wanglab/gogpt-training-data huggingface dataset:
Protein: Homeobox protein Hox-B8 (Homeobox protein Hox-2.4) (Homeobox protein Hox-2D) (P17481)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-B5
- Pre-B-cell leukemia transcription factor 1
- Homeobox protein Hox-B9
- Homeobox protein Hox-B6
- Disks large-associated protein 3
- Homeobox protein Hox-B7
- Pre-B-cell leukemia transcription factor 3
- Homeobox protein Hox-B3
- Homeobox protein Meis1
Sequence:
MSSYFVNSLFSKYKTGESLRPNYYDCGFAQDLGGRPTVVYGPSSGGSFQHPSQIQEFYHGPSSLSTAPYQQNPCAVACHGDPGNFYGYDPLQRQSLFGAQDPDLVQYADCKLAAASGLGEEAEGSEQSPSPTQLFPWMRPQAAAGRRRGRQTYSRYQTLELEKEFLFNPYLTRKRRIEVSHALGLTERQVKIWFQNRRMKWKKENNKDKFPSSKCEQEELEKQKLERAPEAADEGDAQKGDKK
Protein: Protein enabled homolog (Q8N8S7)
Organism: Homo sapiens (Human)
Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation (By similarity).
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Synapse {ECO:0000250}. Cell junction, focal adhesion. Note=Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at filopodial tips with a number of other proteins including vinculin and zyxlin. Colocalizes with N-WASP at the leading edge. Colocalizes with GPHN and PFN at synapses (By similarity). {ECO:0000250}.
Interaction partners:
- Ena/VASP-like protein
- Vasodilator-stimulated phosphoprotein
- BAR/IMD domain-containing adapter protein 2
- Testin
- Tyrosine-protein kinase ABL1
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Zyxin
- Epithelial splicing regulatory protein 1
Sequence:
MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQETGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERLERERMERERLERERLERERLERERLEQEQLERERQERERQERLERQERLERQERLERQERLDRERQERQERERLERLERERQERERQEQLEREQLEWERERRISSAAAPASVETPLNSVLGDSSASEPGLQAASQPAETPSQQGIVLGPLAPPPPPPLPPGPAQASVALPPPPGPPPPPPLPSTGPPPPPPPPPLPNQVPPPPPPPPAPPLPASGFFLASMSEDNRPLTGLAAAIAGAKLRKVSRMEDTSFPSGGNAIGVNSASSKTDTGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDKGEDSEPVTSKASSTSTPEPTRKPWERTNTMNGSKSPVISRRDSPRKNQIVFDNRSYDSLHRPKSTPLSQPSANGVQTEGLDYDRLKQDILDEMRKELTKLKEELIDAIRQELSKSNTA
Protein: Claudin-16 (Paracellin-1) (PCLN-1) (Q9Y5I7)
Organism: Homo sapiens (Human)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:10390358, ECO:0000269|PubMed:14628289, ECO:0000269|PubMed:16234325, ECO:0000269|PubMed:16528408, ECO:0000269|PubMed:18188451, ECO:0000269|PubMed:28028216}. Cell membrane {ECO:0000269|PubMed:10390358, ECO:0000269|PubMed:14628289, ECO:0000269|PubMed:16234325, ECO:0000269|PubMed:16528408, ECO:0000269|PubMed:18188451, ECO:0000269|PubMed:28028216}; Multi-pass membrane protein {ECO:0000255}. Note=Cotrafficks with CLDN19 from ER to tight junctions. {ECO:0000269|PubMed:18188451}.
