wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein phosphatase non-receptor type (EC 3.1.3.48) (Q803M6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR000929}.
Interaction partners:
Sequence:
MVRWFHRDLSGLDAEAVLKSRGVHGSFLARPSKKNVGDFSLSVRVGEIITHIRIQNTGDYYDLYGGEKFATLAELVEYYTGDHGTLQDKDGTVIELKYPLNCSDPTTERWYHGHLSGPNAEKLLRERNEPGTFLVRESLSKPGDFVLSALTDDQTSSGRRVSHIKIMCNNDRYTVGGKDQFDNLTDLVEHFKRVGIEELSGTMVYLKQPYYSTRLNAADIQSRVNQLDQTSEREKMDGADKKIKAGFWEEFDALQKLETKVTKSRDEGMRPENKSKNRYKNILPFDETRVILENADPNVVGSDYINANYVINKLMVTNPQKTYIACQGCLATTVDDFWQMMWQEDSRVIVMTTREVEKGRNKCVPYWPTTEGESKEVGRYVVKLLSEMDAADYKVRVVELTAPHRNEAPRKIWHFQYLSWPDHGVPQEPGGVLSFLDQVNRKQEELRSSAPIVIHCSAGIGRTGTIVVIDMLIDSIDAKGLDCDIDIQKCIMMVRDQRSGMVQTEAQYKFIYLAVLQYVESTKVTRRAIMETETEYGNLSIQSKHPKASRKASSKKNEDVYENLGAKGKKDVKKQKSEEKKGGGSVRKR
Protein: Cytochrome P450 71D181 (Alpha-terpinene hydroxylase) (Carvacrol synthase) (EC 1.14.14.-) (Carveol synthase) (EC 1.14.14.51, EC 1.14.14.53) (Gamma-terpinene hydroxylase) (Limonene hydroxylase) (P0DO41)
Organism: Origanum vulgare (Wild marjoram)
Function: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (Ref.1). Catalyzes the C2-hydroxylation of gamma-terpinene and alpha-terpinene to produce carvacrol (Ref.1). Mediates also the C6-hydroxylation of (4S)-limonene and (4R)-limonene to form carveol (Ref.1).
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDISISWVAIILVISSYFIFMNKWRAAKLPENLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVYSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNNDMIFSRYNDHWRQIRKICVSELLSPKNVRSFGFIRQDEMARLIRVFESSVGVPINASEEISKMSCAIVCRAAFGSVLKDQGLLADLVKEALGMASGFELADLYPSSWLLNLLCFNKYRLRRMRQRLDDILDGFLEEHRVKKSGEFGGEDIIDVLYRMQKDSENKVPITNSGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKLAKAQAEVREKLKGKTNPDVAEVQEIKYLHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRILVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRICPGLHFGLANVEVPLAQLLYHFEWKLPQGMTPADMDMSETPGLSGPRKNPLIMVPTIHNPTS
Protein: Mitotic spindle checkpoint protein MAD1 (Mitotic arrest deficient protein 1) (Q9LTY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and delays the onset of anaphase when this process is not complete. It inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. Required for anchoring MAD2 to the nuclear envelope.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:22457071}. Note=The nucleus envelope association requires the presence of NUA. {ECO:0000269|PubMed:22457071}.
