wanglab/gogpt-training-data huggingface dataset:
Protein: Regulator of nonsense transcripts 1 (EC 3.6.4.-) (ATP-dependent helicase RENT1) (Nonsense mRNA reducing factor 1) (NORF1) (Up-frameshift suppressor 1 homolog) (F1RCY6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. The formation of an upf1-upf2-upf3 surveillance complex is believed to activate NMD.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9EPU0}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q92900}. Nucleus {ECO:0000250|UniProtKB:Q92900}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9EPU0}.
Interaction partners:
- Uncharacterized protein.
- Nonsense-mediated mRNA decay factor SMG5
- SMG7 nonsense mediated mRNA decay factor.
- Telomerase-binding protein EST1A
- Serine/threonine-protein kinase SMG1
- Regulator of nonsense transcripts 3B
- Regulator of nonsense transcripts 3A
- Protein CASC3
- Eukaryotic initiation factor 4A-III
- RNA-binding protein 8A
Sequence:
MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTQGQTQSQLDNQVNGPDGVLPNGEDAVGKTSQLLAELNFEEDEEDTYYTKDLPVHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKENPTATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKRIAYFTLPKTDSGDMRLMQGDEICLRYKGDMAPLWKGIGHVIKVPDNYGDEIAIELRSSAGAPVEVPHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSSDEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRLKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTRLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLNYYKEQKVLVEGPLNNLRESLMQFSKPRKLVNTINPGARFMSTAMYDAREAMIPGSVYDRSSTGRPSNMYFQTHDQVGMIGTGPNPMGSLNIPIPFNLVMPPMPPPGYLGQVNGPAAGRGAPKGKTGGRGGRQRNRGTGNHGSGQPNMPNSQASQDLVSQPFSQGPLTQGYITMSQPSQMSQPGLSQPELSQDSYLGDEFKSQMDVALSQDSTYQGERAYQHGGVTGLSQY
Protein: Acid phosphatase (Q59UY6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Phytase PHO112
- Bifunctional hydroxyethylthiazole kinase/thiamine-phosphate diphosphorylase
- Thiamine pyrophosphokinase
- Trifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase/thiaminase
- Alkaline phosphatase
- Alkaline phosphatase
- Riboflavin synthase
- FAD synthase
- Riboflavin kinase
- Tyrosine protein phosphatase
Sequence:
MVSVSKLLNNGLLLTGQSVFQDVATPQQASVQQYNIVNFLGGSAPYIQRNGYGISTDIPAGCEIAQIQLYSRHGERYPSKSNGKSLEAIYAKFENYKGTFKGDLAFLNDYTYFVTDKNNYEKETSPKNSEGTYAGTTNALRHGAAFRAKYGSLYKENSTLPVFSSNSGRCYQTSRYFARGFLGDDFEEGKTVKFNIISEDADVGANSLTPRSACSKNKESSSSTAKKYNTTYLNAIAERLVKPNPGLNLTTSDVSNLFGWCAYEINVRGSSPFCDLFTNEEFIKYSYGNDLSNYYSNGAGNNYTRIIGSVILNSSLELLKDTKNSNQVWLSFAHDTDLEIFHSALGLLEPAEDLPTSYIPFPNPYVHSSIVPQGARIYTEKLQCGNDAYVRYIINDAVVPIPKCATGPGFSCKLDDFENFVKERIGDVDFVKQCGVNSTYPSELTFYWDYKNVTYNAPLGDF
Protein: Large ribosomal subunit protein mL43 (54S ribosomal protein L51, mitochondrial) (Q9UUC8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS2m
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL34m
- Large ribosomal subunit protein mL44
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL36m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein mL41
