wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Q6ABG8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGSINTIFHRIHRFVNGTGNNARFVPSTNNSTEALTLSPRAVPSTVSDRRFLLKACKFMDQVVKSCHSPRLNLKNSPPFILDILPDTYTHLMLIFTQNNDILQDNDYLKIFLESMINKCKEIIKLFKTSAIYNDQSEERRKLTKMSLTFSHMLFEIKALFPEGIYIEDRFRMTKKEAESFWSHHFTKKNIVPWSTFFTALEKHHGSTIGKMEAAELKATIDLSGDDFISNFEFDVFTRLFYPFKTLIKNWQTLTTAHPGYCAFLTYDEVKKRLEKLTKKPGSYIFRLSCTRPGQWAIGYVAPDGKIYQTIPQNKSLIQALHEGHKEGFYIYPNGRDQDINLSKLMDVPQADRVQVTSEQYELYCEMGTTFELCKICDDNEKNIKIEPCGHLLCAKCLANWQDSDGGGNTCPFCRYEIKGTNRVIIDRFKPTPVEIEKAKNVAAAEKKLISLVPDVPPRTSSQTSSSYVNIKELENVETSGEALAQVVNRQRAPSIQAPPLPPRLSASEHQPHHPYTNTNSERE
Protein: IQ domain-containing protein E (Q6IPM2)
Organism: Homo sapiens (Human)
Function: Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling (By similarity). Required for proper limb morphogenesis.
Subcellular location: Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q6PCQ0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6PCQ0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q6PCQ0}. Note=The EvC complex localizes at the base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent manner. {ECO:0000250|UniProtKB:Q6PCQ0}.
Interaction partners:
- EF-hand calcium-binding domain-containing protein 7
- Limbin
- Ubiquitin-like protein FUBI
- Tetratricopeptide repeat protein 23-like
- EvC complex member EVC
- Zinc finger protein 141
- Tetratricopeptide repeat protein 23
Sequence:
MFLGTGEPALDTGDDSLSAVTFDSDVETKAKRKAFHKPPPTSPKSPYLSKPRKVASWRSLRTAGSMPLGGRASLTPQKLWLGTAKPGSLTQALNSPLTWEHAWTGVPGGTPDCLTDTFRVKRPHLRRSASNGHVPGTPVYREKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGTDFVRTLAEKRPDASWVINGLKQRILKLEQQCKEKDGTISKLQTDMKTTNLEEMRIAMETYYEEVHRLQTLLASSETTGKKPLGEKKTGAKRQKKMGSALLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHPPACLASSSALHRQPRGDRNKDHERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELECAREGEEERREREEVLREEIQTLTSKLQELQEMKKEEKEDCPEVPHKAQELPAPTPSSRHCEQDWPPDSSEEGLPRPRSPCSDGRRDAAARVLQAQWKVYKHKKKKAVLDEAAVVLQAAFRGHLTRTKLLASKAHGSEPPSVPGLPDQSSPVPRVPSPIAQATGSPVQEEAIVIIQSALRAHLARARHSATGKRTTTAASTRRRSASATHGDASSPPFLAALPDPSPSGPQALAPLPGDDVNSDDSDDIVIAPSLPTKNFPV
Protein: Replication initiation control protein YabA (Q04KY8)
Organism: Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Function: Involved in initiation control of chromosome replication.
Subcellular location: Cytoplasm, nucleoid {ECO:0000255|HAMAP-Rule:MF_01159}. Note=Localizes in tight foci, which correspond to the replisome at mid-cell throughout the cell cycle. {ECO:0000255|HAMAP-Rule:MF_01159}.
Interaction partners:
Sequence:
MDKKELFDALDDFSQQLLVTLADVEAIKKNLKSLVEENTALRLENSKLRERLGEVEADAPVKAKHVRESVRRIYRDGFHVCNDFYGQRREQDEECMFCDELLYRE
Protein: Metallothionein-1 (MT-1) (P04357)
Organism: Drosophila melanogaster (Fruit fly)
Function: This protein binds cations of several transition elements. It is thought to be involved in detoxification processes.