Interaction partners:
- Mitotic spindle checkpoint protein MAD2
- Origin of replication complex subunit 2
- At5g05510
- Mitotic spindle checkpoint protein BUBR1
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Serine/threonine-protein kinase MPS1
- Cell division cycle 20.3, cofactor of APC complex
- Cell division cycle 20.5, cofactor of APC complex
- Cell division cycle 20.6, cofactor of APC complex
- Cell division cycle 20.1, cofactor of APC complex
Sequence:
MILRTPQPKRLRSDAGESPFPTGATGSGNQLIIYEDSPLPAPAPLQTSHDHSADQHLCTYQCRQMVKADVLDALSTAEKQVEESKTKLQTLNANFTEADAERKHFRDKFLYSEQELAAAKAREKMLQEQLLMEINNSQERYTKELQSCHELEVKLQNEMNLRKKAESSAATAEEKAKLLEDKLTQLSGSVDREKKRLNNDIAQLGKEAKLSVARIGADLERMQCRAQNAETESNLLRSQLEHLKLIFDECLQEKTEVDKKLSSFTSEAASSSDNSVLVKHLQEELKRYEAEVREARKLKSRHLDAELLNVNLLEEQSRRERAESELSKFHDLQLSMEKLENELSSWKSLLNDIPGVSCPDDIVMRFSVLQNEVVQSTMKIGEASTRIKQLEETLEAIQLGRQNAVSEAALAKEKSEALKTDVKRIEVMLTLVTEEKEQLKAVVNELRKSNSEGSVSGAADGALIQGFESSLAKKENYIKDLEQDLNQLKDVNNRQRTEIELLNEKLVDEARRNKSLERDSDRLRSEISLLESKLGHGDYSAANTRVLRMVNTLGVENEAKQTIEALQAELQKTKERLQAVEELKSQSGDAGKLVDSHITGKIAQLKEQNATLEKREERYKTVFADRISVFRRACCELFGYKIVMDEHQRPNGIPVTRFTLQSIYAQSDDEKLEFEYESGNTSILNNEYASQGDIAKQIEIFIRKFNSIPAFTANLTMESFNRRTLY
Protein: Heme A synthase COX15 (HAS) (EC 1.17.99.9) (Cytochrome c oxidase assembly protein COX15 homolog) (Q7KZN9)
Organism: Homo sapiens (Human)
Function: May be involved in the biosynthesis of heme A.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:9878253}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c oxidase subunit 3
- Surfeit locus protein 1
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 2
- Protein SCO1 homolog
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Protein SCO2 homolog
- Cytochrome c1, heme protein, mitochondrial
- Mitochondrial chaperone BCS1
Sequence:
MQRLLFPPLRALKGRQYLPLLAPRAAPRAQCDCIRRPLRPGQYSTISEVALQSGRGTVSLPSKAAERVVGRWLLVCSGTVAGAVILGGVTRLTESGLSMVDWHLIKEMKPPTSQEEWEAEFQRYQQFPEFKILNHDMTLTEFKFIWYMEYSHRMWGRLVGLVYILPAAYFWRKGWLSRGMKGRVLALCGLVCFQGLLGWYMVKSGLEEKSDSHDIPRVSQYRLAAHLGSALVLYCASLWTSLSLLLPPHKLPETHQLLQLRRFAHGTAGLVFLTALSGAFVAGLDAGLVYNSFPKMGESWIPEDLFTFSPILRNVFENPTMVQFDHRILGITSVTAITVLYFLSRRIPLPRRTKMAAVTLLALAYTQVGLGISTLLMYVPTPLAATHQSGSLALLTGALWLMNELRRVPK
Protein: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCase subunit alpha) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 1) (3-methylcrotonyl-CoA carboxylase biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha) (Q96RQ3)
Organism: Homo sapiens (Human)
Function: Biotin-attachment subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16023992}.
Interaction partners:
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Biotin--protein ligase
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Methylglutaconyl-CoA hydratase, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Peroxisomal bifunctional enzyme
- Pyruvate carboxylase, mitochondrial
- Colorectal mutant cancer protein
Sequence:
MAAASAVSVLLVAAERNRWHRLPSLLLPPRTWVWRQRTMKYTTATGRNITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRKAAAKESLCQAALGLILKEKAMTDTFTLQAHDQFSPFSSSSGRRLNISYTRNMTLKDGKNNVAIAVTYNHDGSYSMQIEDKTFQVLGNLYSEGDCTYLKCSVNGVASKAKLIILENTIYLFSKEGSIEIDIPVPKYLSSVSSQETQGGPLAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEESDKRESE
Protein: High affinity zinc ion transporter, putative (Q4WKR5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362088}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362088}.
