wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein uL13 (60S ribosomal protein L16-A) (Q5AB87)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein eS17
- Large ribosomal subunit protein uL1
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL34
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein uL30
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein eL31
Sequence:
MSSFEKVVVIDGKGHLLGRLASIVSKQILNGQKVVVVRCEELNISGEFFRNKLKYHDYLRKATRYNKKKGPFHFRAPSRILYKAIRGMIPHKTARGKAALERLKVFEGVPPPYDKKKRVVVPQALRVLRLKPGRKYTTVGKLSSAVGWKYESVVEKLEEKRKVQSAEYYAKKKALTKKLNAAKASTAESEAAQKLAAFGY
Protein: Phosphatidylcholine:diacylglycerol cholinephosphotransferase 1 (AtPDCT1) (EC 2.7.8.-) (Protein REDUCED OLEATE DESATURATION 1) (Q9LVZ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as phosphatidylcholine:diacylglycerol cholinephosphotransferase that catalyzes the transfer of the phosphocholine headgroup from phosphatidylcholine (PC) to diacylglycerol, a major reaction for the transfer of 18:1 into phosphatidylcholine for desaturation and also for the reverse transfer of 18:2 and 18:3 into the triacylglycerols synthesis pathway.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phospholipid:diacylglycerol acyltransferase 1
- Lysophospholipid acyltransferase 2
- Delta
- Acyl-lipid omega-3 desaturase
- AT3g15280/K7L4_8
- Lysophospholipid acyltransferase 1
- 3-ketoacyl-CoA synthase 18
- Putative phospholipid:diacylglycerol acyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase 2
- Diacylglycerol O-acyltransferase 3
Sequence:
MSAAAAETDVSLRRRSNSLNGNHTNGVAIDGTLDNNNRRVGDTNTHMDISAKKTDNGYANGVGGGGWRSKASFTTWTARDIVYVVRYHWIPCMFAAGLLFFMGVEYTLQMIPARSEPFDLGFVVTRSLNRVLASSPDLNTVLAALNTVFVGMQTTYIVWTWLVEGRARATIAALFMFTCRGILGYSTQLPLPQDFLGSGVDFPVGNVSFFLFFSGHVAGSMIASLDMRRMQRLRLAMVFDILNVLQSIRLLGTRGHYTIDLAVGVGAGILFDSLAGKYEEMMSKRHLGTGFSLISKDSLVN
Protein: Dual specificity tyrosine-phosphorylation-regulated kinase 4 (EC 2.7.12.1) (Q9NR20)
Organism: Homo sapiens (Human)
Function: Possible non-essential role in spermiogenesis.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:17292540}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:21127067}. Nucleus {ECO:0000269|PubMed:21127067}.
Interaction partners:
- DDB1- and CUL4-associated factor 7
Sequence:
MPASELKASEIPFHPSIKTQDPKAEEKSPKKQKVTLTAAEALKLFKNQLSPYEQSEILGYAELWFLGLEAKKLDTAPEKFSKTSFDDEHGFYLKVLHDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQPRPQTLRKSNSFFPSETRKDKVQGCHHSSRKADEITKETTEKTKDSPTKHVQHSGDQQDCLQHGADTVQLPQLVDAPKKSEAAVGAEVSMTSPGQSKNFSLKNTNVLPPIV
Protein: Uncharacterized protein (Q381R9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFYGTNDVGRPGYARYSESSTPTHSPRGSDRCRTNETSSGMDHWSSPRGIADEVPPILAGSFFSDAEMREMNRVIPAAMPLLVEATSVSWLDASPESYGGSTTAHHPPPGATSSSVGRCAAATPSIPSLAGSLLRKDVRLRGLQMDRRGSNHPVVSSSTASDRTMVDYGVSAECIPVQPPSHVNHEDIDVLSLWTSDHVAATRTHVQQRPCSLRTTPLRVDQKVGVSSSHNLPCKGLERVANLSGNFAVREVIVSRNSYGSLQTRSRSCPVTFCARTSSPAARIVQAPSPSKCMQDVPITFNGKSQAAVDPQKAGDALKQYRLAVENVKKKGYGRSIREILANPCVDDDEDEDEDEEEGVLDGCDVGVYELEEQEE
