wanglab/gogpt-training-data huggingface dataset:
Protein: Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (Centaurin-beta-1) (Cnt-b1) (Q15027)
Organism: Homo sapiens (Human)
Function: GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration.
Subcellular location: Recycling endosome membrane {ECO:0000269|PubMed:16256741}; Peripheral membrane protein {ECO:0000269|PubMed:16256741}; Cytoplasmic side {ECO:0000269|PubMed:16256741}.
Interaction partners:
- ADP-ribosylation factor 6
- ADP-ribosylation factor 5
- ADP-ribosylation factor 1
- Ras-related protein Rab-35
Sequence:
MTVKLDFEECLKDSPRFRASIELVEAEVSELETRLEKLLKLGTGLLESGRHYLAASRAFVVGICDLARLGPPEPMMAECLEKFTVSLNHKLDSHAELLDATQHTLQQQIQTLVKEGLRGFREARRDFWRGAESLEAALTHNAEVPRRRAQEAEEAGAALRTARAGYRGRALDYALQINVIEDKRKFDIMEFVLRLVEAQATHFQQGHEELSRLSQYRKELGAQLHQLVLNSAREKRDMEQRHVLLKQKELGGEEPEPSLREGPGGLVMEGHLFKRASNAFKTWSRRWFTIQSNQLVYQKKYKDPVTVVVDDLRLCTVKLCPDSERRFCFEVVSTSKSCLLQADSERLLQLWVSAVQSSIASAFSQARLDDSPRGPGQGSGHLAIGSAATLGSGGMARGREPGGVGHVVAQVQSVDGNAQCCDCREPAPEWASINLGVTLCIQCSGIHRSLGVHFSKVRSLTLDSWEPELVKLMCELGNVIINQIYEARVEAMAVKKPGPSCSRQEKEAWIHAKYVEKKFLTKLPEIRGRRGGRGRPRGQPPVPPKPSIRPRPGSLRSKPEPPSEDLGSLHPGALLFRASGHPPSLPTMADALAHGADVNWVNGGQDNATPLIQATAANSLLACEFLLQNGANVNQADSAGRGPLHHATILGHTGLACLFLKRGADLGARDSEGRDPLTIAMETANADIVTLLRLAKMREAEAAQGQAGDETYLDIFRDFSLMASDDPEKLSRRSHDLHTL
Protein: Mitochondrial import receptor subunit TOM22, putative (Q8I3L8)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004572}.
Interaction partners:
Sequence:
MGTALSKIITINEENRLVISNKPVFQLAHKDAIRMRNKLRVAKNRINNFLKKSIKTTSWVVWIAGVSVVVLVTPIAFQYEKECQLFEMQAQFFQAQQAANVPQLN
Protein: Ephrin RBD domain-containing protein (VAB-2) (G5EEE7)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Ephrin receptor 1
- Protein sax-3
- Slit homolog 1 protein
Sequence:
MHPPIKIQTILLFILTTVHCSAKRLPQIYWNSTNPLVERYAAIGDTLDIVCPFFDENSDELTEQSIIYRVTEEEYENCERRSKAKELGRCTQPYQEEKLKVAFRLMSPNPSGLDYRPGVTYYFISTSTGSRKGLYNEQGGLCASHNLKMVIHITDRNGDIGPHHHRHHHKKTTTTTTTSTSTSTPKTIPPVVEMDSSAEKLWEQFYEKVMPIDNTWPEITRGERVTLYQGNKKDEYEQVPAEVVDFEIHEIGDVESLYSSSGRLRYVLLLPALLLLRIF
Protein: Acetyl-CoA hydrolase (EC 3.1.2.1) (Acetyl-CoA deacylase) (Acetyl-CoA acylase) (P32316)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation. It may be involved in overall regulation of acetylation during melatonin synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11502169}.
