wanglab/gogpt-training-data huggingface dataset:
Protein: Chloride channel protein (Q9VUY1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}. Membrane {ECO:0000256|RuleBase:RU361221}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361221}.
Interaction partners:
- Polycomb group RING finger protein 3
Sequence:
MEKFPLKGSREAAAEGNSYITAYQTVMKKSNGHTNGAGGDGDLDGTFRDHPLAQHTKLTTSLTAAGTDDEDMIDITPRSSPGDVIGGGGGGGSSSGYHRETATESDTERDFGHSGGNGGGNHHNQRTMHQHVPTHSAFGDPMDGALSFYGSSDVQDDIPGIGQYEDFHTIDWQRDIARDRMRHRYIVKKRQDSLWDLIKGSIDAGSGWLCVLLVGIAAGCVAGMVDIGASWMSDLKHGICPPAFWFNREQCCYPAKQSVFEEGNCSTWKTWPEIFGLDRNGTGPYIVAYIWYVLWALLFASLSASLVRMFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKSVGLMLSVSAGLTLGKEGPMVHIASCIGNIFSHVFPKYGRNEAKKREILSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALIAAFVLRSLTPFGNEHSVLFFVEYNKPWIFFELIPFVFLGIMGGVIGTFFIKANLWWCRYRKFSKLGQYPVMEVLFVTLVTAIICYPNPFTRMNMNELIFLLVSKCSPGDVTNPLCDYKRMNITSGNSFIEVTEPGPGVYSSIWLLMLTFILKLALTIFTFGMKVPAGLFIPSLLLGAIMGRIVGIGVEQFAYSYPNIWFFTGECADSNLITPGLYAVVGAAAVLGGVTRMTVSLVVIMFELTGGVRYIVPLMAAAMASKWVGDALGRQGIYDAHIALNGYPFLDSKEEFAHTTLAADVMQPKRNETLNVITQDSMTVDDVENLLKETEHNGYPVVVSRENQYLVGFVLRRDLNLAIGNAKRLIEGISSSSIVLFTSSQPIQNLGPQPLKLKKILDMAPITVTDQTPMETVVDMFRKLGLRQTLVTHNGRLLGVITKKDVLRHVKQMDNEDPNTVLFN
Protein: Thioredoxin-like fold domain-containing protein (Q73GA4)
Organism: Wolbachia pipientis wMel
Subcellular location: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
Interaction partners:
Sequence:
MIFRLLFLLIFISVNSYAVVKQDLSDNQYIQKKPNEITSNELLLPLPNDKLLGDPKAPILMIEYASLTCYHCSLFHRNVFPKIKEKYIDTGKMLYIFRHFPLDYRGLKAAMLSHCYEKQEDYFNFNKAVFNSIDSWNYYNLSDLTLLQRIAALSNLKQDAFNQCINDKKIMDKIVNDKSLAINKLGITATPIFFIKLNDDKSYIEHNKVKHGGYKELKYFTNVIDKLYGKAIVK
Protein: Kallikrein 1 (Q6IE13)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRFLVLCLILSLGDYGAFPLIQSRIHRGCKGERHSQPWQVAMYHYDKAVGWGWHPSPTTMSTSPSHNKVRLGQHSLDADGDTGQDVPVRHSIPHPLYNRSLQMPTFLSPDADNSHNLMLRQLREPANTTEAVRVTEEPTEEAKLGSRCLASGWGSTRPDKCMPGSLQCVDLTLMSSDVCTYAYSQRVTESMLCAGHQEGSRDTCMGDSGTTLICDRMLQGITSWGGNPCA
Protein: Glucosamine inositolphosphorylceramide transferase 1 (EC 2.7.1.227) (Glycosyltransferase family protein 64 protein C5) (GT64 C5) (Q84WB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycosyltransferase that mediates the glycosylation of glycosylinositol phosphorylceramides (GIPCs), the major sphingolipids in the plasma membrane; acts as a HexN(Ac)-specific GIPC sugar transferase and accepts glucosamine (GlcN) and N-acetylglucosamine (GlcNAc) as the sugar unit. Responsible for the glycosylation of a subgroup of GIPCs found in seeds and pollen that contain GlcNAc and GlcN (GlcN(Ac)). Maybe involved in the maintenance of cell-cell adhesion.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 3-dehydrosphinganine reductase TSC10B
- Inositol phosphorylceramide glucuronosyltransferase 1
- 3-dehydrosphinganine reductase TSC10A
- GDP-mannose transporter GONST2
- GDP-mannose transporter GONST1
- UDP-N-acetylglucosamine transporter UGNT1
- Alkaline ceramidase
- Neutral ceramidase 1
- Ceramide synthase LOH1
- Long chain base biosynthesis protein 2a
Sequence:
MMEETTDNTGTISSQKNVAASGHNHHHRYKYISNYGVGRRFLFFASCFGFYAFVAATYAWFVFPPHIGRTDHVSSSSLGCREDNEGSWSIGVFYGDSPFSLKPIETRNVWRNESGAWPVTNPVITCASFTNSGLPSNFLADPFLYVQGDTLYLFFETKSPITMQGDIGAAKSIDKGATWEPLGIALDEAWHLSFPFVFNYNGEIYMMPESNEIGQLNLYRAVNFPLSWKLEKVILKKPLVDSTIVHHEGIYWLIGSDHTGFGAKKNGQLEIWYSSSPLGTWKPHKKNPIYNGKRSIGARNGGRAFLYDGSLYRVGQDCGENYGKRIRVSKIEVLSKEEYREVEVPFSLEASRKGKNSWNGVRQHHFDVKQLSSGEFIGLVDGDRVTSGDLFHRVILGYASLAAAISVVILLGFLLGVVNCIVPSTWCMNYYAGKRTDALLNLETAGLFSEKLRRIGSRLNRVPPFLRGFVKPNSSMGKFTLGVIVILGLLLTCVGVRYIYGGSGAVEPYPFKGHLSQFTLATMTYDARLWNLKMYVKRYSRCPSVKEIVVIWNKGPPPDLSELDSAVPVRIRVQKQNSLNNRFEIDPLIKTRAVLELDDDIMMPCDDIEKGFRVWREHPERLVGFYPRFVDQTMTYSAEKFARSHKGYNMILTGAAFMDVRFAFDMYQSDKAKLGRVFVDEQFNCEDILLNFLYANASGSGKAVEYVRPSLVTIDTSKFSGVAISGNTNQHYRKRSKCLRRFSDLYGSLVDRRWEFGGRKDGWDL
Protein: Dihydroorotase (DHOase) (EC 3.5.2.3) (P05020)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Interaction partners:
- Dihydroorotate dehydrogenase
- Aspartate carbamoyltransferase catalytic subunit
- Aspartate carbamoyltransferase regulatory chain
- Orotidine 5'-phosphate decarboxylase
- Carbamoyl phosphate synthase large chain
- Orotate phosphoribosyltransferase
- Cytosine deaminase
- Adenylosuccinate lyase
- NAD
- Cytosine permease
Sequence:
MTAPSQVLKIRRPDDWHLHLRDGDMLKTVVPYTSEIYGRAIVMPNLAPPVTTVEAAVAYRQRILDAVPAGHDFTPLMTCYLTDSLDPNELERGFNEGVFTAAKLYPANATTNSSHGVTSIDAIMPVLERMEKIGMPLLVHGEVTHADIDIFDREARFIESVMEPLRQRLTALKVVFEHITTKDAADYVRDGNERLAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFNRVFLGTDSAPHARHRKESSCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSVNGPQFYGLPVNDTFIELVREEQQVAESIALTDDTLVPFLAGETVRWSVKQ
Protein: Proton-coupled zinc antiporter SLC30A8 (Solute carrier family 30 member 8) (Zinc transporter 8) (ZnT-8) (Q8BGG0)
Organism: Mus musculus (Mouse)
Function: Proton-coupled zinc ion antiporter mediating the entry of zinc into the lumen of pancreatic beta cell secretory granules, thereby regulating insulin secretion.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:19095428}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8IWU4}; Multi-pass membrane protein {ECO:0000255}. Note=Associated with insulin and glucagon secretory granules. {ECO:0000269|PubMed:19095428}.