Protein: Uncharacterized protein C29A10.17 (C6Y4C6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized protein C23D3.16
- Uncharacterized protein tam1
- Uncharacterized protein C1778.05c
- GTP-binding protein gtr1
- Folliculin-like protein bhd1
- Uncharacterized RWD, RING finger and WD repeat-containing protein C11E3.05
- Uncharacterized WD repeat-containing protein C12G12.01c
- Protein sat1
- Guanine nucleotide exchange factor subunit ric1
Sequence:
MGNCCSFLFNNSDDIDEQTPLLNNDGIQRTPPSAEADMSLRKREEEEEWESKVYDVAKNKFIDVFSLRLRTEAPQRDPRDNIYEEVLDQIDSLNLDPKYDVAKPTEQETEFIIRKLGVLIDDINNIKLSDKEIKGKMVINLSKVQPNITGSPS
Protein: Adenine DNA glycosylase (EC 3.2.2.31) (Q10159)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Adenine glycosylase active on G-A mispairs. Has glycosylase and nicking activities and is active at A/G and A/GO sites.
Interaction partners:
- Endonuclease III homolog lyase)
- Checkpoint protein hus1
- G/U mismatch-specific uracil DNA glycosylase
- DNA-
- Uracil-DNA glycosylase
- DNA-3-methyladenine glycosylase 1
- Alkylbase DNA glycosidase-like protein mag2
- Apurinic-apyrimidinic endonuclease 1
- Asteroid homolog 1
- DNA damage checkpoint control protein rad1
Sequence:
MSDSNHSLDLHSYTQLEVERFRESLIQFYDKTKRILPWRKKECIPPSEDSPLEDWEQPVQRLYEVLVSEIMLQQTRVETVKRYYTKWMETLPTLKSCAEAEYNTQVMPLWSGMGFYTRCKRLHQACQHLAKLHPSEIPRTGDEWAKGIPGVGPYTAGAVLSIAWKQPTGIVDGNVIRVLSRALAIHSDCSKGKANALIWKLANELVDPVRPGDFNQALMELGAITCTPQSPRCSVCPISEICKAYQEQNVIRDGNTIKYDIEDVPCNICITDIPSKEDLQNWVVARYPVHPAKTKQREERALVVIFQKTDPSTKEKFFLIRKRPSAGLLAGLWDFPTIEFGQESWPKDMDAEFQKSIAQWISNDSRSLIKKYQSRGRYLHIFSHIRKTSHVFYAIASPDIVTNEDFFWISQSDLEHVGMCELGLKNYRAALEIKKRKVTSLSNFKEPKLTSARRIVTKAEC
Protein: Polycystin-2-like protein 1 (Polycystin-2L1) (Polycystic kidney disease 2-like 1 protein) (Polycystin-2 homolog) (A2A259)
Organism: Mus musculus (Mouse)
Function: Pore-forming subunit of a heteromeric, non-selective cation channel that is permeable to Ca(2+). Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in primary cilia, where it controls cilium calcium concentration, but does not affect cytoplasmic calcium concentration. The channel formed by PKD1L2 and PKD1L1 in primary cilia regulates sonic hedgehog/SHH signaling and GLI2 transcription. Pore-forming subunit of a channel formed by PKD1L2 and PKD1L3 that contributes to sour taste perception in gustatory cells. The heteromeric channel formed by PKD1L2 and PKD1L3 is activated by low pH, but opens only when the extracellular pH rises again. May play a role in the perception of carbonation taste. May play a role in the sensory perception of water, via a mechanism that activates the channel in response to dilution of salivary bicarbonate and changes in salivary pH.