Sequence:
MMIEIIPKISIPKNGLGSFTRPCRRIEFSYCNWGGSSKGMKEFLSTKLESLAKESQDVEFHVTNRQGKHPLIRAYYNTGREKVICTRKMSASSIFQKAILCRDSDGLKPRLIKYPVESTNPSVRGIWSPFSDQAKPHEIYKKKSP
Protein: Putative cyclin-D7-1 (G1/S-specific cyclin-D7-1) (CycD7;1) (Q9LZM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Retinoblastoma-related protein 1
- Cyclin-dependent kinase A-1
- Cyclin-dependent kinase B1-1
- Cyclin-dependent protein kinase inhibitor SMR4
- Cyclin-dependent kinases regulatory subunit 2
- Transcription factor MUTE
- Transcription factor FAMA
- Transcription factor SPEECHLESS
- Cyclin-dependent kinases regulatory subunit 1
- Cyclin-dependent protein kinase inhibitor SMR8
Sequence:
MDNLLCEESWPASPLTPEPLPNFRHRSHDNDVVKMYPEIDAATMEEAIAMDLEKELCFNNHGDKFVEFFVSKKLTDYRFHAFQWLIQTRSRLNLSYETVFSAANCFDRFVYMTCCDEWTNWMVELVAVTSLSIASKFNEVTTPLLEELEMEGLTHMFHVNTVAQMELIILKALEWRVNAVTSYTFSQTLVSKIGMVGDHMIMNRITNHLLDVICDLKMLQYPPSVVATAAIWILMEDKVCRESIMNLFEQNHKEKIVKCVDGMKNRDIDHQSSRRRYSEGRSILSLLQRGDVMNMNGDYNVEDLSKIFQIFRYEKKKRDRGNHQDNIRPAKRMTIEMSNYI
Protein: Uncharacterized protein (Q38A45)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTVCLVLLTGLPGAGKTTLGKALKQLGDHITHELSLIVTAVVELDDFMCNVGASNGSRVESTVFDPSRWREAFEAARQATRQELERCLMMERNKAVMHLVFLVDPLPYRSMRASYWKMCKELSAKCAETHFHDSWEVQSIVVLLEVRMNTPEEVCLQRNELRAGTPQYIPPYVIKGISDSFDRGDLTAVLPGTDGNMWAVLPGQRSAPWPVLLLVDEVRCCASPPNLLATQLLERIRGEDIMREMTEQQVSVFNYYKCQVEGGKSKCLASGEAHDNVNNCLHQVDLHMRAVVGHYMVQRQSIGSLKPGTGQRVSKCRSTHYAGIRAAITKGTRNTGGSFSEVQGLLQQLLLEFEHALVDL
Protein: Phosphodiesterase (EC 3.1.4.-) (B1AWD0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKEQGGTVSGAASSRGGGDSAMASLQPLQPNYLSVCLFPEESYQKLAMETLEELDWCLDQLETIQTYRSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKKKQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSHNRPLTCIMYAIFQERDLLKTFKISSDTFVTYMMTLEDHYHSDVAYHNSLHAADVAQSTHVLLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEEHCDIFQNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTSSGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSPSPPLDERSRDCQGLMEKFQFELTLEEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLEETDIDIATEDKSPIDT
Protein: Filamin-A-interacting protein 1 (FILIP) (Q8K4T4)
Organism: Rattus norvegicus (Rat)
Function: By acting through a filamin-A/F-actin axis, it controls the start of neocortical cell migration from the ventricular zone. May be able to induce the degradation of Filamin A.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12055638, ECO:0000269|PubMed:15794127}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12055638}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:12055638}. Note=Localized along actin stress fibers, except at their ends, suggesting colocalization with F-actin (fiber-like). {ECO:0000269|PubMed:12055638}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12055638}. Note=Punctate distribution in the cytoplasm distinct from that of F-actin. {ECO:0000269|PubMed:12055638}.
