wanglab/gogpt-training-data huggingface dataset:
Protein: G-protein coupled receptor 161 (Q90X46)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Key negative regulator of Shh signaling during neural tube development. Recruited to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of gli3 into gli3r and repress the Shh signaling. In presence of shh, it is removed from primary cilia, preventing its activity and allowing activation of the Shh signaling (By similarity). Required in left/right patterning by modulating Ca(2+) levels in the cells surrounding the Kupffer vesicle.
Subcellular location: Cell projection, cilium membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Mainly localizes to primary cilium and is removed from primary cilia in presence of shh. {ECO:0000250}.
Interaction partners:
- Beta-arrestin-1
- Arrb2b protein
- Guanine nucleotide-binding protein G
- Arrestin, beta 2a.
- G-protein coupled receptor 161-like
- cAMP-dependent protein kinase
- Protein smoothened
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MNGSKNGTAVANSTNGLDDNGLMVLESVSIIIIAILACLGNLVIVVTLYKKPYLLTPSNKFVFSLTSSNLLLSVLMLPFVVASSVRRDWMFGVVWCNFTALLHLLVSSSSMLTLGAIAIDRYYAVLYPMIYPMKITGNRAVLAIVYIWLHSLVGCLPPLFGWSSFEFDRFKWTCTVSWHKEISYTAFWVTWCCLLPLVAMLVCYGVIFRVARIKARKVYCGSVVVSQEESSSQNNGRKNSNTSTSSSGSRKSLIYSGSQCKAFITILVVLGTFLTTWGPYVVVISTEALLGKNSVSPQVETLVSWLSFTSAVCHPLIYGLWNKTVRKELLGMCFDDRYYRESFVIRHRTSRLFSISNRITDLGMSPHLTAMLVGGGQLLGRGSSTGDTGFSYTQDSATDVMLLESYTSEASHSAHCTANKRRSSVTFEDQVDHIPQGDPSVVQVTADIHKSLDSFASSLAKAIENDAKLQLLGEWTQIPTSLFTVRNTQRVPRYLDGQRLRMESIDEGIVKDDDDDEEEMEREEKM
Protein: ORF K10.5 (O40940)
Organism: Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Interaction partners:
Sequence:
MYHVGQEMDMLMRAMCDEDLFDLLGIPEDVIATSQPGGDTDASGVVTEGSIAASAVGAGVEDVYLAGALEAQNVAGEYVLEISDEEVDDGAGLPPASRRRPVVGEFLWDDGPRRHERPTTRRIRHRKLRSAYYRVARPPVMITDRLGVEVFYFGRPAMSLEVERKVFILCSQNPLADISHSCLHSRKGLRVLLPKPDDNNTGPGDVNLLAAVLRSFASGLVIVSLRSGIYVKNLCKSTVLYHGNNPPKKFGVICGLSSRAVLDVFNVAQYRIQGHEHIKKTTVFIGGDPTSAEQFDMVPLVIKLRLRSVTCDD
Protein: F-box/kelch-repeat protein At1g30090 (Q9C6Z0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MQRVRVSSQRAVVHKLGDSQMTLSPKFRVAASIQSTLFDRSSELELSLRGEPLIPGLPDDVALNCLLRVPVQSHVSSKSVCKRWHLLFGTKETFFAKRKEFGFKDPWLFVVGFSRCTGKIQWKVLDLRNLTWHEIPAMPCRDKVCPHGFRSVSMPREGTMFVCGGMVSDSDCPLDLVLKYDMVKNHWTVTNKMITARSFFASGVIDGMIYAAGGNAADLYELDCAEVLNPLDGNWRPVSNMVAHMASYDTAVLNGKLLVTEGWLWPFFVSPRGQVYDPRTDQWETMSMGLREGWTGTSVVIYDRLFIVSELERMKMKVYDPVTDSWETINGPELPEQICRPFAVNCYGNRVYVVGRNLHLAVGNIWQSENKFAVRWEVVESPERYADITPSNSQILFA
Protein: Gamma tubulin complex adapter mto1 (Microtubule organizer protein 1) (Morphology defective protein 20) (O94488)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for cytoplasmic astral microtubule growth during mitosis. Involved in localizing components of the gamma-tubulin complex to the non-spindle pole body (non-SPB) microtubule organizing centers (MTOCs). Required for new microtubule nucleation from non-SPB sites during interphase.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:15004232, ECO:0000269|PubMed:15120067, ECO:0000269|PubMed:15659644, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19001497}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:15004232, ECO:0000269|PubMed:15659644, ECO:0000269|PubMed:19001497}. Note=Localizes at the interphase MTOC (iMTOC) and at the equatorial MTOC (eMTOC) at the end of mitosis. {ECO:0000269|PubMed:15004232, ECO:0000269|PubMed:19001497}.