Subcellular location: Cell projection, cilium membrane {ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289}; Multi-pass membrane protein {ECO:0000269|PubMed:29567962}. Cell membrane {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261, ECO:0000269|PubMed:22420714}; Multi-pass membrane protein {ECO:0000269|PubMed:29567962}. Cytoplasmic vesicle {ECO:0000305|PubMed:20538909}. Note=Interaction with PKD1 or PKD1L3 is required for localization to the cell membrane. {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261}.
Interaction partners:
- Polycystin-1-like protein 3
- Polycystin-1-like protein 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- Transient receptor potential cation channel subfamily M member 5
- Taste receptor type 1 member 1
- Polycystin-1
- Taste receptor type 1 member 2
- Taste receptor type 1 member 3
Sequence:
MNSMESPKNQELQTLGNRAWDNPAYSDPPSPNRTLRICTVSSVALPETQPKKPEVRCQEKTQRTLVSSCCLHICRSIRGLWGTTLTENTAENRELYVKTTLRELVVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDSGVSFQTISSMSDFWDFAQGPLLDSLYWTKWYNNQSLGRGSHSFIYYENLLLGAPRLRQLRVRNDSCVVHEDFREDILNCYDVYSPDKEDQLPFGPQNGTAWTYHSQNELGGSSHWGRLTSYSGGGYYLDLPGSRQASAEALQGLQEGLWLDRGTRVVFIDFSVYNANINLFCILRLVVEFPATGGTIPSWQIRTVKLIRYVNNWDFFIVGCEVVFCVFIFYYVVEEILEIHLHRLRYLSSVWNILDLVVILLSIVAVGFHIFRTLEVNRLMGKLLQQPDTYADFEFLAFWQTQYNNMNAVNLFFAWIKIFKYISFNKTMTQLSSTLARCAKDILGFAIMFFIVFFAYAQLGYLLFGTQVENFSTFVKCIFTQFRIILGDFDYNAIDNANRILGPVYFVTYVFFVFFVLLNMFLAIINDTYSEVKEELAGQKDQLQLSDFLKQSYNKTLLRLRLRKERVSDVQKVLKGGEPEIQFEDFTSTLRELGHEEHEITAAFTRFDQDGDHILDEEEQEQMRQGLEEERVTLNAEIENLGRSVGHSPPGELGAEAARGQSWVSGEEFDMLTRRVLQLQCVLEGVVSQIDAVGSKLKMLERKGELAPSPGMGEPAVWENLYNPS
Protein: Serine/threonine-protein kinase mig-15 (EC 2.7.11.1) (Abnormal cell migration protein 15) (Q23356)
Organism: Caenorhabditis elegans
Function: Involved in cell migration and signal transduction. Important in several developmental processes including epidermal development, Q neuroblast migrations and muscle arm targeting. Required with ina-1/pat-3 to stabilize the commissural axons growth cone along a precise direction and are required for the cell to respond appropriately when signaling in the growth cone must change. During gonad morphogenesis, involved in distal tip cell (DTC) migration from the dorsal side of the hermaphrodite body to the midbody to allow for formation of gonad arms.
