wanglab/gogpt-training-data huggingface dataset:
Protein: Cadherin-5 (Vascular endothelial cadherin) (VE-cadherin) (Q68SP4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, adherens junction {ECO:0000269|PubMed:20736288, ECO:0000269|PubMed:23698350, ECO:0000269|PubMed:25373898}.
Interaction partners:
Sequence:
MMKQCARRQMTEPVFRVAVLLALCSLSIGVDVHQAQKTPSISSAALQRHKRDWKWDKLYAYEETRPKNPPEKIGKLENTFFSSSTRYILKGDGAKDKFGVTDNGDIVVLAKLDRETQSVYNLSASLLNIHTGELVDKDESFVIVVLDINDNIPVFDSDQSGSISESSRAGTTIMKVKATDADDSSTENGRIDFKLLNGTDLFKIKPNGDLIALKSDLDREKQSQYLIAVQAKDMPEHLTGNSATTVVTINIKDINDNIATFKKERYQFTVKEDLKPGSEIGLLEVEDKDEIQNKDPTFALQSKFNDVFDIKRTKEKDGMLSLKVPLDYEKEKTHKFIVIVEEHTVSRTPDNKGLLKRTEVIIDVTDVDEPPIFNQTEYTFSVFEGPFKNPVIGAVSAKDPDSASYKIRYTIEDANCPVDVDPVNGYLSLKRTLDREQESLYTFQVTAHEDVLNGLKSSTMVSLKVLDINDNAPELTNGSYVYVCENDKPNTIIGTIGASDKDENSGRFRFTLARKSSNFSLYDNQDNTATIVLKQGGFSTENSEEYVLEIEIADGGTPEQKSVNLLQIKVCTCQSGRRVEYCMSYARTGMSVSALLAILLCIITILVIVILIVLRRRYQKEVLVTKASGEIHEQLVRYDEEGGGEMDTNGYDVSILSSACHDSSFRPSVGPALYAMVKKPPACKGDMAMMIEVKKDEADRDRDGIPYDTLHIYGYEGTESLAGSLSSLDSSSSGSNLDYDFIHEWGPRFRTLAQLYGVDGSDSDSSY
Protein: Valerianol synthase TPS1A (EC 4.2.3.204) (Terpene synthase 1) (ChTPS1) (Terpene synthase 1a) (ChTps1a) (A0A348AUV5)
Organism: Camellia hiemalis (Camellia)
Function: Terpene synthase that catalyzes the biosynthesis of the terpene valerianol, which is a volatile compound of floral scent.
Interaction partners:
Sequence:
MASSQVGDMVNGNAEPTRHLAKFPPSLWGDRFTSFTLDKQLWDKYGNEIEVLKEQVRSMVVAGGRKAAEQINLINVLERLGVSYHFEKEIEEQLEQLFAKFEDNEDYDLFTIALHFRIFRQHGYKMSCDVFNKFRDSNGEFKETVSNDVQGMLSLYEATYLKIRGEGFLDEAHAFTIAQLESLVGGPHLSSDLSEQVMHALKQSIHRGFPRLEAKHFISFYEKDASRNETLLRLAKLDFNQLQLSHREELCHIFRWWKELDLISKVPYARDRAVECFFWSTCAYYEPQHSVGRAVLTKIMLLLSVTDDTYDAYGTYDELKLYTNAVQRWDVSAMDELPDYMKALYRALLNVYDEVERDLAKQGRDYGVHHSKEAFKEIVRSYEIEAEWFKEGYVASFEEYMKNALVTSTGRLHTTSCFMGLEADVATTEAFEWILTKPKMVAASGAIGRLVDDVMSHDEEQERGHVATGLDCYMKQRGVSKQEAIVELYKMIENAWRDINEEMLKPTAISMKLLIRVLNLSRISDVVYKYVDGYTHPEIIKDHVISLFEDPIPM
Protein: Dof zinc finger protein DOF2.4 (AtDOF2.4) (Protein PHLOEM EARLY DOF 1) (O80928)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence (By similarity). Probably involved in early processes for vascular development. The PEAR proteins (e.g. DOF2.4, DOF5.1, DOF3.2, DOF1.1, DOF5.6 and DOF5.3) activate gene expression that promotes radial growth of protophloem sieve elements. Triggers the transcription of HD-ZIP III genes, especially in the central domain of vascular tissue.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00071}. Symplast {ECO:0000269|PubMed:30626969}. Note=Mobile protein observed in symplastic trafficking; movements are repressed by HD-ZIP III proteins. {ECO:0000269|PubMed:30626969}.
Interaction partners:
- Putative cysteine-rich receptor-like protein kinase 32
Sequence:
MVFSSIQAYLDSSNWQQAPPSNYNHDGTGASANGGHVLRPQLQPQQQPQQQPHPNGSGGGGGGGGGSIRAGSMVDRARQANVALPEAALKCPRCESTNTKFCYFNNYSLTQPRHFCKTCRRYWTRGGALRNVPVGGGCRRNRRTKSNSNNNNNSTATSNNTSFSSGNASTISTILSSHYGGNQESILSQILSPARLMNPTYNHLGDLTSNTKTDNNMSLLNYGGLSQDLRSIHMGASGGSLMSCVDEWRSASYHQQSSMGGGNLEDSSNPNPSANGFYSFESPRITSASISSALASQFSSVKVEDNPYKWVNVNGNCSSWNDLSAFGSSR
Protein: Cyclin K (G3V5E1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKENKENSSPSVTSANLDHTKPCWYWDKKDLAHTPSQLEGLDPATEARYRREGARFIFDVGTRLGLHYDTLATGIIYFHRFYMFHSFKQFPRYVTGACCLFLAGKVEETPKKCKDIIKTARSLLNDVQFGQFGDDPKEEVMVLERILLQTIKFDLQVEHPYQFLLKYAKQLKGDKNKIQKLVQMAWTFVNDSLCTTLSLQWEPEIIAVAVMYLAGRLCKFEIQEWTSKPMYRRWWEQFVQDVPVDVLEDICHQILDLYSQGKQQMPHHTPHQLQQPPSLQPTPQVPQVQQSQPSQSSEPSQPQQKDPQQPAQQQQPAQQPKKPSPQPSSPRQVKRAVVVSPKEENKAAEPPPPKIPKIETTHPPLPPAHPPPASTHPP
Protein: Phosphoribosyl pyrophosphate synthase-associated protein 2 (PRPP synthase-associated protein 2) (41 kDa phosphoribosypyrophosphate synthetase-associated protein) (PAP41) (O60256)
Organism: Homo sapiens (Human)
Function: Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis.
Interaction partners:
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 2
- Phosphoribosyl pyrophosphate synthase-associated protein 1
- Ribose-phosphate pyrophosphokinase 3
- Influenza virus NS1A-binding protein
Sequence:
MFCVTPPELETKMNITKGGLVLFSANSNSSCMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTSCAKSIIGVIPYFPYSKQCKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEIPDYRNAVIVAKSPASAKRAQSFAERLRLGIAVIHGEAQDAESDLVDGRHSPPMVRSVAAIHPSLEIPMLIPKEKPPITVVGDVGGRIAIIVDDIIDDVDSFLAAAETLKERGAYKIFVMATHGLLSSDAPRRIEESAIDEVVVTNTIPHEVQKLQCPKIKTVDISMILSEAIRRIHNGESMSYLFRNIGLDD
Protein: Zinc finger protein 480 (Q8WV37)
Organism: Homo sapiens (Human)
Function: Involved in transcriptional regulation as an activator.
Subcellular location: Nucleus {ECO:0000269|PubMed:15219843}.
Interaction partners:
Sequence:
MLCDEKAQKRRKRKAKESGMALPQGHLTFRDVAIEFSQAEWKCLDPAQRALYKDVMLENYRNLVSLGISLPDLNINSMLEQRREPWSGESEVKIAKNSDGRECIKGVNTGSSYALGSNAEDKPIKKQLGVSFHLHLSELELFPDERVINGCNQVENFINHSSSVSCLQEMSSSVKTPIFNRNDFDDSSFLPQEQKVHLREKPYECNEHSKVFRVSSSLTKHQVIHTVEKPYKCNSCGKVFSRNSHLAEHCRIHTGEKPYKCNVCGKVFSYNSNFARHQRIHTREKPYECNECGKVFSNNSYLARHQRIHAEEKPYKCNECGKGFSHKSSLANHWRIYTGEKPYKCDECGKAFYRIALLVRHQKIHTGEKPYKCNECGKVFIQNSHLAQHWRIHTGEKPYKCNECGKVFNQLSNLARHRRIHTGEKPYKCNECGKAFSEYSGLSAHLVIHTGEKPYKCSECGKAFRHKLSLTNHQRIHTGERPYKCNECGKVFNRIAHLARHRKIHTGEKPYKCNECGKAFSRISYLAQHWTIHMG
Protein: Uncharacterized bHLH domain-containing protein C3F10.12c (Q10186)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Checkpoint signal transducer rad25
- Checkpoint signal transducer rad24
Sequence:
MQRDMSINHLLPPLSGPGQVEQLTGFTNDIVYNDFYAHAVSYNPYPSEKIDFPKKNTAHKNSTTSTVASSGNTTMEKPCVGSEEWYKAKRLSHKEVERRRREAISEGIKELANIVPGCEKNKGSILQRTAQYIRSLKEMEEMCREKSNLEKLVADHTIQELARENARLKSECERAWRSVELWKQAARSFDSELDVEENSES
Protein: H-2 class II histocompatibility antigen, A-K beta chain (P06343)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MALQIPSLLLLAAVVVLTVLSSPGTEGGNSERHFVHQFQPFCYFTNGTQRIRLVIRYIYNREEYVRFDSDVGEYRAVTELGRPDAEYWNKQYLERTRAELDTVCRHNYEKTETPTSLRRLEQPSVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ
Protein: DNA polymerase III subunit delta (EC 2.7.7.7) (P28630)
Organism: Escherichia coli (strain K12)
Function: Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The delta subunit is the wrench that will open the beta subunit dimer, which has been modeled to leave a gap large enough for ssDNA to pass through. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open them at one interface. Primed DNA is recognized, ATP is hydrolyzed releasing the gamma complex and closing the beta sliding clamp ring around the primed DNA.
Interaction partners:
- DNA polymerase III subunit chi
- Beta sliding clamp
- DNA polymerase III subunit delta'
- DNA polymerase III subunit psi
- DNA polymerase III subunit tau
- DNA polymerase III subunit alpha
- DNA polymerase III subunit epsilon
- LPS-assembly lipoprotein LptE
- Nicotinate-nucleotide adenylyltransferase
- DNA polymerase III subunit theta
Sequence:
MIRLYPEQLRAQLNEGLRAAYLLLGNDPLLLQESQDAVRQVAAAQGFEEHHTFSIDPNTDWNAIFSLCQAMSLFASRQTLLLLLPENGPNAAINEQLLTLTGLLHDDLLLIVRGNKLSKAQENAAWFTALANRSVQVTCQTPEQAQLPRWVAARAKQLNLELDDAANQVLCYCYEGNLLALAQALERLSLLWPDGKLTLPRVEQAVNDAAHFTPFHWVDALLMGKSKRALHILQQLRLEGSEPVILLRTLQRELLLLVNLKRQSAHTPLRALFDKHRVWQNRRGMMGEALNRLSQTQLRQAVQLLTRTELTLKQDYGQSVWAELEGLSLLLCHKPLADVFIDG
Protein: At5g42000 (ORMDL family protein) (Q9FHY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Long chain base biosynthesis protein 1
- Long chain base biosynthesis protein 2a
- Long chain base biosynthesis protein 2b
- serine C-palmitoyltransferase
- Lecithin-cholesterol acyltransferase-like 1
- Phosphatidylinositol:ceramide inositolphosphotransferase 2
- Methyltransferase-like protein 2
Sequence:
MYVRALPTTDVNRNTEWFTYPGVWTTYILILFFSWLLVLSVFHCSPGIAWTIVHLAHFTVTYHSFHWKKGTPFGDDQGVYNRLTWWEQIDNGKQLTRNRKFLTVVPVVLYLIASHTTDYQHPMLFLNTLAVFVMVVAKFPHMHKVRIFGINGDQ
Protein: Neuropilin-2 (Vascular endothelial cell growth factor 165 receptor 2) (O60462)
Organism: Homo sapiens (Human)
Function: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.
Subcellular location: Membrane {ECO:0000269|PubMed:11112349}; Single-pass type I membrane protein {ECO:0000269|PubMed:11112349}.; SUBCELLULAR LOCATION: [Isoform s9]: Secreted {ECO:0000269|PubMed:11112349}.
Interaction partners:
- Semaphorin-3F
- Plexin-A1
- Vascular endothelial growth factor C
- Semaphorin-3A
- Plexin-A3
- Plexin-A4
- Vascular endothelial growth factor receptor 3
- Semaphorin-3C
- Semaphorin-3B
- Vascular endothelial growth factor receptor 1
Sequence:
MDMFPLTWVFLALYFSRHQVRGQPDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWIVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSMLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPKMEIILQFLIFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSELRSSTGILSLTFHTDMAVAKDGFSARYYLVHQEPLENFQCNVPLGMESGRIANEQISASSTYSDGRWTPQQSRLHGDDNGWTPNLDSNKEYLQVDLRFLTMLTAIATQGAISRETQNGYYVKSYKLEVSTNGEDWMVYRHGKNHKVFQANNDATEVVLNKLHAPLLTRFVRIRPQTWHSGIALRLELFGCRVTDAPCSNMLGMLSGLIADSQISASSTQEYLWSPSAARLVSSRSGWFPRIPQAQPGEEWLQVDLGTPKTVKGVIIQGARGGDSITAVEARAFVRKFKVSYSLNGKDWEYIQDPRTQQPKLFEGNMHYDTPDIRRFDPIPAQYVRVYPERWSPAGIGMRLEVLGCDWTDSKPTVETLGPTVKSEETTTPYPTEEEATECGENCSFEDDKDLQLPSGFNCNFDFLEEPCGWMYDHAKWLRTTWASSSSPNDRTFPDDRNFLRLQSDSQREGQYARLISPPVHLPRSPVCMEFQYQATGGRGVALQVVREASQESKLLWVIREDQGGEWKHGRIILPSYDMEYQIVFEGVIGKGRSGEIAIDDIRISTDVPLENCMEPISAFAGENFKVDIPEIHEREGYEDEIDDEYEVDWSNSSSATSGSGAPSTDKEKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKVKMNHQKCCSEA
Protein: Protein KTI12 homolog (AtKTI12) (At1g13870) (Protein DEFORMED ROOTS AND LEAVES 1) (AtDRL1) (Protein ELONGATA4) (Q9LMH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Elongator complex-associated factor that is not a structural subunit but rather transiently contacts the complex. Regulates both meristem activity and organ growth; acts as a positive regulator of adaxial leaf patterning by modulating both cell division and differentiation. Required for an early step in synthesis of 5-carbamoylmethyl (ncm5) groups present on uridines (ncm5U) at the wobble position in tRNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P34253}. Nucleus {ECO:0000250|UniProtKB:P34253}.
Interaction partners:
- Elongator complex protein 1
- Elongator complex protein 3
- Elongator complex protein 4
- Elongator complex protein 2
- Elongator complex protein 5
- Radical S-adenosyl methionine domain-containing protein 1, mitochondrial
- Elongator complex protein 6
- Vacuolar-sorting receptor 1
- tRNA
- tRNA
Sequence:
MALVVICGQPCSGKSIAAVTLAETLKESETKQSVRIIDEASFHLDRNQNYANMPAEKNLRGKLRSDVDRSVSTGEIVIVDSLNSIKGYRYELWCIARAAGIRYCVVYCDVDEAHCRQWNKERSDRGEDGYDDGIFEDLVRRFEKPERRNRWDSPLFELYPSREVIDKSSPVILEAVTYLTKTVDSKTQDVRILQPSIATQAARFSEANSLYELDRATQEIINAIVEQQSLGAAISRVTLGNELPPIEICRPIGLPELRRLRRTFVKLMGQSSLSGPPLPTDADSAKRRFVDYLNREFGGNNA
Protein: NAD kinase 2, mitochondrial (A0A0C4DGV3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLLAASKVLDRLKPVIGVNTDPERSEGHLCLPVRYTHSFPEALQKFYRGEFRWLWRQRIRLYLEGTGINPVPVDLHEQQLSLNQHNRALNIERAHDERSEASGPQLLPVRALNEVFIGESLSSRSFNINRVATQAVEDVLNIAKRQGNLSLPLNRELVEKVTNEYNESLLYSPEEPKILFSIREPIANRVFSSSRQRCFSSKVCVRSRCWDACMVVDGGTSFEFNDGAIASMMINKEDELRTVLLEQ
Protein: NF-kappa-B inhibitor epsilon (NF-kappa-BIE) (I-kappa-B-epsilon) (IkB-E) (IkB-epsilon) (IkappaBepsilon) (O54910)
Organism: Mus musculus (Mouse)
Function: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel complexes (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Transcription factor p65
- Proto-oncogene c-Rel
- Nuclear factor NF-kappa-B p105 subunit
- NF-kappa-B inhibitor beta
- Transcription factor RelB
- NF-kappa-B inhibitor alpha
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- NF-kappa-B essential modulator
- Nuclear factor NF-kappa-B p100 subunit
Sequence:
MSDARKGPDEADDSQCDSGIESLRSLRSLPEPTAAPGSGSSQSGCPQPWRHAPETHKEPEKEDADGERADSTYASSSLTESFPLLERPEAKDPSPPAPGSPLPPAGVLSPQQLEALTYISEDGDTLLHLAVIHEAPSVLFCCLAFLPQEVLDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACRRQNLACACCLLEEQPEPGRQLSHPLDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDVQEGTSGKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGADSLLLNVEDETPQDLAEDLLSYLPFDDLKISGKPLLCTD
Protein: Antifungal protein 5 (CW-5) (P83139)
Organism: Malva parviflora (Little mallow) (Cheeseweed mallow)
Function: Possesses potent antifungal activity against F.graminearum but not P.infestans.
Interaction partners:
Sequence:
ITCGQVTSQVAGCLSYLQRGGAPAPXXXXGIRNLXXMA
Protein: Transforming acidic coiled-coil containing protein 2 (E9PBC6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MGNENSTSDNQRTLSAQTPRSAQPPGNSQNIKRKQQDTPGSPDHRDASSIGSVGLGGFCTASESSASLDPCLVSPEVTEPRKDPQGARGPEGSLLPSPPPSQEREHPSSSMPFAECPPEGCLASPAAAPEDGPQTQSPRREPAPNAPGDIAAAFPAERDSSTPYQEIAAVPSAGRERQPKEEGQKSSFSFSSGIDQSPGMSPVPLREPMKAPLCGEGDQPGGFESQEKEAAGGFPPAESRQGVASVQVTPEAPAAAQQGTESSAVLEKSPLKPMAPIPQDPAPRASDRERGQGEAPPQYLTDDLEFLRACHLPRSNSGAAPEAEVNAASQESCQQPVGAYLPHAELPWGLPSPALVPEAGGSGKEALDTIDVQGHPQTGMRGTKPNQVVCVAAGGQPEGGLPVSPEPSLLTPTEEAHPASSLASFPAAQIPIAVEEPGSSSRESVSKAGMPVSADAAKEVVDAGLVGLERQVSDLGSKGEHPEGDPGEVPAPSPQERGEHLNTEQSHEVQPGVPPPPLPKEQSHEVQPGAPPPPLPKAPSESARGPPGPTDGAKVHEDSTSPAVAKEGSRSPGDSPGGKEEAPEPPDGGDPGNLQGEDSQAFSSKRDPEVGKDELSKPSSDAESRDHPSSHSAQPPRKGGAGHTDGPHSQTAEADASGLPHKLGEEDPVLPPVPDGAGEPTVPEGAIWEGSGLQPKCPDTLQSREGLGRMESFLTLESEKSDFPPTPVAEVAPKAQEGESTLEIRKMGSCDGEGLLTSPDQPRGPACDASRQEFHAGVPHPPQGENLAADLGLTALILDQDQQGIPSCPGEGWIRGAASEWPLLSSEKHLQPSQAQPETSIFDVLKEQAQPPENGKETSPSHPGFKDQGADSSQIHVPVEPQEDNNLPTHGGQEQALGSELQSQLPKGTLSDTPTSSPTDMVWESSLTEESELSAPTRQKLPALGEKRPEGACGDGQSSRVSPPAADVLKDFSLAGNFSRKETCCTGQGPNKSQQALADALEEGSQHEEACQRHPGASEAADGCSPLWGLSKREMASGNTGEAPPCQPDSVALLDAVPCLPALAPASPGVTPTQDAPETEACDETQEGRQQPVPAPQQKMECWATSDAESPKLLASFPSAGEQGGEAGAAETGGSAGAGDPGKQQAPEKPGEATLSCGLLQTEHCLTSGEEASTSALRESCQAEHPMASCQDALLPARELGGIPRSTMDFSTHQAVPDPKELLLSGPPEVAAPDTPYLHVDSAAQRGAEDSGVKAVSSADPRAPGESPCPVGEPPLALENAASLKLFAGSLAPLLQPGAAGGEIPAVQASSGSPKARTTEGPVDSMPCLDRMPLLAKGKQATGEEKAATAPGAGAKASGEGMAGDAAGETEGSMERMGEPSQDPKQGTSGGVDTSSEQIATLTGFPDFREHIAKIFEKPVLGALATPGEKAGAGRSAVGKDLTRPLGPEKLLDGPPGVDVTLLPAPPARLQVEKKQQLAGEAEISHLALQDPASDKLLGPAGLTWERNLPGAGVGKEMAGVPPTLREDERPEGPGAAWPGLEGQAYSQLERSRQELASGLPSPAATQELPVERAAAFQVAPHSHGEEAVAQDRIPSGKQHQETSACDSPHGEDGPGDFAHTGVPGHVPRSTCAPSPQREVLTVPEANSEPWTLDTLGGERRPGVTAGILEMRNALGNQSTPAPPTGEVADTPLEPGKVAGAAGEAEGDITLSTAETQACASGDLPEAGTTRTFSVVAGDLVLPGSCQDPACSDKAPGMEGTAALHGDSPARPQQAKEQPGPERPIPAGDGKVCVSSPPEPDETHDPKLQHLAPEELHTDRESPRPGPSMLPSVPKKDAPRVMDKVTSDETRGAEGTERSAKDIGLWKAMMPSLDTDTLDVLERRVVLIQHEFLHKKEANGHSRFMYSSPVADDIIQPAAPADLESPTLAASSYHGDVVGQVSTDLIAQRSSDSEEAFETPESTTPVKAPPAPPPPPPEVIPEPEVSTQPPPEEPGCGSETVPVPDGPRSDSVEGSPFRPPSHSFSAVFDEDKPIASSGTYNLDFDNIELVDTFQTLEPRASDAKNQEGKVNTRRKSTDSVPISKSTLSRSLSLQASDFDGASSSGNPEAVALAPDAYSTGSSSASSTLKRTKKPRPPSLKKKQTTKKPTETPPVKETQQEPDEESLVPSGENLASETKTESAKTEGPSPALLEETPLEPAVGPKAACPLDSESAEGVVPPASGGGRVQNSPPVGRKTLPLTTAPEAGEVTPSDSGGQEDSPAKGLSVRLEFDYSEDKSSWDNQQENPPPTKKIGKKPVAKMPLRRPKMKKTPEKLDNTPASPPRSPAEPNDIPIAKGTYTFDIDKWDDPNFNPFSSTSKMQESPKLPQQSYNFDPDTCDESVDPFKTSSKTPSSPSKSPASFEIPASAMEANGVDGDGLNKPAKKKKTPLKTDTFRVKKSPKRSPLSDPPSQDPTPAATPETPPVISAVVHATDEEKLAVTNQKWTCMTVDLEADKQDYPQPSDLSTFVNETKFSSPTEELDYRNSYEIEYMEKIGSSLPQDDDAPKKQALYLMFDTSQESPVKSSPVRMSESPTPCSGSSFEETEALVNTAAKNQHPVPRGLAPNQESHLQVPEKSSQKELEAMGLGTPSEAIEIREAAHPTDVSISKTALYSRIGTAEVEKPAGLLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGKS
Protein: Sodium/potassium-transporting ATPase subunit beta-1 (Sodium/potassium-dependent ATPase subunit beta-1) (P07340)
Organism: Rattus norvegicus (Rat)
Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. Plays a role in innate immunity by enhancing virus-triggered induction of interferons (IFNs) and interferon stimulated genes (ISGs). Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of TAK1 and TBK1 (By similarity).
Subcellular location: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:14749213}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes. Localizes in long striations at the level of Z and M lines. {ECO:0000250|UniProtKB:P14094}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit alpha-1
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit alpha-4
- Potassium-transporting ATPase alpha chain 2
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit beta-3
- Phospholemman
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISELKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIIRFLEKYKDSAQKDDMIFEDCGSMPSEPKERGEFNHERGERKVCRFKLDWLGNCSGLNDESYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPLTMKYNPNVLPVQCTGKRDEDKDKVGNIEYFGMGGFYGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTLDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS
Protein: Probable sucrose utilization protein SUC1 (P33181)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Affects sucrose utilization and alpha-glucosidase activity. Probable transcriptional activator.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Uga33p
Sequence:
MSKGKRAPYTRPCDSCSFRKVKCDMKTPCSRCVLNNLKCTNNRIRKKCGPKKIRDRTREAINNLSNKEDPKTNSFIPHFQLDKLQPCLETYQTWYYGIWPVLSISDLNMKITKRDVSAYALACALSAAILNQIDFISNNGTYCIPEDVKKLDFIGECIRARTFMNYQMTPTLETILTSFFLHVAEVNKGSKPAAIIYLREAITMAQIIGLHNESTYKSKPVAEAHRMRKIYFMLMVTERFMCIDDLIPVVLENSIKEFSLDDEQYSVLIDGFKELVKVFSIPSKAIFDRFIQMNDSISMPPETAGLLNKIQLELESICISPVAPDIQKANIIVSKYWMKALTWKITRKNNLLDDFVTTLCVKYPIELSEQFLGEIKSIPLRAFESNGPGVVFKLLSIATVLIDSINLSNDVSGYESLQRMFDLISKLKKTDMIIPRREYDRIKEALTKMEIDIFFSSAQSGGYISEVESNGSLDAFLTDPLVFYSGSNDNPTPSYIPDYQK
Protein: Thiosulfate/3-mercaptopyruvate sulfurtransferase 1, mitochondrial (EC 2.8.1.1) (EC 2.8.1.2) (AtMST1) (Rhodanese homolog protein 1) (AtRDH1) (Sulfurtransferase 1) (AtStr1) (O64530)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is 3-mercaptopyruvate > thiosulfate. Involved in embryo and seed development.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10601861, ECO:0000269|PubMed:10734224, ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:15181206}.
Interaction partners:
- Adenylyltransferase and sulfurtransferase MOCS3
- 5'-adenylylsulfate reductase 3, chloroplastic
- Cystathionine beta-lyase, chloroplastic
- 5'-adenylylsulfate reductase 1, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- Cysteine desulfurase, mitochondrial
- Assimilatory sulfite reductase
- Aspartate aminotransferase, mitochondrial
- Sulfite oxidase
- Cystathionine gamma-synthase 1, chloroplastic
Sequence:
MASTLFSRTFLAASHRLITPSLPQKIFNPATFLSRSLHSQLGSASTAYKSTTWARRAMASTGVETKAGYSTSSVSTSEPVVSVDWLHANLREPDLKILDASWYMPDEQRNPIQEYQVAHIPRALFFDLDGISDRKTSLPHMLPTEEAFAAGCSALGIDNKDEVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPRWRASGYDVESSASGDAILKASAASEAIEKIYQGQTVSPITFQTKFQPHLVWTLDQVKNNMEDPTYQHIDARSKARFDGTAPEPRKGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPIMASCGTGVTACILAMGLHRLGKTDVPIYDGSWTEWATQPDLPIESVESSS
Protein: Omega-6 fatty acid desaturase, chloroplastic (EC 1.14.19.23) (P46312)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chloroplast omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 16:3 and 18:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglycerol.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:12766230}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Palmitoyl-monogalactosyldiacylglycerol delta-7 desaturase, chloroplastic
- Fatty acid desaturase 4, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Stearoyl-[acyl-carrier-protein] 9-desaturase 7, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Beta-ketoacyl-[acyl-carrier-protein] synthase III, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic
- Delta-9 acyl-lipid desaturase 2
- Phospholipid:diacylglycerol acyltransferase 1
- Glycerol-3-phosphate acyltransferase, chloroplastic
Sequence:
MASRIADSLFAFTGPQQCLPRVPKLAASSARVSPGVYAVKPIDLLLKGRTHRSRRCVAPVKRRIGCIKAVAAPVAPPSADSAEDREQLAESYGFRQIGEDLPENVTLKDIMDTLPKEVFEIDDLKALKSVLISVTSYTLGLFMIAKSPWYLLPLAWAWTGTAITGFFVIGHDCAHKSFSKNKLVEDIVGTLAFLPLVYPYEPWRFKHDRHHAKTNMLVHDTAWQPVPPEEFESSPVMRKAIIFGYGPIRPWLSIAHWVNWHFNLKKFRASEVNRVKISLACVFAFMAVGWPLIVYKVGILGWVKFWLMPWLGYHFWMSTFTMVHHTAPHIPFKPADEWNAAQAQLNGTVHCDYPSWIEILCHDINVHIPHHISPRIPSYNLRAAHESIQENWGKYTNLATWNWRLMKTIMTVCHVYDKEENYIPFDRLAPEESQPITFLKKAMPNYTA
Protein: Epididymis luminal protein 70 (Moesin, isoform CRA_a) (V9HWC0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM
Protein: Hypoxic response protein 1 (HRP1) (P9WJA3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Unlike some other CBS-domain containing proteins does not seem to bind AMP.
Subcellular location: Secreted {ECO:0000269|PubMed:18640126}. Note=Not seen to be associated with the cell wall.
Interaction partners:
- Uncharacterized protein Rv1738
- Alpha-crystallin
- Probable membrane protein Rv1733c
- Universal stress protein Rv2623
- Uncharacterized protein Rv2030c
- Putative NAD
- Universal stress protein Rv2624c
- Putative zinc metalloprotease Rip3
- Probable nitrate/nitrite transporter NarK2
- Putative uncharacterized protein Rv2628
Sequence:
MTTARDIMNAGVTCVGEHETLTAAAQYMREHDIGALPICGDDDRLHGMLTDRDIVIKGLAAGLDPNTATAGELARDSIYYVDANASIQEMLNVMEEHQVRRVPVISEHRLVGIVTEADIARHLPEHAIVQFVKAICSPMALAS