Interaction partners:
- Gamma tubulin complex adapter mto2
- Spindle pole body component alp4
- Spindle pole body component alp16
- Gamma-tubulin complex component gfh1
- DnaJ-related protein rsp1
- Kinesin-like protein 2
Sequence:
MEENSSELDSNNFNVLVDNLAGLSLTDEEVRRILSPRKEGSRQLPSSTSKDEDSEEASHKYDFEIDRDSLKSDSGSPRLHQNATAPTSSTPLQSPDESVNKLNSEDEEGNSSVAPFFLDTTNFDRLNDNITTDDEQLSPVLTANQGFQSQEQYEEDSYNNYDYTSDPSSPNYISSSLDQLPHLDDEDDLQLTPIKEERNYLHSQDAPTTNALSKKISDILIPASAMKDLKDRKNALAKEFEESQPGSSLTLKEQANVIDNLRKEVFGLKLKCYFLYDQLNKFHDQEVQDIMKQNIDLKTLTMELQRAVAGYEKKISGLESRIKPDQSFNLSTPSPAPSNLITLQSRYSQALSELETTKRAFAALRKEKSKKTNYSVGAYNEDRNVLSNMLDNERREKEALLQELESLRVQLSKKVPMPAKNTDERVIETLQRSNELLRMDISMQNEALLLRKQENDRLVKQVEELTVALNSGKMNAIVEAESSKNELWDSMMVSRMKTQEQSIELTRLYKQLQDIEEDYENKLMRMEQQWREDVDQLQEYVEEITQELQDTKEVLSKSSKESDDYEEVVGKLRTEAEREIEKFEKTIRENEESISLFKEEVEKLTDEITQLSERYNDKCHEFDELQKRLQTLEEENNKAKEDSTSKTSNLLEQLKMTEAEVDSLRKENEENKQVIALKESELVKSNDNKLLLNEQIESLNDQLSQLKTEMESVTTSKESLADYLSNLKERHNDELDSLNKKLREFEGILSSNSSLKSEIEERNNQYVTLRENFDSLQNAIMETFDKQVTHCSVNHLVQQIRKLKDENKKDQSGTDKLMKKIYHCEQSLKEKTNSLETLVSEKKELKNLLDAERRSKKAIQLELENLSSQAFRRNLSGSSSPSERSQSRELKLLQASEKRLKEQVEERNSLIKNIVTRFTQLNTGSKPVNTNVEALTTISSMNQAVNMNFRELDKSIQEFKRKCQSMEREFKTELRKLDGVLEARSKRLSQLEERVKLLGAGSTSSIPNSPRASKRVSLDSEDKKLVPASPDKSAVQRGITALKRDAEGMSHIWQLRLREMEFQLKAEQEGRKRDKLGARERLQDLIRQNRSLSRQIKTDKESNSRSPSISSQEHK
Protein: ATsEH (EC 3.3.2.9) (At2g26740/F18A8.11) (Putative epoxide hydrolase ATsEH) (Soluble epoxide hydrolase) (Q42566)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Alpha/beta-Hydrolases superfamily protein
- PEBP family protein
Sequence:
MEHRKVRGNGIDIHVAIQGPSDGPIVLLLHGFPELWYSWRHQIPGLAARGYRAVAPDLRGYGDSDAPAEISSYTCFNIVGDLIAVISALTASEDEKVFVVGHDWGALIAWYLCLFRPDRVKALVNLSVPFSFRPTDPSVKPVDRMRAFYGDDYYICRFQEFGDVEAEIAEVGTERVMKRLLTYRTPGPVIIPKDKSFWGSKGETIPLPSWLTEEDVAYFVSKFEEKGFSGPVNYYRNFNRNNELLGPWVGSKIQVPTKFVIGELDLVYYMPGVKEYIHGPQFKEDVPLLEEPVVMEGVAHFINQEKPQEILQIILDFISKF
Protein: Membralin (Transmembrane protein 259) (Q8CIV2)