Interaction partners:
- Protein kinase domain-containing protein
- NCK adaptor protein family
Sequence:
MSSSGLDEIDLNSLRDPAGIFELIEVVGNGTYGQVYKGRHVKTAQLAAIKIMNINEDEEDEIKLEINMLKKHSHHRNVATYYGAFIKKLPSSTGKHDQLWLVMEFCGSGSITDLVKNTKGGSLKEEWIAYICREILRGLYHLHQSKVIHRDIKGQNVLLTDSAEVKLVDFGVSAQLDKTVGRRNTFIGTPYWMAPEVIACDESPEATYDSRSDLWSLGITALEMAEGHPPLCDMHPMRALFLIPRNPPPKLKRNKKWTKKFETFIETVLVKDYHQRPYTGALLRHPFIKEQPHEQTIRHSIKEHIDRNRRVKKDDADYEYSGSEDDEPSPNNRGPSMGIRDDSESSSMIPMDNTLRKGFQKLQESSRGFAEPGAQQLRRLPQQPAPAPFQYQQSRYVEPRRESSEVKLRAVSSRGAADGPRHSPASRPRPVSHHQRSPQQSHPAAPHLADLANYEKRRRSEREERRERERQAHHAMPIARVSASVPAPQQSRKMSEPLLITHVKPEDLDVLASELSKMGGHHNGRSREESMSPPPPAPPPREASISSITDTIDVGELDNGADAEWDDLKDIMMNGEGTLRGPNKPLPPTPTDGENTLVSDVRRNGNGNSGHGAYKGKKIPEIRPGIISLDDDDSDSDNEEGNEPLMFKPINASSSRGALPDLLPKSPQLRRQINDQTRQMSDDRADESASLFGSFYQPNGFQNSDSRSSIQHSFSNRDREKSFVGYFGGGAGAGGGTVNRPGRPQDINQVQVNVTPNSNGTPAENDAPEIRKYKKKFSGEILCAALWGVNLLIGTDSGLMLLDRSGQGKVYPLISRRRFDQMTVLEGQNILATISGRKRRIRVYYLSWLRQKILRTEGAGSANTTEKRNGWVNVGDLQGAIHFKIVRYERIKFLVVGLESSIEIYAWAPKPYHKFMSFKSFGSLSHVPLIVDLTVEDNARLKVLYGSTGGFHAIDLDSAAVYDIYTPAQSGQTTTPHCIVVLPNSNGMQLLLCYDNEGVYVNTYGRMTKNVVLQWGEMPSSVAYISTGQIMGWGNKAIEIRSVDTGHLDGVFMHKKAQKLKFLCERNDKVFFSSAKGGGSCQIYFMTLNKPGLTNW
Protein: Metalloproteinase inhibitor 4 (Tissue inhibitor of metalloproteinases 4) (TIMP-4) (Q9JHB3)
Organism: Mus musculus (Mouse)
Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor.
Subcellular location: Secreted.
Interaction partners:
- Matrix metalloproteinase-9
- Matrix metalloproteinase-14
- 72 kDa type IV collagenase
- Neutrophil collagenase
- Stromelysin-1
- Collagenase 3
- Matrilysin
- Metalloproteinase inhibitor 2
- Macrophage metalloelastase
Sequence:
MPWSPLAALSWALVLRLLALLWPPGRGEACSCAPAHPQQHFCHSALVIRAKISSEKVVPASKDPADTQKLIRYEIKQIKMFKGFEKAKDIQYVYTPFDSSLCGVKLETNSHKQYLLTGQILSDGKVFIHLCNYIEPWEDLSLVQRESLNHHYHQNCGCQITTCYAVPCTISAPNECLWTDWLLERKLYGYQAQHYVCMKHVDGICSWYRGHLHLRKEYVDIIQP
Protein: Ribosome-inactivating protein momorgrosvin (EC 3.2.2.22) (rRNA N-glycosidase) (P83323)
Organism: Siraitia grosvenorii (Monk's fruit) (Luo han guo)
Function: Inhibits protein synthesis in the rabbit reticulocyte lysate system.
Interaction partners:
Sequence:
DVTFSMLGANGATYYQFF
Protein: Golgin-45 (Basic leucine zipper nuclear factor 1) (JEM-1) (p45 basic leucine-zipper nuclear factor) (Q9H2G9)
Organism: Homo sapiens (Human)
Function: Required for normal Golgi structure and for protein transport from the endoplasmic reticulum (ER) through the Golgi apparatus to the cell surface.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11739401}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:11056056, ECO:0000269|PubMed:9129147}. Note=Detected in the nucleus upon heterologous expression. Not detected in the cytoplasm. {ECO:0000269|PubMed:11056056, ECO:0000269|PubMed:9129147}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:11056056}. Note=Not detected in the nucleus. {ECO:0000269|PubMed:11056056}.
