wanglab/gogpt-training-data huggingface dataset:
Protein: Ankyrin repeat-containing protein (Q54TS2)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MIYYFLVSIFFNEENLESKLKLKLFINKLSKLPILNNNNNQNPLIANLELKQREINTIDLFYKIISFDIESNRFIKKNKGSSIGSIINNNIFCKIDIGSRLLRPAKENAVFQLYYNLYPLNNKQSSSFISPTELSVINNLPPNIIQEENIFIQCSLLVRGKSLDSFLENKINYNNEIQLLDDESYCSHILSSLLLMTTDYKGDNIFIENNINKIIGIDNDECMEFDELNNSASNGKTYINFKNILFTFKSRMSKVVNENIINQFIQHQPNIFILNWLNQIYQESIKYEKFIEFSCLNIFDEILRTNESLQLPIKFKKGWVLKMLNRFKTIIEILKSDKDDNNNSYNKSITYYRLFKEILPTTYYYYQGLLLLETNHPLDQMESLYFEQKRLSIEEMFQKVKHLNETHIKKLLQEIRGTPKNNEGVDLSIIETIKELIKGSELNDFKSDKDLMNWVETIVKLNKTLNTDMELNETFYKSYQLILQKVLNLSSPSSFHLIVKFIEITLNNSFNYSVDGEPILHLIIRLNVSNSIEFIDYLIKKLNIDVNIEHNHLTALDLVADQKKFKLFRHLIDLGAGKNFDSTKISNYYSSLSHSKKIRFKPFLETLFHTNPNIAWCISLNQLLPLANGDDENNNNNNNNNNNNYNNNNNNNNNNNNNNNNNNNNNNNNNNGCKILKTVISGRRRILLKSYEKLLFEEDGKTPKKPNKYGRRPVPSISDDYGNCIHFKFSPQFPGTDFSVFKLSELLFPQDGGGGGCIPCCELASIDGDIAVLLIQNVFGETLFDILEKEPEIINEIDSSNISKQLILSMLTNNGDGNLGNFIISNHLLDSKIYSIDNDQSFMPPISKPIKSGLFKSSSCKVSTVILLFNQMNDFVHQDVIDSINNLDIDMLCSDWLQQMDTFHILSLLHFNETREKLKENKETIIGVAFSSNMMKLLYSKLNRLKHHLNENNNKPITHFQLYEKLEPLVASKIKPLINDENLSIIDRYNKFNNIKYKDNKHRTEILTKSSNPSALLLDSIDIPKGSEIQNELWSADYGPDFALRELKKLKNKYSEIKNIIKSIESGNLNEISDFHFENYLKKTNFLKKTNEKQKLLFQSIKERSNLTSIFIRNSQLLLELSTIMSPNFNNLNEINFSNCKNLNFICGFIGMIRVQLSLPSLQILNVCGCEELYSLKLNCPNLITLLASNCKNLNEFDILAPNLNEINLNSSIKYNSIFNSLSSFGNLEKLDISNSRNLGSKLKFKFENLKYLEAVSIYQVCEITFNLPNILSINIDDCKDLKEINSDRYHDWAWEALKANRRNKIIFQGDRNSVNLKLFNVKLKELPIVDQDYVILFDSKSYYIHSDNAIQGLHNFYNIKKPLTRKTIPSSVESLTIHDGFNYPITKGIIPNTVNRLSLYRIKSDFELGAIPSTVFSLSLKAGFNLSLQPGFITNGVKYLSISEIQSELMDGSIPPSVSNLTLEDGFNQEINNGILSSELKYLDLKFILYPLKVGSIPPTVVGISIDGYNHSLKGGVIPYGVETLSLHKVEEPLDSTCIPSSIKTIFIYDDFNQKLSNGVIPSSVTELYLHAFKEPLEIGSIPSTVKKISLYDGFKHPLDGKVLPEGIETLELYNTVHPLEKESIPNSLLKLEIKDSYDHIIPRDIPNHITLKLPQRILNSRSSIVSSQPYSNTLTEINNNGIVKNLLFFGTLLAIGMISKNKNK
Protein: Erythrocyte membrane protein band 4.1 like 3 (A0A0J9YW31)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
KAEEERDEEEDKRRKGEEVTPISAIRHEGKELEKTQDDLMKHQTNISELKRTFLETSTDTAVTNEWEKRLSTSPVRLAARQEDAPMIEPLVPEEKMETKTESSGIETEPTVHHLPLSTEKVVQETVLVEERRVVHASGDASYSAGDSGDAAAQPAFTGIKGKEGSALTEGAKEEGGEEVAKAV
Protein: Pterin-4-alpha-carbinolamine dehydratase (PHS) (EC 4.2.1.96) (4-alpha-hydroxy-tetrahydropterin dehydratase) (Dimerization cofactor of hepatocyte nuclear factor 1-alpha) (DCoH) (Dimerization cofactor of HNF1) (Phenylalanine hydroxylase-stimulating protein) (Pterin carbinolamine dehydratase) (PCD) (P61459)