Organism: Mus musculus (Mouse)
Function: May have a role in the ERAD pathway required for clearance of misfolded proteins in the endoplasmic reticulum (ER). Promotes survival of motor neurons, probably by protecting against ER stress.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25977983}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transmembrane and ubiquitin-like domain-containing protein 1
- Transmembrane and ubiquitin-like domain-containing protein 2
Sequence:
MSEHAAAPGPGPNGGGGGGAAPVRGPRGPNLNPNPLINVRDRLFHALFFKMAVTYSRLFPPAFRRLFEFFVLLKALFVLFVLAYIHIVFSRSPINCLEHVRDRWPREGVLRVEVRHNSSRAPVILQFCDGGLGGLELEPGGLELEEEELTVEMFTNSSIKFELDIEPKVFKPQSGADALNDSQDFPFPETPAKVWPQDEYIVEYSLEYGFLRLSQATRQRLSIPVMVVTLDPTRDQCFGDRFSRLLLDEFLGYDDILMSSVKGLAENEENKGFLRNVVSGEHYRFVSMWMARTSYLAAFVIMVIFTLSVSMLLRYSHHQIFVFIVDLLQMLEMNMAIAFPAAPLLTVILALVGMEAIMSEFFNDTTTAFYIILTVWLADQYDAICCHTNTSKRHWLRFFYLYHFAFYAYHYRFNGQYSSLALVTSWLFIQHSMIYFFHHYELPAILQQIRIQEMLLQTPPLGPGTPTALPDDLNNNSGSPATPDPSPPLALGPSSSPAPTGGASGPGSLGAGASVSGSDLGWVAETAAIISDASFLSGLSASLLERRPTAPSTPDSSRPDPGVPLEDAPAPAGS
Protein: Probable glutathione peroxidase 4 (EC 1.11.1.9) (Q8L910)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May constitute a glutathione peroxidase-like protective system against oxidative stresses.
Interaction partners:
- Glutathione reductase, chloroplastic
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase DHAR2
- Glutathione synthetase, chloroplastic
- L-ascorbate peroxidase 3
- Monodehydroascorbate reductase 3
- Glutathione S-transferase F9
- Glutathione S-transferase F11
- Glutathione S-transferase F6
- Glutathione S-transferase T1
Sequence:
MGASASVPERSVHQFTVKDSSGKDLNMSIYQGKVLLIVNVASKCGFTETNYTQLTELYRKYKDQDFEILAFPCNQFLYQEPGTSQEAHEFACERFKAEYPVFQKVRVNGQNAAPIYKFLKASKPTFLGSRIKWNFTKFLVGKDGLVIDRYGTMVTPLSIEKDIKKALEDA
Protein: BRD4-interacting chromatin-remodeling complex-associated protein-like (Q8CHH5)
Organism: Mus musculus (Mouse)
Function: Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner.