Interaction partners:
- Golgi reassembly-stacking protein 2
- Ras-related protein Rab-2A
- Golgi reassembly-stacking protein 1
- Golgi resident protein GCP60
- Golgin subfamily A member 2
- Golgin subfamily A member 5
- Methyl-CpG-binding domain protein 4
Sequence:
MTTKNLETKVTVTSSPIRGAGDGMETEEPPKSVEVTSGVQSRKHHSLQSPWKKAVPSESPGVLQLGKMLTEKAMEVKAVRILVPKAAITHDIPNKNTKVKSLGHHKGEFLGQSEGVIEPNKELSEVKNVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDLQYHFERLAREKNQLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNSRAALQRQNRDAHGAIQDLLSEREQFRQEMIATQKLLEELLVSLQWGREQTYSPSVQPHSTAELALTNHKLAKAVNSHLLGNVGINNQKKIPSTVEFCSTPAEKMAETVLRILDPVTCKESSPDNPFFESSPTTLLATKKNIGRFHPYTRYENITFNCCNHCRGELIAL
Protein: Biotinidase (EC 3.5.1.-, EC 3.5.1.12) (RT06651p1) (RT12656p1) (Q9W430)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI02923p
- Folylpolyglutamate synthase
Sequence:
MKSIQLSFLLLSVLFSSSHQLSKPEDPTYTAAVVEHSQPVGDSPRARTTSASESFQKIIREVGDVDIIVFPEHILNSQATATFVPHESQNITPCYQTDYELFLIELSCSARANHLYVVINVVEKELCAHGAGSDTYNPCPSSGVRYFNTNVVFDRRGRIVSRYRKTHLWRHEYVSTSVLRSPDISIFRTDFGVTFGHFICFDMLFYDPAMKLVKEHKITDIVYPTYWFSELPFLGAVQLQEGWAFGNDVNVLAADASNPDGRTSGSGIYAGRGGRLVAEIFEQPTTKLLIAEVPKREHGQLAPTFTPIFEPQRKTQRLTGLATYRDNNVDIFESELLDDDFLSFERQLCHGSFCCTFSIERKVTSAAENELPSSGAKSYRYRIGVYWGNETTVIGVDRTEQATCALFACTDVRLASCGYIYPENEEVINTHHFTKLSISGNFPAAPRGRRLIMPSSLNALFLPVSVSDYEWIESPEAANNLDKTILVDLKLAKAQNDLLTFAIWANYYTDIPSTHNLDHMQPNGTQSNPSTSASSTVSAFWILCVLNCFISVL
Protein: Trypsin inhibitor 2c (BWI-2c) (P86794)
Organism: Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum)
Function: Inhibits bovine trypsin with a Ki of 0.174 nM and trypsin-like proteases from G.mellonella larvae. Has no activity against serine proteases chymotrypsin, subtilisin and elastase. Has no activity against cysteine proteases from beetle gut.
Interaction partners:
Sequence:
SEKPQQELEECQNVCRMKRWSTEMVHRCEKKCEEKFERQQR
Protein: NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 1) (NDH subunit 1) (NADH-plastoquinone oxidoreductase subunit 1) (Q6ENA2)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01350}.