Interaction partners:
- Filamin, alpha
- Ras homolog family member D
Sequence:
MRSRNQGGESSSNGHVSCPKSSIISSDGGKGPSEDAKKNKANRKEEDVMASGTIKRHLKPSGESEKKTKKSVELSKEDLIQLLSIMEGELQAREDVIHMLRTEKTKPEVLEAHYGSAEPEKVLRVLHRDAILAQEKSIGEDVYEKPISELDRLEEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKENAKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAVTYKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLSQRIEELEETNKSLQKAEEELQELREKIAKGECGNSSLMAEVESLRKRVLEMEGKDEEITKTEAQCRELKKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFSRSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKEYSLTKERDELMGKLRSEEERSCELSCSVDLLKKRLDGIEEVEREINRGRSCKGSEFTCPEDNKIRELTLEIERLKKRLQQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQMAKHKAIEKGEAVSQEAELRHRFRLEEAKSRDLQAEVQALKEKIHELMNKEDQLSQLQVDYSVLQQRFMEEETKNKNMGREVLNLTKELELSKRYSRALRPSGNGRRMVDVPVASTGVQTEAVCGDAAEEETPAVFIRKSFQEENHIMSNLRQVGLKKPMERSSVLDRYPPAANELTMRKSWIPWMRKRENGPSTPQEKGPRPNQGAGHPGELVLAPKQGQPLHIRVTPDHENSTATLEITSPTSEEFFSSTTVIPTLGNQKPRITIIPSPNVMSQKPKSADPTLGPERAMSPVTITTISREKSPEGGRSAFADRPASPIQIMTVSTSAAPTEIAVSPESQEVPMGRTILKVTPEKQTVPAPVRKYNSNANIITTEDNKIHIHLGSQFKRSPGPAAEGVSPVITVRPVNVTAEKEVSTGTVLRSPRNHLSSRPGASKVTSTITITPVTTSSTRGTQSVSGQDGSSQRPTPTRIPMSKGMKAGKPVVAASGAGNLTKFQPRAETQSMKIELKKSAASSTASLGGGKG
Protein: Dormancy-associated protein homolog 1 (Auxin-repressed protein 1) (AtARP1) (DRM1 homolog 1) (Dormancy-associated protein 2) (AtDRM2) (P93017)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable inactive DNA
- Leucine-rich repeat protein kinase family protein
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- AT4G23670 protein
- tRNA
Sequence:
MWDETVAGPKPEHGLGRLRNKITTQPLDIKGVGEGSSSKTVAAVAGSPGTPTTPGSARKENVWRSVFHPGSNIATRGMGTNLFDKPSHPNSPTVYDWLYSDDTRSKHR
Protein: Replication protein A 32 kDa subunit-A (RP-A p32) (Replication factor A protein 2) (RF-A protein 2) (Replication protein A 34 kDa subunit) (RP-A p34) (Q6IP18)
Organism: Xenopus laevis (African clawed frog)
Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage.
Subcellular location: Nucleus {ECO:0000269|PubMed:23047005}. Nucleus, PML body {ECO:0000250}. Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner. {ECO:0000250}.
Interaction partners:
Sequence:
MWNNHGGFDGGYGGSGMGGGGGYMQSPGGFGSPAPTQGEKKSRSRSQQIVPCTVSQLLSATQNDEVFRIGEAELSQVTIVGIVRHAEKAPTNILYKVDDMTAAPMDVRQWVDTDEASCENMVVPPGSYVKVAGHLRSFQNKKSVVAFKIAPVEDMNEFVSHMLEVVHAHMAMNSQGAPSGGGSTVALSTPGRVGDSGRAFSGGNDNPTNGLTPHQSQILSLIKSCKGNEGMAFEELKNRLHGMNVNTIRQAVEFLSNEGHIYSTIDDEHYKCTDGD
