wanglab/gogpt-training-data huggingface dataset:
Protein: PHD finger protein 21A (A0A8I6AXM6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MIIEQQLLHLESLRARNLLENSLSDPRENADLKKQLHELQAKITALSEKQLRQLRQNLIVKQEQPDKFQIQPLSQSENKLQTAQQQPLQPLQQQQQQQQQQQQQQQQQQQQQQQQHAQQSAAPPSLTASQVTVWVEQPRLTSMITTKTLPLVLKAATATMPASVVGQRPTIAMVTAINSQKAVLSTDVQNTPVNLQTSSKVTGPGAEAQVQATPPQPIKVPQFIPPPRLTPRPNFLPQVRPKPVAQNNIPIAPAPPPMLAAPQLIQRPVMLTKFTPTTLPTSQNSIHPVRVVNGQTATIAKTFPMAQLTSIVIATPGTRLAGPQTVQLSKPSLEKQTVKSHTEAEEKQAESRTVTPPAAPKPKREENPQKLAFMVSLGLVTHDHLEEIQSKRQERKRRTTANPVYSGAVFEPERKKSAVTYLNSTMHPGTRKRGRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQPVSLPSPTSTDGDIHEDFCSVCRKSGQLLMCDTCSRVYHLDCLEPPLKTIPKGMWICPRCQDQMLKKEEAIPWPGTLAIVHSYIAYKAAKEEEKQKLLKWSSDLKQEREELEQKVKELSSSISKCMEMKNTILARQKEMRSSLDKVKQLIRLIHGIDLSKPVDSEATVGALSNGPDCTPPANAASTPAPSPSSQSCTANCNQGEETK
Protein: Peroxin-2 (Q95Z07)
Organism: Trypanosoma brucei
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004585}.
Interaction partners:
Sequence:
MAWITDAAVSQFPLATVLKQQGALPTSNMFTALPENRVLRIFQLNALTTQEEVVEILRGYLLDIFNIGALQSYRYVYQDEFSFLLDVILFFGSTWRCGQSVGDRMQNLVLRNEIKALESGQSDAVQLVHSLVPSRARLLLYGVLNLFVPYLFRKLQRRALEEGWEDGGAGVVKRKLAKLLKAVSVSWMIISLLHTLHFLATAQYRTPVERMLSLRLVYGSQDTRRFTNLIYLNQHIFWQIWSSFISVLNIGRYTSRVTRFLQAFTAKPGNPSLTDNACSACHNKPTLPQRSNCGHLYCYYCIKSRLLGPGSAKSFRCLRCGTVVSTTTPWAQ
Protein: Vacuolar protein sorting-associated protein 33A (hVPS33A) (Q96AX1)
Organism: Homo sapiens (Human)
Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG.
Subcellular location: Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q63615}. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome {ECO:0000305}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24554770}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Vam6/Vps39-like protein
- Vacuolar protein sorting-associated protein 18 homolog
- Transforming growth factor-beta receptor-associated protein 1
- Vacuolar protein sorting-associated protein 8 homolog
- Spermatogenesis-defective protein 39 homolog
- Syntaxin-7
- Syntaxin-12
Sequence:
MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF
Protein: RanBP2-type domain-containing protein (Q389A9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRPREALTLPSSSVFQMEERLVFEREISGGISDYFANGGVCITGLSHSFYPFTAIALWAGGAPHSPDDVRLPLLLLALKTDGAFMTAHEANLFGGTSVAGCRYAQLTLRCFGASCPAVRPHRDTRCIQLVVSFLNAAWASTNDDGGKQFATISSELEEFRGPVPLHIVQLLLSVPAIPTLLECVVRRELERCSSDEGISKGLFCACVEGLLSSDNFFTSHHFDEMDAILRCIIGKIGDSFDYLSVRWTPILNKLSRIYMRQWRGEALMSLHDELLAKIPALETKLPLSYLLRCVGSLVDAGATGEADDGGDDARIWRKIVAVTTLAVRLYGSCQSNLQSVWVIFFKGAITLKPQSMVYIRVVEAYHVCASLGHPVIVDKSAFSQVVRLLVSVVGVRSLKETATAVSEFYRFLKEHPSINFLWVIDSLIPIMSEIWKAHGELGCSIVQNITANLQADYFPSRCLSGIRLGDNPMVRRLLEDFKVMERSQFWWRCGCGTQLPSCAQRCLTCLRQGNISWTCGVCGARHSGRVVETVCNCGSPHPRMREAELMDVGVCEGCGEILPPTGECGKCGEIDREKQATRECPSCGCLYSKQALCCPTCYAANEAKSSLLWHCDACGEFNHSAWSKCQHCPGKRKVGCIVTPLQPWVCGCGGRNHPCRTSCESCSLLHRGAYTCACCSIVSTCQKAIEVPLHNSKLRLIVCERCGNVHPRDCNVLCSPFLPRHCHRCGVGYTRESMLSEECCNVCHTRLCYDELRPFCCSHCGQKPAQIGFQCTSCRAPREDVAAADVYVWRCLRETTPATAVTGTHVCGQWNYSWSDHCISCREARARSQYECRARFLPWVCASCGSDNLPTDVLLCPNCENGLQMAPECSVCGLPHLSLDCTVKEDI
Protein: Calcium-dependent protein kinase 16 (EC 2.7.11.1) (Q7XJR9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in signal transduction pathways that involve calcium as a second messenger.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12913141, ECO:0000269|PubMed:21219905}; Lipid-anchor {ECO:0000269|PubMed:12913141, ECO:0000305|PubMed:21219905}. Nucleus {ECO:0000269|PubMed:21219905}. Note=Predominantly localized at the plasma membrane. {ECO:0000269|PubMed:21219905}.
Interaction partners:
- Respiratory burst oxidase homolog protein D
- Uncharacterized membrane protein At3g27390
- Protein DEHYDRATION-INDUCED 19 homolog 2
- Glutamate receptor 3.7
- Respiratory burst oxidase homolog protein C
- Plant intracellular Ras-group-related LRR protein 4
- Calcium-binding protein CP1
Sequence:
MGLCFSSAAKSSGHNRSSRNPHPHPPLTVVKSRPPRSPCSFMAVTIQKDHRTQPRRNATAKKTPTRHTPPHGKVREKVISNNGRRHGETIPYGKRVDFGYAKDFDHRYTIGKLLGHGQFGYTYVATDKKTGDRVAVKKIDKAKMTIPIAVEDVKREVKILQALTGHENVVRFYNAFEDKNSVYIVMELCEGGELLDRILARKDSRYSERDAAVVVRQMLKVAAECHLRGLVHRDMKPENFLFKSTEEDSPLKATDFGLSDFIKPGKKFHDIVGSAYYVAPEVLKRRSGPESDVWSIGVISYILLCGRRPFWDKTEDGIFKEVLKNKPDFRRKPWPTISNSAKDFVKKLLVKDPRARLTAAQALSHPWVREGGDASEIPIDISVLNNMRQFVKFSRLKQFALRALATTLDEEELADLRDQFDAIDVDKNGVISLEEMRQALAKDHPWKLKDARVAEILQAIDSNTDGFVDFGEFVAAALHVNQLEEHDSEKWQQRSRAAFEKFDIDGDGFITAEELRMHTGLKGSIEPLLEEADIDNDGKISLQEFRRLLRTASIKSRNVRSPPGYLISRKV
Protein: Uncharacterized protein (A0A1D8PCZ5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Arp9p
- RSC chromatin remodeling complex ATPase subunit
- Chromatin structure-remodeling complex protein RSC8
- SWI/SNF catalytic subunit
- Uncharacterized protein
- RuvB-like helicase 1
- Chromatin structure-remodeling complex protein RSC58
- Bromo domain-containing protein
- Chromatin structure-remodeling complex subunit SFH1
- Snf5p
Sequence:
MENNSEQQVMKLLDDGLIYDFDNIVYNWQYVFDNVDNNNPINSSEFPLVVTEQPWNTSKNKVNSCQVAFETLQVPIFSLVKTPLAQLYRCGKSTGLVIDIGSSVTSVTPILDGVIQSKCSYHSKYAGDFVNLHVLNYLESKTAINSLLPSKFANSSESFKQYYISRNILQEYKNLSLNYQIKDYQLYNHEFINVSDQQNYLENLFDPTLNKLPNIHIPEPSIDKPGSHGLTNLVFLALKNLESTLLPQNTNDNTSQNRYQKFIEIFKLLLSNVLITGGTSAANGLPDHIINDLRALTQKYFPNYPFSYAVQQIRPSNTENAEIWDRQFGAWFGACNLASMLNDNDEKSNSAKIALDNWFITKADYEELGEDLVAEKFK
Protein: Transcriptional regulator Kaiso (Zinc finger and BTB domain-containing protein 33) (xKaiso) (Q8UVQ4)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional regulator with bimodal DNA-binding specificity. Binds to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' and also binds to the non-methylated consensus sequence 5'-CTGCNA-3'. May recruit the N-CoR repressor complex to promote histone deacetylation and the formation of repressive chromatin structures in target gene promoters. Contributes to the repression of target genes of the Wnt signaling pathway and to the methylation-dependent repression of zygotic transcription prior to the mid-blastula transition (MBT). Also required for gastrulation movements.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
METKKLITATDTQYSGILLNALNDQRIQGLYCDVTVIVEDRKFRAHRNILSACSTYFHQLFSVAGQVVELNFVKADIFAEILNYIYSSKIVRVRCDMLEELIKSGKLLGVPFIAELGIPLSQVKSISGAGGKDGGTDAPSNPDHKAPEPQKSSDSPLPCTVKIKADVKTEMPVITESFSLSSDDYKDKKASGSQDHNSEKEDDDDDVIFCSEIVSSKQAPAERKEAAQTQIPPDNEQVPEVKKVTPSSQVQLTQNSLPTNQQSSKNTSSTTQKFTPPVNANISKNPTPAANGFLSPTAQKQGTPNAVQNQHSQNITSGNALPQQKPVVNFSSIKPQQISAIKPKTEVIIHGNGLSPPSSSVIPLGQQPVTPKHISFDGVQKKQVVTFTQGSPSKPGEFKIKIADVVSGSSLDSFKDSEPRRIIDGKKIITLDTASEIEGLSTGCKVYANIGEDTYDIVIPIKEDPEEGEAKLDLDGLPNRKRMKLKHDDHYELIVDGRVYYICIVCKRSYVCLTSLRRHFNVHSWEKKYPCRYCERVFPLAEYRTKHEIHHTGERRYQCLTCGSSFINYQVMASHIRSVHSLDPSGDSKLYRLNPCKTLQIRQYAYVNNSTNGTVINDGAINVPVITDGGINVPVINDGGIVYDIDPDEPQQPASEGNHANSATKPVNWDNIFIQQSNQNMFKLNTSEGGTEFEFVIPESY
Protein: Protein HESO1 (EC 2.7.7.52) (HEN1 suppressor 1) (RNA uridylyltransferase) (Q5XET5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Uridylates small RNAs to trigger their degradation. Catalyzes the uridylation of 5' fragments produced by AGO1-mediated cleavage of miRNA target RNAs. Acts synergistically with URT1 in unmethylated miRNA uridylation, leading to their degradation. URT1 and HESO1 prefer substrates with different 3' end nucleotides and act cooperatively to tail different forms of the same miRNAs. URT1 and HESO1 act sequentially, with URT1 mono-uridylating the miRNAs followed by their further uridylation by HESO1. URT1 and HESO1 are involved in the uridylation and clearance of RISC-generated 5' mRNA fragments. Able to act on AGO1-bound miRNAs and the uridylated species stay associated with AGO1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22464191}. Cytoplasm, P-body {ECO:0000269|PubMed:25928341}. Nucleus {ECO:0000269|PubMed:22464191, ECO:0000269|PubMed:25928341}.
Interaction partners:
- Small RNA degrading nuclease 1
- Protein argonaute 1
- Small RNA 2'-O-methyltransferase
- Inactive exonuclease DIS3L2
- Protein argonaute 10
- Small RNA degrading nuclease 2
- Endoribonuclease Dicer homolog 1
- DnaA initiator-associating protein
- Small RNA degrading nuclease 5
- Protein HASTY 1
Sequence:
MSRNPFLDPTLQEILQVIKPTRADRDTRITVIDQLRDVLQSVECLRGATVQPFGSFVSNLFTRWGDLDISVDLFSGSSILFTGKKQKQTLLGHLLRALRASGLWYKLQFVIHARVPILKVVSGHQRISCDISIDNLDGLLKSRFLFWISEIDGRFRDLVLLVKEWAKAHNINDSKTGTFNSYSLSLLVIFHFQTCVPAILPPLRVIYPKSAVDDLTGVRKTAEESIAQVTAANIARFKSERAKSVNRSSLSELLVSFFAKFSDINVKAQEFGVCPFTGRWETISSNTTWLPKTYSLFVEDPFEQPVNAARSVSRRNLDRIAQVFQITSRRLVSECNRNSIIGILTGQHIQESLYRTISLPSQHHANGMHNVRNLHGQARPQNQQMQQNWSQSYNTPNPPHWPPLTQSRPQQNWTQNNPRNLQGQPPVQGQTWPVITQTQTQQKSPYKSGNRPLKNTSAGSSQNQGHIGKPSGHMNGVNSARPAYTNGVNSARPPSKIPSQGGQIWRPRHEQ
Protein: Centrosomal protein of 63 kDa (Cep63) (Q96MT8)
Organism: Homo sapiens (Human)
Function: Required for normal spindle assembly. Plays a key role in mother-centriole-dependent centriole duplication; the function seems also to involve CEP152, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication. Reported to be required for centrosomal recruitment of CEP152; however, this function has been questioned. Also recruits CDK1 to centrosomes. Plays a role in DNA damage response. Following DNA damage, such as double-strand breaks (DSBs), is removed from centrosomes; this leads to the inactivation of spindle assembly and delay in mitotic progression.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:32402286, ECO:0000269|PubMed:35793002}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:32402286}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:24613305, ECO:0000269|PubMed:32402286}. Note=Colocalizes with CDK5RAP2, CEP152 and WDR62 in a discrete ring around the proximal end of the parental centriole. At this site, a cohesive structure is predicted to engage parental centrioles and procentrioles. {ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:32402286}.
Interaction partners:
- Centrosomal protein of 152 kDa
- Centrosomal protein of 57 kDa
- Coiled-coil domain-containing protein 14
- Serine/threonine-protein kinase PLK4
- WD repeat-containing protein 62
- Serine/threonine-protein kinase PLK1
- Centrosomal protein of 192 kDa
- Protein moonraker
- CDK5 regulatory subunit-associated protein 2
- Centrosomal protein of 135 kDa
Sequence:
MEALLEGIQNRGHGGGFLTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQMCKKQNDRIFKPTHSRTTEFKNTEFKPTHGQHRHDGIKTEHYKTDLHSPRGQASDSINPMSRVLSPLSPQISPCSSTRSLTSYSLCKTHSLPSALDTNEANFSDTMSESMNDQEEFISSCSLPVSPLGSIATRFLEEEELRSHHILERLDAHIEELKRESEKTVRQFTALK
Protein: DDE-recombinase A (EC 3.1.22.-) (EC 6.5.1.-) (DDE-transposase A) (Gene product 03) (gp03) (Gene product A) (gpA) (MuA) (P07636)
Organism: Escherichia phage Mu (Bacteriophage Mu)
Function: Responsible for viral genome integration into the host chromosome. During integration of the incoming virus, DDE-recombinase A cleaves both viral DNA ends and the resulting 3'-OH perform a nucleophilic attack of the host DNA. The 5' flanking DNA attached to the ends of the viral genome (flaps) are resected by the DDE-recombinase A endonuclease activity, with the help of host chaperone ClpX. The gaps created in the host chromosome by the viral genome insertion are repaired by the host primary machinery for double-strand break repair.
Subcellular location: Host cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MELWVSPKECANLPGLPKTSAGVIYVAKKQGWQNRTRAGVKGGKAIEYNANSLPVEAKAALLLRQGEIETSLGYFEIARPTLEAHDYDREALWSKWDNASDSQRRLAEKWLPAVQAADEMLNQGISTKTAFATVAGHYQVSASTLRDKYYQVQKFAKPDWAAALVDGRGASRRNVHKSEFDEDAWQFLIADYLRPEKPAFRKCYERLELAAREHGWSIPSRATAFRRIQQLDEAMVVACREGEHALMHLIPAQQRTVEHLDAMQWINGDGYLHNVFVRWFNGDVIRPKTWFWQDVKTRKILGWRCDVSENIDSIRLSFMDVVTRYGIPEDFHITIDNTRGAANKWLTGGAPNRYRFKVKEDDPKGLFLLMGAKMHWTSVVAGKGWGQAKPVERAFGVGGLEEYVDKHPALAGAYTGPNPQAKPDNYGDRAVDAELFLKTLAEGVAMFNARTGRETEMCGGKLSFDDVFEREYARTIVRKPTEEQKRMLLLPAEAVNVSRKGEFTLKVGGSLKGAKNVYYNMALMNAGVKKVVVRFDPQQLHSTVYCYTLDGRFICEAECLAPVAFNDAAAGREYRRRQKQLKSATKAAIKAQKQMDALEVAELLPQIAEPAAPESRIVGIFRPSGNTERVKNQERDDEYETERDEYLNHSLDILEQNRRKKAI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0B4KG14)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000256|ARBA:ARBA00004132}.
Interaction partners:
Sequence:
MGEFFKSLNLNYFSSSEVNGAAGNGAPEALGGRLDNDFVGQVVEVAGHRLRIKCVIAEGGYAFVYVAQDVQTGTEYALKRLIGADMQASTAIINEINIHKQLSGHENIVAFVGSSYTAPSTQLGAQYLLLTELCKGGSLVDCFRTNNAPFNPTCVLRIFYQMARAVASLHSQSPPIAHRDIKIENFLIGNDKQIKLCDFGSASTEVLSPTFEWSANQRSMLEDQLNTVTTPMYRSPEMLDTWSNNPIGPKVDIWALGCILYFLCYRKHPYEDGGKLRIINANYMLPPDPQYQCFSDIIRGCLKVNPFERLDITMVLEGLAALAETHNWSLKGPLDLHIMPIESLPAESPLKSSAYSEVYTEPLSAAIPSSYNGHGSLLSSLRGGAGTLLKNIKDTSTKVMQTMQQSLARNDLDISHITSRILVMPCPSDGFESTYKTNNIEDVRLSLESRFVPQKLSIYNFGQRTEPRLPPPVRTVEAGSVYGCPQAHAPNLQGLFTVSADMYNFLNADPKSVVIVQTGDSGGCTAATVICALLMYADLLREPEDAVQVFAVKRHTINLRPSEFRYLYYFGDILRPTPLLPHYKNTTLVSLSCQPVPRMTKARDGCRIYMEVYCNGNLLLSTLQDYEKMRLYQAGPGKIVLPINLTACGDVTVVLFHARKGMVRPQGLKICQFQFNTGFIPEPETLITFTNQDLDDLPDPEQVTPRFCVSLSLAVTDSESPPSHKPPWMPAKPKRSPAALFSSDLEYAEMLDNFGARKSDRVSSPLVLPDVTETAHELPSPMPEPSPPIDLLNLNQQPSDVPAADPLTSAKPSTDASFDLLGAFGDDDSTGIGSAPIPDILPPPPLQQPQPKINNDPFDIFGSVDQGGVPSMKPSGFPPFVGSLPTFVAQPAATTNPSPTHPARASADPFANIADLATGLNLNFNRSTLSGKSPVNTSPQPTQFSSPTHKPSPSSQPQATFMHTPPTPQTLPSTSSIRTPTQPQAVPAQSRPDYSRLHFDSQKAAQQPGTGGSKNSDIFADILGQQGYSFGSKMNQCPRSINEMRKEDLFKDMDPKKVRIMEWTDGKKNNIRALLCSMHTVLWDNAKWQRCEMSTMVTPTEVKKAYRRACLAVHPDKHNGTENEEIAKLIFMELNNAWTDFENDATQQNMFNA
Protein: Gamma-aminobutyric acid receptor subunit beta-1 (GABA(A) receptor subunit beta-1) (GABAAR subunit beta-1) (P15431)
Organism: Rattus norvegicus (Rat)
Function: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand-gated chloride channel.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P08220}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08220}. Cell membrane {ECO:0000250|UniProtKB:P08220}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08220}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit beta-3
- Gamma-aminobutyric acid receptor subunit gamma-1
- Gamma-aminobutyric acid receptor subunit alpha-4
- Gamma-aminobutyric acid receptor subunit alpha-2
- Trafficking kinesin-binding protein 2
- Vesicle-fusing ATPase
- Huntingtin-associated protein 1
Sequence:
MWTVQNRESLGLLSFPVMVAMVCCAHSSNEPSNMSYVKETVDRLLKGYDIRLRPDFGGPPVDVGMRIDVASIDMVSEVNMDYTLTMYFQQSWKDKRLSYSGIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWNGGEGAVTGVNKIELPQFSIVDYKMVSKKVEFTTGAYPRLSLSFRLKRNIGYFILQTYMPSTLITILSWVSFWINYDASAARVALGITTVLTMTTISTHLRETLPKIPYVKAIDIYLMGCFVFVFLALLEYAFVNYIFFGKGPQKKGASKQDQSANEKNKLEMNKVQVDAHGNILLSTLEIRNETSGSEVLTGVSDPKATMYSYDSASIQYRKPLSSREGFGRGLDRHGVPGKGRIRRRASQLKVKIPDLTDVNSIDKWSRMFFPITFSLFNVVYWLYYVH
Protein: Calcineurin subunit B type 2 (Calcineurin B-like protein) (CBLP) (Calcineurin BII) (CNBII) (PPP3R1-like) (Protein phosphatase 2B regulatory subunit 2) (Protein phosphatase 3 regulatory subunit B beta isoform) (Q96LZ3)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q63811}. Note=Localizes in the mitochondria in a SPATA33-dependent manner. {ECO:0000250|UniProtKB:Q63811}.
Interaction partners:
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Nuclear factor of activated T-cells, cytoplasmic 1
- Calcineurin subunit B type 1
- Nuclear factor of activated T-cells, cytoplasmic 3
- Nuclear factor of activated T-cells, cytoplasmic 2
- Nuclear factor of activated T-cells, cytoplasmic 4
- Dynein axonemal assembly factor 10
- Protein phosphatase Slingshot homolog 2
Sequence:
MGNEASYPAEMCSHFDNDEIKRLGRRFKKLDLDKSGSLSVEEFMSLPELRHNPLVRRVIDVFDTDGDGEVDFKEFILGTSQFSVKGDEEQKLRFAFSIYDMDKDGYISNGELFQVLKMMVGNNLTDWQLQQLVDKTIIILDKDGDGKISFEEFSAVVRDLEIHKKLVLIV
Protein: Small ribosomal subunit protein bS1m (28S ribosomal protein S28, mitochondrial) (MRP-S28) (S28mt) (Q9CY16)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P82928}.
Interaction partners:
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein mS37
- Small ribosomal subunit protein mS26
- Small ribosomal subunit protein mS34
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein uS9m
Sequence:
MAALCRSHAGTAGSRFLRALVFSKPLRNASTESGSESATHDSSAPRARSGGFASALERHSDLQRKAELRLESPKPVESFASMLRHSPLTQLGPAKDKLVIGRIFHIVEDDLYIDFGGKFHCVCKRPDVDGEKYQRGTRVRLRLLDLELTSRFLGGTTDTTILEADAVLLGLQEIRDSKSREEQPSK
Protein: Monoacylglycerol lipase ABHD6 (EC 3.1.1.23) (2-arachidonoylglycerol hydrolase) (Abhydrolase domain-containing protein 6) (Q8R2Y0)
Organism: Mus musculus (Mouse)
Function: Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol. Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways. Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids. Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism. BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:26491015}; Single-pass type II membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:26491015}; Single-pass type II membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:20657592}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Lysophosphatidylserine lipase ABHD12
- Protein-serine O-palmitoleoyltransferase porcupine
- Palmitoyl thioesterase CPT1C
- Glutamate receptor 2
- Glutamate receptor 1
- Glutamate receptor 3
- Protein shisa-9
- Fatty-acid amide hydrolase 1
- von Willebrand factor C domain-containing protein 2-like
- Protein shisa-6
Sequence:
MDLDVVNMFVIAGGTLAIPILAFVASFLLWPSALIRIYYWYWRRTLGMQVRYAHHEDYQFCYSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSIVGQVKRIHQFVECLKLNKKPFHLIGTSMGGHVAGVYAAYYPSDVCSLSLVCPAGLQYSTDNPFVQRLKELEESAAIQKIPLIPSTPEEMSEMLQLCSYVRFKVPQQILQGLVDVRIPHNSFYRKLFLEIVNEKSRYSLHENMDKIKVPTQIIWGKQDQVLDVSGADILAKSISNSQVEVLENCGHSVVMERPRKTAKLIVDFLASVHNTDNKKLN
Protein: Serine--tRNA ligase, cytoplasmic (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser) synthetase) (Q39230)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser).
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277, ECO:0000305|PubMed:16297076}.
Interaction partners:
- Tryptophan--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, chloroplastic/mitochondrial
- Arginine--tRNA ligase, chloroplastic/mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, chloroplastic/mitochondrial
- Isoleucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, chloroplastic/mitochondrial
- Arginine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
Sequence:
MLDINLFREEKGNNPEIIRESQRRRFASVEIVDEIIKLDKEWRQRQFEVDSFRKEFNKLNKQVAQLKIKKEDASEIIQQTEKNKQDSTAKEAEVREAYAALKAKLEQVGNLVHDSVPVDKDEANNLVIKLWGEKRFSTPGLKLKNHVDLVELLGIADTKRGAEIAGARGFFLKGDGLMLNQALINFGLTFLKKRGFTGLQPPFFMRKDVMAKCAQLAQFDEELYKVTGEGDDKYLIATAEQPLCAYHIDEWIHPTELPLRYAGYSSCFRKEAGSHGRDTLGIFRVHQFEKIEQFCITGPNENASWEMLDEMMKNSEDFYQALKLPYQIVSIVSGALNDAAAKKYDLEAWFPSSETFRELVSCSNCTDYQARRLEIRYGQKKSNEQTKQYVHMLNSTLTATERTICCILENYQREDGVDIPEVLQPFMGGETFLPFKAKPVVADTKGKKSKA