Interaction partners:
- Claudin-19
- Tight junction protein 1
- Sodium/potassium-transporting ATPase subunit gamma
- Solute carrier family 12 member 3
- Occludin
- Claudin-5
- Claudin-3
- Claudin-23
- Claudin-17
- Claudin-1
Sequence:
MRDLLQYIACFFAFFSAGFLIVATWTDCWMVNADDSLEVSTKCRGLWWECVTNAFDGIRTCDEYDSILAEHPLKLVVTRALMITADILAGFGFLTLLLGLDCVKFLPDEPYIKVRICFVAGATLLIAGTPGIIGSVWYAVDVYVERSTLVLHNIFLGIQYKFGWSCWLGMAGSLGCFLAGAVLTCCLYLFKDVGPERNYPYSLRKAYSAAGVSMAKSYSAPRTETAKMYAVDTRV
Protein: Chalcone synthase H1 (CHS_H1) (EC 2.3.1.74) (Naringenin-chalcone synthase CHS_H1) (Phloroisovalerophenone synthase) (3-methyl-1-(trihydroxyphenyl)butan-1-one synthase) (Valerophenone synthase) (EC 2.3.1.156) (Q9FEY5)
Organism: Humulus lupulus (European hop)
Function: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Chalcone synthase that can use 4-coumaroyl-CoA to produce 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can, under specific conditions, spontaneously isomerize into naringenin. Also able to produce phlorisovalerophenone (PIVP) from 3-methylbutanoyl-CoA (isovaleryl-CoA).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29760092}.
Interaction partners:
Sequence:
MVTVEEVRKAQRAEGPATILAIGTATPANCILQSEYPDYYFRITNSEHKTELKEKFKRMCGKSMIRKRYMHLTEEILKENPNLCAYEAPSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSEITHVVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRVAKDLAENNKGARVLVVCSEITAVTFRGPNDTHLDSLVAQALFGDGSAALIIGADPIPEIEKPIFELVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFKPLGISDWNSLFWITHPGGPAILDQVESKLGLKPEKLRATRHVLGEYGNMSSACVLFILDEMRRKCAEDGVKTTGEGLEWGVLFGFGPGLTVETVVLHSVGI
Protein: Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) (W5UKU7)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
Sequence:
MSPNHSRSWKQERKMSTNLLMPFAEKMSTLPLSRSEVFGQLRKELYEDKEFHHTDVHIFIILGASGDLAKKKIYPTLWWLFRDGLLPEQTFFVGFARSDLTMDAIRKACLPHMKVADTEADRLSTFFSRNSYISGKYDDEAAFSKLHSHLLSLPRGAEANRLFYLALPPSIYHDVTKNIQHQCLSTKGWNRVIVEKPFGRDLQSSEELSNHLSSLFTEDQIYRIDHYLGKEMVQNLMVLRFGNRIFGPIWNRDSVACVVLTFKEPFGTQGRGGYFDDFGIIRDVMQNHLLQMLSLIAMEKPASTSSDDVRDEKVKVLKCIAPVSLSDVVLGQYVGDPEGEGDAKLGYLDDPTVPKGSTQATFATAVLYVRNERWDGVPFILRCGKALNERKAEVRLQFTDVPGDIFNSQCRRNELVVRVQPNEAIYAKMMSKKPGVYFSPEETELDLTYRSRYKDVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHHIEKEKVVPLKYKYGSRGPREADELSQKVGFRYEGTYKWINPHRL
Protein: Small ribosomal subunit protein uS19 (30S ribosomal protein S19) (P9WH45)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Interaction partners:
- Large ribosomal subunit protein bL34
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein bS18A
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein uL23
Sequence:
MPRSLKKGPFVDEHLLKKVDVQNEKNTKQVIKTWSRRSTIIPDFIGHTFAVHDGRKHVPVFVTESMVGHKLGEFAPTRTFKGHIKDDRKSKRR