Interaction partners:
- Acetyl-coenzyme A synthetase 1
- Acetyl-coenzyme A synthetase 2
- Succinate--CoA ligase subunit alpha, mitochondrial
- Potassium-activated aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase [NAD
- Malate synthase 1
- Succinate--CoA ligase subunit beta, mitochondrial
- Magnesium-activated aldehyde dehydrogenase, cytosolic
- Aldehyde dehydrogenase 5, mitochondrial
- Acetyl-CoA acetyltransferase
Sequence:
MTISNLLKQRVRYAPYLKKVKEAHELIPLFKNGQYLGWSGFTGVGTPKAVPEALIDHVEKNNLQGKLRFNLFVGASAGPEENRWAEHDMIIKRAPHQVGKPIAKAINQGRIEFFDKHLSMFPQDLTYGFYTRERKDNKILDYTIIEATAIKEDGSIVPGPSVGGSPEFITVSDKVIIEVNTATPSFEGIHDIDMPVNPPFRKPYPYLKVDDKCGVDSIPVDPEKVVAIVESTMRDQVPPNTPSDDMSRAIAGHLVEFFRNEVKHGRLPENLLPLQSGIGNIANAVIEGLAGAQFKHLTVWTEVLQDSFLDLFENGSLDYATATSVRLTEKGFDRAFANWENFKHRLCLRSQVVSNNPEMIRRLGVIAMNTPVEVDIYAHANSTNVNGSRMLNGLGGSADFLRNAKLSIMHAPSARPTKVDPTGISTIVPMASHVDQTEHDLDILVTDQGLADLRGLSPKERAREIINKCAHPDYQALLTDYLDRAEHYAKKHNCLHEPHMLKNAFKFHTNLAEKGTMKVDSWEPVD
Protein: 2-nitroimidazole nitrohydrolase (2NI nitrohydrolase) (EC 3.5.99.9) (F4ZCI3)
Organism: Mycobacterium sp. (strain JS330)
Function: Involved in the biodegradation of 2-Nitroimidazole (2NI) which is a natural antibiotic and an analog of the synthetic nitroimidazoles used for treatment of tuberculosis, Chagas disease (also called American Trypanosomiasis) and cancer. Catalyzes the hydrolytic denitration of 2NI to produce imidazol-2-one and nitrite. It is also active against the 2NI synthetic derivative benznidazole. NnhA confers drug resistance to 2NI.
Interaction partners:
Sequence:
MTTVDKRPSSRGYGDWRLSDIPQYKDGISTYEFVRATHEADYRTHQAEPVAGRTFGFNGIGRLTEVALHMPTKYTLHDQSSQYKESPSFFQGLMGVPDRGPVDLAAFQRETEELATAFENNGIKVHWVDYPEEPANPYGPLMGHVFLSWGSIWRGGSVISRFGFLPGMVGVSEYLAKWAWNTLNIPPLVAITEGAMEPGACNMIADEVLVTCLSASYDQRGTDQLVAAISKTSGTEEFHNLQLRPAVEGFFNKATGACAHPDININAIDVGKLVVSPAALDWDARTWLYDNNFELIEADPDEQREFLAPCNVLLLEPGKVIAHADCHKTNQKIRDAGVEVIEVTGTEIRKACGGIKCRVMQINREPGPTLADVRNRVWR
Protein: Small RNA 2'-O-methyltransferase (EC 2.1.1.386) (HEN1 methyltransferase homolog 1) (Q5T8I9)
Organism: Homo sapiens (Human)
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Stabilization of piRNAs is essential for gametogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q568P9}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q568P9}.
