wanglab/gogpt-training-data huggingface dataset:
Protein: RAR related orphan receptor A (RAR-related orphan receptor A, isoform CRA_c) (A0A0C4DFP5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MNEGAPGDSDLETEARVPWSIMGHCLRTGQARMSATPTPAGEGARSSSTCSSLSRLFWSQLEHINWDGATAKNFINLREFFSFLLPALRKAQIEIIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQSNATYSCPRQKNCLIDRTSRNRCQHCRLQKCLAVGMSRDAVKFGRMSKKQRDSLYAEVQKHRMQQQQRDHQQQPGEAEPLTPTYNISANGLTELHDDLSNYIDGHTPEGSKADSAVSSFYLDIQPSPDQSGLDINGIKPEPICDYTPASGFFPYCSFTNGETSPTVSMAELEHLAQNISKSHLETCQYLREELQQITWQTFLQEEIENYQNKQREVMWQLCAIKITEAIQYVVEFAKRIDGFMELCQNDQIVLLKAGSLEVVFIRMCRAFDSQNNTVYFDGKYASPDVFKSLGCEDFISFVFEFGKSLCSMHLTEDEIALFSAFVLMSADRSWLQEKVKIEKLQQKIQLALQHVLQKNHREDGILTKLICKVSTLRALCGRHTEKLMAFKAIYPDIVRLHFPPLYKELFTSEFEPAMQIDG
Protein: Serine hydroxymethyltransferase (EC 2.1.2.1) (Q6TXG7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Methylenetetrahydrofolate reductase
- Methylenetetrahydrofolate dehydrogenase
- Bifunctional purine biosynthesis protein ATIC
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- Dihydrofolate reductase
- Thymidylate synthase
- Phosphoserine phosphatase
- Sarcosine dehydrogenase, mitochondrial
Sequence:
MELTVEAWVQIFLLPVEKSDPVSRLDPDRMGHVKGPVQMIQNCRISTTQGNNRITQRSPGYTPDSPTKSFSLWNSQNLLVQSMKLAASAVSIWFWGSWRIPRELLVFSLHWNLKEVGLSTSPSNSTNLPARVKGKQAEKQSFLLLSSFIWVAIRSYSSFCQVLPKFLLRARANGAWAAEGGLYLDPPTDWAALGVGRGQPRCAMAERDATVWASHEKMLTQPLKESDAEVYSIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYHLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVYPDTGYINYDQLEENASLFHPKLIIAGTSCYSRNLDYARLRKIADDNGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVRSVDPKTGEETYYELESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTTEFKIYQLQVLANCRALSDALTELGYKIVTGGSDNHLILMDLRPKGTDGGRAEKVLEACSIACNKNTCPGDKSALRPSGLRLGTPALTSRGLLEEDFQKIAHFIHRGIELTLQIQSHMTMRATLKEFKEKLTGDEKFQSAVAALREEVENFASNFSLPGLPDF
Protein: Ankyrin repeat and KH domain containing 1 (A0A0A0MQZ8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDVNSSKYPSLLLHSQEEKTSTATSKTQTRLEGEVTPNSLSTSYKTVSLPLSSPNIKLNLTSPKRGQKREEGWKEVVRRSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIPKNHIRTPASTKSIHANFSSGVGTTAASSKNAFPLGAPTLVTSQATTLSTFQPANKLNKNVPTNVRSSFPVSLPLAYPHPHFALLAAQTMQQIRHPRLPMAQFGGTFSPSPNTWGPFPVRPVNPGNTNSSPKHNNTSRLPNQNGTVLPSESAGLATASCPITVSSVVAASQQLCVTNTRTPSSVRKQLFACVPKTSPPATVISSVTSTCSSLPSVSSAPITSGQAPTTFLPASTSQAQLSSQKMESFSAVPPTKEKVSTQDQPMANLCTPSSTANSCSSSASNTPGAPETHPSSSPTPTSSNTQEEAQPSSVSDLSPMSMPFASNSEPAPLTLTSPRMVAADNQDTSNLPQLAVPAPRVSHRMQPRGSFYSMVPNATIHQDPQSIFVTNPVTLTPPQGPPAAVQLSSAVNIMNGSQMHINPANKSLPPTFGPATLFNHFSSLFDSSQVPANQGWGDGPLSSRVATDASFTVQSAFLGNSVLGHLENMHPDNSKAPGFRPPSQRVSTSPVATSAPPTLGQPKGVSASQDRKIPPPIGTERLARIRQGGSVAQAPAGTSFVAPVGHSGIWSFGVNAVSEGLSGWSQSVMGNHPMHQQLSDPSTFSQHQPMERDDSGMVAPSNIFHQPMASGFVDFSKGLPISMYGGTIIPSHPQLADVPGGPLFNGLHNPDPAWNPMIKVIQNSTECTDAQQIWPGTWAPHIGNMHLKYVN
Protein: Xylosyl- and glucuronyltransferase LARGE1 (EC 2.4.-.-) (Acetylglucosaminyltransferase-like 1A) (Glycosyltransferase-like protein) (LARGE xylosyl- and glucuronyltransferase 1) [Includes: Alpha-1,3-xylosyltransferase LARGE1 (EC 2.4.2.-); Beta-1,3-glucuronyltransferase LARGE1 (EC 2.4.1.-)] (O95461)