Protein: Sulfide quinone oxidoreductase (B0BMT9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Ethylmalonic encephalopathy 1
- Thiosulfate sulfurtransferase
- Methanethiol oxidase
- Sulfite oxidase, mitochondrial
- D-amino-acid oxidase
- Ferredoxin-2, mitochondrial
Sequence:
MAPLVAVVSSPRARLFACFLRLGTQQAGPLQLHTGACCTAKNHYEVLVLGGGSGGITMATRMKRRVGAENVAIVEPSERHFYQPIWTLVGAGAKELSSSDRSTLSVIPSGVQWIQDRVAELNPDQNCIRTDNGKEISYRYLIIALGIQLDYEKIKGLPEGFAYPKIGSNYSVKTVEKTWKALQDFKEGNALFTFPNTPVKCAGAPQKIMYLSEAYFRKTGKRSKANIIFNTALGTIFGVKKYADALQEIIRERNVSVNYKHNLIEVRADKQEAVFENLDKPGETHVIHYEMLHVTPPMSSPDVLKRSPVADSAGWVDVDKETLQHKKYPNVFGIGDCTNLPTSKTAAAVAAQSGILDRTISLIMKNQTPTKKYDGYTSCPLVTGYNRVILAEFDYTAQPLETFPFDQSKERISMYLMKADMMPFLYWNMMLRGYWGGPAFLRKLFHLGLS
Protein: Always early (Q2PNN4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRHQLKKPRKMVAAWQNDELFIKRPNFAPRIRISEKPEIQGRVKPGVASKRTENFTKKPSNISVDVSEDEKAKEKEKEQDPYSNDFILGKRLYNFLKYLSSHRWIWCEFVDSFLDKPTLTMGYDMKRFIAEYCPLLHSCFMPRRGWQLVRRNMGKARRFSAAFIELEREELECQRRIVRQLQQHKFNPKENVGYLDQIPKRVPLPLAKDATVSSFLHGKSFEGIVNGTVMGYDPQDYTYLVRFNRNDNAVVLSLPDSQLYSDEETAAVPLSIIMRGNKSSSVISESAKTEKFGNKRYTKELLESVLRVGKLQDVKHKILMDLARMNEDFETFKEIGSSSSRRDAKVTPQRENLQRRYSASMITLHRVNADILEPLRILHDYLVEYQKQDEEEESKRGRPASEVYQKCRMQAEQDLKTAADEKFLKIESDRTQEFVRNLHTILYLNGKLGRENSSNLETIIADLVTHMVDNIQPSLGRKLKDGVDSLEPLRQQVVQIFKDVKKPERFQITQQAPMQTEDGIYNFVVEAQPDTPS
Protein: Kelch-like protein 8 (G5ED84)
Organism: Caenorhabditis elegans
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates degradation of glutamate receptors in neurons. The BCR(kel-8) ubiquitin ligase complex mediates ubiquitination and subsequent degradation of rpy-1. Indirectly regulates the protein turnover of glr-1, possibly via ubiquitination and degradation of rpy-1.
Subcellular location: Synapse {ECO:0000269|PubMed:16394099}. Note=Localizes to postsynaptic clusters.
Interaction partners:
- Cullin-3
- F-box/WD repeat-containing protein lin-23
- Glutamate receptor 1
- E3 ubiquitin-protein ligase rpm-1
Sequence:
MPVYAKAIFGSFPSVQQVRVENGERCLIEAMDELNKNEKGLYRPVRLENGDQISTTDDVLNGKLARVSYTPFEEFELVSNSKGSCMEYENQEQSSKIMEQMRILRQTEELCDVELLVAGSVIRAHRYILAAASPYFKAMFTNGMVEMKKLTIELQDIPEESVRIIVDYIYTDKIAITMNNVHQLIFTATVLQMDVIVVACQQFLATMITSHNCMSLYHFSDIYNCTNLISSIEDFASSQFRCIRKSPEFNSISFHHLKSLLNRSDLNVSEEQDVFETIVQWVSSNPRDRQHHFVQLFKTLRLHLVGWNFLCEAVNSNSYVKNSQECREIISAMVLDAMTPSKRKHPESNHENTSEYSASMACPSLTASSSSSTSTFRKSVAGAIFCAGGRGKAGGPFSSVEAYDWRRNQWIEVPDMMSQRRHVGVVSANGNLYAIGGHDGTAHLATAEAFQPSIRQWKRIASMKTARRGIAVASIENVIYAVGGLDDTTCYKTVERYDIEEDEWSTVADMDVQRGGVGVAVIGRYLFAIGGNDGTSSLETCERFDPMIDKWKRIASMKNRRAGSGVCVLDGYLYAIGGFDDNAPLETCERYDPDADKWITLDKMSSPRGGVGVAALGGKVYAIGGHDGSDYLNTVECYDPIANRWQPAAEIKECRAGAGVAWANVRMHQLSRTPEKCDSGCAPSGGSYCI