Interaction partners:
- Piwi-like protein 1
- Piwi-like protein 4
- Tudor and KH domain-containing protein
- ATP-dependent RNA helicase TDRD9
- Endoribonuclease Dicer
- RISC-loading complex subunit TARBP2
- Piwi-like protein 2
- RNA helicase Mov10l1
- Tudor domain-containing protein 1
- Mitochondrial cardiolipin hydrolase
Sequence:
MEENNLQCSSVVDGNFEEVPRETAIQFKPPLYRQRYQFVKNLVDQHEPKKVADLGCGDTSLLRLLKVNPCIELLVGVDINEDKLRWRGDSLAPFLGDFLKPRDLNLTITLYHGSVVERDSRLLGFDLITCIELIEHLDSGDLARFPEVVFGYLSPSMIVISTPNSEFNPLFPSVTLRDSDHKFEWTRMEFQTWALYVANRYDYSVEFTGVGEPPAGAENVGYCTQIGIFRKNGGKATESCLSEQHDQHVYKAVFTTSYPSLQQERFFKLVLVNEVSQQVESLRVSHLPRRKEQAGERGDKPKDIGGSKAPVPCFGPVFTEVEKAKIENSPTPFCVGDKFFVPLQRLLAYPKLNRLCANEEMMRSVIADSIPLSSDGSAVVADLRNYFDEQFEF
Protein: Uncharacterized protein C02F12.8 (Q11103)
Organism: Caenorhabditis elegans
Interaction partners:
- TATA-box-binding protein
Sequence:
MQNDRSRWKTEGHSSEVHEDFLRNSVQRRNQLEKILFSYNNLHRLDPSYGEIVQRAFESNDPIALWNFENEVLLNSKDVDDLMQQQFAAPVQNNQCPNPYQNCGYQNNLVSTLDASFKVHPFAQHGNYMPPPAQFASNPNVFPQPVPPYTMDLAASNSGFAHPQIVNQPMHPHVPVGSQNYNPPQFVPAPPTMMPVGAVMVSQGSYSMSPPQIDTSKPPSGYGFSSPIFPSPSYSQYSGPPANEGFPDIIYDNNGVAYCRVVSAPVCVVSMSQSGSSVCSSQSFSSGQSDISMSSRPPINGSSVGNGSLSPMTDSVREESEDEDYGTLTPVGQQDCDLDSVDTESVANEPEPYSSTMSEMPPLDDVDDIMENLDLSKTLIEPETLEHSDNMSVVEIKSEPVSEMTTDSLIVDDDRDTSISEIIKYLDTSDDVLESWQEATGRKKCFVPQKTQKLVYPLPLSKVEKPLQKCQQTLAASTIDEDSKEASTIALPDARKKLTKKEKRLMAAQKANQLETDDDVLEAAYRERQKHVEQAGGDYSSSGQKDQKKKRGKRPVSNPPPSLISPQILHAVQMAIANRAKKISESGRPIFHENFSYQKFYETVDTFVKTWEENSNEMNKVLQFIEKRILAFKMVQRPQSLSRITIYEQLQLNLPPAILPELCFLAGLTSDSTDKLEYYEEIFFNLF
Protein: LD15833p (Q7YU07)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MFNTKLTSVAATSTSGYTVVFVGTSDGFLKKVVIESSSIANEYASFAVDLGSEINRDMQFDNQNLYIYVMSKTKVSKVKVFDCSDYKTCGDCLGARDPYCGWCSLENKCSPRSNCQDDANDPLYWVSYKTGKCTTITSVVPHQLQRTTARTLELIIDHLPQLKENLICAFTTEDKALFTNATKKRNGVNCTTPRTDMLPQIEQGKHHFTAKLSVRTRNGPDLVSTDFTFFDCSTHSSCTRCVSSEFPCDWCVEAHRCTHDTAENCRNDILVTGVSRIGPSYRSGPGFCPTINATGDGSEVLVAGGTSKSIKVKVHIIGQFIVQTRFVCQFNIEGRVTSLNAQLLGDTIYCDSMEFQYTSRSPNLTATFAVIWGGSKPLDNPHNIHVVIYRCREMADSCGICLALSEKYNCGWCSSTNTCEVEEQCNKNKEGKTDWLNRSEICPNPEIHTFQPKTGPWEGGTNITIRGINLGKNYNDIYSGVRIAGINCMPFPQFYIDTKQIVCTVDSPGEQMYRNGKIVVQIGDYRGESKEDYEFVDPKILDFNPKFGPTSGGTEIHITGKHLNAGSRIQASINDHLPCKILSTDSSQAICRTSASPGIIEGRLKMSFDNGPREFNDYNFKYVLDPTVEHVSSGPSGQIKVPKGIPAGGIRISVTGTQFTSIQNPNIYVVYNGEMYASPCRVQSDTEMECASPVVDVDSHVIEAERPILLEYGFLMDNVLRVQNLSKVHNNHFELYPNPEYFIFEERVKYFKSEYLTINGRNLDRACKESDVEVKIGNGFCNITSLSRQQLTCRPPSEATATKSMNGPEVIVRIGTSLEYRIGILSYESSNIILDWGENVIFAVIATIVILLLIFVALLVAYKKKSSESSRVLRNMQEQMDILELRVAAECKEAFAELQTEMTDLTGDLTSGGIPFLDYRSYAMRIKTTLYYNGNVLSFFGKKKAYVFLAN