Interaction partners:
Sequence:
MSAFDPSNVDLNTASKEDVICFLSLSENEYNGHLGARISSIFVIFITSTVFTLFPVVAQRLPQWRIPHHVYLFGRYFGTGVIVATAFIHLLDPAYQSIGPGTCIGMSGAWGEYSWCAAIVLSSVILVFLLDVGAEVYVEWKYSVPREANATATFITQPACSSPHESSDRLTATEPSSPTGGKDLYPRADELSVASERAFRQDIAAFLVLEFGIIFHSVIIGLNLGVAGDEFAALYPVLVFHQSFEGLGIGARMSALHFGRRRWLPWILCLAYGLTTPVAIAIGLGVRTSYSPGSRTALIVQGVLDALSAGILIYSGLVELLARDFLFDPCRTKRRGQILYMLGCTLLGAGMMALIGKWA
Protein: Anhydrin-1 (Q7YUB9)
Organism: Aphelenchoides avenae (Mycophagous nematode worm) (Aphelenchus avenae)
Interaction partners:
Sequence:
MPPIATRRGQYEPKVQQAKLSPDTIPLNPADKTKDPLARADSLHHHVESDSQEDDKAAEEPPLSRKRWQNRTFRRKGRRQAPYKHK
Protein: Protein Jade-1 (Jade family PHD finger protein 1) (PHD finger protein 17) (Q803A0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity. Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H4 acetylation (H4K5ac, H4K8ac and H4K12ac), regulating DNA replication initiation, regulating DNA replication initiation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6IE81}. Chromosome {ECO:0000250|UniProtKB:Q6IE81}. Cytoplasm {ECO:0000250|UniProtKB:Q6IE81}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6IE81}. Note=Localizes to the ciliary transition zone. {ECO:0000250|UniProtKB:Q6IE81}.
Interaction partners:
- Inhibitor of growth protein
- Chromatin modification-related protein MEAF6
- Inhibitor of growth protein
Sequence:
MKRSRVPSTSEDSDNGSNSTSWSQHSNSKHRKQSGKRPSEVFRTDLITAMKLHDSHQLNPEDYYELADPWRQEWEKGVQVPVSPESIPQCAVRTVAEKSTAPLFIKPKKLIRSSESSMLGYVGIQTLADGMCRYDLNEEDVAWLQITNEEFSKMGMQPLDELTMERVMEEFERRCYDNMSHAMETEEGLGIEYDEDVVCDVCQSPDGEDGNEMVFCDKCNICVHQACYGILKVPEGSWLCRTCALGIFPKCHLCPKKGGAMKPTRSGTKWVHVSCALWIPEVSIGNPEKMEPITNVSHIPSNRWALICCLCKEKTGACIQCSAKSCRVAFHVTCGLHCGLKMNTILTEADEVKFKSFCPKHSGLDWNEEEGDDDRPVKVPTREDRSRNRGIDFSASSQTRLSQNPEETRLSERKLRVQQLEDEFYRFVAADEVAEHLQLPLEMVDILFQYWKLKRKVNFNQPLIMPKKEEEDSLARREQEVLLRRLRLFTHLRQDLERVRNLTYMVSRRERIKRTLCRVQEQIFHHHVRLLEQGRVTGVSSTRRLEEAMFYFRTTPPVPASPQPLKGHCGQNSTLSSSEKGSNSYRSSKHIEADKPAKMLMDGVPSSGDSVRSETVMSASSRRSEGRTRSGESHRKEEESERPLEDRRRKSKLWDQVSIKDKLRHAKSMEDTLSSETELDTMDDRLLLSHTNANSVATAPNMYSGSPRKTNASHQGKLVPNGTSGRHLKNWGSFRIPKRSERTSAGRQTERQEADNTADQNSSLKTFSTSPSSPQIRTRLRTGSENRRHLEESDLGQSEQGKRCHTQRLPSPMTRRYGSDVIQRGVLAS
Protein: Gallinacin-4 (Gal-4) (Beta-defensin 4) (Gallinacin-7) (Gal-7) (Q6GXJ1)
Organism: Gallus gallus (Chicken)
Function: Has bactericidal activity. Potent activity against S.typhimurium and S.entiriditis.