Organism: Homo sapiens (Human)
Function: Bifunctional glycosyltransferase with both alpha-1,3-xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the maturation of alpha-dystroglycan (DAG1) by glycosylation leading to DAG1 binding to laminin G-like domain-containing extracellular proteins with high affinity. Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated by B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide. Requires the phosphorylation of core M3 (O-mannosyl trisaccharide) by POMK to elongate the glucuronyl-beta-1,4-xylose-beta disaccharide primer. Plays a key role in skeletal muscle function and regeneration (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15661757, ECO:0000269|PubMed:15958417, ECO:0000269|PubMed:25279699}; Single-pass type II membrane protein {ECO:0000269|PubMed:15661757, ECO:0000269|PubMed:15958417}.
Interaction partners:
- Beta-1,4-glucuronyltransferase 1
- Ribitol-5-phosphate transferase FKTN
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Xylosyl- and glucuronyltransferase LARGE2
- Dystroglycan 1
- Protein O-mannosyl-transferase 1
- Ribitol 5-phosphate transferase FKRP
- Protein O-mannosyl-transferase 2
- Ribitol-5-phosphate xylosyltransferase 1
- Protein O-mannose kinase
Sequence:
MLGICRGRRKFLAASLSLLCIPAITWIYLFSGSFEDGKPVSLSPLESQAHSPRYTASSQRERESLEVRMREVEEENRALRRQLSLAQGRAPSHRRGNHSKTYSMEEGTGDSENLRAGIVAGNSSECGQQPVVEKCETIHVAIVCAGYNASRDVVTLVKSVLFHRRNPLHFHLIADSIAEQILATLFQTWMVPAVRVDFYNADELKSEVSWIPNKHYSGIYGLMKLVLTKTLPANLERVIVLDTDITFATDIAELWAVFHKFKGQQVLGLVENQSDWYLGNLWKNHRPWPALGRGYNTGVILLLLDKLRKMKWEQMWRLTAERELMGMLSTSLADQDIFNAVIKQNPFLVYQLPCFWNVQLSDHTRSEQCYRDVSDLKVIHWNSPKKLRVKNKHVEFFRNLYLTFLEYDGNLLRRELFGCPSEADVNSENLQKQLSELDEDDLCYEFRRERFTVHRTHLYFLHYEYEPAADSTDVTLVAQLSMDRLQMLEAICKHWEGPISLALYLSDAEAQQFLRYAQGSEVLMSRHNVGYHIVYKEGQFYPVNLLRNVAMKHISTPYMFLSDIDFLPMYGLYEYLRKSVIQLDLANTKKAMIVPAFETLRYRLSFPKSKAELLSMLDMGTLFTFRYHVWTKGHAPTNFAKWRTATTPYRVEWEADFEPYVVVRRDCPEYDRRFVGFGWNKVAHIMELDVQEYEFIVLPNAYMIHMPHAPSFDITKFRSNKQYRICLKTLKEEFQQDMSRRYGFAALKYLTAENNS
Protein: Fem-3 mRNA-binding factor 2 (Q09312)
Organism: Caenorhabditis elegans
Function: Involved in the control of stem cells and sex determination in the C.elegans hermaphrodite germline. May also play a role in the hermaphrodite germline proliferation and oogenesis. By binding to the 3'-UTR, represses phosphatase lip-1 expression in the distal part of the germline mitotic zone. Binds specifically to the regulatory region of fem-3 3'-UTR and mediates the sperm/oocyte switch. Negatively regulates gld-3 expression possibly by directly binding to two sites within the gld-3 isoform b 3'-UTR. Suppresses germline tumor formation by preventing the dedifferentiation of secondary spermatocytes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9393998}. Cytoplasmic granule {ECO:0000269|PubMed:27864381}. Note=Recruited to P granules by dlc-1. {ECO:0000269|PubMed:27864381}.