Protein: At5g52960 (tRNA dimethylallyltransferase) (Q9LVV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Alanine-tRNA ligase, putative
- At1g63610
- At4g33110
- At1g32160/F3C3_6
- Pentatricopeptide repeat
- Electron transporter, putative
- AT3g29240/MXO21_9)
- Thioredoxin domain-containing protein
- Uncharacterized protein At3g49140
- ARM repeat superfamily protein
Sequence:
MNCVSAFEFVPSSALFPCAQSSIPAKFLHILSSKASISPRCRSFASSSSSTIRRKPLTLVSSKSSDAEEVSDTEDEWLKKLPEKNKPLYSHSLPCIEAWLRKLGFYQSKDDRAVWLIQKPDWHAQLSLDVTDLCIRYMKSGPGNLERDMERRFSYALSREDTENAILGGP
Protein: Keratin, type II cuticular Hb2 (Keratin-82) (K82) (Type II hair keratin Hb2) (Type-II keratin Kb22) (Q9NSB4)
Organism: Homo sapiens (Human)
Interaction partners:
- Keratin-associated protein 7-1
- Desmoglein-4
Sequence:
MSYHSFQPGSRCGSQSFSSYSAVMPRMVTHYAVSKGPCRPGGGRGLRALGCLGSRSLCNVGFGRPRVASRCGGTLPGFGYRLGATCGPSACITPVTINESLLVPLALEIDPTVQRVKRDEKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQTNIEPIFEGYISALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEEICLLQSQISETSVIVKMDNSRELDVDGIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAGNHCDNLRNRKNEILEMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHRLCEGIGPVNISVSSSKGAFLYEPCGVSTPVLSTGVLRSNGGCSIVGTGELYVPCEPQGLLSCGSGRKSSMTLGAGGSSPSHKH
Protein: PIH1 domain-containing protein 1 (Q1RM55)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in the assembly of C/D box small nucleolar ribonucleoprotein (snoRNP) particles (By similarity). Recruits the SWI/SNF complex to the core promoter of rRNA genes and enhances pre-rRNA transcription (By similarity). Mediates interaction of TELO2 with the R2TP complex which is necessary for the stability of MTOR and SMG1 (By similarity). Positively regulates the assembly and activity of the mTORC1 complex (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9CQJ2}.
Interaction partners:
- RuvB-like 2
- RNA polymerase II-associated protein 3
- RuvB-like 1
- Nucleolar protein 58
- Dynein axonemal assembly factor 10
- Sperm-associated antigen 1A
- Protein UXT
- PIH1 domain-containing protein 2
- Si:ch211-103e16.5.
- TELO2-interacting protein 1 homolog
Sequence:
MDTDASLLLGVEHEQKQQEELYQQLLLQTMGKLQSDSPPSKVIRPQPGLCVKTSSVSDKKKVFLNICQSQTVPPPPHLSQEALVELLESEDPTSYRVPMSLGEPHTEVDNSSQGCTVYDVVINDEFFQKCEKDTLFQQFLIAVSLEGLENKYSLELSRDIKILKNRKFMGSIAEQNIRTKSKPIIQEIDSKESLTLPSAAKRPEFTLLVEPPSGKAEHLIAEILLPGVSSARSLVLDLGEDRLVLIARPSLFHLDIFFPVLIDQENSVAQYNTNTQTLTVTMPVVSL