Protein: Subtilisin-like protease SBT3.14 (EC 3.4.21.-) (Subtilase subfamily 3 member 14) (AtSBT3.14) (Q9SVT4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
Interaction partners:
- Uncharacterized protein
- Cysteine protease-like protein
- Proline-rich receptor-like protein kinase PERK7
- Putative proline-rich receptor-like protein kinase PERK6
- Putative proline-rich receptor-like protein kinase PERK11
- Cyclase-like protein 3
Sequence:
MENCLSTLVFLLSIALVLFPKTGVSFLAAEGASDSDSKVYIVYLGEREHDDPELFTASHHQMLESLLQSKDDAHNSLIYSYQYGFSGFAALLTSSQAKKISEHPEVIHVIPNRILKLKTTRTWDHLGLSPNPTSFSSSSSAKGLLHETNMGSEAIIGVVDTGIWPESKVFNDHGLGPIPQRWRGKCESGEQFNAKIHCNNKLIGAKYYLSGLLAETGGKFNRTIIQDFKSNRDAIGHGTHTATIAGGSFVPNVSFYGLARGTVRGGAPRARIASYKVCWNVVGYDGICTVADMWKAFDDAIHDQVDVLSVSIGAGIPENSEVDSVDFIAAFHAVAKGITVVAAGGNDGPGAQNITNAAPWLLTVAATTLDRSFPTKITLGNNQTLFAESLFTGPEISTSLAFLDSDHNVDVKGKTILEFDSTHPSSIAGRGVVAVILAKKPDDLLARYNSIPYIFTDYEIGTHILQYIRTTRSPTVRISAATTLNGQPAMTKVAEFSSRGPNSVSPAILKPDIAAPGVSILAAVSPLDPDAFNGFGLYSGTSMSTPVVSGIIALLKSLHPNWSPAAMRSALVTTAWRTSPSGEPIFAQGSNKKLADPFDYGGGLVNPDKAAQPGLVYDMGIKDYINYMCSAGYIDSSISRVLGKKTKCTIPKPSILDINLPSITIPNLEKEVTLTRTVTNVGPIKSVYKAVIESPLGITLTVNPTTLVFNSAAKRVLTFSVKAKTSHKVNSGYFFGSLTWTDGVHDVIIPVSVKTTISM
Protein: Protein WRKY1 (WRKY DNA-binding protein 1) (Q32SG4)
Organism: Zea mays (Maize)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- BTB/POZ domain-containing protein POB1
Sequence:
MEGMEEANRTAVESCHRVLALLSNPHGQLVPSKELVAATGEAVAKFGSLTAKLSNSNGDGLLQGHARVRKVKKPLHIFDSNLFLESSAVAAAAAPAKTPSPSPILGLQLFPRYHQFEGSSSKDPVRIPTQFPKRLLLEKPTAGMEGSTSQSPPIVQMVQPVSVAPPAGTPTPALPPAHLHFIQQQQSYQRFQLMQQMKIQSEMMKRSNLGDQGGSLSGGGGGGRKGVNLKFDSSNCTASSSRSFLSSLSMEGSLASLDGSRTSRPFQLLSGSQTASTPELGLVQRRRCAGREDGTGRCATGSRCHCSKKRKLRIRRSIKVPAISNKVADIPADEFSWRKYGQKPIKGSPHPRGYYKCSSVRGCPARKHVERCVDDPSMLIVTYEGDHNHNRVLAQPA
Protein: Molybdopterin synthase catalytic subunit 1 (EC 2.8.1.12) (MPT synthase subunit 2 1) (Molybdenum cofactor biosynthesis protein E 1) (Molybdopterin-converting factor large subunit 1) (Molybdopterin-converting factor subunit 2 1) (P9WJR3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Interaction partners:
- Molybdopterin synthase sulfur carrier subunit
- Molybdopterin synthase sulfur carrier subunit
- Cyclic pyranopterin monophosphate synthase 1
- Cyclic pyranopterin monophosphate synthase 3
- Probable adenylyltransferase/sulfurtransferase MoeZ
- Sulfur carrier protein CysO
- Cyclic pyranopterin monophosphate synthase 2
- Molybdopterin synthase catalytic subunit 1
- GTP 3',8-cyclase 1
- Methyltransferase domain-containing protein
Sequence:
MANVVAEGAYPYCRLTDQPLSVDEVLAAVSGPEQGGIVIFVGNVRDHNAGHDVTRLFYEAYPPMVIRTLMSIIGRCEDKAEGVRVAVAHRTGELQIGDAAVVIGASAPHRAEAFDAARMCIELLKQEVPIWKKEFSSTGAEWVGDRP
Protein: Claudin-6 (Skullin) (P56747)
Organism: Homo sapiens (Human)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space.
Subcellular location: Cell junction, tight junction {ECO:0000250|UniProtKB:Q9Z262}. Cell membrane {ECO:0000269|PubMed:20375010}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Tight junction protein 1
- Occludin
- Claudin-9
- Tight junction protein ZO-3
- Claudin-14
- Claudin-1
- Claudin-12
- Claudin-16
- Claudin-34
- Tight junction protein 2
Sequence:
MASAGMQILGVVLTLLGWVNGLVSCALPMWKVTAFIGNSIVVAQVVWEGLWMSCVVQSTGQMQCKVYDSLLALPQDLQAARALCVIALLVALFGLLVYLAGAKCTTCVEEKDSKARLVLTSGIVFVISGVLTLIPVCWTAHAIIRDFYNPLVAEAQKRELGASLYLGWAASGLLLLGGGLLCCTCPSGGSQGPSHYMARYSTSAPAISRGPSEYPTKNYV
Protein: Protein X (HBx) (Peptide X) (pX) (Q17UT5)
Organism: Hepatitis B virus subtype adw2
Subcellular location: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04074}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04074}. Host mitochondrion {ECO:0000256|HAMAP-Rule:MF_04074}. Note=Mainly cytoplasmic as only a fraction is detected in the nucleus. In cytoplasm, a minor fraction associates with mitochondria or proteasomes. {ECO:0000256|HAMAP-Rule:MF_04074}.
Interaction partners:
Sequence:
MAARLYCQLDPSRDVLCLRPVGAESRGRPLSGPLGTLSSPSPSAVPADHGAHLSLRGLPVCAFSSAGPCALRFTSARCMETTVNAHQILPKVLHKRTLGLPAMSTTDLEAYFKDCVFKDWEELGEEIRLKVFVLGGCRHKLVCAPAPCNFFTSA
Protein: Ubiquitin-like protein ISG15 (Interferon-induced 15 kDa protein) (Interferon-induced 17 kDa protein) (IP17) (Ubiquitin cross-reactive protein) (Q64339)
Organism: Mus musculus (Mouse)
Function: Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Its target proteins include SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, TRIM25, STAT5A, MAPK1/ERK2 and globin. Isgylation of the viral sensor IFIH1/MDA5 promotes IFIH1/MDA5 oligomerization and triggers activation of innate immunity against a range of viruses, including coronaviruses, flaviviruses and picornaviruses. Can also isgylate: RIGI which inhibits its function in antiviral signaling response, IRF3 which inhibits its ubiquitination and degradation as well as EIF4E2 which enhances its cap structure-binding activity and translation-inhibition activity. Exhibits antiviral activity towards both DNA and RNA viruses, including influenza A and B virus, sindbis virus (SV) and herpes simplex type-1 (HHV-1). Plays a significant role in the control of neonatal Chikungunya virus (CHIKV) infection by acting as a putative immunomodulator of pro-inflammatory cytokines. Protects mice against the consequences of Chikungunya virus infection by down-regulating the pathogenic cytokine response, often denoted as the cytokine storm. Plays a role in erythroid differentiation. The secreted form of ISG15 can: induce natural killer cell proliferation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity. The secreted form acts through the integrin ITGAL/ITGB2 receptor to initiate activation of SRC family tyrosine kinases including LYN, HCK and FGR which leads to secretion of IFNG and IL10; the interaction is mediated by ITGAL (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P05161}. Secreted {ECO:0000250|UniProtKB:P05161}. Note=Exists in three distinct states: free within the cell, released into the extracellular space, or conjugated to target proteins. {ECO:0000250|UniProtKB:P05161}.
Interaction partners:
- Ubl carboxyl-terminal hydrolase 18
- Antiviral innate immune response receptor RIG-I
- Ubiquitin-like modifier-activating enzyme 7
- Interferon regulatory factor 3
- Interferon-induced, double-stranded RNA-activated protein kinase
- Ubiquitin/ISG15-conjugating enzyme E2 L6
- Interferon regulatory factor 9
- Antiviral innate immune response effector IFIT1
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Signal transducer and activator of transcription 1
Sequence:
MAWDLKVKMLGGNDFLVSVTNSMTVSELKKQIAQKIGVPAFQQRLAHQTAVLQDGLTLSSLGLGPSSTVMLVVQNCSEPLSILVRNERGHSNIYEVFLTQTVDTLKKKVSQREQVHEDQFWLSFEGRPMEDKELLGEYGLKPQCTVIKHLRLRGGGGDQCA
Protein: Zinc finger protein 251 (Q3USU9)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADKSCSPTPGETPLTFQDVAVYFSRAEGQQLSPQERALYRDVMLENYGNVASLGFPGPKPELISQLEQEEELWVLDLLGAEEPEVLRRCQTDSEIEAEKELSILNQKCFEEVKTPEFISPKFPRAYSQASEPQEACAHEGQGDGSHGSSATQGLKSIAKKDAAVCREQFPKNAQTSVFDKHLNPSQSVVTVQRNKAGQRIFKCDICNKTFKYNSDLSRHRRSHTGEKPYECGPCGRAFTHSSNLILHQRIHTGNKPFKCEECGKTFGLNSYLRLHQRIHTGEKPFGCKECGKAFSRSSSLIQHRIIHTGEKPYKCDECGKAFSQSPQLTQHQRIHTGEKPHGCTWCGKAFSRNASLIQHQRIHTGEKPHKCAQCGKAFSQSSSLFLHHRVHTGEKPYVCGECGRAFGFNSHLTEHVRIHTGEKPYVCGECGKAFSRSSTLMQHRRVHTGEKPYQCAECGKAFIQSSQLTLHQRVHTGEKPYECGLCGKAFSRRSALTQHQRVHMGENPQEFECGPDFVYDSSHLSAGERHGRAFSHSAKLVLQWTIRSDEKSRGCHECGKTYSTSSQSMDYQKSQAGEKPYKCQECGGKAGSGVSPLTPHHVTRVGEKPQLKDGSKRYLIQIKKIFQERDF
Protein: CCAAT-box-binding transcription factor (TGGCA-binding protein) (Q9QY87)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
LLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLGEKAEVKQKWASRLLAKLRKDIRPECREDFVLAVTGKKAPGCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKAAASAHPVLC
Protein: Transcription factor E2F4 (E2F-4) (Q8R0K9)
Organism: Mus musculus (Mouse)
Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F4 binds with high affinity to RBL1 and RBL2. In some instances can also bind RB1. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q16254}.
Interaction partners:
- Retinoblastoma-like protein 2
- Transcription factor Dp-2
- Transcription factor Dp-1
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 4
- Retinoblastoma-like protein 1
- Retinoblastoma-associated protein
- Transcription factor E2F5
- Histone deacetylase 1
- Protein lin-9 homolog
Sequence:
MAEAGPQAPPPPGTPSRHEKSLGLLTTKFVSLLQEAKDGVLDLKLAADTLAVRQKRRIYDITNVLEGIGLIEKKSKNSIQWKGVGPGCNTREIADKLIELKAEIEELQQREQELDQHKVWVQQSIRNVTEDVQNSCLAYVTHEDICRCFAGDTLLAIRAPSGTSLEVPIPEGLNGQKKYQIHLKSMSGPIEVLLVNKEAWSSPPVAVPVPPPDDLLQSPPAVSTPPPLPKPALAQPQESSPPSSPQLTTPTPVLGSTQVSEVACQTSEIAVSGSPGTENKDSGEVSSLPLGLTALDTRPLQSSALLDSSSSSSSSSSSSSSSSSGPNPSTSFEPIKADPTGVLDLPKELSEIFDPTRECMSSELLEELMSSEVFAPLLRLSPPPGDHDYIYNLDESEGVCDLFDVPVLKL
Protein: phosphopyruvate hydratase (EC 4.2.1.11) (Q9NDH8)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MTIQKVHGREVLDSRGNPTVEVEVTTERGVFRSAVPSGASTGVYEACELRDGDKKRYVGKGCLQAVKNVNEVIGPALIGRDELKQEELDTLMLRLDGTPNKGKLGANAILGCSMAISKAAAAAKGVPLYRYLASLAGTKELRLPVPCFNVINGGKHAGNALPFQEFMIAPVKATSFSEALRMGSEVYHSLRGIIKKKYGQDAVNVGDEGGFAPPIKDINEPLPILMEAIEEAGHRGKFAICMDCAASETYDEKKQQYNLTFKSPEPTWVTAEQLRETYCKWAHDYPIVSIEDPYDQDDFAGFAGITEALKGKTQIVGDDLTVTNTERIKMAIEKKACNSLLLKINQIGTISEAIASSKLCMENGWSVMVSHRSGETEDTYIADLVVALGSGQIKTGAPCRGERTAKLNQLLRIEEELGAHAKFGFPGWS
Protein: Beta-toxin Ct6 (P0DUH8)
Organism: Centruroides tecomanus (Scorpion) (Centruroides limpidus tecomanus)
Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
Subcellular location: Secreted {ECO:0000269|PubMed:23840487}.
Interaction partners:
Sequence:
MKTFVLALCLVLIGMVYAKDGYLVSKHTGCKLGCSPKIGDRYCHIECTSMNHKGDEGYCYWLACYCKGMPENAEVYPLPNKSCGK
Protein: Mushroom-body expressed, isoform K (M9NEH9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Pre-mRNA-processing-splicing factor 8
- Zinc finger protein 830
Sequence:
MEDNNTSSSAGGASIKHEDPSVTLTIRLIMQGKEVGSIIGKKGEIVNRFREESGAKINISDGSCPERIVTVSGTTNAIFSAFTLITKKFEEWCSQFNDVGKVGKTQIPIRLIVPASQCGSLIGKSGSKIKEIRQTTGCSIQVASEMLPNSTERAVTLSGSAEQITQCIYQICLVMLESPPRGATIPYRPKPQVTGPVILANGQAFTIQGNYAVPTQETCPVFPLALATGGLHAGISGLADPLLKGAHLQGAIPAHHHHLQQMPDVAKNPLASLAALGLAGMNPASTGGINHTANPANRAQQQQHEMTVSNDLIGCIIGKGGTKIAEIRQISGAMIRISNCEEREGGNTDRTITISGNPDSVALAQYLINMSVELQKANLLEQAQSQQNGGAAAAPGAAAAGVAAVTGAAAPTSATNGAITTVTLTSGTGVVGAGAAGAAGVANGANPAANGGGSNGTISATGYASANGGQATNGSVGVNPAAAAALSSPLASALQLLTKPGALSALSNLSALDLLNLTTLGNTNGAGANPGGPPVQTTGVNRAKGHYATSRFRQHQTETGGEAEKPRNKFNPY
Protein: Protein Wnt-5a (Q9QXQ7)
Organism: Rattus norvegicus (Rat)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. In the presence of FZD4, activates beta-catenin signaling. In the presence of ROR2, inhibits the canonical Wnt pathway by promoting beta-catenin degradation through a GSK3-independent pathway which involves down-regulation of beta-catenin-induced reporter gene expression (By similarity). Suppression of the canonical pathway allows chondrogenesis to occur and inhibits tumor formation. Stimulates cell migration. Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor. Mediates motility of melanoma cells (By similarity). Required during embryogenesis for extension of the primary anterior-posterior axis and for outgrowth of limbs and the genital tubercle. Inhibits type II collagen expression in chondrocytes (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P41221}. Secreted {ECO:0000250|UniProtKB:P41221}.
Interaction partners:
- Frizzled-5
- Receptor-like tyrosine kinase.
- Frizzled-4
- Frizzled-2
- Frizzled-3
- Receptor tyrosine kinase-like orphan receptor 2
- Frizzled-6
- Frizzled-1
- Frizzled-9
- Frizzled class receptor 7
Sequence:
MKKPIGILSPGVALGTAGGAMSSKFFLMALATFFSFAQVVIEANSWWSLGMNNPVQMSEVHIIGAQPLCSQLAGLSQGQKKLCHLYQDHMQYIGEGAKTGIKECQYQFRHRRWNCSTVDNTSVFGRVMQIGSRETAFTYAVSAAGVVNAMSRACREGELSTCGCSRAARPKDLPRDWLWGGCGDNIDYGYRFAKEFVDARERERIHAKGSYESARILMNLHNNEAGRRTVYNLADVACKCHGVSGSCSLKTCWLQLADFRKVGDALKEKYDSAAAMRLNSRGKLVQVNSRFNSPTTQDLVYIDPSPDYCVRNESTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFKTVQTERCHCKFHWCCYVKCKKCTEIVDQFVCK
Protein: Methyl-coenzyme M reductase I subunit beta (MCR I beta) (EC 2.8.4.1) (Coenzyme-B sulfoethylthiotransferase beta) (P11560)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis. Neither N-6-mercaptohexanoylthreonine phosphate (H-S-HxoTP) nor N-8-mercaptooctanoylthreonine phosphate (H-SOcoTP) nor any other thiol compound such as CoA or CoM can substitute for CoB as the electron donor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23533332}. Note=Under growth limiting conditions on nickel-depleted media, a fraction of 70% of the enzyme is localized close to the cytoplasmic membrane, which implies 'facultative' membrane association of the enzyme. {ECO:0000269|PubMed:23533332}.
Interaction partners:
- Methyl-coenzyme M reductase I operon protein D
- Methyl-coenzyme M reductase I subunit alpha
- Methyl-coenzyme M reductase I subunit gamma
- Methyl-coenzyme M reductase II subunit alpha
- Methyl-coenzyme M reductase I operon protein C
- Methyl-coenzyme M reductase II subunit gamma
- CCG domain-containing protein
- Methyl-coenzyme M reductase II, subunit delta
- Tetrahydromethanopterin S-methyltransferase subunit E
- Tetrahydromethanopterin S-methyltransferase subunit G
Sequence:
MAKFEDKVDLYDDRGNLVEEQVPLEALSPLRNPAIKSIVQGIKRTVAVNLEGIENALKTAKVGGPACKIMGRELDLDIVGNAESIAAAAKEMIQVTEDDDTNVELLGGGKRALVQVPSARFDVAAEYSAAPLVTATAFVQAIINEFDVSMYDANMVKAAVLGRYPQSVEYMGANIATMLDIPQKLEGPGYALRNIMVNHVVAATLKNTLQAAALSTILEQTAMFEMGDAVGAFERMHLLGLAYQGMNADNLVFDLVKANGKEGTVGSVIADLVERALEDGVIKVEKELTDYKVYGTDDLAMWNAYAAAGLMAATMVNQGAARAAQGVSSTLLYYNDLIEFETGLPSVDFGKVEGTAVGFSFFSHSIYGGGGPGIFNGNHIVTRHSKGFAIPCVAAAMALDAGTQMFSPEATSGLIKEVFSQVDEFREPLKYVVEAAAEIKNEI
Protein: 60S ribosomal protein L4 (Q582N2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L29
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S26
- 40S ribosomal protein S16, putative
- 40S ribosomal protein S8
- Polyubiquitin, putative
- 40S ribosomal protein S18, putative
- 60S ribosomal protein L5, putative
- Large ribosomal subunit protein eL18
- 60S ribosomal protein L39, putative
Sequence:
MTARPSVSVYSASEDKVVGTCSLPAVFTAPIRHDVVQFVHTNMAKNSRQPYAVNRLSGMKHSAESWGTGRAVARIPRIHGGGTSMSGAGAFGNMCRGGRMFAPTKIFRRWHRKINLHQKRFAVVSALAASSLPALVMSRGHKIENVAEVPLVVEDGVRAYEKTKEAMTFLKTVGAIDDVNRVNDSRQIRAGRGKMRNRRYVARRGPMLVMPDNKGTRAFRNIFGLDLANVNSLNLLHLAPGGHVGRFIIWTKSAFEKLDKIFGTFTEPSTVKSGFMLPAPMLTSTDVTRIMQSEEVRRVLKPKKLQPKRPSRYRQPTNGIRNRRLRLRLNPFQKKEKAMAKGMQNKKNREARHAAKVVRLAKARKNVAKALKKK