Subcellular location: Secreted. Cytoplasmic granule {ECO:0000250}.
Interaction partners:
- Gallinacin-6
- Gallinacin-1
- Gallinacin-2
- Gallinacin-14
- Gallinacin-3
- Gallinacin-5
- Gallinacin-8
- Gallinacin-9
- Gallinacin-7
- Gallinacin-10
Sequence:
MKILCFFIVLLFVAVHGAVGFSRSPRYHMQCGYRGTFCTPGKCPHGNAYLGLCRPKYSCCRWL
Protein: Endonuclease/exonuclease/phosphatase, putative (Q384N6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NOT1
- poly
- Cell differentiation protein, putative
- NOT2/NOT3/NOT5 C-terminal domain-containing protein
- Uncharacterized protein
- Probable eukaryotic initiation factor 4A
Sequence:
MYTTMPNSPLAIPHHFLDIGKDESSPPMTRNDTNSSGLASFQPTDDQVAEGFPSLGVSTASPTHRTTLQERREKLLGGSFLSLCVETLQNDCPEAIEGDCNSNRTVFRGWSKTDLGVSSQALSNNGVVRLVCYNILAQRFLSMQRYPRCPPFALAEDYRCGFAEQELLQADPDIILLQEISVDVFGKPGLLGENLREKHGFIGNHVVVTDLSGRPRHTSFDSSTDGAQAVVFQEVTTSSSKPSPSGTVESRRSNDVAAEKTVEPPRSDLEGVATFFLKDRFELLEVIPIRLNEIANADKTLTQSERRSLRRMSHNVALITVLRDLNKPNVIYVVCNLHLLWSGSRCQLWQLHRVMSYIEQVKGEHESHIENSNGECPIVAVVLGGDFNSESWEPPIAYALNGSLPESSNVGAWCGTPGRETGAFSPISRDTDVDVENSKSGTPMVESPCGAGGGGTCSGFTAPAAGHSLALTDVYEIYRERHPRRVSFVDPGDGGKGKVYDHILIDKRHLGCTDVLRLSSSTNLPAPNCPSDHCPVGAVIVPLCLLS
Protein: Kininogen-1 [Cleaved into: Kininogen-1 heavy chain; Bradykinin; Kininogen-1 light chain] (P08934)
Organism: Rattus norvegicus (Rat)
Function: Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation of thrombocytes. LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- B1 bradykinin receptor
- B2 bradykinin receptor
- Plasma kallikrein
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
- Protachykinin-1
- Thimet oligopeptidase
- Angiotensinogen
- Coagulation factor XII
- Endothelin receptor type B
Sequence:
MKLITILLLCSRLLPSLAQEEDAQEMDCNDESLFQAVDTALKKYNAGLKSGNQFVLYQVTEGTKKDGSKTFYSFKYQIKEGNCSVQSGFAWQDCDFKDAEEAATGECTATLEKRRNNKFSIATQICNITPGKGPIVTNEYHCLGCMHPISVDSPELGPVLKHAVEHFNNNTKHTHLFALGEVKSADRQVVAGMNYQIIYSIVQTNCSKEDFPSLHEDCVPLPSGDDGECKGNAFVDIHKTIAGFSDSCEFYPGDDLFELLPEDCPGCPRNIPVDSPELKEALGHSIAQLNAENNHTFYFKIDTVKKATSQVVAGTKYVIEFIARETKCSKESNAELTADCETKRLGQSLNCNANVYMRPWENKVVPTVKCKVLDMTSVIRRPPGFSPFRAPRVKKPKESTTVSPSYIARVQEERDPGNEQGPIHGHGWLHAKQIKNKNHQGHKHGHGIGHGHQKPHGLGHGHQLKLDDLKQQREDGYDHRHPVGHGHGQRHGHGHGHGHGRDKHTNKDKNNVKHTDQRRAPLTSSSEDNTTSTQIQGRTEGFTLNPPLAQPAVISRGFQDSGFTEGVIATTSPYDTETHDDLIPDIHVQPDSLSFKLISDFPEATSHKCPGRPWKPVSRKDPTIETTEFSDFDLLDALS
Protein: LD34388p (Q7K1W8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Outer segment 5
Sequence:
MPRNLPLLPLTLCAVALLAAVGPMPAHGAVANSHKHEKHLSKERVKDGIYAPRDAHHHGEDGEHNVEFDHEAIIGNTKEAQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEEIDQDADERITWKEYLQDTYAMEDEDFKKETIDYDSYEDEQKMIKQDKEMFNAADTNKDGVLTLEEFVLFQNPEEHPQMLPILLEHTMQDKDADHDGKINFQEFVGDAASHHDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAIANDEVDHLFVSTDEDHDDRLSYLEILNNYDTFVGSEATDYGDHLQNINHLSDEL
Protein: E3 SUMO-protein ligase SIZ1 (EC 2.3.2.-) (E3 SUMO-protein transferase SIZ1) (Q680Q4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 SUMO protein ligase involved in regulation processes. Mediates SUMO/ attachment to PHR1, a MYB transcriptional activator controlling the phosphate deficiency responses. Functions as an upstream negative regulator of salicylic acid (SA) accumulation and subsequent SA-mediated systemic acquired resistance (SAR) signaling. Probably not involved in jasmonic acid (JA)-mediated defense response. Participates in abiotic stress-induced sumoylation. Controls heat shock-induced SUMO1 and SUMO2 conjugation and facilitates basal thermotolerance. Involved in freezing tolerance by mediating sumoylation of ICE1, a transcription activator of the cold signaling regulator CBF3/DREB1A. Acts as positive regulator of drought stress tolerance. Acts as floral repressor that promotes FLC expression by repressing FLD activity through sumoylation. Acts as negative regulator of abscisic acid (ABA) signaling through ABI5 sumoylation. Mediates sumoylation of SCE1, GTE3 and GTE5. Functions as negative regulator of SnRK1 signaling through sumoylation of several components of the SnRK1 complex.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:15894620}.
Interaction partners:
- SUMO-conjugating enzyme SCE1
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 2
- E3 SUMO-protein ligase MMS21
- Small ubiquitin-related modifier 3
- Small ubiquitin-related modifier 5
- Putative small ubiquitin-related modifier 4
- SUMO-conjugating enzyme UBC9
- Putative small ubiquitin-related modifier 6
- Putative small ubiquitin-related modifier 7
Sequence:
MDLEANCKEKLSYFRIKELKDVLTQLGLSKQGKKQELVDRILTLLSDEQAARLLSKKNTVAKEAVAKLVDDTYRKMQVSGASDLASKGQVSSDTSNLKVKGEPEDPFQPEIKVRCVCGNSLETDSMIQCEDPRCHVWQHVGCVILPDKPMDGNPPLPESFYCEICRLTRADPFWVTVAHPLSPVRLTATTIPNDGASTMQSVERTFQITRADKDLLAKPEYDVQAWCMLLNDKVLFRMQWPQYADLQVNGVPVRAINRPGGQLLGVNGRDDGPIITSCIRDGVNRISLSGGDVRIFCFGVRLVKRRTLQQVLNLIPEEGKGETFEDALARVRRCIGGGGGDDNADSDSDIEVVADFFGVNLRCPMSGSRIKVAGRFLPCVHMGCFDLDVFVELNQRSRKWQCPICLKNYSVEHVIVDPYFNRITSKMKHCDEEVTEIEVKPDGSWRVKFKRESERRELGELSQWHAPDGSLCPSAVDIKRKMEMLPVKQEGYSDGPAPLKLGIRKNRNGIWEVSKPNTNGLSSSNRQEKVGYQEKNIIPMSSSATGSGRDGDDASVNQDAIGTFDFVANGMELDSISMNVDSGYNFPDRNQSGEGGNNEVIVLSDSDDENDLVITPGPAYSGCQTDGGLTFPLNPPGIINSYNEDPHSIAGGSSGLGLFNDDDEFDTPLWSFPSETPEAPGFQLFRSDADVSGGLVGLHHHSPLNCSPEINGGYTMAPETSMASVPVVPGSTGRSEANDGLVDNPLAFGRDDPSLQIFLPTKPDASAQSGFKNQADMSNGLRSEDWISLRLGDSASGNHGDPATTNGINSSHQMSTREGSMDTTTETASLLLGMNDSRQDKAKKQRSDNPFSFPRQKRSNNEQDHQTRHRSLNKICIILCAGKN
Protein: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC 2.1.1.14) (Cobalamin-independent methionine synthase) (Delta-P8 protein) (Methionine synthase, vitamin-B12 independent isozyme) (P05694)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Interaction partners:
- Adenosylhomocysteinase
- S-adenosylmethionine synthase 2
- S-adenosylmethionine synthase 1
- Homocysteine/cysteine synthase
- Cystathionine beta-lyase
- Homocysteine S-methyltransferase 1
- Homocysteine S-methyltransferase 2
- Methylenetetrahydrofolate reductase 2
- Cystathionine gamma-lyase
- Cystathionine gamma-synthase
Sequence:
MVQSAVLGFPRIGPNRELKKATEGYWNGKITVDELFKVGKDLRTQNWKLQKEAGVDIIPSNDFSFYDQVLDLSLLFNVIPDRYTKYDLSPIDTLFAMGRGLQRKATETEKAVDVTALEMVKWFDSNYHYVRPTFSKTTQFKLNGQKPVDEFLEAKELGIHTRPVLLGPVSYLFLGKADKDSLDLEPLSLLEQLLPLYTEILSKLASAGATEVQIDEPVLVLDLPANAQAAIKKAYTYFGEQSNLPKITLATYFGTVVPNLDAIKGLPVAALHVDFVRAPEQFDEVVAAIGNKQTLSVGIVDGRNIWKNDFKKSSAIVNKAIEKLGADRVVVATSSSLLHTPVDLNNETKLDAEIKGFFSFATQKLDEVVVITKNVSGQDVAAALEANAKSVESRGKSKFIHDAAVKARVASIDEKMSTRAAPFEQRLPEQQKVFNLPLFPTTTIGSFPQTKDIRINRNKFNKGTISAEEYEKFINSEIEKVIRFQEEIGLDVLVHGEPERNDMVQYFGEQINGYAFTVNGWVQSYGSRYVRPPIIVGDLSRPKAMSVKESVYAQSITSKPVKGMLTGPITCLRWSFPRDDVDQKTQAMQLALALRDEVNDLEAAGIKVIQVDEPALREGLPLREGTERSAYYTWAAEAFRVATSGVANKTQIHSHFCYSDLDPNHIKALDADVVSIEFSKKDDANYIAEFKNYPNHIGLGLFDIHSPRIPSKDEFIAKISTILKSYPAEKFWVNPDCGLKTRGWEETRLSLTHMVEAAKYFREQYKN
Protein: Type 1 encapsulin shell protein (IMEF encapsulin) (A0A0F5HPP7)
Organism: Bacillus thermotolerans (Quasibacillus thermotolerans)
Function: Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous icosahedral shells 42-43 nm in diameter with an iron- and phosphorus-rich core (1Fe:1.1P) which can store over 23,000-35,000 iron atoms (with a calculated maximum of 83,000 Fe). There are 2 types of negatively charged open pores in the cryo-electron structure; a 3-fold pore where 3 hexamers meet with a minimal size of 7.2 Angstroms and a 5-fold pore where pentamers meet with a minimal size of 2.3 Angstroms. The 2-fold pore seen in other encapsulin nanocompartments is closed. Empty compartments can be generated in E.coli. Both types of pore have extra density in their centers in the structure. 2 different cargo proteins have been identified (IMEF and Fer); when both are expressed in E.coli with the shell protein only IMEF is detected within the nanocompartment. E.coli expressing all 3 genes stores the largest amount of iron and is protected from Fe/H2O2-induced oxidative stress. Part of the iron-mineralizing encapsulin-associated Firmicute (IMEF) system (Probable).