Organism: Rattus norvegicus (Rat)
Function: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity. Also acts as a coactivator for HNF1B-dependent transcription (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8444860}. Nucleus {ECO:0000269|PubMed:8444860}. Note=Recruited to the nucleus through the interaction with HNF1B. {ECO:0000250|UniProtKB:P35680}.
Interaction partners:
- Phenylalanine-4-hydroxylase
- Dihydropteridine reductase
- Tryptophan 5-hydroxylase 1
- Tyrosine 3-monooxygenase
- Tryptophan 5-hydroxylase 2
- 4a-hydroxytetrahydrobiopterin dehydratase
- Hepatocyte nuclear factor 1-alpha
- Hepatocyte nuclear factor 1-beta
- Sepiapterin reductase
- Homogentisate 1,2-dioxygenase
Sequence:
MAGKAHRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVSMT
Protein: WD repeat-containing protein 55 homolog (Q8T088)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ribosome biogenesis protein WDR12 homolog
- Beag
- FI02004p
- Probable ATP-dependent RNA helicase Dbp73D
Sequence:
MHTHNNFKTPSDEDELDDLDEDMVVGVIAEIEQEVLNESDSDNDEYDLVDMGAPVPDNDGDISYEGNDSSSSDDSFDPNAADSDSDDSMLDEAGGVTAGGATSAKKRKDDDNPSGSNKQPEATFDLDEDDETDETVRAMIAAIKKPRSSPPEIKLEDFITDICFHPDRDIIALATIIGDVHLYEYDNEANKLLRTIEVHSKACRDVEFTEDGRFLLTCSKDKCVMVTDMETEKLKKLYETAHDDAINTLHVLNENLFASGDDAGTVKLWDLRTKNAIFELKELEDQITQLTTNEQSKLLLATSADGYLTTFNISARKMYVQSEPYEEELNCMGVYRGDSKLVVGTSKGRLYTYNWGQFGYHCDMYPGIKSPISLMIPITDRIACVAGEDGNIRACHIAPYRNLGVVGQHNMPIESLDVNASGELIASSSHNNDVRFWNVKYFEDFGDIKYNEKHNAYKEQRHNLPSSKCSNASDFFSDLTKENADGDDDPGAGPSNMA
Protein: LOB domain-containing protein 6 (Protein ASYMMETRIC LEAVES 2) (Protein indeterminate gametophyte 1) (ZmIG1) (Q32SG3)
Organism: Zea mays (Maize)
Function: Promotes the switch from proliferation to differentiation in the embryo sac. Negative regulator of cell proliferation in the adaxial side of leaves. Regulates the formation of a symmetric lamina and the establishment of venation. Interacts directly with RS2 (rough sheath 2) to repress some knox homeobox genes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Ig1-as2 like1
- non-specific serine/threonine protein kinase
- SBP-domain protein2
Sequence:
MASSVPAPSGSVITVASSSSSAAAAAVCGTGSPCAACKFLRRKCQPDCVFAPYFPPDNPQKFVHVHRVFGASNVTKLLNELHPFQREDAVNSLAYEADMRLRDPVYGCVGVISILQHNLRQLQQDLARAKYELSKYQAAAAASASTAPTGPQAMAEFIGNAMPNGAHNFINIGHSAALGSLGGSASVFGQEQFGNAQMLSRSYDGGEPIARLGINGGGYEFGYSTAMGGSGAVSGLGTLGISPFLKSGTAGGDEKPNGGQ
Protein: Rho GDP-dissociation inhibitor (Rho GDI) (O14224)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cell division control protein 42 homolog