Protein: Methionine--tRNA ligase, cytoplasmic (EC 6.1.1.10) (Methionyl-tRNA synthetase) (Q8MRS4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MIIYTNDGNPLGLQLLMLAKFAKQPVQVQLVNLNDAKYKDLLVLPTLELDNGLRLFSPAAIAKYLFVGEGQQRDEWLEWSATLLAPALAHHMAVGHKADANALPVLNALVKKLDDKLKATPYLAGDKPSAADIAIWSLLAPDGTLKGAQNVDNLRDWYGRVKALPEVQEVLAEQPLKDLSFNALQQSNRYGGLHHVPLKRLSLADASKLLVDTTPTVADTVTNEEISAAKATFTYTAPKEIKEERTVLPKPGERNVLITSALPYVNNVPHLGNIIGCVLSADIYARYSRSAGYNTLLICGTDEYGTATENKALAENLTPREICDKYFELHNAIYRWFGIGFDYFGRTTTQEQTDIVQEAFKDVLKAGYIITESVEQLLCQKCDRFLADRFVEGTCPHPGCGYEDARGDQCDKCGKLVNATELIRPRCKVCNSAPVLRSSDQLFIDLPKAEPQLKEWVDKSEGGWTHNAKVITRAWLKEGLKPRCITRDLKWGIPVPHEGFEKKVFYVWFDAPFGYVSMTKRYTKEYQQWWQPAKGTDVELFQFMAKDNVPFHSVVWPSVLLAINKGHTLVSHIMATEYLNYEDGKFSKSRGIGVFGNDAQETGIPADVWRFYLASARPEGQDSSFSWNDLAARNNSELLNNLGNFVNRALVFCEKNFSSTVPGVITTQDELVLLALINRELRGYINSMEKAKLRDGVRHLLAISRHGNGYMQSQQPWVLLKGTDDQKTRASTIIGLCVNIACLLANLLFPYMPTTARTLFGQLNAKQTPLNAEKPLVTLLLPAGHQIGKPAPLFAKLEQSFIDELKGKYGGAQATNDAAQAVQAQADKVRELKASTKDKAIWQPEVTKLLDLKKQLEEAKKKTATAAAPAATPAPSNGSQSVQDLEKAIQEQGDKVRKLKGSTKDKTVWQPEVNILLDLKKQLEAVQKAAKAAPAANAAPAASPAATADAAKVKALEDKIAQQAEKVRTLKATGDAAVWKPEVDILLSLKNELAALTGTPVAGGQGKGKKKK
Protein: Tryptophan aminotransferase-related protein 1 (EC 2.6.1.27) (EC 2.6.1.99) (Q9LR29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in auxin production. TAA1, TAR1 and TAR2 are required for proper embryo patterning.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable indole-3-pyruvate monooxygenase YUCCA10
- Probable indole-3-pyruvate monooxygenase YUCCA1
- Tryptophan N-monooxygenase 1
- Probable indole-3-pyruvate monooxygenase YUCCA11
- Tryptophan N-monooxygenase 2
- Probable indole-3-pyruvate monooxygenase YUCCA4
- Phenylacetaldehyde synthase
- Indole-3-pyruvate monooxygenase YUCCA2
- Indole-3-pyruvate monooxygenase YUCCA6
- Probable indole-3-pyruvate monooxygenase YUCCA7
Sequence:
MMVGCENSKKSDSGSNEDKSLSDDIINLDQGDPTAFQEYWMKKKDRCTVVIPAWDLMSYFSDTKNVCWFLEPELEKAIKALHGAIGNAATEERYIVVGTGSSQLCQAALFALSSLSEVKPVSIVAAVPYYSTYVEEASYLQSTLYKWEGDARTFDKKGPYIELVTSPNNPDGIMREPVVNRREGGKVIHDLAYYWPHYTPITRRQDHDLMLFTFSKITGHAGSRIGWALVKDIEVAKKMVHYLTINSIGVSKESQTRATTILNELTKTCRTQSESFFEYGYEKMKSRWERLREVVESGDAFTLPNYPQDFCNFFGKTLSTSPAFAWLGYKEERDLGSLLKEKKVLTRGGDRCGCNKRYVRVSMLSRDDDFDVSLQRLATIKDLKCVEP
Protein: Copia-like retroelement pol polyprotein (Mitochondrial ATP synthase subunit G protein) (O82209)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
- AT4g29480/F17A13_300
- Copia-like retroelement pol polyprotein
Sequence:
MASKLVQLQSKACQASKFVAKHGNSYYKQLLEQNKQYIQEPATIEKCSELSKQLLYTRLASIPGRYETFRKEVDYAKNLLKNRANLKVEDAGIAALFGLECFAWFCAGEIVGRGFTFTGYYP
Protein: Cyclin-dependent kinase 18 (EC 2.7.11.22) (Cell division protein kinase 18) (PCTAIRE-motif protein kinase 3) (Serine/threonine-protein kinase PCTAIRE-3) (Q07002)
Organism: Homo sapiens (Human)
Function: May play a role in signal transduction cascades in terminally differentiated cells.