Protein: Fibrinogen alpha chain isoform 2 (A0A0S2Z3E8)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTLNLALSEVSTLLLWGSLPCPPRLS
Protein: Zinc finger protein 420 (Q8TAQ5)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Serine-protein kinase ATM
- p53-regulated apoptosis-inducing protein 1
- Cellular tumor antigen p53
Sequence:
MARKLVMFRDVAIDFSQEEWECLDSAQRDLYRDVMLENYSNLVSLDLPSRCASKDLSPEKNTYETELSQWEMSDRLENCDLEESNSRDYLEAKGKMEKQQENQKEYFRQGMIIYDKMSIFNQHTYLSQHSRCHSTEKPYKCKECGKAFRRASHLTQHQSIHTGEKPYECKQCGKAFSRDSQLSLHQRLHTGEKPYACKECGKAFTQSSQLILHHRIHTGEKPYKCEECGKAFIRSSQLTRHQKVHTGEKPYECKECGKAFTQNSQLTLHQRLHTGEKLYECKECRKVFTQLSQLILHKRIHTGEKPYECKECGKAFICGSQLSQHQKIHNGEKPYECKECGRAFIRGSLLMQHQRIHTGEKPYKCEECGKAFIRGSQLTQHQRIHTNEKPYECKECGKMFSHGSQLTQHQRIHTGEKPYQCKECGKAFNRGSLLTRHQRIHTGEKPYECKECGKTFSRGSELTQHERIHTGEKPYECKECGKSFIRGSQLTQHQRIHTGEKPYECKECRMAFTQSSHLSQHQRLHTGEKPYVCNECGKAFARGLLLIQHQRIHTGEKPYQCKECGKAFIRGSQLTQHQRIHTGEKPYECKECGKAFSHGSQLTLHQRIHTGEKPYECRECRKAFTQSSHLSRHQRIHTGEKPYQCKECGKAFTRGSQLTQHQRIHISEKSFEYKECGIDFSHGSQVYM
Protein: serralysin (EC 3.4.24.40) (E0SC30)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Alkaline protease secretion ATP-binding protein aprD
- Membrane fusion protein
- Outer membrane exporter of proteases
- Alkaline proteinase inhibitor
Sequence:
MQQNEKASLNTSAAAAKAGSYTGYADVYDFWYYHQRGDGLTVNGKPSYTTDKAVSEGLTRPHTTWNGDNVFGKAANLTYSFLNTFSSTPNGHTGPVKFTPVQMQQAKLSLQSWADAANLTFTEVSPNQKANITFANYTRNADGSLNTDTQAYAAYPGTHPVSGSAWFNYNQSSIRNPDTDEYGRHSFTHEIGHALGLSHPAEYNAGEGDISYKNSAAYAEDSRQFSIMSYWEVENTGGDFKGHYSAGPLMDDIAAIQKLYGANMTTRTGDTVYGFNSNTDRDFYTATNSSKALVFSVWDAGGNDTFDFSGYSNNQRINLNEGSFSDVGGLKGNVSIAHGVTIENAIGGSGNDILIGNGADNILQGGAGDDVLYGSTGADTLTGGAGRDIFVYGSGQDSTVSAYDWITDFQTGIDKIDLSAFRNEGQLSFVQDQFTGKGQEVMLQWDAANSTTNLWLHEAGHSSVDFLVRIVGQTAQSDIIV
Protein: Vitamin K epoxide reductase complex subunit 1-like protein 1 (VKORC1-like protein 1) (EC 1.17.4.4) (Q8N0U8)
Organism: Homo sapiens (Human)
Function: Involved in vitamin K metabolism. Can reduce inactive vitamin K 2,3-epoxide to active vitamin K, and may contribute to vitamin K-mediated protection against oxidative stress. Plays a role in vitamin K-dependent gamma-carboxylation of Glu residues in target proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:24532791}; Multi-pass membrane protein {ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:24532791}.