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:31194509, ECO:0000269|PubMed:31282860}.
Interaction partners:
- Ferredoxin
Sequence:
MNKSQLYPDSPLTDQDFNQLDQTVIEAARRQLVGRRFIELYGPLGRGMQSVFNDIFMESHEAKMDFQGSFDTEVESSRRVNYTIPMLYKDFVLYWRDLEQSKALDIPIDFSVAANAARDVAFLEDQMIFHGSKEFDIPGLMNVKGRLTHLIGNWYESGNAFQDIVEARNKLLEMNHNGPYALVLSPELYSLLHRVHKDTNVLEIEHVRELITAGVFQSPVLKGKSGVIVNTGRNNLDLAISEDFETAYLGEEGMNHPFRVYETVVLRIKRPAAICTLIDPEE
Protein: Histone H3.2 (H3-clustered histone 13) (H3-clustered histone 14) (H3-clustered histone 15) (H3-clustered histone 2) (H3-clustered histone 3) (H3-clustered histone 4) (H3-clustered histone 6) (H3-clustered histone 7) (P84228)
Organism: Mus musculus (Mouse)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H4
- Chromobox protein homolog 5
- WD repeat-containing protein 5
- DNA
- V
- Chromobox protein homolog 3
- Bromodomain-containing protein 4
- Histone H3.3
- Histone H2B type 2-B
- DNA
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: Sodium-dependent multivitamin transporter (Na(+)-dependent multivitamin transporter) (Solute carrier family 5 member 6) (O70247)
Organism: Rattus norvegicus (Rat)
Function: Sodium-dependent multivitamin transporter that transports pantothenate, biotin and lipoate (By similarity). Required for biotin and pantothenate uptake in the instestine (By similarity). Plays a role in the maintenance of intestinal mucosa integrity, by providing the gut mucosa with biotin (By similarity). May play a role in the transport of biotin and pantothenate into the brain across the blood-brain barrier (By similarity). May also be involved in the sodium-dependent transport of iodide ions (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9Y289}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q9Y289}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- PDZ domain containing 11
Sequence:
MTVASTAAPSYTTSDTNRVISTFSVVDYVVFGLLLVLSLVIGLYHACRGWGRHTVGELLMADRKMGCLPVALSLLATFQSAVAILGGPAEIYRFGTQYWFLGCSYFLGLLIPAHIFIPVFYRLHLTSAYEYLELRFNKAVRICGTVTFIFQMVVYMGVALYAPSLALNAVTGFDLWLSVLALGIVCNIYTALGGLKAVIWTDVFQTLIMFLGQLVVIIVGAAKVGGLGHVWAVASQHGLISGIELDPDPFVRHTFWTLAFGGVFMMLSLYGVNQAQVQRYLSSHSEKAAVLSCYAVFPCQQVALCMSCLIGLVMFAYYKKYSMSPQQEQAAPDQLVLYFVMDLLKDMPGLPGLFVACLFSGSLSTISSAFNSLATVTMEDLIQPWFPQLTETRAIMLSRSLAFAYGLVCLGMAYVSSHLGSVLQAALSIFGMVGGPLLGLFCLGMFFPCANPLGAIVGLLTGLTMAFWIGIGSIVSRMSSAAASPPLNGSSSFLPSNLTVATVTTLMPSTLSKPTGLQQFYSLSYLWYSAHNSTTVIAVGLIVSLLTGGMRGRSLNPGTIYPVLPKLLALLPLSCQKRLCWRSHNQDIPVVTNLFPEKMGNGALQDSRDKERMAEDGLVHQPCSPTYIVQETSL
Protein: Ankyrin 2 (A0A5F9ZHA1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKELTEELGELEASSDEEAMVTTRVVRRRVIIQGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE
Protein: Serine/threonine kinase 24 (H0Y630)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
XKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRWKAEQSHDDSSSEDSDAETDGQASGGSDSGDWIFTIREKDPKNLENGALQPSDLDRNKMKDIPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQRSIHGNQAPPDCHLAQVQAFGGSGCVLGSRSV