Interaction partners:
- Bromodomain-containing protein 9
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- B-cell CLL/lymphoma 7 protein family member C
- SWI/SNF complex subunit SMARCC1
- B-cell CLL/lymphoma 7 protein family member B
- B-cell CLL/lymphoma 7 protein family member A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- BRD4-interacting chromatin-remodeling complex-associated protein
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- AT-rich interactive domain-containing protein 1A
Sequence:
MDDDDDSCLLDLIGDPQALNYFLHGPSSKSGSDDVTNAGYSAANSNSIFANSTNADPKSALKGVSDQLGEGPSDGLPLASSLQFLEDELESSPLPDLSEDQPFDILQKSLQEANITEQTLAEEAYLDASIGSSQQFAQAQLHPSSSASFTQASNVSNYSGQTLQPIGVTHVPVGASFASNTVGVQHGFMQHVGISVPSQHLPNSSQISGSGQIQLIGSFGNQPSMMTINNLDGSQIILKGSGQQAPSNVSGGLLVHRQTPNGNSLFGNSTSSPVAQPVTVPFNSTNFQASLPVHNIIIQRGLAPNSNKVPINIQPKPVQMGQQSAYNVNNLGIQQHHAQQGISFAPTSSPQGSVVGPHMSVNIVNQQNTRKPVTSQAVSGTGGSIVIHSPMGQPHTPQSQFLIPTSLSVSSNSVHHVQAINGQLLQTQPSQLISGQVASEHVMLNRNSSNMLRTNQPYSGQMLNNQNTAVQLVSGQTFATSGSPVIVNHASPQIVGGQMPLQQASPTVLHLSPGQSSVSQGRPGFATMPAVSGMAGPARFPAVSSASTAHPTLGPTVQSGAPGSNFTGDQLTQANRTPAPVSVSHRLPVSASKSPSTLSNTPGTQQQFFCQAQKKCLNQTSPIPTSKTTDGLRPSQIPGLLSTALPGQDSGSKIMPATLGATQAQPESSVGSSPSQTAVQVDSHPGQKRPAAKQLTKGAFILQQLQRDQAHAVTPDKSQFRSLNDTVQRLLSYHVCQGSMPTEEDLRQVDNEFEEVATQLLKRTQAMLNKYRFLLLEDAMRINPSAEMVMIDRMFNQEERASLSRDKRLALVDPEGFQADFCCSFKLDEAVPETPLDRSDQHRSKTSSLHQVPRAQSRDRAKPGMAEATNHDQFHLVPNHIVVSAEGNISKKSEGHSRTLKFDRGVLGQYRGPPEDKGGRRDPAKVSRCSPGPEGHRKSLPRPDHGSESKLPGVLASSHMEMPCLDSFQDKALRNSPKNEVLHTDIMKGSGEPQPDLQLTKSLEKTFKNILELKNSGRPPSDPTASGAADLDFPSFSPMASQENCLEKFIPDHSEGVVETDSILEAAVNSILEC
Protein: Serrano, isoform F (A0A0B4LFU3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform C
- MD-2-related lipid-recognition domain-containing protein
Sequence:
MQYLNYALQTSTRLLTYQGPNQDLYPDQTGVASAHEEEIKHACCSRGAQLLRLRHRELAKRRALEDQINANQEEQEETEEDSRDQQEPLPEELDSEQGAVGGEQLHPQPVQXNLLSFNVQLARSKLLSFFNRDMAATDGQIILAASRFGDATPVYLRDFSKQPLPAVAKIIKGQHQALGVPTLSAPSLQSTALFLSAGKKYQILAQPIKIKEGRKPTNVGAKVLIPETYGGYFELLSEDGRSTRCIDSVLELSRRRNARVLVRETFRCQQMNRTIHAGELLTTMNDNGKYLQCRNIKDEIINLPLDTKAKFSPIAREDSISGVHTVKNLLLKRMPVIVRLVHGSAPKGLKQPFVPELRLLGCVEIDRIFALPLQKDTDLVPVPLNAKIKLQRAKNMEQLEHFIEYSRFLDKAQRLLADARDRLQIVDLKLSEKEKKDSKFNSRNGGRLPVVMLPSAAGMASGLAESGYVLRKSASCDSWSKQQQQALSSSEIAEEYNEIDHIYDYVRGLTPLSKGLARFEPICESPTLRSHHTDSGSGNYCSLIRAPVHQQATTSGNNNYSSLESNKHSSSGGGHHPGSHHHHHHHVVNHYHHGHIQEDIKPVPPPIETIPGKKPAEKRQRPTLPKLYIKNAHSAGSSSNGNSTGTTHSTSHSHSHSHSHVHSHSHGQSQSQQQPPTPNGNTGNAVANAAASAVAAAHHGSHGSHGSHLHPHPHASVHPHPHPHHGKVLTPNNHLPSKEALEPQSPLFHIRYKSLSSLQLTPDNNNCSSVTPPTISAHGKSSGAGVGSGATASGTPGTPGTPPDVGLKCGSILNVHGYLSSPHPLPLPLPHSRSSSSNNHHNPREGTLDSSRSGGRTSGDSNKLPEKKTRRLSRPRSLSNLVWDLRPSKEKSKKKLYIHHFDQRQQATLYL
Protein: ATP-dependent permease MDL1, mitochondrial (ABC transporter mdl1) (Q9Y7M7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mediates export of peptides generated upon proteolysis of mitochondrial inner membrane proteins.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:16849797}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:16849797}.
Interaction partners:
- Protoheme IX farnesyltransferase, mitochondrial
Sequence:
MDPIRFGLSRVPFAHCYNKRVIFRANYLVPLTWLKNNVAYKSTNTLLLPTPNAEYYSTSKLSSQVNVSLNSLSQKASSGSKIYPFKNSFPLPFSRSILPIRSLAFLKLCVRHNSTVPSKDEQAQDISKINTNGTLQTPNKKVNVFRLFTLARGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIPSGTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLDAKPKIAPTVGIPVPVTVGKAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANCSFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLMRWQLGKVEP
Protein: Rifin (O97327)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLLALSLNILANTHQKPSSTPRHIQTTRLLCECELYMHNYDNDPEMKRVMQQFHDRTTQRFQEYDERLQEKRQVCKDTCDKEIEKIILKDKIEKELNEKFATLQTDIHSDAIPTCICKTSMADKVEKTCLKCTQNLGGIVAPSSGVLAGIAEGALYAWKPNALQTAIEAALKAAADDILVGGIEAGKKVVIGGLDALEIEKLGIGSWEPYFTEGYCINVKSLASIIYEKRQTLCGATKSTLDKATCEQIGISIGTMQHDGTYGAPGTTPIETVLNGIVEGTKEAADVAAEAARESATNAIKVQETRLLEAGFNSSISSINASIIAIVVIILIMVIIYFILRYRRKKKLKKKLQYIKLLEE
Protein: Lysine-specific demethylase 4A (EC 1.14.11.66) (EC 1.14.11.69) (JmjC domain-containing histone demethylation protein 3A) (Jumonji domain-containing protein 2A) ([histone H3]-trimethyl-L-lysine(36) demethylase 4A) ([histone H3]-trimethyl-L-lysine(9) demethylase 4A) (Q8BW72)
Organism: Mus musculus (Mouse)
Function: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}.
