wanglab/gogpt-training-data huggingface dataset:
Protein: Kallikrein-7 (hK7) (EC 3.4.21.117) (Serine protease 6) (Stratum corneum chymotryptic enzyme) (hSCCE) (P49862)
Organism: Homo sapiens (Human)
Function: May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines.
Subcellular location: Secreted {ECO:0000269|PubMed:12738725}. Note=In ovarian carcinoma, secreted and also observed at the apical membrane and in cytoplasm at the invasive front.
Interaction partners:
- Serine protease inhibitor Kazal-type 5
- Corneodesmosin
- Desmoglein-1
- Alpha-2-macroglobulin-like protein 1
- Filaggrin
- Filaggrin-2
- Cadherin-1
- Kallikrein-5
- Kallikrein-8
- Kallikrein-10
Sequence:
MARSLLLPLQILLLSLALETAGEEAQGDKIIDGAPCARGSHPWQVALLSGNQLHCGGVLVNERWVLTAAHCKMNEYTVHLGSDTLGDRRAQRIKASKSFRHPGYSTQTHVNDLMLVKLNSQARLSSMVKKVRLPSRCEPPGTTCTVSGWGTTTSPDVTFPSDLMCVDVKLISPQDCTKVYKDLLENSMLCAGIPDSKKNACNGDSGGPLVCRGTLQGLVSWGTFPCGQPNDPGVYTQVCKFTKWINDTMKKHR
Protein: Proteasome assembly chaperone 1 (PAC-1) (Chromosome 21 leucine-rich protein) (C21-LRP) (Down syndrome critical region protein 2) (Proteasome chaperone homolog 1) (Pba1) (O95456)
Organism: Homo sapiens (Human)
Function: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization.
Subcellular location: Cytoplasm. Endoplasmic reticulum.
Interaction partners:
- Proteasome assembly chaperone 2
- Proteasome maturation protein
- Proteasome subunit alpha type-1
- DnaJ homolog subfamily C member 9
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit theta
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-5
- T-complex protein 1 subunit eta
Sequence:
MAATFFGEVVKAPCRAGTEDEEEEEEGRRETPEDREVRLQLARKREVRLLRRQTKTSLEVSLLEKYPCSKFIIAIGNNAVAFLSSFVMNSGVWEEVGCAKLWNEWCRTTDTTHLSSTEAFCVFYHLKSNPSVFLCQCSCYVAEDQQYQWLEKVFGSCPRKNMQITILTCRHVTDYKTSESTGSLPSPFLRALKTQNFKDSACCPLLEQPNIVHDLPAAVLSYCQVWKIPAILYLCYTDVMKLDLITVEAFKPILSTRSLKGLVKNIPQSTEILKKLMTTNEIQSNIYT
Protein: Autoinducer repressor protein LuxO (Q5E6B4)
Organism: Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri)
Interaction partners:
- Autoinducer phosphorelay protein LuxU
- RNA polymerase sigma-54 factor
- Sigma-54 dependent transcriptional regulator
- Autoinducer 2 sensor kinase/phosphatase LuxQ
- S-ribosylhomocysteine lyase
- Autoinducer 2-binding periplasmic protein LuxP
- histidine kinase
- Quorum sensing transcriptional regulator LitR
- RNA-binding protein Hfq
- acyl-homoserine-lactone synthase
Sequence:
MIQKKYLLMVEDTASVAALYRSYLNPLGFDIDVVAKGVEAIEKIKLRTPDLVLLDLRLPDMTGFDVLAEIRKDNQSIPVVLMTAHGSIDAAVEAMQLGAQDFLIKPCEADRLRVTVNNALRRAQKDQKEFQENPKDTNKQYQGFIGSSSQMHQVYRTIDSAAPSKATVFITGESGTGKEVCAEAIHAASKRGDGPFIAINCAAIPKDLIESELFGHVKGAFTGASVDRKGAAEQADGGTLFLDELCEMDLDLQTKLLRFIQTGTFQKVGSSKMSRVDVRFVCATNRDPWLEVQAGRFREDLYYRLHVIPLTLPPLRDRGNDIIEIGHSILGHFSHEEGREFITFSPEVVDRFLNYDWPGNVRQLQNVIRNVVVLNKGKEVELSMLPPPLSLDSKSGVNIASNVSISDSTKPTESILPSNRILDSKDQETIIPLWQSEKQIIENAIELCGGNIPQAAKQLEVSPSTIYRKLQSWNER
Protein: Candida glabrata strain CBS138 chromosome I complete sequence (Q6FQP8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
- Glutamyl-tRNA
- Candida glabrata strain CBS138 chromosome H complete sequence
Sequence:
MFNRRFAKLVKLVLITVSIVGGLYYLSGFIDGDTSTALGNRLSQEYMDSFWKTYDSSKSSYGSSLLGGSGEKGETDFRSPEAKLKIKDFYKTVFEHILDYSPAGKTAREFDDSCFDSGDISTRPDSYKNWKKLSYHQLSHCMKISPSEINHLRGNHKSYVDKINELVLPKGSYKGEGIVTVGGGKFTLMALTMIKALRTLGTTLPVEVFIPPDEGESTFCESVLPQYNAKCIYISDILPDDMIQKFTFKGYQFKSLAMITSSFENLLLLDADNIPVKKIDHIFESQIFRSAGLILWPDFWRRTTMPAYYEIANLPYNQNKRVRNAFDDITPPEVYTKPDGDLSEVPFHDMEGTLPDPSTESGQLLISKAKHLPTLLLSLYYNVNGPNWYYPIFSQRTAGEGDKETFISAASFYSLSYYQVKTSVGVDGYFRHDGSGYRGVGMLQHDFIQDSKQYMEAFEYSNTKYNNLRSEKGSISYDPSYDPNEFFDKFFSRKKPDGGDESKADVMFVHCNLPKFDPYVSWDTNDLVYQTKHFRSFNNKKVIAQFDIELENFKFFNETLCPYENGKGKFKYLDNKLSEERWPQMCDYISKRLQYLKESHNEALGLEKATEA
Protein: 4-aminobutyrate aminotransferase, mitochondrial (beta-AlaAT I) (EC 2.6.1.19) ((S)-3-amino-2-methylpropionate transaminase) (EC 2.6.1.22) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (GABA-T) (L-AIBAT) [Cleaved into: 4-aminobutyrate aminotransferase, brain isoform; 4-aminobutyrate aminotransferase, liver isoform] (P50554)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:10447691}.
Interaction partners:
- Succinate-semialdehyde dehydrogenase, mitochondrial
- Glutamate decarboxylase 2
- Glutamate decarboxylase 1
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
- Aldehyde dehydrogenase
- Alpha-aminoadipic semialdehyde dehydrogenase
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Beta-Ala-His dipeptidase
Sequence:
MAFLLTTRRLVCSSQKNLHLFTPGSRYISQAAAKVDFEFDYDGPLMKTEVPGPRSQELMKQLNTIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYNHPALAKLVQQPQNASTFINRPALGILPPENFVDKLRESLMSVAPKGMCQLITMACGSCSNENAFKTIFMWYRSKERGQRGFSKEELETCMVNQSPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVTDNQQEEARCLEEVEDLIVKYRKKKRTVAGIIVEPIQSEGGDNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMSFSKKMMTGGFFHKEEFRPSAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNVAHAGKTLLTGLLDLQAQYPQFVSRVRGRGTFCSFDTPDEAIRNKLILIARNKGVVLGGCGDKSIRFRPTLVFRDHHAHLFLNIFSGILADFK
Protein: V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (V-ATPase 69 kDa subunit) (Vacuolar H(+)-ATPase subunit A) (Vacuolar proton pump subunit alpha) (O23654)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17151019}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- V-type proton ATPase subunit d2
- V-type proton ATPase subunit F
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit a3
- V-type proton ATPase subunit a1
- V-type proton ATPase subunit d1
Sequence:
MPAFYGGKLTTFEDDEKESEYGYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIARISGDVYIPRGVSVPALDKDCLWEFQPNKFVEGDTITGGDLYATVFENTLMNHLVALPPDAMGKITYIAPAGQYSLKDTVIELEFQGIKKSYTMLQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEKFDPDFINIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERAAGMDGQKITYTLIKHRLGDLFYRLVSQKFEDPAEGEDTLVEKFKKLYDDLNAGFRALEDETR
Protein: Transmembrane channel-like protein (E7FDU7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU310713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU310713}.
Interaction partners:
- Si:dkey-15b23.3.
- Potassium voltage-gated channel, subfamily H
Sequence:
MRRMSVYPQHGTALENLGLTAHEIQQEVENNTSELVSDLSDLSAGARFQAIRSLPMSYNERKAIRNRVNNIKLSKTILPTDCRQQVSLSFRRFRASLTSARQRLVVWQDTLKEIGGRFGTSVLSYFLFLKWLLKFNVFSFVINFCFITIPQIVHAPNISHVTGFRGLELLTGVGYFNQTVLFYGGYDGEVIVSKPAYNMQLAYFFTIAAYMVLCGLSLIYSMSRSFQKNFVLETGPVSGGAWRLLCSWDFSVVNEKAIQYNKNNLGIQLKESLSERLQMKNKISLSDRIKHLSLNLVAWLLCLLLALGSGAGIYFLGTEQLTFSFNQDPNDLVSEASTLLLPVVVSLINLIVPLLYSLIGKMETYSNPRAKIYISIARNIILKMSLLGILCFYWLNFVPDKIPCWESFVGQSVYRLLIIDFIFCLLGIFFGEFLRNVIGTMCIQSLGVPEFDIARNVLDLIYAQTLAWIGIYFSPLLPVMQVLKLFIIFYLKKLSLSMNCQPPKHTGRAAQIQTVFIALLFFPSFVGALSMVAFTVWSLQPSDQCGPFQGLKTPFHTIFNWTDSIQGPPETHWVWWIFENVLRSELFYYLISLIVLVITFFLWQITQGRKQLIKSLREQIVNGGKDKAFLLNKLQNIQRQRREIASYSPQPIRRSMRGSVRTVAQEFDQTTYYNPNWINTLPMDM
Protein: DNA dC->dU-editing enzyme APOBEC-3H (EC 3.5.4.38) (APOBEC-related protein 10) (ARP-10) (Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3H) (A3H) (Q6NTF7)
Organism: Homo sapiens (Human)
Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. The A3H-var/haplotype 2 exhibits antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity also against T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21653666, ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:29290613}. Nucleus {ECO:0000269|PubMed:18779051, ECO:0000269|PubMed:21653666}. Cytoplasm, P-body {ECO:0000269|PubMed:22915799}. Note=Haplotype 1 is distributed in both the nucleus and cytoplasm, whereas haplotype 2 is predominantly cytoplasmic. {ECO:0000269|PubMed:21653666}.
Interaction partners:
- Putative C->U-editing enzyme APOBEC-4
- Cullin-5
- Cytidine deaminase
- Elongin-B
- Elongin-C
- RING-box protein 2
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- DNA dC->dU-editing enzyme APOBEC-3B
Sequence:
MALLTAETFRLQFNNKRRLRRPYYPRKALLCYQLTPQNGSTPTRGYFENKKKCHAEICFINEIKSMGLDETQCYQVTCYLTWSPCSSCAWELVDFIKAHDHLNLGIFASRLYYHWCKPQQKGLRLLCGSQVPVEVMGFPEFADCWENFVDHEKPLSFNPYKMLEELDKNSRAIKRRLERIKIPGVRAQGRYMDILCDAEV
Protein: Aclacinomycin 10-hydroxylase RdmB (EC 4.1.1.-) (15-demethoxy-epsilon-rhodomycin 10-hydroxylase) (SAM-dependent methyltransferase RdmB) (EC 2.1.1.-) (Q54527)
Organism: Streptomyces purpurascens
Function: Involved in the biosynthesis of the anthracycline aclacinomycin which is an aromatic polyketide antibiotic that exhibits high cytotoxicity and is widely applied in the chemotherapy of a variety of cancers. In vivo and in vitro, RdmB catalyzes the removal of the carboxylic group from the C-10 position of 15-demethoxyaclacinomycin T coupled to hydroxylation at the same C-10 position. It could also catalyze the removal of the carboxylic group at the C-10 position of 15-demethoxy-epsilon-rhodomycin coupled to hydroxylation at the same C-10 position to yield rhodomycin B. The reaction catalyzes by RdmB is intriguing, since the enzyme does not use any of the cofactors usually associated with hydroxylases such as flavins and/or metal ions to activate molecular oxygen.
Interaction partners:
Sequence:
MSSSSPGEPLEPTDQDLDVLLKNLGNLVTPMALRVAATLRLVDHLLAGADTLAGLADRTDTHPQALSRLVRHLTVVGVLEGGEKQGRPLRPTRLGMLLADGHPAQQRAWLDLNGAVSHADLAFTGLLDVVRTGRPAYAGRYGRPFWEDLSADVALADSFDALMSCDEDLAYEAPADAYDWSAVRHVLDVGGGNGGMLAAIALRAPHLRGTLVELAGPAERARRRFADAGLADRVTVAEGDFFKPLPVTADVVLLSFVLLNWSDEDALTILRGCVRALEPGGRLLVLDRADVEGDGADRFFSTLLDLRMLTFMGGRVRTRDEVVDLAGSAGLALASERTSGSTTLPFDFSILEFTAVSEEAAPAAQASEALPAQE
Protein: Kinesin, putative (Q57V46)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Calcium-transporting ATPase
- Calcium-transporting ATPase
Sequence:
MHDSVGTGTRVQVGVRIFPTRQGERSVVHGDPDDNHVVVIDGEGTKGGSALKFDRVFTGSQEEVYDFVGRPMLKEAFEGFNVCLFAYGQTGTGKTYSLFGDLNDKTRCGIAPRFAQAMIEEGQRRMEADNRATIRFSLTMVEVYMEKVRDLLAPRVRGQEPEALEIHEDNQRRVYVKGAGIHPVLSLDRLMELLSIGNANRQKGETKMNETSSRSHAIIQLTISQQHESLETKDVESVAMLVDLAGSERQSKAESTGLAFEEAKKINQSLLMLGRALNSFSDRKGNGGFISLRASKLTRLLSESFGGNSKTWMLATVSPSASNLTETISTLEYAQNASAITNKVRVNRAERRLNFEAIQSRVATLKEQLGCEAKVVSDLDVDIISARDEIQFLQNMLSCRCDFDVEVELREALEEREKLLLHLKSALGQDASSSVHAQPPLSCFYGTCKTSLGSIPLGGSEVETMVVQCYNLSGPPPLLICHVHIHLADENCVAVVVRIREILHLPDYVTGGAQVTMWFEGHSSSSVRTPIVGSNGGNPLFSLKQTYILGPHTKDIERFLRAEVLNFRVDGFILSECV
Protein: Glycogen [starch] synthase (EC 2.4.1.11) (A0A060XXJ7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Glycosyl hydrolase family 13 catalytic domain-containing protein
- Glycogenin-1
- Glycogenin-1
- Tc1-like transposase DDE domain-containing protein
- glycogenin glucosyltransferase
- Uncharacterized protein
- Cytoplasmic tRNA 2-thiolation protein 2
- DNA polymerase delta subunit 3
- Cytoplasmic tRNA 2-thiolation protein 2
- Cytoplasmic tRNA 2-thiolation protein 2
Sequence:
FFFATQPRRPASQSCLFTVDVETGVFLVLFNEAAMGGIYTVIQTKAKITVDEWGENLFMMGPYYEHNFNTQVEQCEPPNPAIKKAMGALIDNGCLVYFGRWLIEGSPYVILFDTGSAAWNLDRWKGDLWDTCGIGMPAHDREANDSLLFGSMVAWFFKELTDELGDSPNVLAHFHEWQVGAGLILCRSRKIPLATIFTTHATLLGRYICAGNVDFYNNLDKFNIDQEAGERQIYHRYCLERAAVHCAHVFTTVSQITAVEANHMLHRKPDVVTPNGLNIKKFSAMHEFQNLHSTNKGQIQEFIRGHFYGHLDFNLEKTLFFFIAGRYEFSNKGVDIFLESLSRLNYLLRVHKNDVTVVVFFIMPAKTNNFNVETLKGQAVRKQLWDTAHTVKDKFGKRLYEALLKGDIPDMNTILDRDDFTIMKRAIYATQRHTLPPVTTHNMLDDTSDPILANVRRIGLFNARTDRVKIVFHPEFLSSTSPLLPMDYEEFVRGCHLGVFPSYYEPWGYTPGECTVMGIPSVTTNLSGFGCFMEEHVSDPTAYGIYIVDRRFRSADDSCNQLTQFMFGFCQQSRRQRIIQRNRTERLSDLLDWRYLGRFYMHARSLALSRAFPDKFKMEPLAPPQTEGFRYPRPGSVPPSPSVSVHSTPHHSDEEDDEEPYDEDMEAERDRQNIKAPFTLGATPEGKKTHPGESAN
Protein: Deoxyguanosine kinase, mitochondrial (EC 2.7.1.113) (Deoxyadenosine kinase, mitochondrial) (EC 2.7.1.76) (Q16854)
Organism: Homo sapiens (Human)
Function: Phosphorylates deoxyguanosine and deoxyadenosine in the mitochondrial matrix, with the highest efficiency for deoxyguanosine. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on DGUOK and TK2. Phosphorylates certain nucleoside analogs (By similarity). Widely used as target of antiviral and chemotherapeutic agents.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9QX60}.
Interaction partners:
- 5'
- Mitochondrial inner membrane protein Mpv17
- Purine nucleoside phosphorylase
- Guanylate kinase
- 5'
- Ribonucleoside-diphosphate reductase subunit M2 B
- Succinate--CoA ligase subunit beta, mitochondrial
- Cytosolic purine 5'-nucleotidase
- Cytosolic 5'-nucleotidase 3A
- DNA polymerase subunit gamma-1
Sequence:
MAAGRLFLSRLRAPFSSMAKSPLEGVSSSRGLHAGRGPRRLSIEGNIAVGKSTFVKLLTKTYPEWHVATEPVATWQNIQAAGTQKACTAQSLGNLLDMMYREPARWSYTFQTFSFLSRLKVQLEPFPEKLLQARKPVQIFERSVYSDRYIFAKNLFENGSLSDIEWHIYQDWHSFLLWEFASRITLHGFIYLQASPQVCLKRLYQRAREEEKGIELAYLEQLHGQHEAWLIHKTTKLHFEALMNIPVLVLDVNDDFSEEVTKQEDLMREVNTFVKNL
Protein: Transcription factor HES-4 (hHES4) (Class B basic helix-loop-helix protein 42) (bHLHb42) (Hairy and enhancer of split 4) (bHLH factor Hes4) (Q9HCC6)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor. Binds DNA on N-box motifs: 5'-CACNAG-3' (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MAADTPGKPSASPMAGAPASASRTPDKPRSAAEHRKSSKPVMEKRRRARINESLAQLKTLILDALRKESSRHSKLEKADILEMTVRHLRSLRRVQVTAALSADPAVLGKYRAGFHECLAEVNRFLAGCEGVPADVRSRLLGHLAACLRQLGPSRRPASLSPAAPAEAPAPEVYAGRPLLPSLGGPFPLLAPPLLPGLTRALPAAPRAGPQGPGGPWRPWLR
Protein: GPI mannosyltransferase 1 (EC 2.4.1.-) (GPI mannosyltransferase I) (GPI-MT-I) (Glycosylphosphatidylinositol-anchor biosynthesis protein 14) (Q9P6R5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly. Required for cell wall integrity (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- GPI mannosyltransferase 2
- GPI mannosyltransferase 3
- GPI-anchored wall transfer protein 1
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Diphthine methyl ester synthase
- Dolichol-phosphate mannosyltransferase
- Dol-P-Man:Man
- Dolichol-phosphate mannosyltransferase subunit 3
- Double-strand break repair protein rad32
- Protein pbn1
Sequence:
MRLVLLNYGIWHDRRSALKFTDIDYFVFSDASKYVSIGMSPYMRDTYRYTPMLAILLLPTQYGFPSWGKYLFSISDLIAGWLMIKLLSRRISYKRSLIYSSFWILNPFVAIISTRGNCEAILGILSIALLYLIEKKSVWLASLILGFSVHFKIYPFMYGIAFLVYFSKPKKGSTFMEKFLSLLSINQLKIVVGSLFMFTICNLLMYYLYGSPFLEHTYLYHFGRTDHRHNFSLHHLNLYYESSFGAKASSLFAFLPQLSLCMLIPLVFGKKNLPGTLFAQTFAFVTFNKVCTSQYFMWYLVFLPLVLPNSKLLSKKGLICLSLWIIGQLLWLISAYNLEMLGKSVFIPLWLSGLLFFFFNVYELKIILDSL
Protein: NEDD4-like E3 ubiquitin-protein ligase WWP2 (EC 2.3.2.26) (Atrophin-1-interacting protein 2) (AIP2) (HECT-type E3 ubiquitin transferase WWP2) (WW domain-containing protein 2) (O00308)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; in embryonic stem cells (ESCs) the ubiquitination is proposed to regulate POU5F1 protein level. Ubiquitinates EGR2 and promotes it to proteasomal degradation; in T-cells the ubiquitination inhibits activation-induced cell death. Ubiquitinates SLC11A2; the ubiquitination is enhanced by presence of NDFIP1 and NDFIP2. Ubiquitinates RPB1 and promotes it to proteasomal degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:20858735}.
Interaction partners:
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- NEDD4 family-interacting protein 1
- Arrestin domain-containing protein 1
- Mothers against decapentaplegic homolog 7
- Arrestin domain-containing protein 3
- Polyubiquitin-C
- POU domain, class 5, transcription factor 1
- WW domain-binding protein 2
- Neurogenic locus notch homolog protein 3
- E2 ubiquitin-conjugating enzyme
Sequence:
MASASSSRAGVALPFEKSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLRNELLGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRELPNGRVYYVDHNTKTTTWERPLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQWQSQRNQLQGAMQHFSQRFLYQSSSASTDHDPLGPLPPGWEKRQDNGRVYYVNHNTRTTQWEDPRTQGMIQEPALPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNALPSHVKISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRHYTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVGKETWLPRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFGQE
Protein: Glutaredoxin, putative (Q387B5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribonucleoside-diphosphate reductase
- peptide-methionine
Sequence:
MPSIASMIKGNKVVVFSWVTCPYCVRAEKLLHARTKDITVHYVDKMSEGEQLRGEIYQAYKHETVPAIFINGNFIGGCSDLEALDKEGKLDGLLS
Protein: WD repeat-containing protein 7 (TGF-beta resistance-associated protein TRAG) (Q9ERH3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Dmx-like 2
- Coiled-coil domain-containing protein 115
- DnaJ homolog subfamily C member 5
- V-type proton ATPase subunit C 1
- Secretion regulating guanine nucleotide exchange factor
- DmX-like protein 1
- Ras-related protein Rab-3A
- Protein rogdi homolog
- Rab3 GTPase-activating protein catalytic subunit
Sequence:
MAGNSLVLPIVLWGRKAPTHCISSILLTDDGGTIVTGCHDGQICLWDLSEELEVNPRALLFGHTAAITCLSKACASGDKQYTVSASANGEMCLWDVNDGRCIEFTKLACTHTGIQFYQFSVGNQREGRLLCHGHYPEILVVDATSLEVLYSLVSKISPDWISSMSIIRSHRTQEDTVVALSVTGILKVWIVTSEISGLQDTEPIFEEESKPIYCQNCQSLSFCAFTQRSLLVVCSKYWRVFDAGDYSLLCSGPSEDGQTWTGGDFVSADKVIIWTENGQSYIYKLPASCLPASDSFRSDVGKAVENLIPPVQHSLLDQKDRELVICPPVTRFFYGCKEYLHKLLIQGDSSGRLSIWNIADIADKQEANEGLKTTTCISLQDAFDKLKPCPAGIIDQLSVIPNSNEPLKVTASVYIPAHGRLVCGREDGSIIIVPATQTAIVQLLQGEHMLRRGWPPHRTLRGHRNKVTCLLYPHQVSARYDQRYLISGGVDFSVIIWDIFSGEMKHIFCVHGGEITQLLVPPENCSARVQHCVCSVASDHSVGLLSLREKKCIMLASRHLFPIQVIKWRPSDDYLVVGCTDGSVCVWQMDTGALDRCAMGITAVEILNACDEAVPAAVDSLSHPAVNLKQAMTRRSLAALKNMAHHKLQTLATNLLASEASDKGNLPKYSHNSLMVQAIKTNLTDPDIHVLFFDVEALIIQLLTEEASRPNTALISPENLQKASGSSDKGGSFLTGKRAAVLFQQVKETIKENIKEHLLDEEEDEEEVMRQRREESDPEYRASKSKPLTLLEYNLTMDTAKLFMSCLHAWGLNEVLDEVCLDRLGMLKPHCTVSFGLLSRGGHMSLMLPGYNQAAGKLLQAKAEAGRKGPATESVGKGTYTVSRAVTTQHLLSIISLANTLMSMTNATFIGDHMKKGPTRPPRPGTPDLSKARDSPPASSNIVQGQIKQAAAPVSARSAADHSGSASASPALRTCFLVNEGWSQLAAMHCVMLPDLLGLGKFRPPLLEMLARRWQDRCLEVREAAQALLLAELRRIEQAGRKETIDTWAPYLPQYMDHVISPGVTAEAMQTMAAAPDASGPEAKVQEEEHDLVDDDITTGCLSSVPQMKKMSTSYEERRKQATAIVLLGVIGAEFGAEIEPPKLLTRPRSSSQIPEGFGLTSGGSNYSLARHTCKALTFLLLQPPSPKLPPHSTIRRTAIDLIGRGFTVWEPYMDVSAVLMGLLELCADAEKQLANITMGLPLSPAADSARSARHALSLIATARPPAFITTIAKEVHRHTALAANTQSQQSIHTTTLARAKGEILRVIEILIEKMPTDVVDLLVEVMDIIMYCLEGSLVKKKGLQECFPAICRFYMVSYYERSHRIAVGARHGSVALYDIRTGKCQTIHGHKGPITAVSFAPDGRYLATYSNTDSHISFWQMNTSLLGSIGMLNSAPQLRCIKTYQVPPVQPASPGSHNALRLARLIWTSNRNVILMAHDGKEHRFMV
Protein: Acetyl-coenzyme A synthetase (EC 6.2.1.1) (Acetate--CoA ligase) (Acetyl-CoA synthetase) (ACS) (AceCS) (Acyl-activating enzyme) (Q9VP61)
Organism: Drosophila melanogaster (Fruit fly)
Function: Activates acetate so that it can be used for lipid synthesis or for energy generation.
Subcellular location: Cytoplasm.
Interaction partners:
- Probable citrate synthase, mitochondrial
- Citrate synthase
- Acetyl-CoA carboxylase, isoform A
- aldehyde dehydrogenase
- Aldehyde dehydrogenase type III, isoform Q
- Uncharacterized protein, isoform B
- Acetyl-CoA acetyltransferase 1, isoform A)
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
Sequence:
MPAEKSIYDPNPAISQNAYISSFEEYQKFYQESLDNPAEFWSRVAKQFHWETPADQDKFLKYNFNISKGPISIKWMEGASTNLCYNLLDRNVRNGLGDQIAYYWEGNHPDDYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITADGAWRGEKPLYLKALCDTALEKVEEMGHSVEKCIVVSHLKRVTPCQPDHVEEEIPWTDDRDYWWHEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTADVGWITGHTYVVYGPLANGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYKYIGKEQCSIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWPGMMRTLYNNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDRNVGDTSTLADEQIVEQLFANRPVEAK