Interaction partners:
- Metallothionein-2
- GEO10380p1
- Metallothionein-4
- Metallothionein-3
- Metal response element-binding transcription Factor-1, isoform C
Sequence:
MPCPCGSGCKCASQATKGSCNCGSDCKCGGDKKSACGCSE
Protein: CYtochrome P450 family (Q27499)
Organism: Caenorhabditis elegans
Interaction partners:
- Fatty acid synthase
- phospholipase A2
- NADP-dependent oxidoreductase domain-containing protein
- NADPH--cytochrome P450 reductase
Sequence:
MILFIVLSIVSIYLFDLFYWKRRNLPPGPLPLPLVGNLHMMSDDVKPGYSLFSNLKEQYGHVYTFWMASLPIVHVTDWNLIKQHFIKDGGNFVGRPEFPMSIELRQGPYGIIESHGDRWVQQRRFALHVLRDFGLGKNLMEEKVLGEVTAMLDRLRKTMDEVDMQSVFDASVGSVINNLLFGYRYDETNIAEFLDLKEKLNNHFQLAAKPIGGLIGMNPWLGYFPYFSGYKNVMIQNWMGLVEMFRKQANEKLATIDYESDDYSDYVEAFLKERKKHENEKDFGGFEMEQLDSVCFDLWVAGMETTSNTLNWALLYVLRNPEVRQKVYEELDREIGSDRIITTSDKPKLNYINATINESQRLANLLPMNLARSTTKDVEIAGYHIKKNTVIIPQISLVLYNPEIFPEPYEFKPERFLESDGSLKKVEELVPFSIGKRQCPGEGLAKMELLLFFANLFNRFDIQLHQSNPNPSVEKEFGVTMKAKSYRLKLKDRH
Protein: Melanoma-associated antigen 2 (Cancer/testis antigen 1.2) (CT1.2) (MAGE-2 antigen) (P43356)
Organism: Homo sapiens (Human)
Function: Reduces p53/TP53 transactivation function through recruitment of HDAC3 to p53/TP53 transcription sites. Also represses p73/TP73 activity. Proposed to enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. In vitro enhances ubiquitin ligase activity of TRIM28 and stimulates p53/TP53 ubiquitination by TRIM28 potentially in presence of Ubl-conjugating enzyme UBE2H. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in embryonal development and tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes. Negatively regulates acetylation and sumoylation of PML and represses PML-induced p53/TP53 acetylation and activation.
Subcellular location: Nucleus. Nucleus, PML body.
Interaction partners:
- Cellular tumor antigen p53
- Cancer/testis antigen 1
- Melanoma-associated antigen 3
- Cancer/testis antigen 2
- Chondrosarcoma-associated gene 1 protein
- Transcription intermediary factor 1-beta
Sequence:
MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQQTASSSSTLVEVTLGEVPAADSPSPPHSPQGASSFSTTINYTLWRQSDEGSSNQEEEGPRMFPDLESEFQAAISRKMVELVHFLLLKYRAREPVTKAEMLESVLRNCQDFFPVIFSKASEYLQLVFGIEVVEVVPISHLYILVTCLGLSYDGLLGDNQVMPKTGLLIIVLAIIAIEGDCAPEEKIWEELSMLEVFEGREDSVFAHPRKLLMQDLVQENYLEYRQVPGSDPACYEFLWGPRALIETSYVKVLHHTLKIGGEPHISYPPLHERALREGEE
Protein: Inositol oxygenase (EC 1.13.99.1) (Aldehyde reductase-like 6) (Myo-inositol oxygenase) (MI oxygenase) (Q8WN98)
Organism: Sus scrofa (Pig)
Subcellular location: Cytoplasm.