Interaction partners:
- Lateral signaling target 1 protein
- Defective in germ line development protein 3
- Nanos-type domain-containing protein
- Sex-determination protein fem-3
- Cytoplasmic polyadenylation element-binding protein 1
- Ecdysone-induced protein 74EF
- Female germline-specific tumor suppressor gld-1
- CCR4-NOT transcription complex subunit 7
- Poly
- FOG-1 protein
Sequence:
MDQSKMRRTNQFRKTSQKPPSTGIDSYPTPAQSPMAQHETPMWDFNSLNPYFSMLNMNDGINYARHQQNHIVTSRPPTPLTDLMSLRSFQSFPNVFMPVSRSRTSSFIQSDTDSSRLESDDFSQNVRCFSADIDRSKSYGSSKHYHLKYSRPALSRNSRSFTRSNNVLPTWSLDSNGEMRSRLSLSEVLDSGDLMKFAVDKTGCQFLEKAVKGSLTSYQKFQLFEQVIGRKDDFLKLSTNIFGNYLVQSVIGISLATNDDGYTKRQEKLKNFISSQMTDMCLDKFACRVIQSSLQNMDLSLACKLVQALPRDARLIAICVDQNANHVIQKVVAVIPLKNWEFIVDFVATPEHLRQICSDKYGCRVVQTIIEKLTADSMNVDLTSAAQNLRERALQRLMTSVTNRCQELATNEYANYIIQHIVSNDDLAVYRECIIEKCLMRNLLSLSQEKFASHVVEKAFLHAPLELLAEMMDEIFDGYIPHPDTGKDALDIMMFHQFGNYVVQCMLTICCDAVSGRRQTKEGGYDHAISFQDWLKKLHSRVTKERHRLSRFSSGKKMIETLANLRSTHPIYELQSSGHDSFKTDYFSTASEHDGPELEKNGIEEGSLMLEPRSNKSSVSVKFSSSGSHGDD
Protein: Riboflavin biosynthesis protein PYRR, chloroplastic [Includes: Inactive diaminohydroxyphosphoribosylaminopyrimidine deaminase (DRAP deaminase) (Riboflavin-specific deaminase); 5-amino-6-(5-phosphoribosylamino)uracil reductase (EC 1.1.1.193) (HTP reductase); Riboflavin biosynthesis intermediates N-glycosidase (EC 3.2.2.-)] (Q9STY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pyrimidine reductase involved in the riboflavin biosynthesis pathway. Has also a non-functional N-terminal deaminase domain that lacks the catalytically essential zinc-binding residues.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:23150645}.
