wanglab/gogpt-training-data huggingface dataset:
Protein: Guanine nucleotide-binding protein G(t) subunit alpha-2 (Transducin alpha-2 chain) (P19087)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P50149}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P50149}. Note=Localizes mainly in the outer segment in the dark-adapted state, whereas is translocated to the inner part of the photoreceptors in the light-adapted state. During dark-adapted conditions, in the presence of UNC119 mislocalizes from the outer segment to the inner part of rod photoreceptors which leads to decreased photoreceptor damage caused by light. {ECO:0000250|UniProtKB:P50149}.
Interaction partners:
- Cyclic nucleotide-gated channel beta-3
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
- Rhodopsin
- Cyclic nucleotide-gated channel alpha-3
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Guanine nucleotide-binding protein G
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 9
Sequence:
MGSGASAEDKELAKRSKELEKKLQEDADKEAKTVKLLLLGAGESGKSTIVKQMKIIHQDGYSPEECLEFKAIIYGNVLQSILAIIRAMTTLGIDYAEPSCADDGRQLNNLADSIEEGTMPPELVEVIRRLWKDGGVQACFERAAEYQLNDSASYYLNQLERITDPEYLPSEQDVLRSRVKTTGIIETKFSVKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDDEVNRMHESLHLFNSICNHKFFAATSIVLFLNKKDLFEEKIKKVHLSICFPEYDGNNSYDDAGNYIKSQFLDLNMRKDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Protein: Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3) (Q92997)
Organism: Homo sapiens (Human)
Function: Involved in the signal transduction pathway mediated by multiple Wnt genes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14641}.
Interaction partners:
- Vang-like protein 2
- Vang-like protein 1
- Axin-1
- Segment polarity protein dishevelled homolog DVL-2
- Prickle-like protein 1
- Protein naked cuticle homolog 1
- Axin-2
- Segment polarity protein dishevelled homolog DVL-1
- Frizzled-7
- Prickle-like protein 2
Sequence:
MGETKIIYHLDGQETPYLVKLPLPAERVTLADFKGVLQRPSYKFFFKSMDDDFGVVKEEISDDNAKLPCFNGRVVSWLVSAEGSHPDPAPFCADNPSELPPPMERTGGIGDSRPPSFHPHAGGGSQENLDNDTETDSLVSAQRERPRRRDGPEHATRLNGTAKGERRREPGGYDSSSTLMSSELETTSFFDSDEDDSTSRFSSSTEQSSASRLMRRHKRRRRKQKVSRIERSSSFSSITDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNEINFENMSNDDAVRVLREIVHKPGPITLTVAKCWDPSPRGCFTLPRSEPIRPIDPAAWVSHTAAMTGTFPAYGMSPSLSTITSTSSSITSSIPDTERLDDFHLSIHSDMAAIVKAMASPESGLEVRDRMWLKITIPNAFIGSDVVDWLYHNVEGFTDRREARKYASNLLKAGFIRHTVNKITFSEQCYYIFGDLCGNMANLSLHDHDGSSGASDQDTLAPLPHPGAAPWPMAFPYQYPPPPHPYNPHPGFPELGYSYGGGSASSQHSEGSRSSGSNRSGSDRRKEKDPKAGDSKSGGSGSESDHTTRSSLRGPRERAPSERSGPAASEHSHRSHHSLASSLRSHHTHPSYGPPGVPPLYGPPMLMMPPPPAAMGPPGAPPGRDLASVPPELTASRQSFRMAMGNPSEFFVDVM
Protein: Major vault protein (X5D2M8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PROSITE-ProRule:PRU00571}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATEEFIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPMRMVTVPPRHYCTVANPVSRDAQGLVLFDVTGQVRLRHADLEIRLAQDPFPLYPGEVLEKDITPLQVVLPNTALHLKALLDFEDKDGDKVVAGDEWLFEGPGTYIPRKEVEVVEIIQATIIRQNQALRLRARKECWDRDGKERVTGEEWLVTTVGAYLPAVFEEVLDLVDAVILTEKTALHLRARRNFRDFRGVSRRTGEEWLVTVQDTEAHVPDVHEEVLGVVPITTLGPHNYCVILDPVGPDGKNQLGQKRVVKGEKSFFLQPGEQLEQGIQDVYVLSEQQGLLLRALQPLEEGEDEEKVSHQAGDHWLIRGPLEYVPSAKVEVVEERQAIPLDENEGIYVQDVKTGKVRAVIGSTYMLTQDEVLWEKELPPGVEELLNKGQDPLADRGEKDTAKSLQPLAPRNKTRVVSYRVPHNAAVQVYDYREKRARVVFGPELVSLGPEEQFTVLSLSAGRPKRPHARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVNDRKDPQETAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARIIRTAVFGFETSEAKGPDGMALPRPRDQAVFPQNGLVVSSVDVQSVEPVDQRTRDALQRSVQLAIEITTNSQEAAAKHEAQRLEQEARGRLERQKILDQSEAEKARKELLELEALSMAVESTGTAKAEAESRAEAARIEGEGSVLQAKLKAQALAIETEAELQRVQKVRELELVYARAQLELEVSKAQQLAEVEVKKFKQMTEAIGPSTIRDLAVAGPEMQVKLLQSLGLKSTLITDGSTPINLFNTAFGLLGMGPEGQPLGRRVASGPSPGEGISPQSAQAPQAPGDNHVVPVLR
Protein: Serotonin N-acetyltransferase (Serotonin acetylase) (EC 2.3.1.87) (Aralkylamine N-acetyltransferase) (AA-NAT) (Q64666)
Organism: Rattus norvegicus (Rat)
Function: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q16613}.
Interaction partners:
- Acetylserotonin O-methyltransferase
- Aromatic-L-amino-acid decarboxylase
- Amine oxidase [flavin-containing] A
- Indoleamine 2,3-dioxygenase 2
- Amine oxidase [flavin-containing] B
- Indoleamine 2,3-dioxygenase 1
- Indolethylamine N-methyltransferase
- Esco1 protein
- Establishment of sister chromatid cohesion N-acetyltransferase 2
- Neutral amino acid transporter B
Sequence:
MLSIHPLKPEALHLPLGTSEFLGCQRRHTLPASEFRCLTPEDATSAFEIEREAFISVSGTCPLHLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLTQESLTLHRPGGRTAHLHVLAVHRTFRQQGKGSVLLWRYLHHLGSQPAVRRAVLMCENALVPFYEKFGFQAMGPCAITMGSLTFTELQCSLRCHTFLRRNSGC
Protein: Phosphoglycerate mutase 1 (EC 5.4.2.11) (EC 5.4.2.4) (BPG-dependent PGAM 1) (Phosphoglycerate mutase isozyme B) (PGAM-B) (P18669)
Organism: Homo sapiens (Human)
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglyceratea crucial step in glycolysis, by using 2,3-bisphosphoglycerate. Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate.