Interaction partners:
- Inositol monophosphatase 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- Uncharacterized protein
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- Aldo-keto reductase family 1 member A1
- Klotho
Sequence:
MKDPDPSQVYRPDMDPEAAKDKGSFRNYTSGPLLDRVFRTYKLMHTWQTVDFVRKKHAQFGGFSYKRMTVLEAVDMLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKVLVLAGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPVYSTELGMYQPHCGLENALMSWGHDEYMYQMMKFNKFSLPGEAFYIIRFHSFYPWHTGGDYRQLCNEQDLAMLPWVQEFNKFDLYTKGSDMPDVDELRPYYQGLIDKYCPGVLCW
Protein: mRNA interferase toxin YafQ (EC 3.1.-.-) (Endoribonuclease YafQ) (Toxin YafQ) (Q47149)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific mRNA endoribonuclease that inhibits translation elongation and induces bacterial stasis. Cleavage occurs between the second and third residue of the Lys codon followed by a G or A (5'AAA(G/A)3'), is reading-frame dependent and occurs within the 5' end of most mRNAs. Ribosome-binding confers the sequence specificity and reading frame-dependence. When overexpressed in liquid media YafQ partially inhibits protein synthesis, with a reduction in growth rate and colony growth rate. This effect is counteracted by coexpression with cognate antitoxin DinJ. YafQ and DinJ together bind their own promoter, and repress its expression.
Interaction partners:
- Antitoxin DinJ
- Endoribonuclease toxin ChpB
- Endoribonuclease toxin MazF
- mRNA interferase toxin HigB
- Antitoxin MazE
- Toxin YoeB
- Antitoxin MqsA
- mRNA interferase toxin RelE
- Antitoxin YefM
- Serine/threonine-protein kinase toxin HipA
Sequence:
MIQRDIEYSGQYSKDVKLAQKRHKDMNKLKYLMTLLINNTLPLPAVYKDHPLQGSWKGYRDAHVEPDWILIYKLTDKLLRFERTGTHAALFG
Protein: GPI transamidase component PIG-S (Phosphatidylinositol-glycan biosynthesis class S protein) (Q6PD26)
Organism: Mus musculus (Mouse)
Function: Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI-anchor transamidase component GPAA1
- GPI-anchor transamidase component PIGT
- GPI-anchor transamidase
- GPI-anchor transamidase component PIGU
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- GPI inositol-deacylase
- GPI ethanolamine phosphate transferase, stabilizing subunit
- Calpain small subunit 1
- Caspase-9
- Caspase-6
Sequence:
MAAAGAAATDLEVVRGKRSALFFAAVAILLGLPLWWKTTETYRAPLPYSDISGLNALLLRLMVPVTVVFTRDSVPLDDQEKLPFTVVHEREIPLKYKMKIKCRFQKAYRRALEHEEEALSLGSVHEAEAMLAEPEKQAEGSLTVYVISEHSSLLPQDMMSYIGPERTAVVRGLIHREAFNIIGRRIVQVAQAMSLTEDVLAAALADHLPEDKWSSDKRRPLKSSLGYEITFSLLNPDPKSHDVHWDIEGAVQRFVQPFLNRLSVAGNFSVDSQILYYAMLGVNPRFDPASSSYSLAMHSLPHVINPVESRLGSSAASLYPVLHFLLYVPELAHSPLYIQDKDGAPVATNAFHSPRWGGIMVYNVDPKIYNASELPVRVEVDMVRVMEVFLAQLRLLFGIAQPQVPPKCLLSGPKSEGLMTWELDRLLWARSVENLATATTTLTSLAQLLGKISNIVIKDDVASEVYRAVAAVQKAAKALALGHLSSAFAASQEAVTSSERAFFDPSLLHLLYFPDDQKFAIYIPLFLPMAVPILLSLVKIFQETRKSWKKPEKID
Protein: Pdp3-interacting factor 1 (EC 3.1.3.50) (Q9P6N2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the mst2 complex which is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with gcn5 to regulate global levels of H3K14 acetylation (H3K14ac), critical for DNA damage checkpoint activation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Acireductone dioxygenase-requiring))
- Histone acetyltransferase mst2
- Mst2 complex subunit nto1
- Chromatin modification-related protein eaf6
- Pdp3-interacting factor 2
- Protein CSN12 homolog
- Uncharacterized protein C1020.05
- Ammonium transporter 3
- Methylthioribose-1-phosphate isomerase
- PWWP domain-containing protein 3
Sequence:
MAQKKQLYVFSDFDGTITLQDSNDYLTDNFGMGNANRVNLNQQVLDGSISFRDAFAKMLDSVHLSYDEALEVLKKNVAIDPSFKPFYEWCKSQDIRVIILSSGMEPFIRALFEQYLGKEEASSIEIVSNDINVHPDGQWNIVYHDDSHFGHDKSLTIRPYAQLPESKRPHMVYCGDGVSDLSAAKETEHLFAKKGRDLIKYCEREKISFSEFETFADIHKDLQKLFFSS
Protein: Protein HUA2-LIKE 1 (HUA2-like protein 1) (Q9LEY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that acts with partial redundancy with HULK2 and HULK3. Plays diverse and essential roles in the control of plant development, physiology and flowering time.
Subcellular location: Nucleus {ECO:0000269|PubMed:25070081}.
Interaction partners:
- Uncharacterized protein At1g51745
- Tudor/PWWP/MBT superfamily protein.
- Dehydrogenase/reductase SDR family member FEY
- Zinc finger CCCH domain-containing protein 37
- KH domain-containing protein HEN4
- DExH-box ATP-dependent RNA helicase DExH10
- Uncharacterized protein At5g66000
- Tubulin beta-4 chain
Sequence:
MAPGRKRGANKAMAIGEMRLGDLVLAKVKGFPAWPAKIGQPEDWNQAPDPKKHFVQFYGTGEIGFVTPPDIQPFTSETKKKLSARCQGKTVKYFSQAVEEISAAFEESQKQKSDIVGNEALLNAVEPSVTKPKYLNQASSDGKSDKFSSRADPCLGKLVENNGAEINPDVGEQDSSISNNRNTSPSSEPVEHGSPDPILKVAVDDKIDNVTCTDHSDGTGNNLVNDQRIIRKTTDDSNKRCKDEVRAKRVPDSRAATDNHILGPNQKLKGSIKGQDHGSKKGQDHGCRKESSDSKVVTDLNIASSKKPKELLKEKKKRFENELGKSASGADESKRAAKRPRSEDAKDQKQCKSKRLVPVGEGKAEISDSTGVVSIFKREIVLGISALGGKNQFDKDMVAYTKRRKQTVEHTSVSSFPGSLVKEGANHPEQKISSSSDSDIKVQAAQLPKRRRAVCIYDDDDDDEDPKTPVHGGLSNIPIASTDAPKSANASHNTSIKAKLLAGSTDSVKTGKVPLYKHNKDASLALPDSVEGYNSRMGKPFKALLQKNIKPILRSPKNSYQLVSFKKQVTGQNKTAKVAGAGMPDSVEGPSNSSYMGKPVIKLPPQNVKQTLRSPKKSPQLFSTKELVAVQNKIAKVSGAGIPKKYHGDSSKDVVAGSDRVSSSHSQTANQRSKPAFGEKPTSTPKVATRLDVEVSRDTFVNLSADVIDVNQENGNAPLFSFGMSDSSSSCMKDLIAAAQAKRKQAHSQFSPFVNLDHNSLNIDSMQTSKSPFMVQNVSSPAADATLIVAQEHQEVLTPSNHGRQSSSSNQAGTEENEERRFSSGHRSVGGSLSGATEAAISRDTFEGMIETLSRTKESIRRATRVAIDCAKYGIANEVVELLIRKLEIEPHFPRKVDLFFLLDSIIQSSHSQKGRARSLYIPTVQAALPRLLGAAAPPGTGARENRHQCRKVLRLWLKRKIFPDFLLRRYIGDLGASGDDKTVGFSLRRPSRSERAVDDPLRDMEGMLVDEYGSNANFQLPGYLASLTFGDDEEEDLPSTSQEVKNTHMEVKITHMEEPVLALGKLEAHDSSSDKPHCVVDVNGGLEMEDASCQLKDDVCGIEAKEDSPATTCATELPSFPAGSPPLPHESPPSPPPQPPSSPPPPSSPPQLAPAPPPSDHCLPPPTAPLAPAQSIALPPSSITRPSMPSHPSLPLQPGFAPPAYPLLQHEYQISMQRDHSSIATSNQIAPVPVNAAHGRHADGGVKSEYLMPQSSSFAPVGMCSYGEPLPFISSKQLEYGNSDVLFKQEASSQNQQLRPINTSFLQRPMIRNLAPAPSSHFPLPCRIVQSEPQRSSFPHPYHFPSQPVDGRQHMNEEWRMPPNGCSADPQYGAWIGVRNPFPGSRTVTDGVFQPPPERPPSGTVRYQLAANNLQGGSTISGNIASQMLLSRPDVPSAAQYRPS
Protein: Non-selective voltage-gated ion channel VDAC2 (Outer mitochondrial membrane protein porin 2) (A0A0A0MR02)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
MATHGQTCARPMCIPPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRNNFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSINAG
Protein: Erythroid transcription factor (Eryf1) (GATA-binding factor 1) (GATA-1) (NF-E1 DNA-binding protein) (NF-E1a) (P17678)
Organism: Gallus gallus (Chicken)
Function: Transcriptional activator or repressor which serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P15976}.
Interaction partners:
Sequence:
MEFVALGGPDAGSPTPFPDEAGAFLGLGGGERTEAGGLLASYPPSGRVSLVPWADTGTLGTPQWVPPATQMEPPHYLELLQPPRGSPPHPSSGPLLPLSSGPPPCEARECVNCGATATPLWRRDGTGHYLCNACGLYHRLNGQNRPLIRPKKRLLVSKRAGTVCSNCQTSTTTLWRRSPMGDPVCNACGLYYKLHQVNRPLTMRKDGIQTRNRKVSSKGKKRRPPGGGNPSATAGGGAPMGGGGDPSMPPPPPPPAAAPPQSDALYALGPVVLSGHFLPFGNSGGFFGGGAGGYTAPPGLSPQI
Protein: Transcription initiation factor TFIID subunit 2 (TBP-associated transcription factor 2) (Q9TYN3)
Organism: Caenorhabditis elegans
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs), including taf-2 (By similarity). May regulate RNA polymerase II activity and thereby may control transcription initiation by RNA polymerase II.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6P1X5}.