Interaction partners:
- Bifunctional riboflavin biosynthesis protein RIBA 1, chloroplastic
- Monofunctional riboflavin biosynthesis protein RIBA 3
- Monofunctional riboflavin biosynthesis protein RIBA 2
- Riboflavin biosynthesis protein PYRD
- Flavin mononucleotide hydrolase 1, chloroplatic
- tRNA-specific adenosine deaminase TAD3
- 5-amino-6-
- Riboflavin synthase
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MALSFRISSSSPLICRATLSNGDNSRNYHTTDAAFIRRAADLSEMSAGLTSPHPNFGCVIATSSGKVAGEGYLYAQGTKPAEALAVEAAGEFSRGATAYLNMEPGDCHGDHTAVSALVQAGIERVVVGIRHPLQHLRGSAIRELRSHGIEVNVLGEDFESKVLEDARKSCLLVNAPLIHRACSRVPFSVLKYAMTLDGKIAASSGHAAWISSKLSRTRVFELRGGSDAVIVGGNTVRQDDPRLTARHGQGHTPTRIVMTQSLDLPEKANLWDVSEVSTIVVTQRGARKSFQKLLASKGVEVVEFDMLNPREVMEYFHLRGYLSILWECGGTLAASAISSSVIHKVVAFVAPKIIGGSKAPSPVGDLGMVEMTQALNLIDVCYEQVGPDMLVSGFLQPIPDLLPVIPSEDATVEIDPSVDPFEPSIIFFYKTWDLYGMWNITIRYHTTVHVKWYLALSKKHNLLILHPKTLKANKFVGVENPKAYDCVEKIRTARSPEEAALIGRSTLRQKPELVRNDWEDVKIEVMYKALKCKFSTYPHLKSMLLSTIGTVLVEASPHDLFWGGGREGEGLNYLGRLLMQLRSEYLGESSVSAEKTSSA
Protein: Matrix metalloproteinase-B (MMP-B) (MMP-H19) (EC 3.4.24.-) (Zinc metalloprotease 2) (O44836)
Organism: Caenorhabditis elegans
Function: Metalloprotease involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed. Plays a role in thermotolerance probably by preventing the accumulation of oxidized lipoproteins and cholesterol.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:24957743}.
Interaction partners:
- Peptidase M20 dimerisation domain-containing protein
- ELRR ONly
- Putative metalloproteinase inhibitor tag-225
- NTR domain-containing protein
Sequence:
MTKWSPNGNPLSTIYLILSLFTLAHTAPTTQHSRTTTQLRLEDEDGGGGVDEDSIHFVKGQMEKYGYLKGIDHSSPQEFRQALMFFQEVLEVEQTGNVDEMTVEAASKPRCTQTDVRQEQTKRTKRFTLSKRAKWAHASGQSVTLKWYISDYTSDIDRLETRKVVEKAFKLWSSQSYIKNEKKVTLTFQEASSKDEADINILWAEGNHGDEHDFDGANGKIEGNKKENVLAHTFFPGYARPLNGDIHFDDAEDWEIDVDQVGHGSNKRFFPYVLAHEIGHALGLDHSQKADALMHPYYKNVPINEIQLDIDDKCGVIWNYGGASDFCLYVWLMSQIVEAHNSSAQNNHGVGSITSSRTNKKSFKSEGFFLFQLKFPHSTLTHTDDVVMREKDKRSYRGDSKIPKCSSNNSSQRTLAEKKLTLGLHLSEADAKRYTEMVCNFLAGLHMWRTNPNHHASESLEKEYKGVSQEMGTFSGKSIAVRRLIRHAEHQKERSEKGPLDPDYFDDDFFENFFMEYSK
Protein: U3 small nucleolar RNA-associated protein 6 homolog (Hepatocellular carcinoma-associated antigen 66) (Multiple hat domains protein) (Q9NYH9)
Organism: Homo sapiens (Human)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:34516797}.
