wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c1, isoform A (Cytochrome c1, isoform B) (GM14501p) (Q9VRL0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- Cytochrome b-c1 complex subunit 7
- AT02348p
- Cytochrome b-c1 complex subunit 6
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 9
- Mitochondrial-processing peptidase subunit beta
- NADH dehydrogenase 23 kDa subunit
Sequence:
MAATLRRFHGLRLLKSAPALSLQQAKNLSSAGSWASGNKKLIGALGAITGGVGALIYALEQSVQASGGEVHSPAQLWNHKGLFDALDHQSVRRGYEVYKQVCSACHSMQYIAYRNLVGVTHTEAEAKAEAEQITVKDGPDDTGNYYTRPGKLSDYFPSPYPNEEAARAANNGAYPPDLSYIVSARKGGEDYIFSLLTGYHDAPAGVVLREGQYFNPYFPGGAISMAQVLYNEVIEYEDGTPPTQSQLAKDVATFLKWTSEPEHDDRKQLLIKVIGILGFLTVISYYIKRHKWSSLKSRKIVFVPKEK
Protein: Protein INCREASED PETAL GROWTH ANISOTROPY 1 (Q8L7S5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:31198941, ECO:0000269|PubMed:35975703}. Cytoplasm, cytosol {ECO:0000269|PubMed:35975703}. Cell membrane {ECO:0000269|PubMed:35975703}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Colocalizes with cortical microtubules and binds directly to microtubules (PubMed:31198941, PubMed:35975703). In young pavement cells, observed as granules in the cytosol and at the cell periphery (PubMed:35975703). Formation to granules on microtubules is promoted by mechanical perturbations (PubMed:35975703). {ECO:0000269|PubMed:31198941, ECO:0000269|PubMed:35975703}.
Interaction partners:
- Putative defensin-like protein 27
- Peptidyl-prolyl cis-trans isomerase FKBP16-1, chloroplastic
Sequence:
MVAGKVRVTMGFHKSPSTKKTKDMPSPLPLPPPPPPPLKPPSSGSATTKPPINPSKPGFTRSFGVYFPRASAQVHATAAAASHNGVVSELRRQVEELREREALLKTENLEVKLLRESVSVIPLLESQIADKNGEIDELRKETARLAEDNERLRREFDRSEEMRRECETREKEMEAEIVELRKLVSSESDDHALSVSQRFQGLMDVSAKSNLIRSLKRVGSLRNLPEPITNQENTNKSISSSGDADGDIYRKDEIESYSRSSNSEELTESSSLSTVRSRVPRVPKPPPKRSISLGDSTENRADPPPQKSIPPPPPPPPPPLLQQPPPPPSVSKAPPPPPPPPPPKSLSIASAKVRRVPEVVEFYHSLMRRDSTNSRRDSTGGGNAAAEAILANSNARDMIGEIENRSVYLLAIKTDVETQGDFIRFLIKEVGNAAFSDIEDVVPFVKWLDDELSYLVDERAVLKHFEWPEQKADALREAAFCYFDLKKLISEASRFREDPRQSSSSALKKMQALFEKLEHGVYSLSRMRESAATKFKSFQIPVDWMLETGITSQIKLASVKLAMKYMKRVSAELEAIEGGGPEEEELIVQGVRFAFRVHQFAGGFDAETMKAFEELRDKARSCHVQCQSQTHQHKLCFRSTPC
Protein: Piperamide synthase (BAHD-type acyl transferase 1) (PipBAHD1) (Hexanoyl-CoA:piperidine piperoyl transferase) (EC 2.3.1.-) (Octanoyl-CoA:piperidine piperoyl transferase) (EC 2.3.1.-) (Piperoyl-CoA:piperidine piperoyl transferase) (Piperidine N-piperoyltransferase) (EC 2.3.1.145) (P0DO57)
Organism: Piper nigrum (Black pepper)
Function: Involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl-piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Can use piperidine and benzylamine as acceptors and various CoA-esters with aliphatic and aromatic amines as CoA-donors, including piperoyl-CoA, hexanoyl-CoA and octanoyl-CoA, and, to a lower extent, benzoyl-CoA. Mediates the conversion of piperidine to three piperine isomers in the presence of piperoyl-CoA. Its ability to convert in vitro piperidine to hexanoylpiperidine in the presence of hexanoyl-CoA, and to octanoylpiperidine in the presence of octanoyl-CoA is not confirmed in vivo according to fruits metabolome analysis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:35634755}. Note=Localized at residual cytoplasmic structures in special cells of the fruit perisperm. {ECO:0000269|PubMed:35634755}.
Interaction partners:
Sequence:
MASSQLEFNVERKQPELLGPAEPTPYELKELSDIDDQDGVRLFLTAIFIYPPPTKTSMPTRKTDPASDIRRGLSKAMVYYYPFAGRIREGPNRKLSVDCTGEGIVFCEADADIRLDGLGDVEVLRPPYPFIDKMTLGEGSAILGAPLVYVQVTRFACGGFIITGRFNHVMADAPGFTMFMKAAADLARGATVPMPLPVWERERYRSRVPPRVTFAHHEYMHVDDPPPRPTSEPWSLHSAFFTKADVATLRAQLPADLRKAATSFDIITACMWRCRVSALQYGPDEVVRLIVAVNSRTKFDPPLTGYYGNGLMLPAAVTEAGKLVGSDLGYAVELVREAKGKVTEEYVRSAADFLVLNGRVHFVVSNTFLVSDLRRLIDLANMDWGWGKAVSGGPVDVGENVISFLATSKNSAGEEGAVVPFCLPDSALGRFTSEVKKLVCFRPLENAAASNPDHGYMSRM
Protein: Protein NODULATION SIGNALING PATHWAY 2 (Q5NE24)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Transcriptional regulator essential for Nod-factor-induced gene expression. Acts downstream of calcium spiking and DMI3, a calcium/calmodulin-dependent protein kinase (CCaMK). Transcription factor involved in the control of strigolactone biosynthesis in roots through the activation of the beta-carotene isomerase D27, which participates in a pathway leading to biosynthesis of strigolactones.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:15961668}. Endoplasmic reticulum {ECO:0000269|PubMed:15961668}. Note=Mainly localized to the nuclear envelope. Also found in the endoplasmic reticulum. Upon Nod-factor application, the nuclear envelope localization disappears and the protein accumulates in the nucleus. {ECO:0000269|PubMed:15961668}.
Interaction partners:
- Protein CYCLOPS
- Glycerol-3-phosphate acyltransferase RAM2
- Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase DMI-3
- Ethylene-responsive transcription factor ERN2
- ABC transporter G family member STR2
- Serine/threonine receptor-like kinase NFP
- Protein VAPYRIN
- Early nodulin-11
- Protein NODULATION SIGNALING PATHWAY 1
Sequence:
MDLMDMDAINDLHFSGHSSLTNTPTSDEDYGCTWNHWSPIVNWDTFTGAPDDFHHLMDTIIEDRTTVLEQLSPSITTTTTTTTTTDEEEEEMETTTTTTTTAIKTHEVGDDSKGLKLVHLLMAGAEALTGSTKNRDLARVILIRLKELVSQHANGSNMERLAAHFTEALHGLLEGAGGAHNNHHHHNNNKHYLTTNGPHDNQNDTLAAFQLLQDMSPYVKFGHFTANQAIIEAVAHERRVHVIDYDIMEGVQWASLIQSLASNNNGPHLRITALSRTGTGRRSIATVQETGRRLTSFAASLGQPFSFHHCRLDSDETFRPSALKLVRGEALVFNCMLNLPHLSYRAPESVASFLNGAKTLNPKLVTLVEEEVGSVIGGFVERFMDSLHHYSAVFDSLEAGFPMQNRARTLVERVFFGPRIAGSLGRIYRTGGEEERRSWGEWLGEVGFRGVPVSFANHCQAKLLLGLFNDGYRVEEVGVGSNKLVLDWKSRRLLSASLWTCSSSDSDL
Protein: Interleukin (A0A060Y5T2)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Uncharacterized protein
- Fibronectin type-III domain-containing protein
- UDP-N-acetylglucosamine transferase subunit ALG13
- UDP-N-acetylglucosamine transferase subunit ALG13
- Tudor domain-containing protein
- UDP-N-acetylglucosamine transferase subunit ALG13
- Fibronectin type-III domain-containing protein
- Interleukin-7 receptor subunit alpha
- Fibronectin type-III domain-containing protein
- Interleukin 21 receptor, tandem duplicate 1
Sequence:
MTGFLTVLLFCIRLLERRTKKSVRWICLFWGFHYYPHQRLNIELWNCFIILSCLSATAHLPIAGAAETHGMTIHDVKELQSELKNLKSTIEKSDACLYAPTNDDIYNDHCIFKFMHCYLLELEVVLFEDMSVTDNYHDEIKTSIYHRKKHLEEHERQYNSSRCSPCEAQRVANSTIFLYNLERLLERIGQTVS
Protein: Transmembrane protein 216 (Thymus atrophy-related protein) (Q9CQC4)
Organism: Mus musculus (Mouse)
Function: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21725307}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme.
Interaction partners:
- Tectonic-1
- B9 domain-containing protein 1
- Meckelin
- B9 domain-containing protein 2
- Transmembrane protein 231
- Coiled-coil and C2 domain-containing protein 2A
- Tectonic-2
- Centrosomal protein of 290 kDa
- Tectonic-3
- Transmembrane protein 17
Sequence:
MAPRDKRLSSTPLEVLFFLNGWYYATYFLLELLIFLYKGLLLPYPTANLVLDVVMLLLYLGIEVIRLFFGTKGNLCQRKMPLGISVALTFPSAMMASYYLLLQTYVLRLEAIMNSILLFFCGSELLLEMLTLATFSSMDRI
Protein: F-box/LRR-repeat protein 14 (F-box and leucine-rich repeat protein 14) (Q8N1E6)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin-protein ligase complexes. The SCF(FBXL14) complex acts by mediating ubiquitination and subsequent degradation of SNAI1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19955572}.
Interaction partners:
- Cullin-1
- S-phase kinase-associated protein 1
- Zinc finger protein SNAI1
- E3 ubiquitin-protein ligase RBX1
- F-box only protein 11
- F-box/LRR-repeat protein 5
Sequence:
METHISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWRGVEAKLHLRRANPSLFPSLQARGIRRVQILSLRRSLSYVIQGMANIESLNLSGCYNLTDNGLGHAFVQEIGSLRALNLSLCKQITDSSLGRIAQYLKGLEVLELGGCSNITNTGLLLIAWGLQRLKSLNLRSCRHLSDVGIGHLAGMTRSAAEGCLGLEQLTLQDCQKLTDLSLKHISRGLTGLRLLNLSFCGGISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGLKSLSLCSCHISDDGINRMVRQMHGLRTLNIGQCVRITDKGLELIAEHLSQLTGIDLYGCTRITKRGLERITQLPCLKVLNLGLWQMTDSEKEARGDFSPLFTVRTRGSSRR
Protein: Fusion protein SYT-SSX2 (A4PIW0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSVAFAAPRQRGKGEITPAAIQKMLDDNNHLIQCIMDSQNKGKTSECSQYQQMLHTNLVYLATIADSNQNMQSLLPAPPTQNMPMGPGGMNQSGPPPPPRSHNMPSDGMVGGGPPAPHMQNQMNGQMPGPNHMPMQGPGPNQLNMTNSSMNMPSSSHGSMGGYNHSVPSSQSMPVQNQMTMSQGQPMGNYGPRPNMSMQPNQGPMMHQQPPSQQYNMPQGGGQHYQGQQPPMGMMGQVNQGNHMMGQRQIPPYRPPQQGPPQQYSGQEDYYGDQYSHGGQGPPEGMNQQYYPDGNSQYGQQQDAYQGPPPQQGYPPQQQQYPGQQGYPGQQQGYGPSQGGPGPQYPNYPQGQGQQYGGYRPTQPGPPQPPQQRPYGYDQIMPKKPAEEGNDSEEVPEASGPQNDGKELCPPGKPTTSEKIHERSGPKRGEHAWTHRLRERKQLVIYEEISDPEEDDE
Protein: ZEB2-regulated ABC transporter 1 (I1RL06)
Organism: Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum)
Function: ABC transporter involved in zearalenone production.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21833740}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:21833740}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MALPEANMSSTRSEQSSRSHDTIVGNEQPHSEKPAASAPGDQMSSDDEDEGPQTEEMIRRHSIVRDLARNYTNTSHHFTGSSADLFNAADANSPLNPSSENFNARAWARAMAKTMGENGSGFRQSGLCFQDMNVFGYGAETDYQKDVGNVWLGLPDMVHQMISPNANKRRIDILRGFDGVINAGEMCVVLGPPGSGCSTFLKSISGETNGIYIDDSTYFNYNGIPAEEMHKSHAGETIYTAEVDIHFPMLSVGDTLTFAARARCPQNLPPGIDHNLYSEHMRDVVMAMYGISHTINTQVGDNYIRGVSGGERKRVTIAEATLSNAPFQCWDNSTRGLDSANAIEFCKTLRLQSELFGQTCAVSIYQAPQTAYDLFDKALVIYEGRQIFFGPADEAKAYFINLGFECPDRQTTPDFLTSMTAPSERVVRPGWENKVPRTPDEFHARWKESQQYQIVRAEIESYKSLYPLNGSSADAFRENKHSAQAKGQRLKSPFTLSYMQQVQLCLWRGFRRLLGSPGVTIFQLIANTAVAFIASSLFYNMKPETGDFFKRGATLFLAVLSNAFASALEILTQYSQRPIVEKQARYAFYHPSAEAFASILVDMPYKITNSILFNVTLYFMTNLNRDAGAFFFFLLVSFIMVLAMSGVFRSIASLSRTLSQAMVPASLLILALVIFAGFVVPVDYMLGWCRWINYLDPVAYGFESLMVNEFSGRNFTCTAFVPNAQIPGYADVGGLNRACSTVGAIPGQSYVNGDAYINLEYKYFHAHKWRNVGILIAMTIFNHVVYIVATEFISAKKSKGEVLVFRRSNMPSKAKSDPEASSSRPIPTTEKNNNEVANIQGSTSVFHWNDVCYDIKIKGEPRRILDHVDGWVKPGTLTALMGVSGAGKTTLLDCLADRISMGVITGEMLVDGKIRDSSFQRRTGYVQQQDLHLETSTVREALTFSALLRQPASTPREEKIAYVDEVIKLLDMQEYADAVVGVLGEGLNVEQRKRLTIGVELAAKPPLLLFVDEPTSGLDSQTSWAILDLLEKLSKAGQSILCTIHQPSAMLFQRFDRLLFLAKGGRTIYFGDIGKNSETLTNYFVKHGSQECPNGENPAEWMLEVIGAAPGSHTDIDWHQTWRDSSEYQAVQTELQRLKAEGSANSVDQKSDPESYREFAAPFGQQLLIATKRVFEQYWRTPSYIYSKAALCIQVGLFLGLVFLNAPLSLRGLQNQMFAIFQMLTVFGQLVQMQMPHFVTQRSLYEVRERPSKTYSWKVFMLSQIIAEIPWNTLMSVFLFVCIYYPVGFNKNAEFAGQTAERGGLMWLLIWQFLIFTCTFAHAAIAITDTAEAGGNLANVVFMMSLFFCGVLAAPDKMPGFWIWMYRVSPFTYLVSAILSTGIANAEVKCAANELTTFNPTNGTTCGEYMDSYIKAAGGYLTNPDATSDCKFCTIKSTNVYLKALSASYDDRWRNFGIGMVYIVVNIVGALFLYWLIRMPKNKNKKKTA
Protein: CUB-like domain-containing protein (Q21327)
Organism: Caenorhabditis elegans
Interaction partners:
- CUB-like domain-containing protein
- ShKT domain-containing protein
- C-type lectin domain-containing protein
- CUB-like domain-containing protein
- Mitogen-activated protein kinase pmk-1
- CUB-like domain-containing protein
- ShKT domain-containing protein
- Cation-transporting P-type ATPase N-terminal domain-containing protein
- F-box domain-containing protein
- TransThyretin-Related family domain
Sequence:
MSEKSLQSKMLSTVFLLATLIAFASADGYTCAGNTLINPFLNLSEPYYYPGTWRENMEPAEYAPDQKCNWKINVPQGTYATVIFYKKTQYESGIKCAYPGKDLEYISDNDQNPYIFTSPQFQVDLKVGDKPGEFSFKVVWSKYPPGSRMNMQLDGIHSLAGVASSFYTTYTAINRVMLVGFSIPDFDSAVLRQSAIYDGDSVNAKYLGNLIDTLHGQIVSTGNKLTIYTFGLENHINNTLFMGLDTAAAGDIQKYNGLNCPADTTRGCSIILQSYFYATAVAKISRQPDYLMLPNAFPYNANVRVYGDKMDINYQTFGNYTQGFEVDILTTKNG
Protein: Collagen alpha-1(XIX) chain (Collagen alpha-1(Y) chain) (Q14993)
Organism: Homo sapiens (Human)
Function: May act as a cross-bridge between fibrils and other extracellular matrix molecules. Involved in skeletal myogenesis in the developing esophagus. May play a role in organization of the pericellular matrix or the sphinteric smooth muscle.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- von Willebrand factor A domain-containing protein 1
Sequence:
MRLTGPWKLWLWMSIFLLPASTSVTVRDKTEESCPILRIEGHQLTYDNINKLEVSGFDLGDSFSLRRAFCESDKTCFKLGSALLIRDTIKIFPKGLPEEYSVAAMFRVRRNAKKERWFLWQVLNQQNIPQISIVVDGGKKVVEFMFQATEGDVLNYIFRNRELRPLFDRQWHKLGISIQSQVISLYMDCNLIARRQTDEKDTVDFHGRTVIATRASDGKPVDIELHQLKIYCSANLIAQETCCEISDTKCPEQDGFGNIASSWVTAHASKMSSYLPAKQELKDQCQCIPNKGEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKGDLGPHGPPGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKTGPPGKPGPPGPPGPPGIQGIHQTLGGYYNKDNKGNDEHEAGGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEKGDRGEPGVIGSQGVKGEPGDPGPPGLIGSPGLKGQQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEKGDPGGIIGPPGLPGPKGEAGPPGKSLPGEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDIGPQGIGIPGRTGAQGPAGEPGIQGPRGLPGLPGTPGTPGNDGVPGRDGKPGLPGPPGDPIALPLLGDIGALLKNFCGNCQASVPGLKSNKGEEGGAGEPGKYDSMARKGDIGPRGPPGIPGREGPKGSKGERGYPGIPGEKGDEGLQGIPGIPGAPGPTGPPGLMGRTGHPGPTGAKGEKGSDGPPGKPGPPGPPGIPFNERNGMSSLYKIKGGVNVPSYPGPPGPPGPKGDPGPVGEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGMSGKPGAPGPPGVPGEPGERGPVGDIGFPGPEGPSGKPGINGKDGIPGAQGIMGKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPGHQGPPGSPGIPGIPADAVSFEEIKKYINQEVLRIFEERMAVFLSQLKLPAAMLAAQAYGRPGPPGKDGLPGPPGDPGPQGYRGQKGERGEPGIGLPGSPGLPGTSALGLPGSPGAPGPQGPPGPSGRCNPEDCLYPVSHAHQRTGGN
Protein: Lipoate-protein ligase A subunit 1 (EC 6.3.1.20) (Lipoate--protein ligase subunit 1) (Q9HKT1)
Organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Function: Part of a lipoate-protein ligase complex that catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Can also use octanoate as substrate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Lipoate-protein ligase A subunit 2
- Probable glycine cleavage system H protein
- dihydrolipoyllysine-residue
- Probable 3-methyl-2-oxobutanoate dehydrogenase chain E1-beta
- Dihydrolipoyl dehydrogenase
- Dihydrolipoamide dehydrogenase component
- Mercuric reductase
- Probable 3-methyl-2-oxobutanoate dehydrogenase alpha chain
Sequence:
MEGRLLLLETPGNTRMSLAYDEAIYRSFQYGDKPILRFYRHDRSVIIGYFQVAEEEVDLDYMKKNGIMLARRYTGGGAVYHDLGDLNFSVVRSSDDMDITSMFRTMNEAVVNSLRILGLDARPGELNDVSIPVNKKTDIMAGEKKIMGAAGAMRKGAKLWHAAMLVHTDLDMLSAVLKVPDEKFRDKIAKSTRERVANVTDFVDVSIDEVRNALIRGFSETLHIDFREDTITEKEESLARELFDKKYSTEEWNMGLLRKEVV
Protein: Uncharacterized protein (Q2YLL1)
Organism: Brucella abortus (strain 2308)
Interaction partners:
Sequence:
MASKTTLNAKNLEALGAKRLAELLIEISTGNANHKRLLRMELVGNSSGAELAREVRKRLGSIGRSKSWIDWQNAKSVRADLEAQRKSIAEKIAPTDPNEAFELIWQFLSLADPIFERSCDGSGALIESFHAACEDAGRIAAMAKVPIDRLVEKIFSVLQDNGYGQYDALIEAMAPALGEAGLRKLQRAFEAWAKEPQPKVASKDKEVIAWSSDGPVYRDQLYASGKSITVKVVLQQVADALGDVDLYIEQQSKESQTFATVTTDIARRLLAAGRAEDALTALEKTKFDSCREIPFEWQILRAEVLESLGRAEEAQQFRWKSFEQNLNDELLREYVKRLPDFDDVEAEEKAFAFVRAVADANHALYFFLQYPSLSEASKLVVSRASEMDGDHYELMSDAAEKLSAKFPLAATILLRAMIDFTLNNARSSRYKHAARHLLECGALSRSIEDYHSFAPHEAYIADLRKMHGRKHGFWPLVDR
Protein: Uncharacterized lipoprotein YfgH (P65290)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
Interaction partners:
- Uncharacterized protein YceK
- Uncharacterized protein YfgI
- Protein HdeD
Sequence:
MMKFKKCLLPVAMLASFTLAGCQSNADDHAADVYQTDQLNTKQETKTVNIISILPAKVAVDNSQNKRNAQAFGALIGAVAGGVIGHNVGSGSNSGTTAGAVGGGAVGAAAGSMVNDKTLVEGVSLTYKEGTKVYTSTQVGKECQFTTGLAVVITTTYNETRIQPNTKCPEKS
Protein: Clathrin light chain (B5ATG0)
Organism: Sus scrofa (Pig)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180, ECO:0000256|RuleBase:RU363137}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180, ECO:0000256|RuleBase:RU363137}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180, ECO:0000256|RuleBase:RU363137}. Membrane, coated pit {ECO:0000256|RuleBase:RU363137}; Peripheral membrane protein {ECO:0000256|RuleBase:RU363137}; Cytoplasmic side {ECO:0000256|RuleBase:RU363137}. Note=Cytoplasmic face of coated pits and vesicles. {ECO:0000256|RuleBase:RU363137}.
Interaction partners:
Sequence:
GSAGPQPHGEPPGGPDAVDGVMNGEYYQESNGPTDSYAAISQVDRLQSEPESIRKWREEQTERLEALDANSRKREAEWKEKAIKELEEWYARQDEQLQKTKANNRAAEEAFVNDIEESSPGTEWERVARLCDFNPRSSKQAKDVSRMRSVLISLKQAPLVH
Protein: At3g47000 (Beta-D-glucan exohydrolase-like protein) (Glycosyl hydrolase family protein) (Q9SD73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Beta-glucosidase 19
- Beta-glucosidase 24
- Beta-glucosidase 44
- Putative serine carboxypeptidase-like 30
- F8A5.27 protein
- Beta-fructofuranosidase, insoluble isoenzyme CWINV5
- Beta-fructofuranosidase, insoluble isoenzyme CWINV6
- Beta-fructofuranosidase, insoluble isoenzyme CWINV3
- Beta-fructofuranosidase, insoluble isoenzyme CWINV4
- Beta-fructofuranosidase, insoluble isoenzyme CWINV2
Sequence:
MVVEESSCVYKNGDAPVEARVKDLLSRMTLPEKIGQMTQIERRVASPSAFTDFFIGSVLNAGGSVPFEDAKSSDWADMIDGFQRSALASRLGIPIIYGTDAVHGNNNVYGATVFPHNIGLGATRDADLVRRIGAATALEVRASGVHWAFSPCVAVLRDPRWGRCYESYGEDPELVCEMTSLVSGLQGVPPEEHPNGYPFVAGRNNVVACVKHFVGDGGTDKGINEGNTIASYEELEKIHIPPYLKCLAQGVSTVMASYSSWNGTRLHADRFLLTEILKEKLGFKGFLVSDWEGLDRLSEPQGSNYRYCIKTAVNAGIDMVMVPFKYEQFIQDMTDLVESGEIPMARINDAVERILRVKFVAGLFGHPLTDRSLLPTVGCKEHRELAQEAVRKSLVLLKSGKNADKPFLPLDRNAKRILVTGTHADDLGYQCGGWTKTWFGLSGRITIGTTLLDAIKEAVGDETEVIYEKTPSKETLASSEGFSYAIVAVGEPPYAETMGDNSELRIPFNGTDIVTAVAEIIPTLVILISGRPVVLEPTVLEKTEALVAAWLPGTEGQGVADVVFGDYDFKGKLPVSWFKHVEHLPLDAHANSYDPLFPFGFGLNSKPV
Protein: Retinoic acid receptor beta (Nuclear receptor subfamily 1 group B member 2) (A0A8I6A7Z0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MSSSSHACPVPAVRGHMTHYPAAPYPLLFPPVIGGLSLPPLHGLHGHPPPSGCSTPSPATIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEPSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPTKVDKLQEPLLEALKIYIRKRRPSKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPNSSGNTAEHSPSVSPSSVETSGVSQSPLLQ
Protein: Potassium transport protein 1 (P47946)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Together with TRK2, defines the major, high-affinity potassium influx transport system. Involved in maintenance of the proper sodium/potassium ratio in the cell and in regulating the plasma membrane potential.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Serine/threonine-protein kinase hal4
- Na
- K
Sequence:
MVLNYIQRWFKWVIPTFGFLAIHYIYIISLTIIASILLFTGGTTTKIKYIDALFLASSATTQTGLNSVDLNSLSIWQQFILYGFTAITVPIWMHGSISFIRLYWFRRKFKDVVRQNRTRKFQRKLRKSLMKKSEDDEEQGVRGRKIRVMLPYLHSLRSPTSLKNFSRFDTHDSTNNPYFPDNPPSPKADISKDEYFGKYLPKKSDTLDMDLESHNMTFHDYEPSIENKNYDFGSSHSASMQMYEMDDLHPRLRRQSSFISSVNPLEADDTRETLSEGALVQESLPMAYSYSDTNLVVSRDSFTLTGDDNLFPEGGLRPANTIDGIVRSSLSSSSLSKDTEPSTVDMHIAFTGLNKPTIERERNLKLRKKSRFYKKSLRSRFSRGLHRPIRWTKSFTSNRRNLTLERVLSSAFAKKREPSISSRHTTMSLPYLSYNPTVDRNSAFVALSKEQRDELGGIEYRALKCVCSMVTLYFIIFNIAAFVTFIVFAYTAVGSREVIDSYDLRRGWWALFSSASSFNDLGFSLIPSSFVPMNRNIFLLLISSLFIIAGNTGFPCFFRTFIWTTYKLYPFSFEKKEAMAFLLDHPRRCFTLLFPSGATWVLFFVLLLLNVIDLVLFMVLDTGSKAVASLPKGIRVVNAIFQSVCTRTAGFTSVSISELHPAVLVSYMVMMYISVYPVAINMRNTNVYEERSLGVYRTEDDEGKSFLKDHLTEQLSYDLWYIFLGLFIICICEGGKISNPLDTDFSIFTVLFEVVSAYGTVGLSTGLSSSNCSLSARFTTISKLVIIALELRGRHRGLPRAVDRAILLPSEKNNLKEEEDYQRRHGFSIDNARGSIAVSRD
Protein: Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein (Cnt-b) (Centaurin-beta) (Q3UH98)
Organism: Mus musculus (Mouse)
Subcellular location: Endosome membrane {ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369028}.
Interaction partners:
Sequence:
MTVEFEECIKDSPRFRATIDEVETDVVEIEAKLDKLVKLCSGMIEAGKAYVTTNRLFVSGVRDLSQQCQGDTVISECLQRFGDSLQEMVNYHTILFDQAQRSVRQQLHNFAKEDVRKFKETKKQFDKVREDMELSLVRNAQAPRHRPHEVEEATGALTVTRKCFRHLALDYVLQINVLQAKKKFEILDSMLSFMHAQYSFFQQGYSLLHQLDPYMKKLAAELDQLVIDSAVEKREMERKHAAIQQRTLLQDFSYDEPKVEFDVDAPSGVVMEGYLFKRASNAFKTWNRRWFSIQNSQLVYQKKLKDALTVVVDDLRLCSVKPCEDIERRFCFEVVSPTKSCMLQADSEKLRQAWVQAVQASIASAYRESPDSCYSERLDRTASPSTSSIDSTTDSRERGVKGESVLQRVQSVAGNSQCGDCGQPDPRWASINLGVLLCIECSGIHRSLGVHCSKVRSLTLDSWEPELLKLMCELGNSTVNQIYEAQCEGPGVRKPTASSSRQDKEAWIKDKYVEKKFLRKLTSAPAREPPRRWRAQKCQRPHSSPHAPTTRRKVRLEPVLPSVAALSSAATMERKFRRDSLFCPDELDSLFSYFDAGAAGAGPRSLSSDSGLGGSSDGSSDVLAFGTGSVVDSVTEEEGAESEESSSEVDGEAEAWSLADVRELHPGLLAHQAARTRDLPALAAALAHGAEVNWADAADEGKTPLVQAVLGGSLIVCEFLLQNGADVNQRDSLGRAPLHHATLLGRTGQVCLFLKRGADQHALDQEQQDPLTIAVQAANADIVTLLRLARMAEEMREAEAPPGQPGPLPGSSPTELQYRRCIQEFIGLHLEES
Protein: Potassium voltage-gated channel, subfamily H (eag-related), member 3 (A8WHX9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Potassium voltage-gated channel, shaker-related subfamily, beta member 2 a.
- Potassium voltage-gated channel subfamily KQT member 2 isoform X2
- Voltage-dependent N-type calcium channel subunit alpha
- K2P10.1 potassium channel subunit
- A-type voltage-gated potassium channel KCND1
- Potassium voltage-gated channel subfamily C member 3b
- Voltage-dependent L-type calcium channel subunit beta-2
- Scn4ba protein
Sequence:
MPVMRGLLAPQNTFLDTIATRFDGTHSNFVLGNAQVQSLYPIVYCSDGFCELTGYARAELMQKSCACHFLYGPETSDRLMAQIQGALDERREFKTELVFYKKGGTQFWCLLDIVPIKNEKGEVVLFLVSHKDITDNKKDQDEEQSPERDEETGLEVHKVTRPPGFNANRRRSRAVLYQLSGHLQKQDKSKLKINNNMFGEKPPIPEYKVAAIQKSRFILLHYGTFKAGWDWLILLATFYVAVTVPYNVCFTVVGGRDEASTPRSPPSVSDILVEILFMLDIVLNFRTTFVSTSGQVVYDARSICVHYVTTWLFVDLIAALPFDLLYAFNVSVYFGVHLLKTVRLLRLLRLLQKLERYSQYSAVVLTLLMSMFALLAHWMACVWYIIGRSEIENNSPGSWDIGWLHELGKRLGTPYFLSPLASLIPDSLRPTILDGLVVNSSQWNGSDLVAHEPVWNSSQLNSTGTAPAAPSNAGQTGAVLGGGPSIRSSYVTSLYFALSSLTSVGFGNVSANTDSEKIFSICTMLIGALMHAAVFGNVTAIIQRMYSRRSLYHTRTKDLKDFIRVHRLPKALAQRMLECFQTTWSVNNGIDVSELLKDFPDELRADIAMHLNKELLQLPLFESASRGCLRSLSLIIKTSFCAPGEFLIRQGDALQAIYFVCSGSMEVLKDNTVLAILGKGDLIGSDSLTKEQVIKTNANVKALTYCDLQYISLKGLREVLRLYPEYAQKFVSEIQHDLTYNLREGSGADLDWESNGGLVKKLPAIREDEENDEEQNSVSRAPRSPLRLTRALSSPLRSPLLPPRPFRAPSESMRPATLQIPVVSFSSAPPELSPRFVDGIETESNSSSTQRFEFGPSLPQSGPPSPSPVSQEQLESKQSITKLSEEMTSLSQQVSQLSKELQEMTRLLRPILVM
Protein: Pickpocket 26 (Q9VS73)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Pickpocket 17, isoform A
Sequence:
MSTDSTQPHTPSHEVAVRPPPCAANQWKRAALMARMAPAFRETVSDDSEDEVDTKKQIKYGSGFQAAKAIIHEYCDYTTIHGIRYLGEKKRPLLERLFWISVLVLSVFTCVKLTLNIWDKWNNNPVIVSFAEKSTPVWQIPFPAVTVCPETKTRREIFNFTDSYHQVRDFQSNVSGIVDLSDKQKGLYGAVSQVCEPHLHDVTLGNKTRRGMEIIDALTEVSPHFDDTYLNCKWRNSPVKCSDIFHKFVTEDGVCFSFNSLSPAEIFRAEGIIPDFIFREENRLSMDWNVEDGYSASADTSPYPNRVLGPGARAGLYLFMGGAEIDFDDMCRGPVQGFKILLHTPGDVAQVSKQYFRIPFDQEVLISIRPKIITTSDGLKHYEPNRRQCYFQKERELRYFNIYSQSNCELECLANFTLTKCGCVKFSMPRNVNMPVCGDASLKCYNQAEDELLLREFTQGLVNAGENTRGETECNCLPSCTSIAYEAEISQADFDYKTVINTDSPEGKEEQSKRQGMKMSRVSIFFKEAQFLTSRRSELYGTTDFLANCGGLLGLFMGVSMLSIVELIYFCTVRLISNLRMRRKTRKELLKAVNKDA