 1.13.11.54) (Acireductone dioxygenase (Ni(2+)-requiring) 4) (ARD 4) (Ni-ARD 4) (EC 1.13.11.53) (Q8H185)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03154}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03154}.
Interaction partners:
- Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
- At1g77670
- Aromatic aminotransferase ISS1
- Acireductone dioxygenase 2-requiring) 2)
- Acireductone dioxygenase 3-requiring) 3)
- Acireductone dioxygenase 1-requiring) 1)
- DNA ligase-like protein
- Tyrosine aminotransferase
- Probable aminotransferase TAT2
- Thioredoxin superfamily protein
Sequence:
MALEAWFMDDSNEDQRLPHHRNPKELVSLDYLAELGVLYWKLNPENYENDSELSKIREDRGYDYMDLLDLCPEKVSNYEEKLKNFFTEHIHKDEEIRYCLAGSGYFDVRDKDDRWIRIWMQPGDLIVLPAGIYHRFTLDASNYIKLMRLFVGEPVWTPYNRPQEEHPVRKKYIHGLTYKFGETVKAH
Protein: Transmembrane protease serine 11E (EC 3.4.21.-) (Serine protease DESC1) [Cleaved into: Transmembrane protease serine 11E non-catalytic chain; Transmembrane protease serine 11E catalytic chain] (Q5S248)
Organism: Mus musculus (Mouse)
Function: Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15328353}; Single-pass type II membrane protein {ECO:0000269|PubMed:15328353}.; SUBCELLULAR LOCATION: [Transmembrane protease serine 11E catalytic chain]: Secreted {ECO:0000269|PubMed:15328353}. Note=Activated by cleavage and secreted. {ECO:0000269|PubMed:15328353}.
Interaction partners:
- Kunitz-type protease inhibitor 2
Sequence:
MYRSCVVRARKRTCVEPWVIGIISFLSLIVLAVCIGLTVHYVRYNHRRTYNYYSTLSFTSDKLYSEFGREASKNFTEMSQRIETMVKHAFHKSPLRGQLVKAHIIKFSKEDDGVLAHMLLIFRIRSTEDPETVHKIIEYVLHEKLKYATGPPNVDPESVKIKKINKTESDNYFNHCCGTRRNKSTVQTSVRIVGGTPVEEEEWPWQSSLRWDGSHRCGATLINNTWLVTAAHCFRTHKDPSRWSATFGATLQPRKLTTGIRRIIVHEKYKYPSHDYDIALAELSKPVPCTNAVHKVCLPDANHEFQPGQRMFVTGFGALKNDGFTQNNLRQVQVDYIDTQTCNQPQSYNGAITPRMLCAGFLKGEKDACQGDSGGPLVTADVRDIWYLAGVVSWGDECGQPNKPGVYTRVTAFRHWIASNTGI
Protein: LysM domain-containing GPI-anchored protein 3 (Q6NPN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required as a cell surface receptor for peptidoglycan (PGN) elicitor signaling leading to innate immunity. Plays an essential role in detecting PGNs and restricting bacterial growth (of Pseudomonas syringae pv. tomato DC3000 for example).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Chitin elicitor receptor kinase 1
- Protein LYK5
- LysM domain receptor-like kinase 3
- LRR receptor-like serine/threonine-protein kinase EFR
- Protein LYK2
- Leucine-rich repeat receptor-like protein kinase PEPR1
- Receptor like protein 23
- Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Receptor-like protein 30
Sequence:
MKNPEKPLLLFLILASSLASMATAKSTIEPCSSKDTCNSLLGYTLYTDLKVTEVASLFQVDPVSMLLSNSIDISYPDVENHVLPAKLFLKIPITCSCVDGIRKSLSTHYKTRTSDTLGSIADSVYGGLVSPEQIQVANSETDLSVLDVGTKLVIPLPCACFNGTDESLPALYLSYVVRGIDTMAGIAKRFSTSVTDLTNVNAMGAPDINPGDILAVPLLACSSNFPKYATDYGLIIPNGSYALTAGHCVQCSCVLGSRSMYCEPASISVSCSSMRCRNSNFMLGNITSQQSSSGCKLTTCSYNGFASGTILTTLSMSLQPRCPGPQQLAPLIAPPDNVPKELMYLPSPSPSPSPEFDDIAGGGSSIAAVPAASPGGATVSSSNSIPGNPANGPGGSISIASCPLSYYSFIALLIPIGSCFFVF
Protein: cDNA: FLJ22332 fis, clone HRC05753 (Q9H6F0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQEEPLPQGNDPEPSGDSPLGLCQSECMEMSEVFDDASDQDSTDKPWRPYYNYKPKKKSRQLKKMRKVNWRKEHGNRSPSHKCKYPAELDCAVGKAPQDKPFEEEETKEMPKLQCELCDGDKAVGAGNQGRPHRHLTSRPYACELCAKQFQSPSTLKMHMRCHTGEKPYQCKTCGRCFSVQGNLQKHERIHLGLKEFVCQYCNKAFTLNETLKIHERIHTGEKRYHCQFCFQRFLYLSTKRNHEQRHIREHNGKGYACFQCPKICKTAAALGMHQKKHLFKSPSQQEKIGDVCHENSNPLENQHFIGSEDNDQKDNIQTGVENVVL
Protein: Retinol-binding protein 4 (Plasma retinol-binding protein) (PRBP) (RBP) (P18902)
Organism: Bos taurus (Bovine)
Function: Retinol-binding protein that mediates retinol transport in blood plasma. Delivers retinol from the liver stores to the peripheral tissues. Transfers the bound all-trans retinol to STRA6, that then facilitates retinol transport across the cell membrane.
Subcellular location: Secreted {ECO:0000269|PubMed:12787682, ECO:0000269|PubMed:2209607, ECO:0000269|PubMed:8496140}.
Interaction partners:
- Transthyretin
- Receptor for retinol uptake STRA6
- Retinol-binding protein 1
- Vitamin D-binding protein
- Albumin
- Haptoglobin
Sequence:
ERDCRVSSFRVKENFDKARFAGTWYAMAKKDPEGLFLQDNIVAEFSVDENGHMSATAKGRVRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIIDTDYETFAVQYSCRLLNLDGTCADSYSFVFARDPSGFSPEVQKIVRQRQEELCLARQYRLIPHNGYCDGKSERNIL
Protein: Transcription factor VBP (Thyrotroph embryonic factor homolog) (Vitellogenin gene-binding protein) (Q92172)
Organism: Gallus gallus (Chicken)
Function: Transcription factor that binds to and transactivates the vitellogenin II (VTG2) promoter. Binds to the palindromic sequence 5'-GTTTACATAAAC-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Uncharacterized protein.
- Period circadian clock 3
Sequence:
MPGRAAHQEAAAAGGAAAEPTAAGGSAGAVAQQPEQQGLAGAFPLVLKKLMENPPRDARLDKEKKIKLEEDEAAAASTMAVSASLMPPIWDKTIPYDGESFHLEYMDLDEFLLENGIPSSPTHLDLNQNPLMPVAKLEEKEPASASTGSPVSSSSTAVYQQSEAASSTESPPQNERNTPSPIDPDCVEVEVNFNPDPADLVLSSVPGGELFNPRKHKFTEEDLKPQPMIKKAKKVFVPDEQKDEKYWTRRKKNNVAAKRSRDARRLKENQITIRAAFLEKENTALRTEVAELRKEVGRCKNIVSKYETRYGPFDLSDSE
Protein: Alpha/beta-Hydrolases superfamily protein (Putative phospholipase; alternative splicing isoform) (O80628)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
Sequence:
MAIETEDIKYEESFIKNTRGFKLFTCRWLPTNREPRALVFLCHGYGMECSITMNSTARRLVKAGFAVYGMDYEGHGKSDGLSAYISNFDRLVDDVSTHYTAICEREENKWKMRFMLGESMGGAVVLLLGRKNPDFWDGAILVAPMCKIAEEMKPSPFVISILTKLISIIPKWKIIPSQDIIEISYKEPEIRKQVRENPLCSKGRPRLKTAYELLRISNDLEKRLQEVSLPFLVLHGDDDKVTDKAVSQELYKVALSADKTLKLYPGMWHGLLTGETPENIEIVFADVISWLEKRSDYGNDRFESELKQRNDRLNFKK
Protein: E3 ubiquitin-protein ligase ATL4 (EC 2.3.2.27) (Protein ARABIDOPSIS TOXICOS EN LEVADURA 4) (Protein ATL4) (RING-H2 finger X1a) (RING-H2 zinc finger protein ATL4) (RING-H2 zinc finger protein RHX1a) (RING-type E3 ubiquitin transferase ATL4) (Q9LY41)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase able to catalyze polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable LRR receptor-like serine/threonine-protein kinase At1g29720
- Transcription factor LHW
- Squamosa promoter-binding-like protein 1
- ATP sulfurylase 1, chloroplastic
Sequence:
MESLINPSHGGGNYDSHSSSLDSLKPSVLVIILILLMTLLISVSICFLLRCLNRCSHRSVLPLSSSSSVATVTSDSRRFSGHRVSPETERSSVLDSLPIFKFSSVTRRSSSMNSGDCAVCLSKFEPEDQLRLLPLCCHAFHADCIDIWLVSNQTCPLCRSPLFASESDLMKSLAVVGSNNGGGENSFRLEIGSISRRRQTPIPESVEQHRTYSIGSFDYIVDDVDSEISESNFNRGKQEDATTTTATATAVTTNPTSFEASLAADIGNDGSRSWLKDYVDRLSRGISSRAMSFRSSGRFFTGSSRRSEELTVMDLEANHAGEEISELFRWLSGV
Protein: Anaerobic glycerol-3-phosphate dehydrogenase subunit B (Anaerobic G-3-P dehydrogenase subunit B) (Anaerobic G3Pdhase B) (EC 1.1.5.3) (P13033)
Organism: Escherichia coli (strain K12)
Function: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.
Subcellular location: Cell inner membrane; Peripheral membrane protein. Note=Loosely bound to the cytoplasmic membrane often occurring in vesicles associated with fumarate reductase.
Interaction partners:
- Anaerobic glycerol-3-phosphate dehydrogenase subunit C
- Anaerobic glycerol-3-phosphate dehydrogenase subunit A
- Aerobic glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate transporter
- Glycerophosphodiester phosphodiesterase, periplasmic
- Glycerol-3-phosphate dehydrogenase [NAD
- Probable glycerol-3-phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase
- Glycerol kinase
- PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM
Sequence:
MRFDTVIMGGGLAGLLCGLQLQKHGLRCAIVTRGQSALHFSSGSLDLLSHLPDGQPVTDIHSGLESLRQQAPAHPYSLLEPQRVLDLACQAQALIAESGAQLQGSVELAHQRVTPLGTLRSTWLSSPEVPVWPLPAKKICVVGISGLMDFQAHLAAASLRELGLAVETAEIELPELDVLRNNATEFRAVNIARFLDNEENWPLLLDALIPVANTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVLGIRLQNQLQRQFVRQGGVWMPGDEVKKVTCKNGVVNEIWTRNHADIPLRPRFAVLASGSFFSGGLVAERNGIREPILGLDVLQTATRGEWYKGDFFAPQPWQQFGVTTDETLRPSQAGQTIENLFAIGSVLGGFDPIAQGCGGGVCAVSALHAAQQIAQRAGGQQ
Protein: Protocadherin related 15 (A0A8I6A7Z6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MSPQFALWKCMPHGILLASLLIVSWGQYDDDCKLARGGPPATIVAIDEESRNGTILVDNMLIKGTAGGPDPTIELSLKDNVDYWVLLDPVKQMLFLNSTGRVLDRDPPMNIHSIVVQVQCVNKKVGTVIYHEVRIVVRDRNDNSPTFKHESYYATVNELTPVGTTIFTGFAGDNGATDIDDGPNGQIEYVIQYNPEDPDRAQNLNERRTTTTTLTVDVLDGDDLGPMFLPCVLVPNTRDCRPLTYQAAIPELRTPEELNPILVTPPIQAIDQDRNIQPPSDRPGILYSILVGTPEDYPRFLHMHPRTAELTLLEPVNRDFHQKFDLVIKAEQDNGHPLPAFASLHIEILDENNQSPYFTMPSYQGYILESAPVGATISESLNLTTPLRIVALDKDIEDTKDPELHLFLNDYTSVFTVTPTGITRYLTLLQPVDREEQQTYTFLITAFDGVQESEPVVVNIRVMDANDNTPTFPEISYNVYVYTDMSPGDSVIQLTAVDADEGSNGEISYEILVGSKGDFVINRTTGLVSIAPGVELVVGQTYALTVQASDNAPPAERRHSICTVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAVLLNLQATDREGDPITYAIENGDPQRVFNLSETTGILSLGKALDRESTDRYILIVTASDGRPDGTSTATVNIVVTDVNDNAPVFDPYLPRNLSVVEEEANAFVGQVRATDPDAGINGQVHYSLGNFNNLFRITSNGSIYTAVKLNREARDHYELVVVATDGAVHPRHSTLTLYIKVLDIDDNSPVFTNSTYTVVVEENLPAGTAFLQIEAKDVDLGANVSYRIRSPEVKHLFALHPFTGELSLLRSLDYEAFPDQEASITFLVEAFDIYGTMPPGIATVTVIVKDMNDYPPVFSKRIYKGMVAPDAVKGTPITTVYAEDADPPGLPASRVRYRVDDVQFPYPASIFDVEEDSGRVITRVNLNEEPTTIFKLVVVAFDDGEPVMSSSATVRILVLHPGEIPRFTQEEYRPPPVSELAARGTVVGVISAAAINQSIVYSIVAGNEDDKFGINNVTGVIYVNSPLDYETRTSYVLRVQADSLEVVLANLRVPSKSNTAKVYIEIQDENDHPPVFQKKFYIGGVSEDARMFTSVLRVKATDRDTGNYSAMAYRLIIPPIKEGKEGFVVETYTGLIKTAMLFHNMRRSYFKFQVIATDDYGKGLSGKADVLVSVVNQLDMQVIVSNVPPTLVEKKIEDLTEILDRYVQEQIPGAKVVVESIGARRHGDAFSLEDYSKCDLTVYAIDPQTNRAIDRNELFKFLDGKLLDINKDFQPYYGEGGRILEIRTPEAVTSIKKRGESLGYTEGALLALAFIIILCCIPAILVVLVSYRQRQAECTKTARIQSAMPAAKPAAPVPAAPPPPPPPPPPGAHLYEELGESAILFLLYHFEQSRGNNPVPEDRSSHRDGMAFSSSTTESHEPAHVEGPLDNQANPARTFSFLPDEDDLSTHNPLYMESIGQRSTNSDLQPGTEFGELFVPRTQVKSQSLRGPREKIQRVWNQSVRFPRRLMWKTPNRPETIDLVEWQITRQRAECEKTRCHPSQQGSSNLMVTTEDARGSEKEGGHRDTLIVQQTEQLKSLSSGSSFSSSWSHFSFSTLPTISRAVELGSEPDVVTSPADCTLELSPPRRPRVLNSLGSKRETPTCASDTETKRNSFEMVPHPPSISAPLPQLPLPQPPIAFTTFPLPLSSPNPPRPQLLTFSLPISTTPASSLPPPPPPSLPPPPRPPAPRLFPLPPSTSVPSTDSISTPAAKCTASVTHARETMSTTQPPASNPPCGAEPHRHPKGILRHVKNLAELEKSVSNMYSHIEKNCPPTELSKLHPFCPAEKTNMKITCDQSQETLVRVVEGIDVQTHSQSTSL
Protein: Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (NMN/NaMN adenylyltransferase 3) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide-nucleotide adenylyltransferase 3) (NMN adenylyltransferase 3) (Nicotinate-nucleotide adenylyltransferase 3) (NaMN adenylyltransferase 3) (Q99JR6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD(+), NADH, NaAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (By similarity). Protects against axonal degeneration following injury.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16914673}.
Interaction partners:
- Nicotinate phosphoribosyltransferase
- Nicotinamide phosphoribosyltransferase
- Nicotinamide riboside kinase 1
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- NAD kinase
- Glutamine-dependent NAD
- Nicotinamide riboside kinase 2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- NAD kinase 2, mitochondrial
Sequence:
MKNRIPVVLLACGSFNPITNMHLRLFEVARDHLHQTGRYQVIEGIISPVNDSYGKKDLVASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHRELLRSSAQMDGPDPSKTPSASAALPELKLLCGADVLKTFQTPNLWKDTHIQEIVEKFGLVCVSRSGHDPERYISDSPILQQFQHNIHLAREPVLNEISATYVRKALGQGQSVKYLLPEAVITYIRDQGLYINDGSWKGKGKTG
Protein: Basement membrane proteoglycan (H9G351)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKRSSTVLAALLALLLVATNDAARHRKYRQTYQDIDSDDDDTSDVQITVFPSEKEVRDGRDVSFECRARTSDNSVYPTVRWARVGGPLPSSAHDSGGRLTINPVQLSDAGTYICVSDYNGNTVEARATLSVVSYGPQEVSNGLRQAGQCMADEKACGNNECVKNDYVCDGEPDCRDRSDEANCPAISRTCEPNEFKCNNNKCVQKMWLCDGDDDCGDNSDELNCNAKPSSSDCKPTEFQCHDRRQCVPSSFHCDGTNDCHDGSDEVGCVQPTVVDPPQTNLQVPRGTTFSLTCKAVAVPEPYINWRLNWGPVCEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINVKGRVLATPDCIVRVVDDPRPQPPQPPTAPPQRASCDTRGAVTPYPNNYGTCECKSQVTGPNCDQCKPGAFHLSEKSPEGCLKCFCFGVSNDCRSSGHYRTKDRLMFAGDAEGVTISDIEERTIDRNTPFSFFKTGYLTFDGTTDGVAKYWRLPQRFLGDKVTAYGGKMEFEIEFSGSGHHSSEPMVVLKGNQNILVHRVRNQEHVLRSDSPVRITVETYETNYEQLNGAAATREDLLMVLADLDAFLIRATHVAHQTSTSLGDVSWEIAVDRYTPDGLALEVEQCVCPPGYLGTSCEDCAPGYERSGYGPYLGTCVPIQPRHQQCGPGAVAPTAPAQGQCQCKASVIGPNCDRCAPNSFGLAPTNPQGCIPCFCSGVTQQCSASSYRRTSVSIDYARGDRDQLELTTSDSRQPYSPQTRAELSGQAIEFRSFEEARGQTLYWKLPEKFLGDKVTSYGGTLEYTFKFSGNGNSDQSADVILRGNDIALQYKHREPFYADRENKVQIKIIETSWQRVDGQQATREHLLMTLADLDTLLIKSTYNDDCTDSQLLSANLEFAEPYGQGLTAAEVEQCICPPGYVGTSCEDCAPGYSRTGGGLYLGLCEKCECNGHASQCDKEYGYCLDCQHNTEGDQCERCKPGFVGDARRGTPNDCQPEATRAPCHCNNHSPRGCDSFGRCLLCEHNTEGTHCERCKKGYYGDATKGSPYDCTPCPCPGASDCYLDNEGQVACRICPAGLQGRLCNECAPGYTRSNKPAGRVCEPIGQVTNEDITFVQKPHEAVIPPKVDPIRQTVDRDQPARFKCWVPGNSNVQLRWSRPGGAPLPSGVQEQQGILHIPRASDQEVGQYVCTATDPSDNTPLQSEPVQLNIRDPAPPQRGAAPQIDPPNQTVNVNDPAQFRCWVPGQPRAQLKWSRKDGRPLPNGILERDGFLRIDKSQLHDAGEYECTSTEPDGSTQLSPPARLNVNQPQAIQPQVDPPVQTVNEGEPSRIRCWVPGHPNIQLQFVKRGRRPLPAHARFSQGNLEIPRTLKSDEDEYICIATDPTTNRPVESNPARVIVKSPIRPIIDPAEQTVPEGSPFKIRCYVPGHPSVQLTFRRVSGQLNEDADENNGLLAVQRAELTDEGDYICTARDPDTGAPIDSTPATVHVTNAAAPPQVEARPPQHPVITPQTQTIPEGDPARIQCTVPGNPSAAQHLSFERVDGKGLPFGSSDDRGVLTIPSTQLQDAGEYVCLYSPENSPPVKTNPSTLNVTPEGTPPRPVATPPLLSVAPGSPARFNCVAHSDTPARIRWGFREENGPLPEHVNQDGDDIVISEAGDRNVGEYVCSATNDFGTGVADPVRLEVTEDQEPPTAVVEPRTWNGKPGERHQFRCITTGSPTPKITWTGPNGSPLPHDVTPLEPNILDFSNGRSELNGDYTCTASNPIGEASDHGNVNIGPSLTVKTNPPGPKLIVTVGEPLQVKCEAFGAPGDPEPEVEWLHDPGPERGDLPDDFKPVTISEQFIRHPNVGLGNAGVYTCKGSSAHATATKNIYIEVVEPSRIATVSILGGSSQWFDQGEKGELICTATGSSLVDRLEWEKVDDQLPTDVEEHNEPGLLHFPSFKNSYAGEYRCNGYRNNEIIASAAVHVHSSANADDEPKVEIEPPRVRVVSQGDNIVLKCSVQGAENGEHFKWALLRGGSLVRQLGTEPTLEITKADPSNDFGVYRCNVEDNNGLVIGSAFTAVSVGQQDKSHAQIVKFDDKSDASFTCPIYSVPGSKVDWTYENGDLPSKAVPNGNKIEIKEFDDASAGTYVCKVSFDGNVVEGFVTAQMFVPDTIIQVLLEVSSESPQIGDRAWFDCKVTGDPSAVISWTKEGNDDLPPNAQVTGGRLLFTDLKEDNAGVYRCVAKTKAGPLQTRTVLNVGSGKRKRKHLGNRRGRRLRHRRRNAQNGPLSRKTRTTTKLFGSWF
Protein: Acyl-homoserine-lactone synthase (EC 2.3.1.184) (Autoinducer synthesis protein VanI) (P74945)
Organism: Vibrio anguillarum (Listonella anguillarum)
Function: Required for the synthesis of N-(3-oxodecanoyl)-L-homoserine lactone (ODHL), an autoinducer molecule which binds to VanR.
Interaction partners:
- Transcriptional activator protein VanR
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
- Methionine adenosyltransferase
Sequence:
MTISIYSHTFQSVPQADYVSLLKLRYKVFSQRLQWELKTNRGMETDEYDVPEAHYLYAKEEQGHLVGCWRILPTTSRYMLKDTFSELLGVQQAPKAKEIYELSRFAVDKDHSAQLGGVSNVTLQMFQSLYHHAQQYHINAYVTVTSASVEKLIKRMGIPCERLGDKKVHLLGSTRSVALHIPMNEAYRASVNA