Interaction partners:
- Bystin
- KRR1 small subunit processome component homolog
- WD repeat-containing protein 46
- Neuroguidin
- U3 small nucleolar RNA-associated protein 14 homolog A
- WD repeat-containing protein 75
- U3 small nucleolar RNA-associated protein 15 homolog
- U3 small nucleolar RNA-associated protein 4 homolog
- HEAT repeat-containing protein 1
- U3 small nucleolar ribonucleoprotein protein IMP4
Sequence:
MAEIIQERIEDRLPELEQLERIGLFSHAEIKAIIKKASDLEYKIQRRTLFKEDFINYVQYEINLLELIQRRRTRIGYSFKKDEIENSIVHRVQGVFQRASAKWKDDVQLWLSYVAFCKKWATKTRLSKVFSAMLAIHSNKPALWIMAAKWEMEDRLSSESARQLFLRALRFHPECPKLYKEYFRMELMHAEKLRKEKEEFEKASMDVENPDYSEEILKGELAWIIYKNSVSIIKGAEFHVSLLSIAQLFDFAKDLQKEIYDDLQALHTDDPLTWDYVARRELEIESQTEEQPTTKQAKAVEVGRKEERCCAVYEEAVKTLPTEAMWKCYITFCLERFTKKSNSGFLRGKRLERTMTVFRKAHELKLLSECQYKQLSVSLLCYNFLREALEVAVAGTELFRDSGTMWQLKLQVLIESKSPDIAMLFEEAFVHLKPQVCLPLWISWAEWSEGAKSQEDTEAVFKKALLAVIGADSVTLKNKYLDWAYRSGGYKKARAVFKSLQESRPFSVDFFRKMIQFEKEQESCNMANIREYYERALREFGSADSDLWMDYMKEELNHPLGRPENCGQIYWRAMKMLQGESAEAFVAKHAMHQTGHL
Protein: Integrin alpha-7 [Cleaved into: Integrin alpha-7 heavy chain; Integrin alpha-7 light chain] (Q61738)
Organism: Mus musculus (Mouse)
Function: Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. Involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Mice carrying a ITGA7 null allele are viable and fertile, but show progressive muscular dystrophy starting soon after birth, but with a distinct variability in different muscle types. Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells. Acts as Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin beta-1
- Integrin beta-4
- Integrin beta-8
- Integrin beta-5
- Laminin subunit alpha-4
- Integrin alpha-6
- Tetraspanin-32
- Peripheral myelin protein 22
- Fibronectin
- Integrin beta-6
Sequence:
MARIPRCDFLRPPGIYYLITSLLAGLFLPPAIAFNLDVMGAIRKEGEPGSLFGFSVALHRQLQPRPQSWLLVGAPQALALPGQQANRTGGLFACPLSLEETDCYRVDIDRGANVQKESKENQWLGVSVRSQGAGGKIVTCAHRYESRQRVDQALETRDVIGRCFVLSQDLAIRDELDGGEWKFCEGRPQGHEQFGFCQQGTAATFSPDSHYLVFGAPGTYNWKGTARVELCAQGSPDLAHLDDGPYEAGGEKEQDPRLIPVPANSYLGLLFVTNIDSSDPDQLVYKTLDPADRLTGPAGDLTLNSYLGFSIDSGKGLMRSEELSFVAGAPRANHKGAVVILRKDSATRLIPEVVLSGERLTSGFGYSLAVTDLNNDGWADLIVGAPYFFERQEELGGAVYVYMNQGGHWADISPLRICGSPDSMFGISLAVLGDLNQDGFPDIAVGAPFDGDGKVFIYHGSSLGVVVKPSQVLEGEAVGIKSFGYSLSGGLDVDGNHYPDLLVGSLADTAALFRARPVLHVSQEIFIDPRAIDLEQPNCADGRLVCVDIKICFSYVAVPSSYSPSVALDYMLDGDTDRRLRGQVPRVTFLSRGLDDLRHQSSGTVWLKHQHDRVCGDTVFQLQENVKDKLRAIVVTLSYGLRTPPLGRQAPGQELPTVAPILNAHQPSTQRTEIHFLKQGCGQDKICQSNLQLERYQFCSRISDTEFQALPMDLDGRTALFALSGQPFIGLELTVTNLPSDPSRPQADGDDAHEAQLLVTLPASLRYSGVRALDSVEKPLCLSNDSASHVECELGNPMKRGAQVTFYLILSTSGITIETTELEVKLLLATISEQELDPVSVRAHVFIELPLSISGVATPQQLFFSGEVKGESAMRSERELGRKVKYEVTVSNQGQSLNTLGSANLNIMWPHEIANGKWLLYPMRVELEGGQGPGKRGICSPRPNILQLDVDSRDRRRRELGQPEPQEPPEKVEPSTSWWPVSSAEKRNMTLDCPRTAKCVVFSCPLYSFDRAAVLHVWGRLWNSTFLEEYMAVKSLEVIVRANITVKSSIKNLLLRDASTVIPVMVYLDPMAVVVEGVPWWVILLGVLAGLLVLALLVLLLWKLGFFKRAKHPEATVPQYHAVKIPREDRQQFKEEKTGTIQRSNWGNSQWEGSDAHPILAADWHPELGPDGHPVPATA