Interaction partners:
- Tudor domain-containing protein 7
- CDK5 and ABL1 enzyme substrate 1
Sequence:
MIMNKMKNFKRRFSLSVPRTETIEESLAEFTEQFNQLHNRRNENLQLGPLGRDPPQECSTFSPTDSGEEPGQLSPGVQFQRRQNQRRFSMEDVSKRLSLPMDIRLPQEFLQKLQMESPDLPKPLSRMSRRASLSDIGFGKLETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDLIHTDRSLTLVFEYLDSDLKQYLDHCGNLMSMHNVKIFMFQLLRGLAYCHHRKILHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCIHYEMATGRPLFPGSTVKEELHLIFRLLGTPTEETWPGVTAFSEFRTYSFPCYLPQPLINHAPRLDTDGIHLLSSLLLYESKSRMSAEAALSHSYFRSLGERVHQLEDTASIFSLKEIQLQKDPGYRGLAFQQPGRGKNRRQSIF
Protein: Delta(9)-fatty-acid desaturase fat-7 (FAT-7) (EC 1.14.19.-) (EC 1.14.19.1) (Fatty-acid desaturase 7) (Stearoyl-CoA desaturase fat-7) (G5EGH6)
Organism: Caenorhabditis elegans
Function: Delta(9)-fatty acid desaturase that acts preferentially on stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols. Also acts on palmitoyl-CoA (hexadecanoyl-CoA), heptadecanoyl-CoA and (11E)-octadecenoyl-CoA (trans-vaccenoyl-CoA), the monounsaturated fatty acids (MUFAs) produced are further used by several other desaturases and elongases as substrates to synthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity). Partially inhibits expression of genes involved in beta-oxidation, such as ech-1 and acs-2, perhaps signaling via the actions of one of its fatty acid products. May form part of a negative feedback loop with the transcription factor nhr-49 to limit beta-oxidation, in which nhr-49 stimulates expression of fat-7 and acs-2, and in turn fat-7 indirectly inhibits acs-2 and other genes also involved in beta-oxidation.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nuclear hormone receptor family member nhr-49
- Delta
- Delta
- Mediator of RNA polymerase II transcription subunit 15
- Acetyl-CoA carboxylase
- Sterol regulatory element binding protein sbp-1
- Long chain fatty acid elongase 2
- Nuclear hormone receptor family member nhr-80
- Medium-chain acyl-CoA ligase ACSF2
- Delta
Sequence:
MTVKTRASIAKKIEKDGLDSQYLFMDPNEVLQVQEESKKIPYKMEIVWRNVALFAALHVAAAIGLYELVFHAKWQTAVFSFALYVFSGFGITAGAHRLWSHKSYKATTPMRIFLMLLNNIALQNDIIEWARDHRCHHKWTDTDADPHNTTRGFFFTHMGWLLVRKHPQVKEHGGKLDLSDLFSDPVLVFQRKHYFPLVILFCFILPTIIPVYFWKETAFIAFYVAGTFRYCFTLHATWCINSAAHYFGWKPYDTSVSAVENVFTTVVAVGEGGHNFHHTFPQDYRASEYSLIYNWTRVLIDTAAVLGLVYDRKTIADEFISRQVANHGSEESRKKSIM
Protein: Uncharacterized protein (Q38CH0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLPWLLFINAITFAALLIAVAVPPLYFQFGNANDTPTDSYPAGNSFPGRNAEGEIVWQRLYILFAVPLCGCLNGLFLYFTYYRHMRHMQFRVELCCTEQRNLKTALFVFLHKKKKPSGMFSESEEEGNFSADLEGNWRLPGDSFIRGSFAFQPKEGKAPPIRTEGLSHRAYSTTPWLPELRELQDIIASVFIQRADKLRDEVMELLHETVLMHIERDKGLTERSIQKSILLLLQQKEELSVPVMTKCLKQIEIEGFSKVVS
Protein: Anti-bacteriophage protein A (P52127)
Organism: Escherichia coli (strain K12)
Function: Part of an antiviral system composed of AbpA and AbpB; when both are expressed from a plasmid they confer resistance to phages T2, T4, T7 and lambda but not RB32 or RB69. Resistance is temperature dependent, it can be seen at 30 degrees Celsius but not at 37 or 42 degrees Celsius. The system impairs phage but not bacterial DNA synthesis (shown for T4, T7 and lambda). Partially suppressed by mutations in T4 gene 41, a replicative helicase.
Interaction partners:
- Anti-bacteriophage protein B
Sequence:
MESNDSGGVAAKHGFLFQDCVAAYHVTRMLRDKTIRSVRCEVTDDIDIVSDGYIDFVQVKSTGKTRWNISDIVQNSKGADKKTIPCSSILHKSMQCESDLSLGRRYSIVTEEKVNKTLEYLTISPNARLDKPGRQELIDDLNKRTDNFLTDSGISVSDWIDAATWEVFSSLRELELLGIKNIRLASQDLHGVILSSETVAEDIWCRILDTVTRKGEHSRRIHSADDKSYLRPDLLEWFKQRVEDDQSRSGRKIYVKRDLPHILTPFRAPMASVCAKRKGQVLHQQYSLKKYRYKHIADNVCQWLDEVFLRPKEMSDIHKLTFIEKRERLKNSVFKSLHDVSEFLGRVLLHATIRQHHESQPIPCMLYVEKAGAEKILENVHIVRRDPEGDQLWIGFSELVTDINIAVRLPEIRDQLYEDISDCIDTARKKILDIKDDNYLLRHDIDEILDGSQPFDAHLDRFTFVLFVGYDSNLLTEPETPGFEDDLEKETAVLFEKFAADLIEDSPFANLCIHVFIYPAPSLERLTQLVDEKVREVV
Protein: Farnesyl pyrophosphate synthase (MhFPPS) (MhIDS-2) (EC 2.5.1.10) (A0A343W970)
Organism: Murgantia histrionica (Harlequin bug)
Function: Farnesyl pyrophosphate synthase involved in murgantiol biosynthesis, a male-released aggregation pheromone, by catalyzing the formation of (2E,6E)-farnesyl diphosphate.
Interaction partners:
Sequence:
MPFTKMCTSKLANPLMKYYLNLNGKSPLSKLSNSLNSSSFKFISCSPHIVCRELNTVSGVAIRPQTITKDDKRDFMAVFPDIVRDLTQLNPGISDLSTLISKLMQYNVSGGKKVRGLTVVYSYRMLAPDHALTPENIRLAQILGWCVEMLQGFFVVIDDLADQSVTRRGRPCWYRLPGVGLRASSDALLIQSGCFQLLQQHCKDKEFYVDLVELFLDALRRTTYGQTLDYVSSFPNINHLTMDRYNFITKYKTAYYTYHLPVATAMYMAGIYNAELHRQAKSVLLEMGHYFQVQDDYLDVFGDEEMIGKKGTDIQEGKCTWLAIIAFQRASPPQREVLESCYGTKEPEKIKKVKDIFIELSLPAVYHAYEEETYNLITRQIQQLSQGLPHELFLTLLHKLYGRKQ
Protein: Zinc finger CCHC-type containing 8 (F5GX80)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKDCPMPRNAARISEKRKEYMDACGEANNQNFQQRYHAEEVEERFGRFKPGVISEELQDALGVTDKSLPPFIYRMRQLGYPPGWLKEAELENSGLALYDGKDGTDGETEVGEIQQNKSVTYDLSKLVNYPGFNISTPRGIPDEWRIFGSIPMQACQQKDVFANYLTSNFQAPGVKSGNKRSSSHSSPGSPKKQKNESNSAGSPADMELDSG
Protein: Cta24p (A0A1D8PP87)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Tlo9p
- Tlo1p
- Cta2p
- Cta26p
- Tlo13p
- Mitochondrial inner membrane protease subunit
- Zcf22p
- Zcf4p
Sequence:
MPENLQTRLHNSLDEILKSSGYIFEIIDQNRKQSNVITSPNNELIQKSITQSLNGEIQNFHAILDQTVSKLNDAEWCLGVMVEKKKKHDELKVKEEAARKKREEEAKKKAEEAKKAEEIKKAEEAKKVEEAKKAEEAKKAEEAKKAEEAKKAEEAAKKAEEAAPQKFDNFDDFIGFDINDNTNDEDILSNMDYEDLKLDDKVPATTDNNLDMNNILENDESILDGLNMTLLDNGDHVNEEFDVDSFLNQFGN
Protein: Interferon a3 (Type I interferon 1) (rtIFN1) (Type I interferon a3) (IFN1-a3) (P0DMS7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Key player in antiviral response. Induces expression of TLRs, including that of TLR3, TLR9 and TLR8a1, and that of cytosolic pattern recognition receptors, including RIGI, IFIH1/MDA5 and DHX58/LGP2. Also induces MX1 and its own expression. In the presence of intracellular IFNAR2 (iIFNAR2) and IFNAR1B, intracellular isoform 3 may mediate STAT1 and STAT2 phosphorylation and induction of EIF2AK2, MX1 and RSAD2.