Interaction partners:
- Histone H3.1
- Histone H3.2
- Histone H3.3
- Lysine-specific histone demethylase 1A
- Histone H4
- Nuclear receptor corepressor 1
- Lysine-specific demethylase 7A
- E3 ubiquitin-protein ligase RNF8
- Lysine-specific demethylase 3A demethylase 3A)
- E3 ubiquitin-protein ligase RNF168
Sequence:
MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRTSYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPPIYGADVNGTLYEQHVDEWNIGRLKTILDLVEKESGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRRFQPERYKLWKAGKDSMVIDHTLPTPEAAEFLKDSGGLTPRAGSEECPEEDVEAADQGEEGDVKRSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEELSSGQYEMTECPATLAPVRPTHSSVRQVEDSLPFPDYSDPTEVKFEELKNVKLEEEDEEDEPEAAALDLSVNPASVGGRLVFSGSKKKSSSSLGSTSSQDSVSSDSETAESVSCQGQEKTGVLTVHSYARGDGKAATGEPSVKKKRSAPRSISEQELAEVADEYMLSLEENKKTKGRRQPLSKLPRHHPLVLQECGSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNEIMAQQAPHCAVCMIFQTYHQVEFGAFSQSCGDASEPAAQTQRTKPLIPEMCFTTTGCSTDINLSTPYLEEDGTSMLVSCKKCSVRVHASCYGVPPAKASEEWMCSRCSANALEEDCCLCSLRGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCVFCKKRRKRNAGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKIPNLERAKGALLSITAGQKVISKHKNGRFYQCEVVRLTTETFYEVNFDDGSFSDNLYPEDIVSQDCLQLGPPAEGEVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVKRDDVYTLDEELPKRVKSRLSVASDMRFNEIFTEKEVKQEKKRQRVINSRYREDYIEPALYRAIME
Protein: Glutathione peroxidase (D6XK30)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase
- Glutathione peroxidase
- Glutathione peroxidase
- Tryparedoxin
Sequence:
MSTIFDFEVLDADHKPYNLVQHKGSPLLIYNVASKCGYTKGGYETATALYNKYKSQGFTVLVFPCNEFGGQEAGNEEEIKEFVCTKFKAEFPIMAKINVNGENAHPLYEYMKKTKPGILATKAIKWNFTSFLIDRDGVPVERFSPGASVKDIEEKLIPLLESTQSA
Protein: Serine/threonine-protein kinase TAO3 (EC 2.7.11.1) (Cutaneous T-cell lymphoma-associated antigen HD-CL-09) (CTCL-associated antigen HD-CL-09) (Dendritic cell-derived protein kinase) (JNK/SAPK-inhibitory kinase) (Jun kinase-inhibitory kinase) (Kinase from chicken homolog A) (hKFC-A) (Thousand and one amino acid protein 3) (Q9H2K8)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that acts as a regulator of the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Inhibits basal activity of MAPK8/JNK cascade and diminishes its activation in response epidermal growth factor (EGF).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:13679851}. Cell membrane {ECO:0000269|PubMed:13679851}; Peripheral membrane protein {ECO:0000269|PubMed:13679851}. Note=Also localized to the peripheral cell membrane.
Interaction partners:
- Serine/threonine-protein kinase TAO1
- Serine/threonine-protein kinase TAO2
- Dual specificity mitogen-activated protein kinase kinase 3
- Dual specificity mitogen-activated protein kinase kinase 6
Sequence:
MRKGVLKDPEIADLFYKDDPEELFIGLHEIGHGSFGAVYFATNAHTSEVVAIKKMSYSGKQTHEKWQDILKEVKFLRQLKHPNTIEYKGCYLKEHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALHGLAYLHSHALIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLQSNEWTDSFRRFVDYCLQKIPQERPTSAELLRHDFVRRDRPLRVLIDLIQRTKDAVRELDNLQYRKMKKILFQETRNGPLNESQEDEEDSEHGTSLNREMDSLGSNHSIPSMSVSTGSQSSSVNSMQEVMDESSSELVMMHDDESTINSSSSVVHKKDHVFIRDEAGHGDPRPEPRPTQSVQSQALHYRNRERFATIKSASLVTRQIHEHEQENELREQMSGYKRMRRQHQKQLIALENKLKAEMDEHRLKLQKEVETHANNSSIELEKLAKKQVAIIEKEAKVAAADEKKFQQQILAQQKKDLTTFLESQKKQYKICKEKIKEEMNEDHSTPKKEKQERISKHKENLQHTQAEEEAHLLTQQRLYYDKNCRFFKRKIMIKRHEVEQQNIREELNKKRTQKEMEHAMLIRHDESTRELEYRQLHTLQKLRMDLIRLQHQTELENQLEYNKRRERELHRKHVMELRQQPKNLKAMEMQIKKQFQDTCKVQTKQYKALKNHQLEVTPKNEHKTILKTLKDEQTRKLAILAEQYEQSINEMMASQALRLDEAQEAECQALRLQLQQEMELLNAYQSKIKMQTEAQHERELQKLEQRVSLRRAHLEQKIEEELAALQKERSERIKNLLERQEREIETFDMESLRMGFGNLVTLDFPKEDYR
Protein: Acyl-CoA (8-3)-desaturase (EC 1.14.19.44) (Delta(5) fatty acid desaturase) (D5D) (Delta(5) desaturase) (Delta-5 desaturase) (Fatty acid desaturase 1) (Q920R3)
Organism: Rattus norvegicus (Rat)
Function: Acts as a front-end fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 5 located between a preexisting double bond and the carboxyl end of the fatty acyl chain. Involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors. Specifically, desaturates dihomo-gamma-linoleoate (DGLA) (20:3n-6) and eicosatetraenoate (ETA) (20:4n-3) to generate arachidonate (AA) (20:4n-6) and eicosapentaenoate (EPA) (20:5n-3), respectively. As a rate limiting enzyme for DGLA (20:3n-6) and AA (20:4n-6)-derived eicosanoid biosynthesis, controls the metabolism of inflammatory lipids like prostaglandin E2, critical for efficient acute inflammatory response and maintenance of epithelium homeostasis. Contributes to membrane phospholipid biosynthesis by providing AA (20:4n-6) as a major acyl chain esterified into phospholipids. In particular, regulates phosphatidylinositol-4,5-bisphosphate levels, modulating inflammatory cytokine production in T-cells (By similarity). Also desaturates (11E)-octadecenoate (trans-vaccenoate)(18:1n-9), a metabolite in the biohydrogenation pathway of LA (18:2n-6).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A4UVI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A4UVI1}. Mitochondrion {ECO:0000250|UniProtKB:O60427}.
Interaction partners:
- Very long chain fatty acid elongase 5
- Very long chain fatty acid elongase 2
- Very-long-chain
- Very-long-chain 3-oxoacyl-CoA reductase
- Very-long-chain enoyl-CoA reductase
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Acyl-CoA desaturase 1
- Lathosterol oxidase
Sequence:
MAPDPVQTPDPASAQLRQMRYFTWEEVAQRSGREKERWLVIDRKVYNISDFSRRHPGGSRVISHYAGQDATDPFVAFHINKGLVRKYMNSLLIGELAPEQPSFEPTKNKALTDEFRELRATVERMGLMKANHLFFLFYLLHILLLDVAAWLTLWIFGTSLVPFTLCAVLLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPLFFALGKVLSVELGKEKKKHMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVVQRKKWVDLAWMLSFYVRVFFTYMPLLGLKGLLCLFFIVRFLESNWFVWVTQMNHIPMHIDHDRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKESGQLWLDAYLHQ
Protein: RNA polymerase sigma factor sigD, chloroplastic (Sigma factor D) (Sigma-D) (RNA polymerase sigma factor sig4) (Atsig4) (Sigma factor 4) (Q9ZSL6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. Regulates transcription of the ndhF gene which codes for a subunit of the plastid NDH [NAD(P)H dehydrogenase] complex.