Protein: Heat shock transcription factor 4 (D4A5A8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGAGRRPRHRPPHPLEPDGFRKVVSIEQGGLLRPERDHVEFQHPSFVRGCEQLLERVRRKVPALRGDDTRWRPEDLGRLLGEVQALRGVQESTEARLQELRQQNEILWREVVTLRQSHSQQHRVIGKLIQCLFGPLQTGPSSTGAKRKLSLMLDEGSACSASAKFNACPVSGALLQDPYFIQSPLPETTVGLSPHRARGPIISDIPEDCPSPEGHRLSPSSAGRRVKGLALLKEEPASPGGDGEAGLALAPNECDFCVTAPPPLPVAVVQAILEGKGSFSPEGPRSIQQPEPRGPREVPDRGTLGLDRGNRSPESLLPPVLLRPPPETVEPMDALGPSLHGREWTLMDLDMELSLMQPLAPERAEAELTVKDLTSSGVGKDHTLGTPLMLDVQADLEGAALSVPGALTLYNATESNASYLDPGASPSSP
Protein: AT28702p (Q8MZ70)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTYLLTAIPSLDSDKTISIVEGVPNLDLQTVGSNRKSQILKPNLLSDEMREEFRKMPVGGFKFQFPWSRRERNLKNEKVERDLGIFCVAFKDKPVEWNYLHQPDYIFKYSVALGWGIGCCLIYIQSVNNSDIFYTGVVINIIAFFVLTFLLFICWYKKVCWWHSGQNEHRSYGKLSCAIFHLFEKIQHSFVLRLTVYMMIILCYYMVISLILMSCEKDQYELDIIESKLYNYDMDPFTCFHPWAYTNMMALILGMSYTFARIPFALKTFIGCAEAVVFVLVVCFQYAFIFEHSVTTSPYLKAEIAHSCRVCMMLITMYAKERQSEFNTKMNYKLNLDLQNKQKSADVTNQSIIILLNNILPSHVVLFRSRGISQLYSQTRTLL
Protein: Transforming growth factor beta (Q66I23)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- TGF-beta receptor type-2
- Receptor protein serine/threonine kinase
- TGF-beta receptor type-2
- Serine/threonine-protein kinase receptor
- Decorin
- Fibromodulin a.
- Fibromodulin b.
- Left-right determination factor.
- Left-right determination factor
- Latent transforming growth factor beta binding protein 3
Sequence:
MHLGKGLLFVLLLNSVTMSLSLSTCTTVDIDNIKKKRVEAIRGQILSKLRLTSPPQTLGPSQVPYQVLALYNSTRDLLDGFGKDRHQSCGQDNTETEYYAKEIHKFNMIQGSPENNDLPYCPKGITSKVFRFDVSIMEKNASNLFRAEFRALRMPNLSTSRTEQRIELYQILRPDEHIGKQRYIGRKNVMIGGTDEWVSFDVTETVREWLTNRATNLGLEISVHCPCHTFRPNGEIIENVNEALEVKFRGMDVEDDGPIRSDMGRLKKPKEQNLPHLILMMLPPHRLDVLPTSRRRKRALDTKYCFSNYEENCCVRKLYIDFRQDLGWRWIHEPKGYHANFCSGPCPYLRSADTTHSSLLSLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMIVKSCKCS
Protein: 16.9 kDa class I heat shock protein 3 (16.9 kDa heat shock protein 3) (OsHsp16.9C) (Q943E7)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- 23.6 kDa heat shock protein, mitochondrial
- 18.0 kDa class II heat shock protein
- 19.0 kDa class II heat shock protein
- 16.9 kDa class I heat shock protein 2
Sequence:
MSLVRRSNVFDPFADFWDPFDGVFRSLVPATSDRDTAAFANARVDWKETPESHVFKADLPGVKKEEVKVEVEEGNVLVISGQRSKEKEDKNDKWHRVERSSGQFMRRFRLPENAKVDQVKASMENGVLTVTVPKAEVKKPEVKAIEISG
Protein: Glycogen phosphorylase, brain form (EC 2.4.1.1) (P53534)
Organism: Rattus norvegicus (Rat)
Function: Glycogen phosphorylase that regulates glycogen mobilization (By similarity). Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Interaction partners:
- Glycogen debranching enzyme
- Phosphoglucomutase-1
- 1,4-alpha-glucan branching enzyme
- UTP--glucose-1-phosphate uridylyltransferase
- Alpha-amylase.