Interaction partners:
- NAD
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Uncharacterized protein
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
Sequence:
MIIDRVQVEAINSFSNLELLKEVYGLIWILPILTLLLGITIEVLVIVWLEREISASIQQRIGPEYAGPLGLLQAIADGTKLLFKEDILPSRGDIPLFSIGPSIAVISILLSFLVIPLGYRFVLADLSIGVFLWIAISSIAPIGLLMAGYSSNNKYSFLGGLRAAAQSISYEIPLTFCVLAISLLSNSLSTVDIVEAQSKYGFFGWNLWRQPIGFLVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKYGLFYLVSYLNLLVSSLFVTVLYLGGWNLSIPYISFFGFFQMNKMVGILEMTMSIFITLTKAYLFLFISITIRWTLPRMRMDQLLNLGWKFLLPISLGNLLLTTSFQLVSL
Protein: Ferripyochelin binding protein (Q8YHR0)
Organism: Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M)
Interaction partners:
Sequence:
MPIYAYNGHKPQFADRESNWIAPDATLIGKVVVGENAGFWFGAVLRGDNEPITIGADTNVQEQTIMHTDIGFPLTIGAGCTIGHRAILHGCTIGENTLIGMGAIVLNGAKVGKNCLIGAGTLVKEGMEIPDNSLVVGSPARVLRQLDDAAVEKLRASAKHYVERGHSFMRGMEPA
Protein: Myosin motor domain-containing protein (Q9TZI9)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- PDZ domain-containing protein
- Palmitoyltransferase spe-10
- PDZ domain-containing protein
- Sperm vesicle fusion protein fer-1
Sequence:
MDSSTHSTADFGRLVWISDEAEGFVAARITDIAENGFTLATEKTSETVNRRYEDTWACEEDPQKSVEDNCALVHLNEATLLNNCRLRYANGKIYTYVANILISINPYQLIDGLYSPETIKEYRGKSLGQMEPHIFAIADKAYREMRRIKTSQSIIVSGESGAGKTESQKAVLKYLCENWGTDAGPIQQRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFSDNGTVAGGFVSHYLLETSRVCRQAAGERNYHIFYQLIAGSSPDLYKKLRLAPASSFNYLKHGATLFFVNSKSSLKTDASRFSETNSSVSDSIISDIDDFAKLERALALSGVSDDEKMFIWSTVAGILHLGNIEFEENASDSRGGCMITSGTENSLMAAAELLGLEPEEMKLGLCARIMQTTKGGVKGTLIRVPLKAHEASAGRDALAKAIYSKLFDWLVAQINKSIPFEKSTGYIGVLDVAGFEYFAVNSFEQFCINFCNEKLQHFFNERILKQEQEMYEAEGLNIQKIEFTDNLDCIELFEKKASGLFDLLDEEAKLPRATFQHFTQRAHESNKNHFRLDAPRKSKVKSHREMRDDEGLLIRHYAGTVCYETRYFVEKNNDQLHNSLEMLIEQSSFPLVVSLFTSEATGAVKTGGRLKAVSVGAKFKSQLSSLLDKLNNTGTHFVRCVKPNSQMKAWHFDGSAILGQLQCAGMASVLRLMQEGFPSRTSFADLYAMYEKNLPPSLARLDPRLFSKCLFHALGLDQNDFQFGNTKVFFTAGKFAEFDQMMKQDPETVMELISKVTDWLVKARWRKVQYGAWSVIKLKNKILYRAEKIKKIQAWIRGYLVRKRFHKRLAIFRKACALLENSREMTDILARMNESSQDKWREAADSTTGELDELVKTIKNDDLNTEIDRAVKCYEDCVKRVDSIIADLKLQLENDELAEVERARKEAEDKERREAEEKAAAEQEKILRRKMEEEREKAQKEYELQLEMQKQKLAAEAEEEVKRRNKEERDRLDAAVSSRLASSDGVALVAQEASAAPPKQQSKYDLGNWKYADLRDAINTSNDMELLVACKEEFHRRLRIYNEWKSKNSANRDVPPTRAPLTVYNQQKPSSSSMMVSRVQAAPHLNPALTQQRYFKVSFATDNKKKNGGSQSGMWYAHFNGQYIRRQLTIRPSQKPQLLVAGKDDLQMCELPLEQTGLLRKKGAEISSNDFETMWYHYGGKPIQEWTP
Protein: Cholesterol side-chain cleavage enzyme, mitochondrial (EC 1.14.15.6) (CYPXIA1) (Cholesterol desmolase) (Cytochrome P450 11A1) (Cytochrome P450(scc)) (P00189)
Organism: Bos taurus (Bovine)
Function: A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones. Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C20 to yield 20R,22R-hydroxycholesterol that is further cleaved between C20 and C22 to yield the C21-steroid pregnenolone and 4-methylpentanal. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P14137}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Steroidogenic acute regulatory protein, mitochondrial