Subcellular location: [Isoform 1]: Secreted {ECO:0000305|PubMed:24244163}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:24244163}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol {ECO:0000269|PubMed:24244163}.
Interaction partners:
Sequence:
MYTMQSWSCIFLIICSMQSVCHCCDWIRHHYGHLSAEYLSLLDQMGGDITKQNAPVLFPTSLYRHIDDAEFEDKVIFLKETIYQITKLFDGNMKSVTWDKKNLDDFLNILERQLENLNSCVSPAMKPERRLKRYFKKLNSKVLRKMNYSAQAWELIRKEIKRHLQRLDILAAQMY
Protein: Putative lysophosphatidic acid:oleoyl-CoA acyltransferase (LPAAT) (Lysophosphatidic acid acyltransferase) (EC 2.3.1.51) (Vacuolar protein sorting-associated protein 66) (Q9US27)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acyl-CoA-dependent lysophosphatidic acid acyltransferase with preference for oleoyl-CoA. Involved in triacylglyceride homeostasis and lipid droplet formation. Involved in vacuolar protein sorting (By similarity).
Subcellular location: Lipid droplet {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Note=Lipid droplets consist of a surface phospholipid monolayer and a hydrophobic interior. The latter makes embedding of proteins containing transmembrane segments difficult, and these may instead adopt a hairpin or monotonic conformation when associated with lipid droplet membranes (By similarity). {ECO:0000250}.
Interaction partners:
- Lysophospholipid acyltransferase
- Putative phosphatidate cytidylyltransferase
- Uncharacterized acyltransferase C1851.02
- Uncharacterized acyltransferase C1718.04
- Nuclear elongation and deformation protein 1
- Probable diacylglycerol pyrophosphate phosphatase 1
- CTP-dependent diacylglycerol kinase 1
- Phospholipase D1
- NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- Triacylglycerol lipase ptl3
Sequence:
MEKFTRWRDPGTGIAPFHPINTETPSGFNFKWILIVVVMILRVPLCIISVTLWFLWSCFLKPILSIQPKLSFFIDSSLSRLLLLCFGCLKLSKSTSGSFVQGDSLQPGDILAVNHSSPLDVLVLSCLYNCTFAVCDSKTSNVSIISAQAYFWSCFFSPSKLKITDAKPLAKVAAKASKIGTVVILFPEGVCTNGRALCQFTPCFDSAKETDRIFPLYIKYLPPCVTLPVPSLLSFARSVLLTVSFEIRIRFSAEPLIPRNCTDVTESAQEVLSKLGRSRVVKLGKSDKLSYLDARSKKHV
Protein: Uncharacterized protein C13E7.08c (Q9P6R2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cell division control protein 73
- RNA polymerase-associated protein C651.09c
- Tetratricopeptide repeat protein 1
- RNA polymerase II-associated protein 1 homolog
- FACT complex subunit pob3
- FACT complex subunit spt16
- Transcription elongation factor spt5
- Transcription elongation factor spt4
- Transcription elongation factor spt6
- Transcription elongation factor S-II
Sequence:
MSDSKEDIRNGQEEDDLFSENEDNHTSQQDELINGHIENDSETAVSDDGLFSNTEEATEAPEADVPVKKVLEVAVPNFKSPASASNDVFHAHIPNFLSVEQTPYDPEQYAAEAEADAALLEHDAHWGQRIKHKVDNTVRWRLGPSGSYQSNAQIVQWSDGSYSLRIGNDIYDTQNKLISQPTFVTASHEAQHLLRVQTSFKSSFTFLPSAINTATRSKLPSMRLTTVQVPSRSVQEIIIEKDPELLKRQAEKYEEERSRARRRLEKRKQLNNYQNGTGEEEEDYSSFYGPRSTYSEQNEIIDSDRMDRLKRIKQEGAGQYRGYNKDLEENEEDDLGDFIAEEEEEEEQEEEQEEDEEDEEEVGAGSDIKGFDADKEASVARATINKYEDDEVIPSAVETDRSETVTETSVGDGSVQRRVKRRIVESDSE