- Pancreatic alpha-amylase
- Phosphoglucomutase 2-like 1
- Receptor-interacting serine/threonine-protein kinase 3
- Glycogen phosphorylase, liver form
- Glycogen [starch] synthase, liver
Sequence:
MAKPLTDSERQKQISVRGIAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTVRDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQTACDEATYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHTPNGVLWLDTQVVLAMPYDTPVPGYKNNTVNTMRLWSAKAPNDFKLKDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKVDWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFPGDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKFQNKTNGITPRRWLLLCNPGLAEIIVERIGEGFLTDLSQLKKLLSLVDDEAFIRDVAKVKQENKLKFSAQLEKEYKVKINPCSMFDVHVKRIHEYKRQLLNCLHIITLYNRIKKDPTKTFVPRTVMIGGKAAPGYHMAKMIIKLVTSIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRVEDVEALDQKGYNAQEFYERLPELRQAVDQISSGFFSPKDPDCFKDVVNMLMYHDRFKVFADYEAYIQCQAQVDHLYRNPKDWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPP
Protein: Cyclo(L-leucyl-L-leucyl) synthase (EC 2.3.2.22) (Cyclodileucine synthase) (Cyclodipeptide synthase) (CDPS) (Q4L2X9)
Organism: Staphylococcus haemolyticus (strain JCSC1435)
Function: It uses activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-independent formation of cyclodipeptides which are intermediates in diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation of cyclo(L-Leu-L-Leu) (cLL) from L-leucyl-tRNA(Leu). Can incorporate various nonpolar residues, such as L-phenylalanine, L-leucine and L-methionine, into cyclodipeptides.
Interaction partners:
Sequence:
MQNFKVDFLTKNCKQIYQRKKHVILGISPFTSKYNESYIRKIIQWANSNFDDFSILLAGEESKNLLECLGYSSSKANQKVRKEIKRQIRFCEDEIIKCNKTITNRIHRFSDFKNNIYYIDIYKTIVDQFNTDSNFKNSCLKMSLQALQSKGKNVNTSIEITDETLEYAAQYVLAELPFFLNANPIINTQETLMAYHAPWELGTNIINDQFNLKMNEKQGYIILTEKGDNYVKSV
Protein: GM04269p (Q95SB0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGKALNIGDQFPNFTAETSEGRIDFYDWMQDSWAILFSHPADFTPVCTTELSRVAALIPEFQKRGVKPIALSCDTVKSHKGWIEDIKSFGKLSSFDYPIIADDKRELALKFNMLDKDEINAEGIPLTCRAVFVVDDKKKLRLSILYPATTGRNFDEILRVIDSLQLTQTKSVATPADWKQGGKCMVLPTVKAEDVPKLFPDGIETIELPSGKSYLRITPQP
Protein: NACHT, LRR and PYD domains-containing protein 1a allele 4 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)] (D9I2G1)
Organism: Rattus norvegicus (Rat)
Function: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}.
Interaction partners:
Sequence:
MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEAHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWETKLKLLRSIIGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL