wanglab/gogpt-training-data huggingface dataset:
Protein: Calcium-activated potassium channel subunit alpha-1 (BK channel) (BKCA alpha) (Calcium-activated potassium channel, subfamily M subunit alpha-1) (K(VCA)alpha) (KCa1.1) (Maxi K channel) (MaxiK) (Slo-alpha) (Slo1) (Slowpoke homolog) (Slo homolog) (Q28265)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX) (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q12791}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Calcium-activated potassium channel subunit beta-1
- Potassium calcium-activated channel subfamily M regulatory beta subunit 3.
- Leucine rich repeat containing 26.
Sequence:
EPNMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGDKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDNLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNSQALTYWECVYLLMVTMSTVGYGDVYAKTTPGGLFIVFFILGGLAMFASYVPEIIEIIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSHFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCDDPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELRLGFIAQSCLAQGLSTMLANLFSIGSFIKIEEDTWHKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTSGFFIASDAKEVKRAFFYCKACHNDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSPSSSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVISTRSEAAMTVLSGHVVVCIFGHVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILPGTPLTRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDKSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYRFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRQNRPKSRESRDKQTEKKWFTDEPDNAYPRNIQIEPMSTHMANQINQYKSTSSLIPPIREVEDEC
Protein: L-methionine/branched-chain amino acid exporter YjeH (P39277)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the efflux of L-methionine, L-leucine, L-isoleucine and L-valine. Activity is dependent on electrochemical potential.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:26319875}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Homoserine O-succinyltransferase
Sequence:
MSGLKQELGLAQGIGLLSTSLLGTGVFAVPALAALVAGNNSLWAWPVLIILVFPIAIVFAILGRHYPSAGGVAHFVGMAFGSRLERVTGWLFLSVIPVGLPAALQIAAGFGQAMFGWHSWQLLLAELGTLALVWYIGTRGASSSANLQTVIAGLIVALIVAIWWAGDIKPANIPFPAPGNIELTGLFAALSVMFWCFVGLEAFAHLASEFKNPERDFPRALMIGLLLAGLVYWGCTVVVLHFDAYGEKMAAAASLPKIVVQLFGVGALWIACVIGYLACFASLNIYIQSFARLVWSQAQHNPDHYLARLSSRHIPNNALNAVLGCCVVSTLVIHALEINLDALIIYANGIFIMIYLLCMLAGCKLLQGRYRLLAVVGGLLCVLLLAMVGWKSLYALIMLAGLWLLLPKRKTPENGITT
Protein: Nuclear Pore complex Protein (P91350)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear pore complex protein 5
- Nsp1_C domain-containing protein
- WD_REPEATS_REGION domain-containing protein
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein 15
- Protein SEC13 homolog
- Nuclear Pore complex Protein
- Nuclear pore complex protein Nup98-Nup96
- Nucleoporin SEH1
- Nuclear pore protein
Sequence:
MELVYGSEISFTDGFAIKPARTFVVNTNAPLHSNGFDVQPSAGVATFPHCSNYGDRIFLWRAIGQKLFIEERSLLYSITDGSLCIDFTRTPIIPGTSITIFEEGVLCIVVPTASAIHRFYARLHSKGHDTFSILARIKEDDDFRRFRTSHSLSTPGRPIRASVTHHPSRNTISYCTAEGQLVIVTLGSYTESSDKHEEFTMGEVGLLGKLLGGTDKRVSDACVMKNLRPTSGVTRERKISVQSDIVFAVTRDGWVQAWNVETKKQLPSTIDLNNYFASDGKSLNRDLESADFEEEKSPMEPTETVYSIRAYSFDVDILLIVGCDLAVSGKSVGMRVHILKVSNDQIQHLQMFETSMSVDERLVDLELIQNYFPSKESESLDETQDGELYNPLTAALFSLSALFKSSSAKKTYSMKRISFAIQWKKGRVFTDFDWHSVRQFTSPATTKEEPIGNTDEVEPAIERPYNLSADSSIETLIDVVFDTDIYPFDIVFRAVQIVSDNFRGTLGQVRNNNWPELSKLVDTYLTSVEFNRKFQQKTDRSIRLRLNAPQESQKTALKDFWWALLRACEELDFAARGAISLAPIQFCGDLRIMAVVHRDRMTFLGDNNTEFLEIISSENIPKQGNVEEKFRKLPNKHFIDLIEEASKFADRRVFLMNRERARLTNAKNGVAVVEDDNVENAYDYDSDGRFINIKTALEGPIVKLAAAFVEASTFDNSKPFEDPHPQIFGGSFTQSVVSANIRVSVESRVHFALTLQTLLNAITEKKSRAGAPSFGDVEALSCELREIIRVYRELNEQLDIKIVQNGAKMSIGTWLTSDAEGLSMMKKEGGYGPHGYDEIRENDFNWFVGVTTEAAIRALLSSSEILVLPRRLVLQKQYKVLLTILNSYISETRALKPVITFYRGIAYSGTDHPVKALNSFQSCLDAFSEGNNALRKAVYFLLPKRFDVAQGKDPVEELTASEYFLTVVRFLQEHNHAEEVCSVAVKAIENLPIENESVQLISNTLFNHLTNRREWFQSLKLILRTTLRSETRRASIRELLSLMLACGEWEAIATMKFGEHEQVVEDFLRDAACRQSPSEKKHYFELLFAFYVARKDFRKGACAMYEYARHIESTTCMTPELLRRKRDCLAVVLNLQSVLGMEPDDDRAIYDDATDTNLVFPEPSDDEDELITESDSSGENGKLPSGNKDSGSGTGNNSSPDNSNGTSSSGTGVDLVALKARQMAYALGSDDMDTDDTEDDMKGGSIPLFKRRKLLVLSEKDIRDELVLCSARVGLLSSDQFKGVPPTDLNELFSLLVDNQHFDEAFDIARQFNLDSHRLFFTMTREAIMIDALRDDLNIEMAATHQAGWVRLNRRHCAAVATAEEHWSVVRGLVDAAQAEWPGDSRPLRGSTEAFLSFKLNVPVWLHSVFENNDANDYLRCLVDYESYSIALQVLSDIVEQETLQASQSNARTWLPYGIIDELMIRSADYIRKMSLKSPEDQVVAAEVANLRKSADQKMLIYFRKVADFEQAQKMSSRFFDK
Protein: Ubiquitin-conjugating enzyme E2 variant 1D (Ubc enzyme variant 1D) (Protein MMS ZWEI HOMOLOG 4) (Q9SVD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has no ubiquitin ligase activity on its own. The heterodimer with UBC catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. May play a role in the control of progress through the cell cycle and differentiation. Involved in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 36
- Ubiquitin-conjugating enzyme E2 35
- Ubiquitin-conjugating enzyme E2 13
- Ubiquitin-conjugating enzyme E2 1
- Ubiquitin-conjugating enzyme E2 27
- Ubiquitin-conjugating enzyme E2 22
- Ubiquitin-ribosomal protein eL40y fusion protein
- Ubiquitin-ribosomal protein eL40z fusion protein
- F-box family protein-like protein
- Membrane-anchored ubiquitin-fold protein 5
Sequence:
MTLGSGGSSVVVPRNFRLLEELERGEKGIGDGTVSYGMDDGDDIYMRSWTGTIIGPHNTVHEGRIYQLKLFCDKDYPEKPPTVRFHSRVNMACVNHETGVVDPKKFGLLANWQREYTMEDILVQLKKEMSTSHNRKLVQPPEGTCF
Protein: DNA-directed RNA polymerase subunit (EC 2.7.7.6) (Q7TSI4)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVKEQFRETDVAKKISHICFGMKSPEEMRQQAHIQVVSKNLYSQDNNHAPLLYGVLDHRMGTSEKDRPCETCGKNLADCLGHYGYIDLELPCFHVGYFRAVIGILQMICKTCCHIMLSQEEKQQFLDFLKRPGLTYLQKRGLKKKISDKCRKKSTCHYCGAFNGTVKKCGLLKIIHEKYKTNKKVVDPIVSNFLQSFETAIEHNKEVEPLLGRAQENLNPLVVLNLFKRIPAEDVPLLLMNPESGKPSDLILTRLLVPPLCIRPSVVSDLKSGTNEDDLTMKLTEIIFLNDVIKKHRISGAKTQMIMEDWDFLQLQCALYINSELSGIPLNMAPKKWTRGFVQRLKGKQGRFRGNLSGKRVDFSGRTVISPDPNLRIDEVAVPVHVAKILTFPEKVNKANINFLRKLVRNGPDVHPGANFIQQRHMQMKRFLKYGNREKMAQELKFGDIVERHLIDGDVVLFNRQPSLHKLSIMAHLARVKPHRTFRFNECVCTPYNADFDGDEMNLHLPQTEEAKAEALVLMGTKANLVTPRNGEPLIAAIQDFLTGAYLLTLKDTFFDRAKACQIIASILVGKDEKIKVRLPPPTILKPVTLWTGKQIFSVILRPSDDNPVRANLRTKGKQYCGKGEDLCVNDSLSPFQMSPSRTVS
Protein: Alpha-tocopherol transfer protein (Tocopherol (alpha) transfer protein) (B0S5J5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Sulfotransferase
Sequence:
MKSEEVDETEELNNLPVDSSRIAPYLSELKEKAEAELRIRDLDLSKTFLIRFLQARDFDVALALKLLINYHKWRQECPEITADLRPSSVIGLLQNNYHGVLRSRDDAGSRVLIYRIGKWNPKEFTAYEVFRVSLITSELIVQEWETQRNGLKAIFDLQDWCFAHALQINPSLAKKISSVLTDSFPLKVRGIHLINEPIFFRPVFAMIRPFLPDKIKQRIHMHGCSYARSLCNYFPKAVLPPVYGGTGPSVDEVCQEWTEYIMQSEDYLHRLSVDLGGEGGHASQS
Protein: FAM10 family protein At4g22670 (Q93YR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transcription elongation factor 1 homolog
- Heat shock 70 kDa protein 14
- Probable inactive receptor kinase At5g58300
- Probable plastid-lipid-associated protein 4, chloroplastic
- Probable plastid-lipid-associated protein 9, chloroplastic
- 14-3-3-like protein GF14 mu
- Probably inactive leucine-rich repeat receptor-like protein kinase IMK2
- Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial
- Camphor resistance CrcB family protein
Sequence:
MDSTKLSELKVFIDQCKSDPSLLTTPSLSFFRDYLESLGAKIPTGVHEEDKDTKPRSFVVEESDDDMDETEEVKPKVEEEEEEDEIVESDVELEGDTVEPDNDPPQKMGDSSVEVTDENREAAQEAKGKAMEALSEGNFDEAIEHLTRAITLNPTSAIMYGNRASVYIKLKKPNAAIRDANAALEINPDSAKGYKSRGMARAMLGEWAEAAKDLHLASTIDYDEEISAVLKKVEPNAHKLEEHRRKYDRLRKEREDKKAERDRLRRRAEAQAAYDKAKKEEQSSSSRPSGGGFPGGMPGGFPGGMPGGFPGGMGGMPGGFPGGMGGMGGMPGGFPGGMGGGMPAGMGGGMPGMGGGMPAGMGGGGMPGAGGGMPGGGGMPGGMDFSKILNDPELMTAFSDPEVMAALQDVMKNPANLAKHQANPKVAPVIAKMMGKFAGPQ
Protein: GDNF family receptor alpha-3 variant (K9J968)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MVRPLNPRPLPPVVLMLLLLLPPSPLPLAAGDPLPTESRLMNSCLQARRKCQADPTCSAAYHHLDSCTSSISTPLPSEEPSVPADCLEAAQQLRNSSLIGCMCHRRMKNQVACLDIYWTVHRARSLDSDLCLKFAMLCTLNDKCDRLRKAYGEACSGPHCQRHVCLRQLLTFFEKAAEPHAQGLLLCPCAPNDRGCGERRRNTIAPNCALPPVAPNCLELRRLCFSDPLCRSRLVDFQTHCHPMDILGTCATEQSRCLRAYLGLIGTAMTPNFVSNVNTSVALSCTCRGSGNLQEECEMLEGFFSHNPCLTEAIAAKMRFHSQLFSQDWPHPTFAVMAHQNENPAVRPQPWVPSLFSCTLPLILLLSLW
Protein: Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide) (Proto-oncogene c-Sis) (Becaplermin) (P01127)
Organism: Homo sapiens (Human)
Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA (By similarity).
Subcellular location: Secreted. Note=Released by platelets upon wounding.
Interaction partners:
- Platelet-derived growth factor receptor beta
- Platelet-derived growth factor receptor alpha
- Platelet-derived growth factor subunit A
- Platelet-derived growth factor C
- Platelet-derived growth factor D
- Epidermal growth factor receptor
- Pro-epidermal growth factor
- Fibroblast growth factor 2
- Insulin-like growth factor 1
- Protransforming growth factor alpha
Sequence:
MNRCWALFLSLCCYLRLVSAEGDPIPEELYEMLSDHSIRSFDDLQRLLHGDPGEEDGAELDLNMTRSHSGGELESLARGRRSLGSLTIAEPAMIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQLRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETVAAARPVTRSPGGSQEQRAKTPQTRVTIRTVRVRRPPKGKHRKFKHTHDKTALKETLGA
Protein: Paired box 6b (Paired box protein Pax-6b isoform X1) (A0A0R4IQL7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Achaete-scute homolog 1a
- Neurogenic differentiation factor 1
- Insulinoma-associated protein 1a
Sequence:
MPQKEYHNQPTWESGVASMMQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQTHDDAKVQLDNKNVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVGKIAQYKRECPSIFAWEIRDRLLSEGVCTNDNIPSVSSINRVLRNLASEKQQMGADGMYDKLRMLNGQSGTWGTRPGWYPGTSVPGQPNQDGCQQQDNGGENTNSISSNGEDSDETQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNSSSHIPISSSFNTSVYQAIPQPTTPVSFTTGSMLGRPDTALTNTYTGLPPMPSFTMANNLPMQPSQTSSYSCMLPSSPSVNGRSFDTYTPPHMQAHMNSQTMATSGTASTGLISPGVSVPVQVPGTEPDMSQYWSRLQ
Protein: T. brucei spp.-specific protein (Q385X3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPQSLFGHSLFVLLTPRSATKKRQQRKQILCASQPRYRDVSFRTHAHTRRCDRTAHVQFPLVPPPPRPARVMNSLEHIPAPREPNGKNKELKRNGPTRTVGYLDPIKVITAPASPPGDHALLSPRSGGSEYAPNTFTGVWDTTPFTTATKHSHTEHRCDLRYPSCSPSRKMPHATATTTNGSERQDGGDAKARRQEPTHWTPAARPARHVSPSRTISTAPCEGPSRPTKSHCPCGLHRRGK
Protein: Ras-related protein Rab-6C (EC 3.6.5.2) (Rab6-like protein WTH3) (Q9H0N0)
Organism: Homo sapiens (Human)
Function: May be involved in the regulation of centrosome duplication and cell cycle progression.
Subcellular location: Nucleus {ECO:0000269|PubMed:16103095}. Cytoplasm {ECO:0000269|PubMed:16103095}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20064528}.
Interaction partners:
- Vacuolar protein sorting-associated protein 53 homolog
- Vam6/Vps39-like protein
Sequence:
MSAGGDFGNPLRKFKLVFLGEQSVAKTSLITRFRYDSFDNTYQAIIGIDFLSKTMYLEDGTIGLRLWDTAGQERLRSLIPRYIRDSAAAVVVYDITNVNSFQQTTKWIDDVRTERGSDVIITLVGNRTDLADKRQVSVEEGERKAKGLNVTFIETRAKAGYNVKQLFRRVAAALPGMESTQDGSREDMSDIKLEKPQEQTVSEGGCSCYSPMSSSTLPQKPPYSFIDCSVNIGLNLFPSLITFCNSSLLPVSWR
Protein: tRNA ligase (EC 6.5.1.3) (P09880)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: One of the two proteins required for the splicing of precursor tRNA molecules containing introns. The ligation activity requires three enzymatic activities: phosphorylation of the 5' terminus of the 3' half-tRNA in the presence of ATP, opening of the 2'3'-cyclic phosphodiester bond of the 5' half-tRNA leaving a 2'-phosphomonoester and ligation of the two tRNA halves in an ATP-dependent reaction.
Interaction partners:
- tRNA 2'-phosphotransferase
- tRNA-splicing endonuclease subunit SEN34
- tRNA-splicing endonuclease subunit SEN54
- tRNA-splicing endonuclease subunit SEN2
- Serine/threonine-protein kinase/endoribonuclease IRE1
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
- tRNA-splicing endonuclease subunit SEN15
- Transcriptional activator HAC1
- Endoplasmic reticulum chaperone BiP
- Exportin-T
Sequence:
MPSPYDGKRTVTQLVNELEKAEKLSGRGRAYRRVCDLSHSNKKVISWKFNEWDYGKNTITLPCNARGLFISDDTTNPVIVARGYDKFFNVGEVNFTKWNWIEENCTGPYDVTIKANGCIIFISGLEDGTLVVCSKHSTGPRADVDRNHAEAGEKQLLRQLAAMNINRSDFARMLYTHNVTAVAEYCDDSFEEHILEYPLEKAGLYLHGVNVNKAEFETWDMKDVSQMASKYGFRCVQCITSNTLEDLKKFLDNCSATGSFEGQEIEGFVIRCHLKSTEKPFFFKYKFEEPYLMYRQWREVTKDYISNKSRVFKFRKHKFITNKYLDFAIPILESSPKICENYLKGFGVIELRNKFLQSYGMSGLEILNHEKVAELELKNAIDYDKVDERTKFLIFPISVIGCGKTTTSQTLVNLFPDSWGHIQNDDITGKDKSQLMKKSLELLSKKEIKCVIVDRNNHQFRERKQLFEWLNELKEDYLVYDTNIKVIGVSFAPYDKLSEIRDITLQRVIKRGNNHQSIKWDELGEKKVVGIMNGFLKRYQPVNLDKSPDNMFDLMIELDFGQADSSLTNAKQILNEIHKAYPILVPEIPKDDEIETAFRRSLDYKPTVRKIVGKGNNNQQKTPKLIKPTYISAKIENYDEIIELVKRCIASDAELTEKFKHLLASGKVQKELHITLGHVMSSREKEAKKLWKSYCNRYTDQITEYNNNRIENAQGSGNNQNTQVKTTDKLNFRLEKLCWDEKIIAIVVELSKDKDGCIIDENNEKIKGLCCQNKIPHITLCKLESGVKAVYSNVLCEKVESAEVDENIKVVKLDNSKEFVGSVYLNF
Protein: Syntaxin pep12 (O94651)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in vesicle-mediated transport but not with protein transport from Golgi to vesicle.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Synaptobrevin homolog ykt6
- Vesicle transport v-SNARE protein vti1
- Vacuolar protein sorting-associated protein 33
- Synaptobrevin homolog 1
- t-SNARE affecting a late Golgi compartment protein 1
- Syntaxin-like protein fsv1
- Probable vacuolar protein sorting-associated protein 16 homolog
- Probable vesicular-fusion protein sec17 homolog
- Protein transport protein gos1
- Protein transport protein sec22
Sequence:
MSFVDLEQGRHKIEQNGDFPALASSIAQEIHALRGNTAAIHRYLVNNLTKNLHEVLEQSRELSQKVRSDLVRLANIKDTKYGEEASSFALSKLTRDFNTVLAELQRVQQKCAQQESDSVAAAQAALNQDVGQHFIEEEERNVSLSNNSSGQRQPLTESKISNSQLEYQQRLINERQGEIENLTQGINELNEIFRDLSTIINEQGELVTNIEYNVGNTSTNTKNASRQLQIANEHSRKARKRSFCFLVILVVILGVILTALIMG
Protein: Cytolysin RtxA (Repeats in toxin A) (A1YKW7)
Organism: Kingella kingae
Function: Bacterial cytolysin that attacks host cell membranes and causes cell rupture by forming a pore. Binds and permeabilizes target cells by forming cation-selective pores. Constitutes the key virulence cytotoxin of K.kingae. Binds cholesterol and oligosaccharides on the surface of host cells. Does not bind beta-2 integrin (ITGB2) on the host cell surface.
Subcellular location: Secreted {ECO:0000269|PubMed:21443941}. Host cell membrane {ECO:0000269|PubMed:25858109, ECO:0000269|PubMed:30405113, ECO:0000269|PubMed:33260488}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MNLATTKAKLKSGAQAGVQALNKAGHAAKTGTVAAGKATVAGAKSLYLTIPKDYDIEKGGSLNELIKAADELGIARLQEDANNIESAKKSIDTVEKLLSFTQTGVAVSAKKLDELLQKYSSSQLAKSLGSSANIDSKLTKTNHILSTLSSFLGTALAGMDLDSLVKQGDASATDLAKASLDLINELVNNISNSVQSIEAFSEQLGRLGAAISQTKGLSGLGNKLQNLPNFGKANLALEMISGLLSGISAGFTLADKNASTEKKVAAGFELSNQVIGNVTKAISSYVLAQRAAAGLSTTGAVASLITASIMLAISPLAFMNAADKFKNASLIDEFAKQFKKFGYDGDSLLAEYQRGAGTIEASLTAINTALGAVSAGVSAAAVGSVVGSPVALLVAGVTGLISGILEASKQAMFESVANRLQSKILAWEKENGGKNYFENGYDARHAHYLERNLKLLSELNKELQAERVIAITQQRWDANIGELAGITKLGDRISSGKAYADAFEDGKKLDGASNVTVDTRTGVVDISNANGKKTQALHFTSPLLTAGTETRERVQNGKYSYINQLKFNRVKSWTVKDGEANSRLDFSKVIQHVAFNDEDGRLSGKTEEIALNVNAGSGNDDIFAGQGKMNVDGGTGHDRVFYSKDGGLGQVNVDGTKATEAGSYTVNRSINNGSFYHEVIKRQTTQVGKRTETLEYRDFELKRPEHGYQTTDTLKSVEEIVGSQFSDTFKGSKFADIFHGGDGNDTLEGNDGDDRLFGGNGDDHLYGGNGDDLLDGGKGNDVINGGDGNDVYISRKGDGNDTLYDSHGSDKLAFADADLSELTIERTAQGIMIKRNDGSGSINMAEWYKTLSQQNYHGNATDDKIEQIIGKNGDYITSEQIDKLLKDKQTGTITSAQLQQLAQENKSKSIDSGNLASTLNKLIESMASFGSRGATASNYLQPAHKSPQNVLAPSAV
Protein: RAD50-interacting protein 1 (RAD50 interactor 1) (HsRINT-1) (RINT-1) (Q6NUQ1)
Organism: Homo sapiens (Human)
Function: Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER. May play a role in cell cycle checkpoint control. Essential for telomere length control.
Subcellular location: Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein.
Interaction partners:
- Vesicle transport protein SEC20
- Centromere/kinetochore protein zw10 homolog
- NBAS subunit of NRZ tethering complex
- Syntaxin-18
- Vesicle transport protein USE1
- Vesicle-trafficking protein SEC22b
- Ras-related protein Rab-18
- Sec1 family domain-containing protein 1
- Sec1 family domain-containing protein 2
- UPF0449 protein C19orf25
Sequence:
MLPAGEIGASPAAPCCSESGDERKNLEEKSDINVTVLIGSKQVSEGTDNGDLPSYVSAFIEKEVGNDLKSLKKLDKLIEQRTVSKMQLEEQVLTISSEIPKRIRSALKNAEESKQFLNQFLEQETHLFSAINSHLLTAQPWMDDLGTMISQIEEIERHLAYLKWISQIEELSDNIQQYLMTNNVPEAASTLVSMAELDIKLQESSCTHLLGFMRATVKFWHKILKDKLTSDFEEILAQLHWPFIAPPQSQTVGLSRPASAPEIYSYLETLFCQLLKLQTSDELLTEPKQLPEKYSLPASPSVILPIQVMLTPLQKRFRYHFRGNRQTNVLSKPEWYLAQVLMWIGNHTEFLDEKIQPILDKVGSLVNARLEFSRGLMMLVLEKLATDIPCLLYDDNLFCHLVDEVLLFERELHSVHGYPGTFASCMHILSEETCFQRWLTVERKFALQKMDSMLSSEAAWVSQYKDITDVDEMKVPDCAETFMTLLLVITDRYKNLPTASRKLQFLELQKDLVDDFRIRLTQVMKEETRASLGFRYCAILNAVNYISTVLADWADNVFFLQLQQAALEVFAENNTLSKLQLGQLASMESSVFDDMINLLERLKHDMLTRQVDHVFREVKDAAKLYKKERWLSLPSQSEQAVMSLSSSACPLLLTLRDHLLQLEQQLCFSLFKIFWQMLVEKLDVYIYQEIILANHFNEGGAAQLQFDMTRNLFPLFSHYCKRPENYFKHIKEACIVLNLNVGSALLLKDVLQSASGQLPATAALNEVGIYKLAQQDVEILLNLRTNWPNTGK
Protein: Low molecular weight protein-tyrosine-phosphatase Wzb (EC 3.1.3.48) (P0AAB2)
Organism: Escherichia coli (strain K12)
Function: Dephosphorylates Wzc. Required for the extracellular polysaccharide colanic acid synthesis, probably involved in the export of colanic acid from the cell to medium. Involved in protection of cells against contact-dependent growth inhibition (CDI), probably due to the loss of a physical impediment to cell-cell contact.
Interaction partners:
- Tyrosine-protein kinase wzc
- Putative polysaccharide export protein Wza
- Tyrosine-protein kinase etk
- Lipopolysaccharide biosynthesis protein WzxC
- Putative O-antigen transporter
- UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase
- Low molecular weight protein-tyrosine-phosphatase Etp
- Lipid III flippase
- Mannose-1-phosphate guanylyltransferase
- Probable ECA polymerase
Sequence:
MFNNILVVCVGNICRSPTAERLLQRYHPELKVESAGLGALVGKGADPTAISVAAEHQLSLEGHCARQISRRLCRNYDLILTMEKRHIERLCEMAPEMRGKVMLFGHWDNECEIPDPYRKSRETFAAVYTLLERSARQWAQALNAEQV
Protein: NLR family pyrin domain-containing protein 2B (Pyrin domain-containing protein 2-like protein POP4) (Pyrin-only protein 4) (P0DMW2)
Organism: Homo sapiens (Human)
Function: May function as a negative regulator of NF-kappa-B by preventing RELA/p65 phosphorylation at 'Ser-536', thereby inhibiting its transcriptional activity. Through NF-kappa-B regulation may control cytokine release upon Toll-like receptors activation and therefore play a role in modulation of innate immunity. May also play a role in cell cycle progression and apoptotic process.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24871464}. Nucleus {ECO:0000269|PubMed:24871464}. Note=Targeted to the nucleus upon TNF-alpha treatment. {ECO:0000269|PubMed:24871464}.
Interaction partners:
Sequence:
MVSSAQLDFNLQALLGQLSQDDLCKFKSLIRTVSLGNELQKIPQT
Protein: Imidazole glycerol phosphate synthase subunit HisH (EC 4.3.2.10) (IGP synthase glutaminase subunit) (EC 3.5.1.2) (IGP synthase subunit HisH) (ImGP synthase subunit HisH) (IGPS subunit HisH) (P61779)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00278}.
Interaction partners:
- Imidazole glycerol phosphate synthase subunit HisF
- 1-
- Imidazoleglycerol-phosphate dehydratase
- Histidinol-phosphate aminotransferase
- Phosphoribosyl-AMP cyclohydrolase
- Histidinol dehydrogenase
- ATP phosphoribosyltransferase
- Aminotransferase, putative
- Phosphoribosylaminoimidazolecarboxamide formyltransferase, putative
- Adenylosuccinate lyase
Sequence:
MLAILDYKAGNQTSVRRALDHLGIPCVITADPEVIQGAAGVIFPGVGAAGQAMNELVTTGLDEVLRRQVQAGRPLLGICVGCQIMLDYSQENDTKALGIIPGECRLFNPAWTDEDGAPIRVPHMGWNHIVQRRPCELLKGIEPEAEFYFVHSYYPAPPEEYVIATCTYGAEFCAIHGGPGLWAVQFHPEKSGRPGLRLLANFHRYCTEAADAQ