Interaction partners:
- Insulin-1
- Insulin-2
- Threonylcarbamoyladenosine tRNA methylthiotransferase
- Glutamate decarboxylase 2
- Hematopoietically-expressed homeobox protein Hhex
- ATP-binding cassette sub-family C member 8
- Insulinoma-associated protein 2
- Transcription factor 7-like 2
- ATP-sensitive inward rectifier potassium channel 11
- Solute carrier family 2, facilitated glucose transporter member 2
Sequence:
MEFLERTYLVNDQATKMYAFPLDRELRQKPVNKDQCPGDRPEHPEAGGIYHCHNSAKATGNRSSKQAHAKWRLCAASAICFIFMVAEVVGGHVAGSLAILTDAAHLLIDLTSFLLSLFSLWLSSRPPSKRLTFGWYRAEILGALLSVLCIWVVTGVLLYLACERLLYPDYQIQAGIMITVSGCAVAANIVLTMILHQRNFGYNHKDVQANASVRAAFVHALGDVFQSISVLISALIIYFKPDYKIADPVCTFIFSILVLASTVMILKDFSILLMEGVPKGLSYNSVKEIILAVDGVISVHSLHIWSLTVNQVILSVHVATAASQDSQSVRTGIAQALSSFDLHSLTIQIESAADQDPSCLLCEDPQD
Protein: Adenosine receptor A3 (TGPCR1) (P28647)
Organism: Rattus norvegicus (Rat)
Function: Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. May play a role during reproduction.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q28309}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Adenosine receptor A1
- Guanine nucleotide-binding protein G
- Kininogen-1
Sequence:
MKANNTTTSALWLQITYITMEAAIGLCAVVGNMLVIWVVKLNRTLRTTTFYFIVSLALADIAVGVLVIPLAIAVSLEVQMHFYACLFMSCVLLVFTHASIMSLLAIAVDRYLRVKLTVRYRTVTTQRRIWLFLGLCWLVSFLVGLTPMFGWNRKVTLELSQNSSTLSCHFRSVVGLDYMVFFSFITWILIPLVVMCIIYLDIFYIIRNKLSQNLTGFRETRAFYGREFKTAKSLFLVLFLFALCWLPLSIINFVSYFNVKIPEIAMCLGILLSHANSMMNPIVYACKIKKFKETYFVILRACRLCQTSDSLDSNLEQTTE
Protein: LIM domain-binding protein 1 (G5EEL0)
Organism: Caenorhabditis elegans
Function: Binds to the LIM domain of LIM domain-containing transcription factors. Required for the blmp-1-mediated transcriptional activation or repression of several hypodermal genes, such as bed-3. Regulates sam-10 nuclear localization in PLM neurons. Has a role in synaptic differentiation of PLM mechanosensory neurons. Involved in gonadogenesis.
Interaction partners:
Sequence:
MYGHHPDYGYGNYGHPPPFAGPESSNSHYGMPPSQGTNSQNNMMMRSQATEPQPIGNTVSPLEFRIHDMNRRLYIFSSTGVSENDQQQWWDAFSHEFFDDDCKLWFVIGSEPVAFASRERYIINRQFIPKFFRSIFDSGMRELQYVLRGPSRECTLANGSQAYENENVLQITRYDQSSQFEVNTEGKLYVEFAPFDEVMNYRIKAWTLELKRSNEFVYNQNTADYRVEAQNPEQENKPRMGFFKSTFNLMTMLKILDPMQSIMSSAKSAPAITPREVMKRTLFQHHQVRQQNMRQQQLNQQMMIPAPEPEKPKPARKRQRKPAANPRGSKKATAAAAAAAAAATNGVPPTVPTASPANNQQFPPNPMTSQFQQMSYPDVMVVGEPSMMGSEFGENDERTISRVENSQYDPNAMQMQSLGQGPNSSMNINGRNMMNQHHPGMQPPPGQQHMPPHSMGSQMPTSMHNPMHMPPGSMQGHGGMPPMPSTMANQMPPPNLPPHTMSNQMPNSRMPPMQGQMPPSGMPGQMSNPNMMGSGMPPMSMSSQMPGSMSNPMPNQMPGGMQMNQMPPPNYSQYTGGPPPQWPPPNSAMITG
Protein: Lysosomal phospholipase A and acyltransferase (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (1-O-acylceramide synthase) (ACS) (LCAT-like lysophospholipase) (LLPL) (EC 3.1.1.5) (Lysophospholipase 3) (Lysosomal phospholipase A2) (LPLA2) (Phospholipase A2 group XV) (Q8VEB4)
Organism: Mus musculus (Mouse)
Function: Has dual calcium-independent phospholipase and O-acyltransferase activities with a potential role in glycerophospholipid homeostasis and remodeling of acyl groups of lipophilic alcohols present in acidic cellular compartments. Catalyzes hydrolysis of the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 or A2 activity) and transfer it to the hydroxyl group at the first carbon of lipophilic alcohols (O-acyltransferase activity). Among preferred fatty acyl donors are phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols and phosphatidylserines. Favors sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of phosphatidylcholines and phosphatidylethanolamines. Among preferred fatty acyl acceptors are natural lipophilic alcohols including short-chain ceramide N-acetyl-sphingosine (C2 ceramide), alkylacylglycerols, monoacylglycerols, and acylethanolamides such as anandamide and oleoylethanolamide. Selectively hydrolyzes the sn-1 fatty acyl group of truncated oxidized phospholipids and may play a role in detoxification of reactive oxidized phospholipids during oxidative stress. Required for normal phospholipid degradation in alveolar macrophages with potential implications in pulmonary surfactant clearance. At neutral pH, hydrolyzes the sn-1 fatty acyl group of the lysophosphatidylcholines (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:19017977, ECO:0000269|PubMed:20410020}. Lysosome {ECO:0000269|PubMed:19017977}. Membrane {ECO:0000250|UniProtKB:Q8NCC3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NCC3}.
Interaction partners:
- Patatin-like phospholipase domain-containing protein 6
- Acyl-protein thioesterase 1
- Phospholipase B1, membrane-associated
- Patatin-like phospholipase domain-containing protein 7
- Phosphatidylcholine-sterol acyltransferase
- Glycerophosphocholine phosphodiesterase GPCPD1
- 85/88 kDa calcium-independent phospholipase A2
- Cytosolic phospholipase A2
- Group 3 secretory phospholipase A2
- Phospholipase A and acyltransferase 3
Sequence:
MDRHLCTCRETQLRSGLLLPLFLLMMLADLTLPAQRHPPVVLVPGDLGNQLEAKLDKPKVVHYLCSKKTDSYFTLWLNLELLLPVIIDCWIDNIRLVYNRTSRATQFPDGVDVRVPGFGETFSMEFLDPSKRNVGSYFYTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQMYGGPVVLVAHSMGNVYMLYFLQRQPQVWKDKYIHAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNHTWSHEKVFVYTPTTNYTLRDYHRFFRDIGFEDGWFMRQDTEGLVEAMTPPGVELHCLYGTGVPTPNSFYYESFPDRDPKICFGDGDGTVNLESVLQCQAWQSRQEHRVSLQELPGSEHIEMLANATTLAYLKRVLLEP
Protein: Pectin acetylesterase 11 (EC 3.1.1.-) (Q9FH82)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties.
Subcellular location: Secreted, cell wall {ECO:0000305}.
Interaction partners:
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Subtilisin-like protease SBT1.5
- Probable polygalacturonase At1g80170
Sequence:
MTWLKQMWSSILVLAVVVIGARAVPITYLESAVAKGAVCLDGSAPAYHFDKGSGSGVNNWIVHMEGGGWCTDIATCVQRKSTMKGSSKLMNKDFGFSGILGGKQSTNPDFYNWNRIKVRYCDGSSFTGDIEAVDPTHKLFFRGARVWRAVIDDLMAKGMSNAQNAILSGCSAGALAAILHCDQFKSTLPKTAKVKCVSDAGYFIHGKDITGGSYIQSYYAKVVATHGSAKSLPASCTSSMKPDLCFFPQYVAKTLQTPLFVINAAFDSWQIKNVLAPTSVDKSKAWKTCKLDLKKCTAAQLQTVQGYRDQVLAALAPVRSATTNGLFLDSCHAHCQGGSAATWSGDKGPTVANTKMAKAVGDWFFERSTFQNVDCSSLNCNPTCPAVSTED
Protein: Serine hydroxymethyltransferase (EC 2.1.2.1) (V9HW06)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFDEH
Protein: Cellular retinoic acid-binding protein 2 (Cellular retinoic acid-binding protein II) (CRABP-II) (P51673)
Organism: Rattus norvegicus (Rat)
Function: Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors (By similarity).
Subcellular location: Cytoplasm. Endoplasmic reticulum {ECO:0000250}. Nucleus {ECO:0000250}. Note=Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. {ECO:0000250}.
Interaction partners:
- Retinoic acid receptor beta
- Retinoic acid receptor, alpha
- Retinoic acid receptor, gamma
- Cytochrome P450, family 26, subfamily C, polypeptide 1
- Arginine--tRNA ligase, cytoplasmic
- Retinoic acid receptor RXR-beta
- Cytochrome P450 26A1
- Retinoic acid receptor RXR-alpha
Sequence:
MPNFSGNWKIIRSENFEEMLKALGVNMMMRKIAVAAASKPAVEIKQENDDTFYIKTSTTVRTTEINFKIGEEFEEQTVDGRPCKSLVKWESENKMVCEQRLLKGEGPKTSWSRELTNDGELILTMTADDVVCTRVYVRE
Protein: Turripeptide Pal9a (P86166)
Organism: Polystira albida (White giant-turris) (Pleurotoma albida)
Subcellular location: Secreted {ECO:0000269|PubMed:18948154}.
Interaction partners:
Sequence:
NVCDGDACPDGVCRSGCTCDFNVAQRKDTCFYPQ
Protein: Secreted beta-glucosidase SIM1 (EC 3.2.1.-) (Q5AKU5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Cell surface beta-glucosidase involved in cell wall maintenance and cytokinesis. Plays a role redundant to SUN41.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:17905924, ECO:0000269|PubMed:18227255, ECO:0000269|PubMed:21622905}.
Interaction partners:
- Probable circularly permuted 1,3-beta-glucanase TOS1
- Cell surface mannoprotein MP65
- Repressed by EFG1 protein 1
Sequence:
MKYLTLLTVLSTALATPLQHQHHHHHEHARRAEVTKVVYVNGNGDEVQSQVTENASSGASSGETAETIQTRSSSDVSSSSDSNPVASIASSVASSASSILSNIEGDLSAFSSPSKKFEDGVYDCDSVPVGQGVIGVDWISGLNGGWTTIMNENGDTSLNCKDGYYCSYACQAGMSKTQWPSEQPSNGMSIGGLYCKNGKLYRSNTDNDYLCEWGSKDVNFVSEISEDVAICRTDYPGSENMNIPTLLSAGGKAPCSVVDGDTYFKWQGGKTSTQYYVNNAGVSVEDGCIWGTEGSGVGNWAPVVLGSGTTGGKTYLSLIPNPNNKDKPNYNIKIVGDDVNGDCKYENGQYNGSGSDGCTVTVNSGSAKFVFY
Protein: DDB1- and CUL4-associated factor 13 (WD repeat and SOF domain-containing protein 1) (A0A087WT20)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MQWPPPWRRSPLVSATPPPGPTRGLLCPRRVSEAGDSSTEGARTGHRHYVTPAESAMEGRSQPLPSLRPASPTNAPAHGRGSDCTAKEPPLANVCRQNYGAAQDPVEPAGRRSASHVTGSSLGKAEVACGRRWRWAELLADTSWSPAGRATEMKVKMLSRNPDNYVRETKLDLQRVPRNYDPALHPFEVPREYIRALNATKLERVFAKPFLASLDGHRDGVNCLAKHPEKLATVLSGACDGEVRIWNLTQRNCIRTIQAHEGFVRGICTRFCGTSFFTVGDDKTVKQWKMDGPGYGDEEEPLHTILGKTVYTGIDHHWKEAVFATCGQQVDIWDEQRTNPICSMTWGFDSISSVKFNPIETFLLGSCASDRNIVLYDMRQATPLKKVILDMRTNTICWNPMEAFIFTAANEDYNLYTFDMRALDTPVMVHMDHVSAVLDVDYSPTGKEFVSASFDKSIRIFPVDKSRSREVYHTKRMQHVICVKWTSDSKYIMCGSDEMNIRLWKANASEKLGVLTSREKAAKDYNQKLKEKFQHYPHIKRIARHRHLPKSIYSQIQEQRIMKEARRRKEVNRIKHSKPGSVPLVSEKKKHVVAVVK
Protein: U2 small nuclear ribonucleoprotein B'' (U2 snRNP B'') (P08579)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as component of the spliceosome. Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}.
Interaction partners:
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein-associated proteins B and B'
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein F
- Splicing factor 3B subunit 3
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 2
- Splicing factor 3A subunit 3
- Splicing factor 3B subunit 4
- Small nuclear ribonucleoprotein Sm D1
Sequence:
MDIRPNHTIYINNMNDKIKKEELKRSLYALFSQFGHVVDIVALKTMKMRGQAFVIFKELGSSTNALRQLQGFPFYGKPMRIQYAKTDSDIISKMRGTFADKEKKKEKKKAKTVEQTATTTNKKPGQGTPNSANTQGNSTPNPQVPDYPPNYILFLNNLPEETNEMMLSMLFNQFPGFKEVRLVPGRHDIAFVEFENDGQAGAARDALQGFKITPSHAMKITYAKK
Protein: DNA-directed RNA polymerase subunit alpha (RNAP subunit alpha) (EC 2.7.7.6) (RNA polymerase subunit alpha) (Transcriptase subunit alpha) (Q5SHR6)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Interaction partners:
Sequence:
MLDSKLKAPVFTVRTQGREYGEFVLEPLERGFGVTLGNPLRRILLSSIPGTAVTSVYIEDVLHEFSTIPGVKEDVVEIILNLKELVVRFLNPSLQTVTLLLKAEGPKEVKARDFLPVADVEIMNPDLHIATLEEGGRLNMEVRVDRGVGYVPAEKHGIKDRINAIPVDAVFSPVRRVAFQVEDTRLGQRTDLDKLTLRIWTDGSVTPLEALNQAVEILREHLTYFSNPQAAAVAAPEEAKEPEAPPEQEEELDLPLEELGLSTRVLHSLKEEGIESVRALLALNLKDLKNIPGIGERSLEEIKEALEKKGFTLKE
Protein: Transcriptional repressor scratch 1 (Scratch homolog 1 zinc finger protein) (SCRT) (Scratch 1) (hScrt) (Q9BWW7)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor that binds E-box motif CAGGTG. Can modulate the action of basic helix-loop-helix (bHLH) transcription factors, critical for neuronal differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:11274425}.
Interaction partners:
- Sodium-dependent noradrenaline transporter
Sequence:
MPRSFLVKKVKLDAFSSADLESAYGRARSDLGAPLHDKGYLSDYVGPSSVYDGDAEAALLKGPSPEPMYAAAVRGELGPAAAGSAPPPTPRPELATAAGGYINGDAAVSEGYAADAFFITDGRSRRKASNAGAAAAPSTASAAAPDGDAGGGGGAGGRSLGSGPGGRGGTRAGAGTEARAGPGAAGAGGRHACGECGKTYATSSNLSRHKQTHRSLDSQLARRCPTCGKVYVSMPAMAMHLLTHDLRHKCGVCGKAFSRPWLLQGHMRSHTGEKPFGCAHCGKAFADRSNLRAHMQTHSAFKHFQCKRCKKSFALKSYLNKHYESACFKGGAGGPAAPAPPQLSPVQA
Protein: Palmitoyl thioesterase CPT1C (EC 3.1.2.22) (Carnitine O-palmitoyltransferase 1, brain isoform) (CPTI-B) (Carnitine palmitoyltransferase 1C) (Carnitine palmitoyltransferase I) (CPT I-C) (Q8TCG5)
Organism: Homo sapiens (Human)
Function: May play a role in lipid metabolic process.
Subcellular location: Cell projection, dendrite {ECO:0000269|PubMed:25751282}. Cell projection, axon {ECO:0000269|PubMed:25751282}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:30135643}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the soma and dendritic and axonal projections. {ECO:0000269|PubMed:25751282}.
Interaction partners:
- Acetyl-CoA carboxylase 2
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Mitochondrial carnitine/acylcarnitine carrier protein
- Choline/ethanolamine kinase
- Carnitine O-palmitoyltransferase 1, liver isoform
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Beta-alanine-activating enzyme
- Long-chain-fatty-acid--CoA ligase 1
- Putative mitochondrial transporter UCP3
- Fatty acid CoA ligase Acsl3
Sequence:
MAEAHQAVGFRPSLTSDGAEVELSAPVLQEIYLSGLRSWKRHLSRFWNDFLTGVFPASPLSWLFLFSAIQLAWFLQLDPSLGLMEKIKELLPDWGGQHHGLRGVLAAALFASCLWGALIFTLHVALRLLLSYHGWLLEPHGAMSSPTKTWLALVRIFSGRHPMLFSYQRSLPRQPVPSVQDTVRKYLESVRPILSDEDFDWTAVLAQEFLRLQASLLQWYLRLKSWWASNYVSDWWEEFVYLRSRNPLMVNSNYYMMDFLYVTPTPLQAARAGNAVHALLLYRHRLNRQEIPPTLLMGMRPLCSAQYEKIFNTTRIPGVQKDYIRHLHDSQHVAVFHRGRFFRMGTHSRNSLLSPRALEQQFQRILDDPSPACPHEEHLAALTAAPRGTWAQVRTSLKTQAAEALEAVEGAAFFVSLDAEPAGLTREDPAASLDAYAHALLAGRGHDRWFDKSFTLIVFSNGKLGLSVEHSWADCPISGHMWEFTLATECFQLGYSTDGHCKGHPDPTLPQPQRLQWDLPDQIHSSISLALRGAKILSENVDCHVVPFSLFGKSFIRRCHLSSDSFIQIALQLAHFRDRGQFCLTYESAMTRLFLEGRTETVRSCTREACNFVRAMEDKEKTDPQCLALFRVAVDKHQALLKAAMSGQGVDRHLFALYIVSRFLHLQSPFLTQVHSEQWQLSTSQIPVQQMHLFDVHNYPDYVSSGGGFGPADDHGYGVSYIFMGDGMITFHISSKKSSTKTDSHRLGQHIEDALLDVASLFQAGQHFKRRFRGSGKENSRHRCGFLSRQTGASKASMTSTDF
Protein: Cytochrome P450 18a1 (EC 1.14.-.-) (CYPXVIIIA1) (Q95078)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probably involved in steroid hormones biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ecdysone 20-monooxygenase
- Cholesterol 7-desaturase nvd
- Nuclear hormone receptor FTZ-F1
Sequence:
MLADSYLIKFVLRQLQVQQDGDAQHLLMVFLGLLALVTLLQWLVRNYRELRKLPPGPWGLPVIGYLLFMGSEKHTRFMELAKQYGSLFSTRLGSQLTVVMSDYKMIRECFRREEFTGRPDTPFMQTLNGYGIINSTGKLWKDQRRFLHDKLRQFGMTYMGNGKQQMQKRIMTEVHEFIGHLHASDGQPVDMSPVISVAVSNVICSLMMSTRFSIDDPKFRRFNFLIEEGMRLFGEIHTVDYIPTMQCFPSISTAKNKIAQNRAEMQRFYQDVIDDHKRSFDPNNIRDLVDFYLCEIEKAKAEGTDAELFDGKNHEEQLVQVIIDLFSAGMETIKTTLLWINVFMLRNPKEMRRVQDELDQVVGRHRLPTIEDLQYLPITESTILESMRRSSIVPLATTHSPTRDVELNGYTIPAGSHVIPLINSVHMDPNLWEKPEEFRPSRFIDTEGKVRKPEYFIPFGVGRRMCLGDVLARMELFLFFASFMHCFDIALPEGQPLPSLKGNVGATITPESFKVCLKRRPLGPTAADPHHMRNVGAN
Protein: NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial (EC 1.6.5.3) (Q387C0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- Electron transfer protein, putative
- Acyl carrier protein
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
- Cytochrome c1, heme protein, mitochondrial
- Reiske iron-sulfur protein, mitochondrial
- Mitochondrial carrier protein, putative
- Mitochondrial processing peptidase alpha subunit, putative
Sequence:
MLRRTSFNFTGRAMISRGSPEWSHRLDLKKGKKTTMMHKLGTSKPNNALQYAQMTLHDLTEWCLAYSPWPLTFGLACCAVEMMHAYASRYDLDRFGIVPRPTPRQAEIIIVSGTVTNKMAPILRNIYVQMVNPKWVISMGSCANGGGYYHFSYAVLRGCERAIPVDFWIPGCPPSAESLVFCLHTLQKKIRWHEIQKYSVRD
Protein: Mitochondrial chaperone TCM62 (P38228)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Chaperone. Required for the assembly of succinate dehydrogenase subunits. Ensures mitochondrial gene expression at elevated temperatures and prevents heat-aggregation of the ribosomal subunit VAR1.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9822678}; Single-pass membrane protein {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9822678}; Matrix side {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9822678}.
Interaction partners:
- 10 kDa heat shock protein, mitochondrial
- Heat shock protein 60, mitochondrial
- T-complex protein 1 subunit theta
- ATP-dependent molecular chaperone HSC82
- ATP-dependent molecular chaperone HSP82
- GrpE protein homolog
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Import motor subunit, mitochondrial
- Succinate dehydrogenase cytochrome b subunit
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MLRNCLRKLGNHQTKCSVKTLHTPIYRTKNLQVLRDTLSGIKLLEKIITSSSYNKTLIYEPKYKSKPQVVSSHDTMRLHNVMRELLDSLQVDEATNTRLQSNRPRKLGRVGLQLFMDCIQDNLTATSTSLTCSLLEHYFKYPEKEVTNGIKAGLRYIRDFLAKNKIIVKSQNDVDALVEQLTMSSSDSQSIKRVLKAINYELFSDDIVRVINGNKTYDEVDVSKGWKYPAGILDSNEAYLRSLELPTKKLVSIDKDMLVLMYDGTLRDANKILPTITYARKLRKSVLLIVNGDCTGDALTSVTINNNRNKRENNESRIVVLKYSKKANNDLAPQENLDFIKFLRLPCGYDSIYSPEYSPLVPSKMCADKYYGSIESIKATTGEAFLYNSIDAEAIPNKVPKSFLQNTVTLSIGGHNEIEIDRRRNAIDNCLNNVLCHGLAKGFIPGYGISLLKAIPGLNELKANEPNFMTKVGINAVLSAVILPSEVAFKNAYGYNYYEINSLIAGAINEKSFPMAKFSPNSEPVNTVKDGNLEPWSKMDSCLAGVETFIELLTSCNTIITCVYKKPERHKA