Interaction partners:
- Vitamin K-dependent gamma-carboxylase
- Vitamin K epoxide reductase complex subunit 1
- NAD
Sequence:
MAAPVLLRVSVPRWERVARYAVCAAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLLGSIFGKDGVLNQPNSVFGLIFYILQLLLGMTASAVAALILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLIINYKRLVYLNEAWKRQLQPKQD
Protein: TNF receptor-associated factor 1 (P39428)
Organism: Mus musculus (Mouse)
Function: Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- TNF receptor-associated factor 2
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Baculoviral IAP repeat-containing protein 3
- Baculoviral IAP repeat-containing protein 2
- Tumor necrosis factor receptor superfamily member 1A
- Receptor-interacting serine/threonine-protein kinase 1
- Tumor necrosis factor
- Tumor necrosis factor receptor superfamily member 9
- TNF receptor-associated factor 3
- Caspase-8
Sequence:
MASSSAPDENEFQFGCPPAPCQDPSEPRVLCCTACLSENLRDDEDRICPKCRADNLHPVSPGSPLTQEKVHSDVAEAEIMCPFAGVGCSFKGSPQSMQEHEATSQSSHLYLLLAVLKEWKSSPGSNLGSAPMALERNLSELQLQAAVEATGDLEVDCYRAPCCESQEELALQHLVKEKLLAQLEEKLRVFANIVAVLNKEVEASHLALAASIHQSQLDREHILSLEQRVVELQQTLAQKDQVLGKLEHSLRLMEEASFDGTFLWKITNVTKRCHESVCGRTVSLFSPAFYTAKYGYKLCLRLYLNGDGSGKKTHLSLFIVIMRGEYDALLPWPFRNKVTFMLLDQNNREHAIDAFRPDLSSASFQRPQSETNVASGCPLFFPLSKLQSPKHAYVKDDTMFLKCIVDTSA
Protein: Keratin-associated protein 13-1 (High sulfur keratin-associated protein 13.1) (Q8IUC0)
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 7-1
- Keratin-associated protein 8-1
- Keratin-associated protein 3-1
- Keratin-associated protein 20-2
- Keratin-associated protein 24-1
- Keratin-associated protein 20-1
- Keratin-associated protein 6-2
Sequence:
MSYNCCSGNFSSRSCGGYLHYPASSCGFSYPSNQVYSTDLCSPSTCQLGSSLYRGCQQTCWEPTSCQTSYVESSPCQTSCYRPRTSLLCSPCQTTYSGSLGFGSSSCRSLGYGSRSCYSVGCGSSGFRSLGYGGCGFPSLGYGVGFCRPTYLASRSCQSSCYRPTCGSGFYY
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (P50097)
Organism: Tritrichomonas foetus (Trichomonas foetus) (Tritrichomonas suis)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}.
Interaction partners:
Sequence:
MAKYYNEPCHTFNEYLLIPGLSTVDCIPSNVNLSTPLVKFQKGQQSEINLKIPLVSAIMQSVSGEKMAIALAREGGISFIFGSQSIESQAAMVHAVKNFKAGFVVSDSNVKPDQTFADVLAISQRTTHNTVAVTDDGTPHGVLLGLVTQRDYPIDLTQTETKVSDMMTPFSKLVTAHQDTKLSEANKIIWEKKLNALPIIDDDQHLRYIVFRKDYDRSQVCHNELVDSQKRYLVGAGINTRDFRERVPALVEAGADVLCIDSSDGFSEWQKITIGWIREKYGDKVKVGAGNIVDGEGFRYLADAGADFIKIGIGGGSICITREQKGIGRGQATAVIDVVAERNKYFEETGIYIPVCSDGGIVYDYHMTLALAMGADFIMLGRYFARFEESPTRKVTINGSVMKEYWGEGSSRARNWQRYDLGGKQKLSFEEGVDSYVPYAGKLKDNVEASLNKVKSTMCNCGALTIPQLQSKAKITLVSSVSIVEGGAHDVIVKDRINDYHPK
Protein: mannose-1-phosphate guanylyltransferase (EC 2.7.7.13) (Q9HTB7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- GDP-mannose 4,6-dehydratase
- ABC subunit of A-band LPS efflux transporter
- Glycosyltransferase WbpX
- Transport permease protein
- Glycosyltransferase WbpY
- Phosphomannomutase/phosphoglucomutase
- GDP-6-deoxy-D-mannose reductase
- D-rhamnosyltransferase WbpZ
- PslA
- Glucose-6-phosphate isomerase
Sequence:
MLIPVVLSGGAGTRLWPVSREGQPKPFMRLPDGQTLLGKTYRRAAGLLAGHGEIVTVTNREHYFQSKDQFHAARLGRHRGHFILEPTGRNTAPAIAVAALALQAEHGDAAVLVVMPADHLIRNEEAFREAVGHAARLAVAGHLVTFGVVPDAAETGFGYIELGDRLDEQGAAKVRRFVEKPDEETARRYVESGGFLWNSGMFCFTASTLVDELAQHAPALLEQARACLAASAAVKMADGIQHELAGEAFAALPDISIDYALMERSARVAVVPAAFDWSDIGSWGAMSALLDADAEGNRGSGDTLFVDTRNTFVQSDGRLVATVGVDDLVVVDTSDALLIARADRVQEVRRVVQRLKDERHEAYRLHRTVNRPWGSYTVLEEGPRFKIKRIVVRPGERLSLQMHHHRSEHWIVVQGMARVTNGDGARLVNSNESTYIPAGHRHRLENPGVIDLVMIEVQSGEYLGEDDIVRFEDQYGRVV
Protein: ANK_REP_REGION domain-containing protein (H2KYL3)
Organism: Caenorhabditis elegans
Interaction partners:
- Dynein regulatory complex subunit 7
- Nuclear exosome regulator NRDE2
- Nuclear RNAi defective-3 protein
- Argonaute protein hrde-1
- SET domain-containing protein
- Chromo domain-containing protein.