Interaction partners:
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 10
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 8
- PHD-type domain-containing protein
Sequence:
MDFSEASTSGDRVNGFAKPFPPKPREGAPPPAPPLAPGASTSQAPPPLQPPPVIESAEKFYVPGVEEKSKFRILSQQVEISNLNISTRSFNVRTEIVLLPCEKSLYQLDLHIGKCSLLPNEVPGSASKVTLNGVECEYSRRDFWKDLAQEKSISSLEPVLYEKLAENDYELQILIPKEVRKKIKHRKAVRLRVDTVVRDPPRGLQFVDFNEHDCHVFTYHTPHISGAREWTVCLDEPDQLALWELTFELEPHLVPVASGELEEKREVSENGKIRYKFHQTVPTSACNIGWAIGRFKLEPHPESPTIYTFSLPGLEPFVNHTTMYLDKMVEFLEEKLSCRFPYPTLKVVFVDQCTEEIQVYSSLLIVPTAMLYHKKIIDVVQEARQKLIFSIALQFFGCLISPAQWWHWWIPVSIARFLTSLYVETKLGTAEARWQLKRAMDDVCDYEHQWGKIVLSPPEPTKKLPLHVDPRHEYTASPLYVEAMLKKGFLTMRMLQRRIGLEPFMRVLHRVLTVGLDMSEKKTTPAAWRHLLTTTESFFRSVISVTGKEIPSFLSQFVRTGGHAAFAVKFDFNRKRNIVEIEIKQDDTEGNGRTQYTGPLSVVVQEVDGAFTHTIQIDGAVSHAEISCHSKGRKQRKKKVPLLTGEEIEIDLTNMDAESPILWLRIDPDYLLIREITISQPMFHWEYMLRYERDVIAQMEALERIQALPSAHSRSVIVDAVANEKFFYRIRYRAAFVLTFVQNRKSEALTVGTPVLINMFRESFGSKAATNIPRSNNFVVTAQNLQQYFVMQALPQAIARLRRQSGECHEDVQPFLLDLIKFNDNSTNRYSDDFYRAALYNSLASSVFPHDALPCHVELPENLSNDVRVLIKEFTYALNMDTVSPSWGRVVGAAALTGLYQLQKCGYLPLDSQLLWTFSHPNCCVQMRRCAITLIIDRIVNDPHAADTRMLDLSRILELAELEQDPSIRRMIPRLLAQTPPTIFGSENAANTAETAERLWKLCTNSSIDSCIRSGFLDVYYSLYALGAPPALGGPEESVGIHRAYVTVPNAASTFATSQWHNSGYEAARRSPPRRDFGDETMNLMQ
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (A0A2R8YF58)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
RLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDEEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
Protein: Mitochondrial glutamate carrier 2 (GC-2) (Glutamate/H(+) symporter 2) (Solute carrier family 25 member 18) (Q505J6)
Organism: Rattus norvegicus (Rat)
Function: Responsible for the transport of glutamate from the cytosol into the mitochondrial matrix with the concomitant import of a proton (symport system).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:19584051}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MIACRMSSQDLSITAKLINGGIAGLVGVTCVFPIDLAKTRLQNQQGKDVYKGMTDCLVKTARAEGFLGMYRGAAVNLTLVTPEKAIKLAANDFLRQLLMQDGTQRNLKMEMLAGCGAGICQVVITCPMEMLKIQLQDAGRLAVCQQASASATPTSRPYSTGSTSTHRRPSATLIAWELLRTQGLSGLYRGLGATLLRDIPFSIIYFPLFANLNQLGVSELTGKASFTHSFVAGCAAGSVSAVAVTPLDVLKTRIQTLKKGLGEDTYRGVTDCARKLWTQEGAAAFMKGAGCRALVIAPLFGIAQGVYFIGIGERILKCFE
Protein: nicotinamidase (EC 3.5.1.19) (Nicotinamide deamidase) (A7WK39)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVHSDNSATTNNNTILGNQSLEAIPEQLSELTGITVEESERIMESWLGNRQLDLRTSVLFDQEVLSRLRSLRVALLVVDFQNDFVDGSLKIGDGDAGQEPSSAITPLNELLQLSSWDLVVYTKDWHPHNHISFLSQAHNSDRVMDEKDENKTLGFFDSVQFLKPIKTEQVLYPDHCIQKSWGSDIHPEIYIADNAEYIMKGVDPYLDSYSAFNDNNGRSKTELEDLLRRENIDAVVIAGLAYDICVRFTCLDAVKQNFLAAVIPECSAGLTKKGIEESEMAFKKQGVAMISKDEARGITEGGFLPREWVQRIVKK
Protein: Mitochondrial transcription termination factor family protein (O64685)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Mitochondrial transcription termination factor family protein
- Peptidyl-prolyl cis-trans isomerase CYP26-2, chloroplastic
- Putative chloroplast RNA binding protein family protein)
- Pentatricopeptide repeat-containing protein At1g01970
- Probable membrane metalloprotease ARASP2, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP37, chloroplastic
- At2g27680/F15K20.22
- Peptidyl-prolyl cis-trans isomerase FKBP17-2, chloroplastic
- ATP-dependent protease La
- Mitochondrial transcription termination factor family protein
Sequence:
MSAALSSSLYISPKKPSCPQQSQSTFLSTKPTTIKTNLHSHPLFTVADQTVTLQMKEKILCLELMGIDSGKALSLNPCLCSAPLDSIQSVLHFLQSKGIYPNDLPRILGMCPKILTSDVRTELYPVFMFLSNDLHVPENAFRRVIKKCPRLLISSVEDQLKPALFYLQRLGLKDLEALAYQDPILLVSSVEHTLIPKLRFLESIGFSRPEAIGMILRCPALFTFSIENNFKPKLDYFMSEIKGKLENLKEFPQYFAFSLEKRIKPRHLESMERGLELPLSLMLKSTDEEFEQLLTNPSSVANV
Protein: Cytochrome P450 1A2 (EC 1.14.14.1) (CYPIA2) (Cholesterol 25-hydroxylase) (Cytochrome P(3)450) (Cytochrome P450 4) (Cytochrome P450-P3) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (P05177)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation (Probable).
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:21576599}; Peripheral membrane protein.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Cytochrome P450 2E1
- Cytochrome P450 7A1
- Arylamine N-acetyltransferase 2
- Cytochrome P450 4A11
- Cytochrome P450 2A6
- Cytochrome P450 3A4)
- UDP-glucuronosyltransferase 1A8
- Cytochrome P450 2B6
- Epoxide hydrolase 1
Sequence:
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDGQSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFPILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLSDRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPELWEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLEFSVPPGVKVDLTPIYGLTMKHARCEHVQARLRFSIN
Protein: Mitogen-activated protein kinase kinase kinase 10 (EC 2.7.11.25) (Q66L42)
Organism: Mus musculus (Mouse)
Function: Activates the JUN N-terminal pathway.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 7
- Huntingtin
- Kinesin-like protein KIF3A
- Kinesin light chain 2
- Protein phosphatase 1 regulatory subunit 37
Sequence:
MEEEEGAAAREWGATPAGPVWTAVFDYEAVGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPAAPAAPSDLQLPQEIPFHELQLEEIIGVGGFGKVYRAVWRGEEVAVKAARLDPERDPAVTAEQVRQEARLFGALQHPNIIALRGACLSPPNLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKQLEVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREMDIVERELHLLMSQLSQEKPRVRKRKGNFKRSRLLKLREGSSHISLPSGFEHKITVQASPTLDKRKGSDGASPPASPSIIPRLRAIRLTPMDCGGSSGSGTWSRSGPPKKEELVGGKKKGRTWGPSSTLQKERAGGEERLKALGEGSKQWSSSAPNLGKSPKHTPMAPGFASLNEMEEFAEADEGNNVPPSPYSTPSYLKVPLPAEPSPCVQAPWEPPAVTPSRPGHGARRRCDLALLSCATLLSAVGLGADVAEARAGDGEEQRRWLDSLFFPRPGRFPRGLSPTGRPGGRREDTAPGLGLAPSATLVSLSSVSDCNSTRSLLRSDSDEAAPAAPSPPPSPLAPSPSTNPLVDVELESFKKDPRQSLTPTHVTAAHAVSRGHRRTPSDGALRQREPLELTNHGPRDPLDFPRLPDPQALFPTRRRPLEFPGRPTTLTFAPRPRPAASRPRLDPWKLVSFGRTLSISPPSRPDTPESPGPPSVQPTLLDMDMEGQSQDNTVPLCGVYGSH