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerase III subunit 1
- DNA-directed RNA polymerase I subunit 1
- Dynein beta chain, ciliary protein
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerases II, IV and V subunit 3
- DNA-directed RNA polymerases IV and V subunit 3B
- DNA-directed RNA polymerase family protein
- DNA-directed RNA polymerases I and III subunit RPAC1
Sequence:
MATTIPTTATATMCPSPPVPTISPLLRTTHQCQPSPSLSSPFSIKLSTALVCGDTTVDRVVDSSVMIKPEKWGIQSEKRRKRRRRRRVGYERLEPEEEENAGVEAEAETISVPVVGASRSGFLSRLEEVQLCLYLKEGAKLENLGTSVEENEMVSVLLASGRGKKKRSANEILCRRKEAREKITRCYRRLVVSIATGYQGKGLNLQDLIQEGSIGLLRGAERFDPDRGYKLSTYVYWWIKQAILRAIAHKSRLVKLPGSMWELTAKVAEASNVLTRKLRRQPSCEEIAEHLNLNVSAVRLAVERSRSPVSLDRVASQNGRMTLQEIVRGPDETRPEEMVKREHMKHEIEQLLGSLTARESRVLGLYFGLNGETPMSFEEIGKSLKLSRERVRQINGIALKKLRNVHNVNDLKIYYSSSE
Protein: Serine protease DegP homolog (EC 3.4.21.-) (Q8IAR5)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Serine protease which also acts as a protein chaperone. Plays a role in the parasite development in host erythrocytes possibly by protecting it against thermal and oxidative stresses.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24494818}. Parasitophorous vacuole {ECO:0000269|PubMed:24494818}. Host cell membrane {ECO:0000269|PubMed:24494818}; Peripheral membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000269|PubMed:24494818}. Note=Localizes to the cytoplasm and cell membrane of host erythrocytes. {ECO:0000269|PubMed:24494818}.
Interaction partners:
Sequence:
MDIIFCTPTYCKIMLMIIMLISLRTRCDTNNFLNCSVEKEEGEEEIISTNLKRINDDMNILGRILNDERNIKITDIVEMLQNEYDDKKKKKKKKKYIYRKKKSNNKINEINSVQHFNVKENILNEKKKNPLNDNFKNPKLRKHSPNNKKNKNKIGQIKFHIVGYDKKKITKYLTPSMISSIQKRLMNKNKKTNVNVNMSNGRVLPFFPKEYFLHSSTHEKKDKMATKKNNKEESIINERLLENLENISLSRTIKDIRGEEGNERKVKEEDNNIKEEGNSFKKYFKGVVKLYVDITEPNLEMIWQNYPPKSITGSGFIIEGHLIITNAHNISYSTRILIRKHGNSGKYEAKILYVAHDVDIAILTTDDKTFFDDVYALHFGALPSLKDEIITIGYPAGGDKLSVTEGIVSRIDVQYYKHSNYKFLLTQIDAPLNPGNSGGPALVRGKVVGICFQSYKVSNNISYIIPSTIISHFLLDIHKNKDYTGYAFLGVKYEPLENPSLREALGLEEMERKKIIKKNVGILITEVFEGHMSKQDDKYHDMDNKHHNVGDTHHNVGDTHHNVGDDHTDNLQGDTDYCTYILNSNIITSDKKNIYSDKKKKKIYSDNNNNNNNFNYYYNMHGEDEQSCYGLKKNDIILRVDGKDINNDGSVILRDNETVGFQHLFNEKFINDLCIIKIVRNKKIKSVMVKLYKVKYLLNQHNWDKRNKYFIYGGIVFSILTRSLYVYTQNPEINKLMLYNNFKKKSKDEIVVLKNILPTKITTGYYYTDSIVLRVNNIKVKNLKHLIELIEMTKYTNRLMYLKNNKHTLQSYINYYNTKITSLNINTIIHILILTTSGQKVPIVLNKRDVEKYNEEIKKIYSITRDRYVY