Interaction partners:
- Phosphoglycerate kinase 1
- Alpha-enolase
- Beta-enolase
- Triosephosphate isomerase
- Gamma-enolase
- Phosphoglycerate mutase 2
- Phosphoglycerate kinase 2
- Fructose-bisphosphate aldolase A
- Pyruvate kinase PKM
- Enolase 4
Sequence:
MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAMEAVAAQGKAKK
Protein: 60S ribosomal protein L17, putative (Q385T6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 40S ribosomal protein S8
- 40S ribosomal protein S16, putative
- Small ribosomal subunit protein uS5
- Signal recognition particle 54 kDa protein
- 40S ribosomal protein S26
- 60S ribosomal protein L29
- Uncharacterized protein
- 60S ribosomal protein L19, putative
- Large ribosomal subunit protein eL18
- 60S ribosomal protein L5, putative
Sequence:
MVHYSRKPQVSSKTAKAKIADLRCHYKNTFETANVINGMKLRKAQQLYRQVLAKTRCIPFKRYNGKIGNTAQAKEWGQTKGRWPRKSVVAMLSLLKNAEANAIEKGLDPGKMVIKHVQVDQAPRVRRRTFRAHGRITPYMRSPCHVQLFMTQPQERVPVPKSKPKK
Protein: Putative non-heme bromoperoxidase BpoC (P9WNH1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- o-succinylbenzoate synthase
- Conserved protein
- Putative amidase AmiB2
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- Probable conserved transmembrane protein
- Lipase LipV
- Possible non-heme haloperoxidase Hpx
- GDP-mannose-dependent alpha-mannosyltransferase
Sequence:
MINLAYDDNGTGDPVVFIAGRGGAGRTWHPHQVPAFLAAGYRCITFDNRGIGATENAEGFTTQTMVADTAALIETLDIAPARVVGVSMGAFIAQELMVVAPELVSSAVLMATRGRLDRARQFFNKAEAELYDSGVQLPPTYDARARLLENFSRKTLNDDVAVGDWIAMFSMWPIKSTPGLRCQLDCAPQTNRLPAYRNIAAPVLVIGFADDVVTPPYLGREVADALPNGRYLQIPDAGHLGFFERPEAVNTAMLKFFASVKA
Protein: 40S small subunit processome assembly factor 1 (Q8NDD1)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000269|PubMed:20813266}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.
Interaction partners:
- U3 small nucleolar ribonucleoprotein protein MPP10
- DDB1- and CUL4-associated factor 13
- U3 small nucleolar RNA-associated protein 4 homolog
- RNA cytidine acetyltransferase
- Something about silencing protein 10
- U3 small nucleolar ribonucleoprotein protein IMP3
- Nucleolar protein 11
- WD repeat-containing protein 75
- U3 small nucleolar RNA-associated protein 14 homolog A
- rRNA-processing protein FCF1 homolog
Sequence:
MRVDSSADPTMSQEQGPGSSTPPSSPTLLDALLQNLYDFGGTEGETEQKKIIKKRENKKRDVMASAALAAEPSPLPGSLIRGQRKSASSFFKELREERHCAPSGTPTGPEILAAAVPPSSLKNNREQVEVVEFHSNKKRKLTPDHNKNTKQANPSVLERDVDTQEFNLEKARLEVHRFGITGYGKGKERILEQERAIMLGAKPPKKSYVNYKVLQEQIKEKKAAKEEEKRLAQETDIFKKKKRKGQEDRKSKKKSAPSILSNGRIGQVGKFKNGTLILSPVDIKKINSSRVAK
Protein: Diacylglycerol O-acyltransferase 2 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase 2) (Q9DCV3)
Organism: Mus musculus (Mouse)
Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides. Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Long-chain fatty acid transport protein 1
- Patatin-like phospholipase domain-containing protein 2
- Phosphatidate phosphatase LPIN1
- Phospholipid phosphatase 2
- 1-acylglycerol-3-phosphate O-acyltransferase Pnpla3
- Phosphatidate phosphatase LPIN2
- Phosphatidate phosphatase LPIN3
- Phospholipid phosphatase 3
- Pancreatic triacylglycerol lipase
Sequence:
MKTLIAAYSGVLRGERRAEAARSENKNKGSALSREGSGRWGTGSSILSALQDIFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSVILMYTFCTDCWLIAVLYFTWLAFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLKNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITVPKLEHPTQKDIDLYHAMYMEALVKLFDNHKTKFGLPETEVLEVN
Protein: Ubiquitin-conjugating enzyme E2 29 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 29) (Ubiquitin carrier protein 29) (Q9SLE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Interaction partners:
- E3 ubiquitin-protein ligase UPL4
- E3 ubiquitin-protein ligase UPL3
- Putative RING zinc finger protein
- Anaphase-promoting complex subunit 10
- At5g64360
- O-fucosyltransferase 7
- F-box protein SKIP31
- Ubiquitin-activating enzyme E1 2
- Ubiquitin-activating enzyme E1 1
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 1
Sequence:
MATRRILKELKELQRDPPVSCSAGPTGEDMFHWQATIMGPNESPYSGGVFLVNIHFPPDYPFKPPKVVFRTKVFHPNINSNGNICLDILKDQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHIYKTDKTKYEAMARSWTQKYALF
Protein: Diacylglycerol pyrophosphate phosphatase 1 (DGPP phosphatase) (EC 3.6.1.75) (Lysophosphatidate phosphatase) (EC 3.1.3.106) (Phosphatidate phosphatase) (EC 3.1.3.4) (Q05521)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Together with LPP1, regulates intracellular DGPP and PA levels, which are phospholipid molecules believed to play a signaling role in stress response. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. Substrate preference is DGPP > LPA > PA. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:11139591, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8567632}; Multi-pass membrane protein {ECO:0000269|PubMed:11139591, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8567632}.
Interaction partners:
- Phosphatidic acid phosphohydrolase 1
- Diacylglycerol O-acyltransferase 1
- Phospholipid:diacylglycerol acyltransferase
- CTP-dependent diacylglycerol kinase 1
- Lysophospholipid acyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Phospholipase D1
- Phosphatidate cytidylyltransferase
- Triacylglycerol lipase 3
- Cholinephosphotransferase 1
Sequence:
MNRVSFIKTPFNIGAKWRLEDVFLLIIMILLNYPVYYQQPFERQFYINDLTISHPYATTERVNNNMLFVYSFVVPSLTILIIGSILADRRHLIFILYTSLLGLSLAWFSTSFFTNFIKNWIGRLRPDFLDRCQPVEGLPLDTLFTAKDVCTTKNHERLLDGFRTTPSGHSSESFAGLGYLYFWLCGQLLTESPLMPLWRKMVAFLPLLGAALIALSRTQDYRHHFVDVILGSMLGYIMAHFFYRRIFPPIDDPLPFKPLMDDSDVTLEEAVTHQRIPDEELHPLSDEGM
Protein: K+/H+ antiporter subunit F (Q9I4R6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|PIRNR:PIRNR028784}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|PIRNR:PIRNR028784}.
Interaction partners:
- Na+/H+ antiporter subunit G
- Na+/H+ antiporter subunit C
- Na+/H+ antiporter subunit E
- Probable NADH dehydrogenase
- Probable NADH dehydrogenase
- HMA domain-containing protein
- NADH-quinone oxidoreductase subunit C/D
- NADH-quinone oxidoreductase subunit L
- Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Sequence:
MLAYVIPLCLALLGLALLLTLARLVKGPCLPDRALALDTLYVNAIALLVLYGIWRDSDLFFEAALLIAVLGFVGTVAVAKYMLRGDIIE
Protein: Soluble inorganic pyrophosphatase 3 (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase 3) (PPase 3) (O82793)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q93V56}.
Interaction partners:
- ATPase 7, plasma membrane-type
- Putative ATPase, plasma membrane-like
- ATP synthase subunit b, chloroplastic
- ATPase 6, plasma membrane-type
- ATPase 8, plasma membrane-type
- ATPase 9, plasma membrane-type
- Pyrophosphate-energized vacuolar membrane proton pump 1
- ATPase 11, plasma membrane-type
- ATPase 4, plasma membrane-type
- V-type proton ATPase subunit c''1
Sequence:
MSEEAYEETQESSQSPRPVPKLNERILSTLSRRSVAAHPWHDLEIGPEAPLVFNVVVEITKGSKVKYELDKKTGLIKVDRILYSSVVYPHNYGFIPRTLCEDNDPLDVLVLMQEPVLPGCFLRARAIGLMPMIDQGEKDDKIIAVCADDPEYKHFTDIKQLAPHRLQEIRRFFEDYKKNENKKVAVNDFLPSESAHEAIQYSMDLYAEYILHTLRR
Protein: Spa2p (A0A1D8PFH4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Bud6p
- Formin BNI1
- Cell division control protein 42 homolog
- Pea2p
- mitogen-activated protein kinase kinase
- Mitogen-activated protein kinase MKC1
- Mlc1p
- Actin
- Formin BNR1
- Exocyst complex protein EXO70
Sequence:
MSEKDLVQHYKVLKQFLAISDDQQSRSKSNSSRAQRAREKLLKLSSAQFKELSTDVYDELRRRIDESRSEPDYLLPKSSFHPKRNQARQKLASLPQTRFKDLVADISYEIERRDLHVERQSQHSHTTSMSSNGSQFQHERKSSLASSHHRNDSANGYHSRSASHHLNDFAATKEVDEEKESDSRDDLNNTSSKNITMPNAEASNQSIGIQPSQVVPTKANLDWSSDDEGDDEQEEEEEEKGKVKNISDPKHTQAEQHQNQHQHSNSLSNNKDINTKSDRGLTHDEKDNELAKLETLVNDLKNKLQASESERSKLKGKLESLQEDYNFSVSQNKSLSNELETLGKEKERWITKHDNLTKSMSNSDENLKEIERLKSINAALRLENQSLKNTSSSPRSVGSPPSAINAITTNSGNSGNSAKLSQKSVDEFLEKLETIQLSPGSTSNNPSTLELKNQIKLWQRRYEDSRSNAIARDIKKASLPKMELKPFVASHGLISIKLVSDALALIDSFLGYLVSEKCDSDILFEKISKLAIVINEIANQGDRQRLGSNEHSVMLREAVAYSLTATRYHATYKQLFPRYIVEKSIGELNCILCDLIAECKLNENSTNLRVLEVETKVPKKSVNEDFGVRPLRMANKLKVNQSQQEPTQKSNSETRALQYEEQSPFIEETRDKPLKSKANSAFTTLRAQREKAKEEKSPTNATHGTSFSKGATVAATVGSASIPAAAQVGDPRTKKSTHNVAFNDNPISISLRYQNYDSDENEDDLNDDVPTNDNFNAHSNKETKFDRKPYGTETQTNNLTSGALSTNTTPTKVKISRSINEDSDELVSATNNSNFHDNSGYQQSRNLDSSNNFVTQNSGNLNSYKPNLDNSPVRKTSLDSSEDKYASPMRDTDQSFDNDQDDSFETAYTFGKNLDNVHDSNTRKEDVATRGLGTNNEVVPQKENFETEGKKKGSIASLASKYENNVSDQSTSRNYSPIKNKSDKSSQGVQELARRITSPEASPESQKSISQASKISPSKKGVLDKVKQFESPQREDVPSSPSPRKSPGQDKVPFKSMRTSLESSKPFKNEEDPGQLSAPFSAIHSKNEVGEETSKKEIENSAAAETSTLSDTSTSSSAPVKSKGLFQSLKDRFTGETKKEEEEEKVQQQQQQEEEESAKHIESSQSDATISDNEKQNDTQNENLMNTVETSPPKDVNDEIISKPVQVQYPEQKTTHSGEQEVEKSKDLPIERRDVVTEPSTGIKHEPAESNKTEPKLQQQKSLLQKSKQQKPVTPESEESYSEEETEEEIRARQRQEYRKSMAAATFNVDLFDIDDPDNTLTQVLLYLEHQTVQVINTIQSLLAAIKKPNATRGELREKTKAITIVISQMTEATNTSMNQTRNAQLKEHGSWVVRSLEDCYHRMNILCKPGEKPDTSFADKNFKQRLAGISFDIAKCTKELVKTVEEASLKEDIAYLDARISQNLE
Protein: Amino acid transporter (A0A2K5WLA0)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004146}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004414}. Membrane {ECO:0000256|RuleBase:RU361216}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361216}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004565}. Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
- Amino acid transporter
Sequence:
MSGAWKARQTPVEGCGAGLRIPGEAAPAPAAALGALPRLLPRDPRRPTHPPSFPGPPLLPPSSLVGPGAAEHGGGRRSRARLPRKTTGLAGRQARCAIPGGGGNGGGDRGDCSGQLSPIPCAPASRRAAKQPAVPGSPSPRAHGRAQGTIAATAMGKPARKGCEWKRFLKNNWLLLSTVAAVVLGITTGVLVREHSNLSTLEKFYFAFPGEILMRMLKLIILPLIISSMITGVAALDSNVSGKIGLRAVVYYFCTTLIAVILGIVLVVSIKPGVTQKVAEIDRTGSTPEVSTVDAMLDLIRNMFPENLVQACFQQYKTKREEVKPPRDPETNMTEESFTAVMTTAISKNKTKEYKIIGMYSDGINVLGLIVFCLVFGLVIGKMGEKGQILVDFFNALSDATMKIVQIIMCYMPLGILFLIAGKIIEVEDWEIFRKLGLYMATVLTGLAIHSIVILPLIYFIVVRKNPFRFAMGMAQALLTALMISSSSATLPVTFRCAEEKNQVDKRITRFVLPVGATINMDGTALYEAVAAVFIAQLNDLDLGIGQIITIRDRFRTMVNVLGDAFGTGIVEKLSKKELEQMDVSSEVNIVNPFALESTILDNEDSDTKKSYVNGGFAVDKSDTISFTQTSQF
Protein: Beckwith-Wiedemann syndrome chromosomal region 1 candidate gene B protein (Organic cation transporter-like protein 2 antisense protein) (Solute carrier family 22 member 1-like antisense protein) (Solute carrier family 22 member 18 antisense protein) (p27-Beckwith-Wiedemann region 1 B) (p27-BWR1B) (Q8N1D0)
Organism: Homo sapiens (Human)
Interaction partners:
- Solute carrier family 67 member A1
- Pleckstrin homology-like domain family A member 2
- E3 ubiquitin-protein ligase RNF167
- Potassium voltage-gated channel subfamily KQT member 1
- Pleckstrin homology-like domain family A member 1
Sequence:
MGELPGSEGMWENCPLGWVKKKASGTLAPLDFLLQRKRLWLWASEPVRPQPQGIHRFREARRQFCRMRGSRLTGGRKGFGSSGLRFGRGGFSEEVMPQPVLKAMRCAEGAWWFSPDGPAGSAASIWPAEGAEGLPGQLGRDRLEVVYSVPDNVPGQNGSRRPLVCKITGKCLSVCSEENAKAGGCSAFPLLLSQLGARMTGREHAHKGPELTTPDSGLPRPPNPALAGFRALAQHSPPLGTSTPSAVLLSAAT
Protein: Bifunctional helicase and thymine dioxygenase JBP2 (J-binding protein 2) (TbJBP2) [Includes: Probable DNA helicase JBP2 (EC 3.6.4.12); Thymine dioxygenase JBP2 (EC 1.14.11.6)] (Q57X81)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Probably also acts as a DNA helicase. Recognizes and binds specific regions of the genome, hydrolyzes ATP and allows the DNA base J de novo synthesis. Involved in initial synthesis of DNA base J, JBP1 being able to act via the basal level of DNA base J and propagate further synthesis. In contrast to JBP1, it does not specifically bind DNA base J, however it binds chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:15694344, ECO:0000269|PubMed:19136460}.
Interaction partners:
- DNA repair protein RAD51 homolog
- Histone H3 variant
- Protein artemis
- DNA 3'-5' helicase
- thymidine kinase
- Histone H3, putative
- Exonuclease, putative
Sequence:
MPMFMDGASQVLQQVLQTVLVTSEPAIVIPGSFLGELDVIVDEAKNHGMKLVSIPKGGITILPPIPMSESSLTRLCKDYYGLKTDAERLALFSNLEETFPTAPGVSLPCRLLYHPRDYICRIVHLCAELVTASDEEYQKAYDIVPLLHIRPVQNVCEELRRQFRAGALTQRLPLGQRVDVQFKRTVVHLDGSMDPFPRNAAEAAVNIAPVALDAVDDIYEGFDVTGTEVVDIPTGKVSEYLSEKDFELVTEDSVLLDPTGKRVQAIFIRGGIDKDICRRAAADVEGVATKQNMRRLTNGGVRNPDTGILGYYDYLNNPTKRKCRMTEFTRRNWGKIIGPCGELLQLLDQLYKENAPDHYELQRRVIPPEYMLFNTVFSTVSVNKNFRTAVHRDKGDFRGGLTALCVLDGNYEGCYLALKSARKAFCLQVGDVLFFDSSLEHGNTEVHNREGSWRRISIVCYLRCGLMSHTCETERSMRLRNQIMSDRLHADSADSVVNLNGVTGHLPPLCIPFKIAKTLSLTQHAALRFVSRRIKEGDGCVLALTMGLGKTLVSLTICYSYIYNNGPCDILIVAPKTLLQHWMQEAKKWKDYGLVFPGFIVLNNVDSSSFEDDLSNYEQQGTTTNPKKSYVFVINPGYIKSFLSRVKGFRPALIVVDEGHCISSKESKLREVLDSLYCSARVVLTGTPVQNNAEELYRLVGWVDDKVHSTLPQRDFNEFSNSINRYVNGDDSAFCDALFAQRYIHEWMSPYVFTVMKVDLPPLHDYIIICNFSAVQQKMFEERIKVDATDNLLCLKASEHRPYHLSTHPLCFLGFLTGIWRTGQVDIEEEPGEFEELGTYRLSRDDDALAKDCSSLLENGKLADFVALSGKLTALISILHSIFEKMEKAVIFSQYIGSQDFIARTLTAYKISVVTIRGKDCQQRRRRVVEMFRDDKNVLCLVVSTQIGAYGLDLTAANHVILWDTWWNPQVESQAIARCYRQNQSKAVIAYKLASGFEDATVLKAQARKRALFKCLINEETSQVVPGHDLVDYTSSEEDDDRRHLWETLKTCTLEGGKPAVTKIIRNIDTVKSERWI
Protein: DNA-binding protein inhibitor ID-3-A (Inhibitor of DNA binding 3) (XId3) (XIdI) (XIdIa) (XIdIb) (XIdx) (Inhibitor of differentiation 3-A) (Q91399)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Influences cell fate decisions in the embryo by sequestering and blocking the activity of the bHLH transcription factors that control these decisions. Inhibits the binding of myogenic bHLH-containing complexes to E-box DNA, thereby preventing activation of muscle-specific target genes. Also inhibits the activity of neurogenic factor neurod1/neuroD. Plays a role in cell cycle progression and survival of neural crest progenitors; binding to either hes4-B/hairy2b or stat3 blocks the formation of transcription factor complexes and the repressor function of hes4-B/hairy2B, to allow neural crest progenitors to differentiate. May play a role in the regulation of the circadian rhythm.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q02535, ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MKAISPVRSMSSCYQAVCCLSEQSLSIARGSSHKGPGMDEPMGLLYDMNGCYSKLKELVPGIPQGSKLSQVEILQHVIDYIFDLQIVLGEDQQQSSILSLQKSDFSELATQGDTSVCH
Protein: (thale cress) hypothetical protein (A0A178V236)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGICSSSESTQVATAKLILQDGRMMEFANPVKVGYVLLKYPMCFICNSDDMDFDDAVAAISADEELQLGQIYFALPLCWLRQPLKAEEMAALAVKASSALMRGGGGGCRRKCVEPIVSDKLRMRVGSGDDTVGSGSGRRKVRNGDGGGSVSSSRRRKCYAAELSTIDE
Protein: Ribosomal protein S30, isoform A (Ribosomal protein S30, isoform B) (Ribosomal protein S30, isoform C) (Q9VDH8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL15
- IP17351p
- Small ribosomal subunit protein eS19A
- Small ribosomal subunit protein uS7A
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL13
Sequence:
MQLFVRGLETIEALEVSQDATIAGVKNQLAQIHGFNAEEFSLDCEGITLANETPVTALSSFELDLNIPMLGGKVHGSLARAGKVKGQTPKVEKQEKKKKKTGRAKRRIQYNRRFVNFVQGFGRRRGPNANST