- GTP-binding protein rho1
- GTP-binding protein rho4
- GTP-binding protein rho3
- GTP-binding protein rho2
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Actin
- Probable Rho-type GTPase-activating protein 4
- GTP-binding protein rho5
- Ras-like protein 1
Sequence:
MSVNNEVSADQHNPELEDDTFEHGPPVSLGEKKSLNEYMKMDAEDESLQKWKASLGITGTGYSPSNDRRTVVILKLSLLVDGRDPVDVNMEDAASVEQIRKKGFTIKEGSEFKIGVKFRVQHEVISGLRYVQTVRRRGFVVDKTSTMIGSYGPSETPYDFTSEPDEAPTGMLARGHYEANGKFVDDDKVVHHEFVWAFDVAKSWK
Protein: acetyl-CoA carboxylase (EC 6.4.1.2) (Q73VY8)
Organism: Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) (Mycobacterium paratuberculosis)
Interaction partners:
- AccA2
- Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit
- biotin carboxylase
- biotin--[biotin carboxyl-carrier protein] ligase
- FadD13
- Fas
- AccD3
- Multifunctional 2-oxoglutarate metabolism enzyme
- Ketosynthase family 3
- Pks5
Sequence:
MTASLLVANRGEIALRIIRTATELGMRTVAVYAADDAHSPHVHAADEAMPLPGSGPPAYLNQAALLAVAENTGATLIHPGYGFLSENAEFAKACAAASHTFVGPDGRVLELLGNKTAARRAAIAAGVPTLAATDGPSGVEDIEAFFAAHPGGIMIKALAGGGGRGMRKVHNAAQIAGAYQRCAAEARLGFGDPALFAEALLGDARHIEVQVVAAPAGHQTHALAVGDRDCSMQRRYQKLIEIAPAQGLSEELRRALHQAAVRLCARVGLRGLATVEFLVSGERFVFLEVNPRIQVEHTVTEQTTGLDLVAVQLAIAGGESYYRLGLPAGIASDGTEVIGEPAAQRGIAIQLRVNAETFGADFSVLPSAGTLTAFCPPSGPGVRVDTYGRPGLVVSPQYDSLLAKVIVAVHGSSWRAAMRKADTALSEFGVEGVATNIGFLRRLLAEQRLETGWVNTDFVDEKLPELAAAALTHQPGPQPGAVELYPGEDALRAQLAGTVVEVAPEGADYPAGAQLVVLEAMKMQHVLAAPDALRTVRVLVTPGQVVGTGDPLLVFTRTTGGDDGESETAATDLDLTRADLDEVIERHARTLDEGRPDAVAKRHRQGRRTARENIDDLVDPGSFVEYGALAIAAQRSRRSEEDLIANTPADGLVAGLATVGADRFGPAAAQAVVASYDYTVLAGTQGMRNHAKTDRVFDLAARKRLPVVLFAEGGGGRPGDTDVGGAAGLDVPTFRMLAGLRGRVPLVSVVSGRCFAGNAALAGVCDVIIATPDANIGMGGPAMIEGGGLGVYPPEAIGPIAVQRRNGVVGLVARDEAHAVSLAKQYLSYFQGRLDRWQAPDPRVARHVVPQNRLRAYDVHRAIEAIVDVGSVLELRPDYGVGIVTALVRVEGVPYGLIANSTHHLGGAIDAEAADKAGDFLALCESFGLPVISLCDTPGFMVGPDAETQAAVRRFGRMFVLGARLTVPLGMIILRKGYGLGAMAMAGGSFRAPQFTVAWPTGEIGGMGLESAVRLGYRKELAAVTDPAERQNLFDRLVAAAYQHGKALRAATTFELDDVIDPAASRAWITRLSGG
Protein: Ephrin type-B receptor 4a (EC 2.7.10.1) (Eph receptor B4a) (Eph-like receptor tyrosine kinase rtk5) (O73875)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 is involved in the regulation of cell adhesion and cell migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells (By similarity). Involved in somitogenesis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P54760}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P54760}.
Interaction partners:
- Ephrin-B2a
- Ephrin-B1
- Efnb3 protein
- Ephrin-B2b
- Ephrin-A5b
- Si:dkey-246i14.3
- Delta-like protein
- COUP transcription factor 2
- Ephrin-A3
- Ephrin-B3
Sequence:
MELFSRNVAAFWIILLEFLLGSVAEEEVLMNTKTETSDLKWTTHSRSKPEWEEVSGLDEENNSVRTYQICQADGSSSHWLRSKLIERRGASQVYVELFFTMVECSSRNTHHRSCKETFNLYYYQSDTDDATATHPAWMENPYTKVDTVAADFLLRKGGEKKVNVKTLRLGPLSKRGFYLAFQAQGACMALLSVRVFFKKCPALTRSLSVFPETVPRSLVQEAVGQCVANAAQPGPSPRPPKMFCGEDGQWVDQPTTTCTCLPGFEASHGELECRACPVGLFKMGSGTGPCSVCPENSQTGETGSAACVCRSGFYRALSDSADTPCTRPPSSPRSPVPQVNDTSLTLEWSEPLDSGGRSDLSYSVECRMCSTPGSPCTLCSDGVNYRPSQTGIQGRRVSIWGLRPHTTYSFTVMALNGVSAQSQQGPAGETINITTSPNVPVLVSGLRKSTATESSLTLYWNTPTQSHYRILQYQIRYCEKERGSEENSCHYMESNNNEVVLSDLRRATQYEVQVRARTFAGYGSFGKAILFRTLPDEDDSSSPLLVTGILIAMGMLLLIIVIGAAIYCIRKQNNYKDPELSDKNGQYLMGQGVKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLRIPGKKENYVAIKTLKGGYTDKQRRDFLAEASIMGQFQHPNIIHLEGIITASCPVMILTEFMENGALDSFLRLNDGQFTPIQLVGMLRGIASGMKYLSEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLQENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTCASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTYLHQLMLDCWQKERTARPRFANIVSALDKLIRNPASLKITAQEGAGPSHPLLDQRSPLTPSSCGTVGDWLRAIKMERYEETFLQAGYTSMQLVTHINTEDLLRLGITLAGHQKKILSSIEALGIQNKAPGNVLY
Protein: Triple specificity protein phosphatase PtpB (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (MPtpB) (Phosphoinositide phosphatase) (Protein-serine/threonine phosphatase) (Protein-tyrosine phosphatase B) (TSP PTP) (I6WXK4)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Essential virulence factor that promotes mycobacterial survival within host macrophages. Acts as a phosphatase that possesses triple substrate specificity toward phosphotyrosine, phosphoserine/threonine and phosphoinositides. Supports mycobacteria survival during infection by modulating the normal host signaling pathways, attenuating the bactericidal immune responses and promoting the host cell survival. Inhibits host pyroptosis by disrupting the membrane localization of host gasdermin-D (GSDMD): acts by catalyzing dephosphorylation of phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol 4-phosphate, thereby inhibiting the membrane targeting of GSDMD and subsequent cytokine release and pyroptosis. Inhibits host inflammatory responses and apoptosis through impeding the NF-kappa-B and MAPK signal pathways and TP53/p53 expression in the macrophage. Blocks the IL6/IL-6 production by down-regulating ERK1/2, p38 and p65 activity. Prevents macrophage cell death by activating the Akt pathway and blocking caspase 3 activity. Reduces the expression of iNOS in activated macrophages and inhibits the generation of destroying reactive nitrogen intermediate NO.
Subcellular location: Secreted {ECO:0000269|PubMed:10986245}. Host cytoplasm {ECO:0000269|PubMed:36227980}. Host cell membrane {ECO:0000269|PubMed:36227980}. Note=Further investigation is required to determine whether PtpB is direct substrate for SecA2, the ESX/type VII secretion system, or an alternate mechanism. {ECO:0000305|PubMed:23084287}.
Interaction partners:
- Low molecular weight protein-tyrosine phosphatase A
- NADH-quinone oxidoreductase subunit M
- Probable acyl-CoA dehydrogenase FadE2
- Phosphatidylinositol-3-phosphatase
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit D
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit C
Sequence:
MAVRELPGAWNFRDVADTATALRPGRLFRSSELSRLDDAGRATLRRLGITDVADLRSSREVARRGPGRVPDGIDVHLLPFPDLADDDADDSAPHETAFKRLLTNDGSNGESGESSQSINDAATRYMTDEYRQFPTRNGAQRALHRVVTLLAAGRPVLTHCFAGKDRTGFVVALVLEAVGLDRDVIVADYLRSNDSVPQLRARISEMIQQRFDTELAPEVVTFTKARLSDGVLGVRAEYLAAARQTIDETYGSLGGYLRDAGISQATVNRMRGVLLG
Protein: Eukaryotic translation initiation factor 3 subunit J (eIF3j) (Q7K550)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit H
Sequence:
MADDWESAADSEVVIRPTAAASVNKWEGEDEDEDIKDSWEDEEEKKDEEKPTKTEAPAKPKPNKALKAKLEQQALLEEEAEAKRLANLSPAEKLAEKLRLQKIQEASDLKHAQEAFGVTSTCGGLDAFNPETKEEFKEFGATLSWKVGQFRESEHFPQFVEDLVRSLCVNLSAADIKKVKMNVEILHSEKLKLEKANAKKPAGKGKGKVTLRTENDDIDGYQKYGNDFTEDYDDFM
Protein: Stromal interaction molecule 2 (P83093)
Organism: Mus musculus (Mouse)
Function: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Dynamically translocates from a uniform endoplasmic reticulum distribution to punctual endoplasmic reticulum-plasma membrane junctions in response to decrease in endoplasmic reticulum Ca(2+) concentration. {ECO:0000250}.
Interaction partners:
- Protein orai-3
- Protein orai-2
- Calcium release-activated calcium channel protein 1
- Stromal interaction molecule 1
- Short transient receptor potential channel 1
- Short transient receptor potential channel 6
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Short transient receptor potential channel 3
- Short transient receptor potential channel 4
Sequence:
MLLFGLLVAGVADGCDLVPRHLRGRRASGSAGAAASPSAAAAGERQALLTDPCMSLSPPCFTEEDRFSLEALQTIHKQMDDDKDGGIEVDESDEFIREDMKYKDATNKHSHLHREDKHITVEDLWKQWKTSEVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFGPLTRPPHNWMKDFILTISIVIGVGGCWFAYTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSWSVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSLTSSLYSDHSWVVMPRVSIPPYPIAGGVDDLDEDTPPIVPQFPGTVAKPAGSLARSSSLCRSRRSIVPSSPQSQRAQLPAHAPLAAHPRHPHHPQHPQHSLPSPDPDILSVSSCPALYRNEEEEEAIYFTAEKQWEVPDTASECDSLNSSSGRKPSPPSSLEMYQTLSSRKISRDELSLEDSSRGESPVTADVSRGSPECVGLTETKSMIFSPASRVYNGILEKSCSMHQLSSGIPVPHPRHTSCSSAGNDSKPVQEASNVSRVSSIPHDLCHNGEKSKKPSKIKSLFKKKSK
Protein: Tafazzin family protein (A0A0G2K0X0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side {ECO:0000256|ARBA:ARBA00004137}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00024323}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00024323}; Intermembrane side {ECO:0000256|ARBA:ARBA00024323}.
Interaction partners:
Sequence:
MPLHVKWPFPAVPRLTWTLASSVVMGLVGTYSCFWTKYMNHLTVYNKEVLYELIENRGPATPLITVSNHQSCMDDPHLWGILKLRHIWNLKLMRWTPAAADICFTKELHSHFFSLGKCVPVCRGDGVYQKGMDFILEKLNHGDWVHIFPEGKVNMSSEFLRFKWVGIGRLIAECHLNPIILPLWHVGMNDVLPNSPPYFPRFGQKITVLIGKPFSTLPVLERLRAENKSAVEMRKALTDFIQEEFQRLKMQAEQLHNHFQPGR
Protein: ABC transporter G family member 1 (ABC transporter ABCG.1) (PhABCG1) (H9BZ66)
Organism: Petunia hybrida (Petunia)
Function: ABC transporter controlling the release of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26). This scent, mostly produced in the evening and night by the petals, attracts the pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22345641}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTNQLPNKVELAEVVPQNGGVFLTWEDLWVTASSVKDGSKAILKGLTGYAMPGELLAIMGPSGSGKSTLLDTIAGRLGSSTRQSGDILINGRRQTLAYGSSAYVTQDDTLLATLTIKEAVYYSAELQLPNSMSKSEKKEIADVTLKGMGLQDAMETRIGGWSGKGISGGQKRRVSICLEILTRPKLLFLDEPTSGLDSAASYYVMKAIASQCQGRTIIASIHQPSVDVFSLFHSLCLLSSGRTVYFGPASAANEFFALSGFPCPTLQNPSDHFLKTINSDFDQDIEEGSTRRKSTEEVIDILIKSYKASDKYNAVQSQVAEICQQEGEMLDKRSHASFITQSLVLTRRSFINMSRDLGYYWLRLAVYVVIAVGLGSLYYDVGFSAASVQARGSMLMFVASFITFMAIGGFPSFVEDMKVFQREKLNGHYGSGSFVIANTLSAMPYLLLVSLIPGAIAYFMTGLQNGFEHFIYFALVLFTCMMIVESLMMIVASMVPNFLMGLIAGAGIQALMLLSGGFFRLPNDLPKPFWKYPLHYVAFHKYAYEGMFKNEFEGLKIHDVNGEDILRNTWQMNMDYSKWIDLVILLGMLVLYRVLFLLVVKAGEIVKPAIRAFMSHSPNQINSAERPLDVFDS
Protein: Uncharacterized protein (Q382G8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000256|ARBA:ARBA00004230}.
Interaction partners:
Sequence:
MSCMFHSSLQLLPSNFQSPRSALVKAAMESIFCVEQVNVPPELGTIMKQYTKAILRDRPADLYKYSANFFAALCGQAAPFDKDGRFIEEEGECRTLDRHAEGGQCDVEVMDTTLPADQEDHDIVRSVLNEYDMNGEGRMPRESIPMLLAGMQKTLQLSDDEVVAAEQVLASLETDENDTIDLLEFRQMFFSSGYEQ
Protein: Uncharacterized protein C191.03c (Q9Y7P7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRSNNSSLVHCCWVSPPSLTRLPAFPSPRILSPCYCYNKRIRPFRGLTSYRQASYSLGFPLGLLVFLHSLIVARFFVASKSRSCIVRSLLFWINLDSADSRISVLFQCFFCIDIWTV
Protein: UDP-N-acetylglucosamine transporter ROCK1 (CMP-sialic acid transporter 5) (CMP-SA-Tr 5) (CMP-Sia-Tr 5) (Protein REPRESSOR OF CYTOKININ DEFICIENCY 1) (Q8LES0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the transport of UDP-linked acetylated hexosamines across the endoplasmic reticulum (ER) membrane. Facilitates UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-N-acetylgalactosamine (UDP-GalNAc) transport. Regulates the cytokinin signal in meristematic cells through modulating activity of cytokinin oxidases/dehydrogenases. Part of the ER quality control system, which determines the fate of aberrant proteins in the secretory pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25535363}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transmembrane protein
- Organic cation/carnitine transporter 5
- Probable beta-1,3-galactosyltransferase 8
- Protein FLX-like 2
Sequence:
MATANGAKSPSSMGPKVLFYSILLTLQYGAQPLISKRCIRKDVIVTSSVLTCEIVKVICALILMARNGSLKGLAKEWTLMGSLTASGLPAAIYALQNSLLQISYRSLDSLTFSILNQTKIFFTAFFTFIILRQKQSILQIGALCLLIMAAVLLSVGEGSNKDSSGINADQKLFYGIIPVLAASVLSGLASSLCQWASQVKKHSSYLMTVEMSIVGSLCLLVSTLKSPDGEAIKKYGFFHGWTALTLVPVISNALGGILVGLVTSHAGGVRKGFVIVSALLVTALLQFAFEGKPPSSYCLVALPLVMSSISMYQKYPYIDKKKKKV
Protein: Pentatricopeptide repeat-containing protein At1g10910, chloroplastic (Q0WVV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
METPLLVGLELRCPPHLFNTHSRPSSSLSIPALSLRILTPTAATTSSAVIELPANVAEAPRSKRHSNSYLARKSAISEVQRSSDFLSSLQRLATVLKVQDLNVILRDFGISGRWQDLIQLFEWMQQHGKISVSTYSSCIKFVGAKNVSKALEIYQSIPDESTKINVYICNSILSCLVKNGKLDSCIKLFDQMKRDGLKPDVVTYNTLLAGCIKVKNGYPKAIELIGELPHNGIQMDSVMYGTVLAICASNGRSEEAENFIQQMKVEGHSPNIYHYSSLLNSYSWKGDYKKADELMTEMKSIGLVPNKVMMTTLLKVYIKGGLFDRSRELLSELESAGYAENEMPYCMLMDGLSKAGKLEEARSIFDDMKGKGVRSDGYANSIMISALCRSKRFKEAKELSRDSETTYEKCDLVMLNTMLCAYCRAGEMESVMRMMKKMDEQAVSPDYNTFHILIKYFIKEKLHLLAYQTTLDMHSKGHRLEEELCSSLIYHLGKIRAQAEAFSVYNMLRYSKRTICKELHEKILHILIQGNLLKDAYIVVKDNAKMISQPTLKKFGRAFMISGNINLVNDVLKVLHGSGHKIDQVQFEIAISRYISQPDKKELLLQLLQWMPGQGYVVDSSTRNLILKNSHMFGRLLIAEILSKHHVASRPMIKSRPEQKFRCK
Protein: Sliding-clamp-loader large subunit (EC 3.6.4.-) (Clamp loader gp44 subunit) (Gene product 44) (gp44) (P04526)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Forms the sliding-clamp-loader together with the small subunit. Functions as an ATPase enzyme. The clamp loader holds the clamp in an open conformation and places it onto the DNA. 4 ATP molecules must bind to the sliding-clamp-loader before the latter can open the sliding clamp. ATP hydrolysis triggers the detachment of the sliding clamp from the sliding-clamp-loader, freeing the sliding clamp to track along DNA.
Interaction partners:
Sequence:
MITVNEKEHILEQKYRPSTIDECILPAFDKETFKSITSKGKIPHIILHSPSPGTGKTTVAKALCHDVNADMMFVNGSDCKIDFVRGPLTNFASAASFDGRQKVIVIDEFDRSGLAESQRHLRSFMEAYSSNCSIIITANNIDGIIKPLQSRCRVITFGQPTDEDKIEMMKQMIRRLTEICKHEGIAIADMKVVAALVKKNFPDFRKTIGELDSYSSKGVLDAGILSLVTNDRGAIDDVLESLKNKDVKQLRALAPKYAADYSWFVGKLAEEIYSRVTPQSIIRMYEIVGENNQYHGIAANTELHLAYLFIQLACEMQWK
Protein: Heterogeneous nuclear ribonucleoprotein R (Q7SZC9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAAEVNGSSVLLKEEEEPMEVTAPRSENYQALLDAGLPQKVAESLDNIFQTGESAEHGLVAYADLDERALDALREFNEEGALSVLQQFKESDLSHVQNKSAFLCGVMKTYRQREKQGNKVQESSKGPDETKIKALLDRTGYTLDVTTGQRKYGGPPPDAVFSGPQPGIGTEVFVGKIPRDLYEDELVPLFEKAGSIWDLRRDVWPLLSHILLLF
Protein: mitogen-activated protein kinase kinase (EC 2.7.12.2) (A8BZ76)
Organism: Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
Interaction partners:
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- 14-3-3 protein
Sequence:
MKRRPMALTLDASTASADGGVEDVQKGGSGTQYIKITDSGSLNTLHESLQISAHGITKTSSPEHILNVQESDLEVVKPLGAGAFGTVNLVKVKTTGQLCAMKEIRISDEEQTQKNIYREIKASISLSCNPYMVKTYNIYSHPGSILHILLEFCKYGSSQDMLKKLKTGKLTENALAVFIIDTLRGLAYLHDNCKIIHRDIKSANILIDEHGYCKLADFGVASSVLPNDDEAAMKTFVGSLSYMSPERIQNQPYSYVSDVWSMGLTYVELLTGSYPYDNVNSFWDAMNVIVNGAPPLLKEDAGYSPGLCDLVNAMLEKDPSKRMTAAQLLKLPFCKKYLAKEEDLRKLFVKWVQDNLK
Protein: NLR family pyrin domain containing 2 (J3KN39)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVSSAQMGFNLQALLEQLSQDELSKFKYLITTFSLAHELQKIPHKEVDKADGKQLVEILTTHCDSYWVEMASLQVFEKMHRMDLSERAKDEVREAALKSFNKRKPLSLGITRKERPPLDVDEMLERFKTEAQETKGNVICLGKEVFKGKKPDKDNRCRYILKTKFREMWKSWPGDSKEVQVMAERYKMLIPFSNPRVLPGPFSYTVVLYGPAGLGKTTLAQKLMLDWAEDNLIHKFKYAFYLSCRELSRLGPCSFAELVFRDWPELQDDIPHILAQARKILFVIDGFDELGAAPGALIEDICGDWEKKKPVPVLLGSLLNRVMLPKAALLVTTRPRALRDLRILAEEPIYIRVEGFLEEDRRAYFLRHFGDEDQAMRAFELMRSNAALFQLGSAPAVCWIVCTTLKLQMEKGEDPVPTCLTRTGLFLRFLCSRFPQGAQLRGALRTLSLLAAQGLWAQTSVLHREDLERLGVQESDLRLFLDGDILRQDRVSKGCYSFIHLSFQQFLTALFYTLEKEEEEDRDGHTWDIGDVQKLLSGVERLRNPDLIQAGYYSFGLANEKRAKELEATFGCRMSPDIKQELLRCDISCKGGHSTVTDLQELLGCLYESQEEELVKEVMAQFKEISLHLNAVDVVPSSFCVKHCRNLQKMSLQVIKENLPENVTASESDAEVERSQDDQHMLPFWTDLCSIFGSNKDLMGLAINDSFLSASLVRILCEQIASDTCHLQRVVFKNISPADAHRNLCLALRGHKTVTYLTLQGNDQDDMFPALCEVLRHPECNLRYLGLVSCSATTQQWADLSLALEVNQSLTCVNLSDNELLDEGAKLLYTTLRHPKCFLQRLSLENCHLTEANCKDLAAVLVVSRELTHLCLAKNPIGNTGVKFLCEGLRYPECKLQTLVLWNCDITSDGCCDLTKLLQEKSSLLCLDLGLNHIGVKGMKFLCEALRKPLCNLRCLWLWGCSIPPFSCEDLCSALSCNQSLVTLDLGQNPLGSSGVKMLFETLTCSSGTLRTLRLKIDDFNDELNKLLEEIEEKNPQLIIDTEKHHPWAERPSSHDFMI