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Lutropin-choriogonadotropic hormone receptor
- Steroid 21-hydroxylase
- Cytochrome P450 family 7 subfamily B member 1
- Adrenodoxin, mitochondrial
- Steroid sulfatase
- Sulfotransferase
Sequence:
MLARGLPLRSALVKACPPILSTVGEGWGHHRVGTGEGAGISTKTPRPYSEIPSPGDNGWLNLYHFWREKGSQRIHFRHIENFQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAPEAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKMFHTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFRNYPGILYCLLKSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQHIGDVDTIFNLILTPDKPIFLVFRPFNQDPPQA
Protein: Platelet-activating factor receptor (PAF-R) (PAFr) (Q9TTY5)
Organism: Bos taurus (Bovine)
Function: Receptor for platelet activating factor, a chemotactic phospholipid mediator that possesses potent inflammatory, smooth-muscle contractile and hypotensive activity. Seems to mediate its action via a G protein that activates a phosphatidylinositol-calcium second messenger system. May be involved in the morphological and physical modifications of the oviduct and uterus during the estrus cycle and early pregnancy (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11438398}; Multi-pass membrane protein {ECO:0000269|PubMed:11438398}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit alpha-14
- Toll-like receptor 4
- Coiled-coil domain containing 117
Sequence:
MEPNNSFRVDSEFRYTLFPIFYSIVFVLGVIANSYVLWVFARLYPSKKFNEIKIFMVNLTMADLLFLVTLPLWIVYYYNQGDWILPKFLCNLAGCFFFINTYCSVAFLAVITYNRFQAVTRPIKTAQATTRKRGILLSLIIWVSIVGAASYFFVLDSTNREPNKTGSANITRCFEHYEKGSIPVLTIHIFLVFSFFLVFLIILFCNLVIIRTLLTQQVQIQRNAEVKRRALWMVCTVLAVFIICFVPHHLVQLPWTLAELGFQDTDFHQAINDAHQVTLCLLSTNCVLDPIIYCFLTKKFRKHLTEKLYSMRESRKCSRATSETGTEVVMQLKDVPVKSLKY
Protein: Serine/threonine-protein kinase S6KL (EC 2.7.11.-) (Protein kinase-like 17E) (S6 kinase-like protein) (Q9VWQ2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Displays kinase activity. Inhibits neuromuscular junction (NMJ) growth by interacting with and promoting the proteasome-mediated degradation of the receptor tkv which inhibits bone morphogenetic protein (BMP) signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25748449}.
Interaction partners:
- RAC serine/threonine-protein kinase
- Ribosomal protein S6 kinase
- receptor protein serine/threonine kinase
Sequence:
MGNSQPRNASRSRRTSQWPQGAAELGASASDHHYHQEELYQEQQQQQQQPQQEQPSSRRIQFQAHTNQPTQSHPPGDEEQPVQSQQQQLSTWSLGSLSGGRLNWSFSGARNSFRHRNKATRKSLTSLHGSRRGKTQWHRPLTNSIFNSHFKETSKNDLYRIDHLVAKGAFGVVFKVSSKSDISQCYALKVLKKSKLIEDNSVRQIKDEADIQKVCGHHPFIVKQIDLWQNRHNLHILSEYVPNGELFSKITHFSIDLVRLYIGEIALALDFLHNAGIIYRDAKPENILLTEQFHIKLTDFGLSKWLKLGANTRTMCGTFKYMAPEILCGEPYGHAVDWWALGVIACQMLTQKSPNIKRHLLRRRESVEPEDGLSNAPSIAQINGCLQDSDGDSEDFLPEEVQHLTHEGRDVLRKLLTIEPRQRIRSVMALQRIAIYKDYNLSSKQLLSLSPREIIARDGIRIYEDRHFDQLTNQCAIDAFLDF