- Histone-lysine N-methyltransferase set-25
Sequence:
MNTRQRVQSQQNERNDEAVLLNSLRNVTLRNVEKFASVKLPKEQNKRNQSENAKLRKKQADKDSRERREIESLRERERHVEMCGSSGPEKYIVPISHFDLSRPTDRPMETVIEESVLSRRRAEEARNEQKHNEPLIDSNRKPIKLNIQAFKHGLHKSARQSNADEKLLLDNEHWMNLDNINSDDHKCPDGYFEPDTGQVLTMNVYRCPFVQAVIYSNSDRFFDLVIKNMNTIGRFCNQSCFCKQGRKNNLPHDKSNLLHFAAAYSTREFLERVTLEKFYRREIERRLRKQPKVDQTTVNFWISHYRDTIDQYQKDPHGNERLIPSEVAAEEGRLDIVEVFLETSLSKSLANLKASATSKYCSFLQYRHWCYGSLLSRLVENGILHELSEKHLLRVFAYITTDNFLHAADTALAKGYGEALDILERLGVGFKSVYASKQYTQYSDPNTRNNDIPGIISSDGNELFKRCDSSQPAHILAQYGHFKLFDKLTVEEKNDTDFHRVSALIELLEFSDDEVRSQLRFFRNIRRDNIFLFISQVIIRNRIGLLEDALQLAFTNSNNFTPINTRKLIYKDYGTPEHIALPMETALQRTGNMDTVEQIAKYYTKTDRHARKMIEEDALRCIRSIQNRARVCTEHLRLSIIFMMIKFVDPFSPKFRNILRMYLDQAMNDNVSQYVLKSFSMIRSKRFLSKQSFVTWSTAVNEAFQIVSQWNGSLEEADFVPKFLSETKKCGAQMFFPKQEFRSLLLTEEKRTEKKKYQAERRPRTEDDVMSKLAKAIEDFENLNL
Protein: Hydroxymethylglutaryl-CoA lyase, mitochondrial (HL) (HMG-CoA lyase) (EC 4.1.3.4) (3-hydroxy-3-methylglutarate-CoA lyase) (P38060)
Organism: Mus musculus (Mouse)
Function: Mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase that catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in ketogenesis. Terminal step in leucine catabolism. Ketone bodies (beta-hydroxybutyrate, acetoacetate and acetone) are essential as an alternative source of energy to glucose, as lipid precursors and as regulators of metabolism.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:7527399}. Peroxisome {ECO:0000269|PubMed:7527399}. Note=Unprocessed form is peroxisomal.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial
- D-beta-hydroxybutyrate dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Trifunctional enzyme subunit beta, mitochondrial
- Methylglutaconyl-CoA hydratase, mitochondrial
- 3-ketoacyl-CoA thiolase A, peroxisomal
Sequence:
MASVRKAFPRRLVGLTSLRAVSTSSMGTLPKQVKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKWVPQMADHSDVLKGIQKFPGINYPVLTPNMKGFEEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCPYEGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGCPYAKGASGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQALNRKTSSKVAQATCKL