wanglab/gogpt-training-data huggingface dataset:
Protein: Melatonin receptor type 1A (Mel-1A-R) (Mel1a receptor) (CKA) (P49285)
Organism: Gallus gallus (Chicken)
Function: High affinity receptor for melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibits adenylate cyclase activity (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Melatonin receptor type 1C
- Melatonin receptor type 1B
- Serotonin N-acetyltransferase
- Period circadian clock 3
- Vacuolar ATPase assembly integral membrane protein VMA21
Sequence:
MRANGSELNGTVLPRDPPAEGSPRRPPWVTSTLATILIFTIVVDLLGNLLVILSVYRNKKLRNAGNIFVVSLAIADLVVAIYPYPLVLTSVFHNGWNLGYLHCQISGFLMGLSVIGSIFNITGIAINRYCYICHSLKYDKLYSDKNSLCYVGLIWVLTVVAIVPNLFVGSLQYDPRIYSCTFAQSVSSAYTIAVVFFHFILPIAIVTYCYLRIWILVIQVRRRVKPDNNPRLKPHDFRNFVTMFVVFVLFAVCWAPLNFIGLAVAVDPETIIPRIPEWLFVSSYYMAYFNSCLNAIIYGLLNQNFRREYKKIVVSFCTAKAFFQDSSNDAADRIRSKPSPLITNNNQVKVDSV
Protein: Protein leg1b (Leg1-B) (Liver-enriched gene protein 1-B) (Q4QRF7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in early development of liver, exocrine pancreas and intestine, probably through cell cycle regulation. In liver, its function is partially redundant with leg1a function.
Subcellular location: Secreted {ECO:0000269|PubMed:21857963}.
Interaction partners:
- Microtubule cross-linking factor 3
Sequence:
MSEMGFLRSVAAVLLLAVFSHAAVVTENGLPIQWRKAPSDLSHLPISNTGVQVNPWVYSQRMTMLKMVINATNAYMSSMGPGEQENPLWSLPLQLGWKLKSGRLADPTPDSSSTCGSEASDPVCISPLSFFGCVNYYLSVLPFLAAVETGVVSSGGHQMLIQVPAEVAQDYCSSYSDCSTKHPNTMAKWHLFFQSLRQVSQSKESDFNKKDSILGLMWAAEEESIQTASGACTERQKLYSSPEVSFQQSSVNLGAFISAAHYHASIERSGKFMSHLPSRVLQEADSPPNIADLSTEENHALYMLSWMNSINQLLGGSLVDLWRKAMCSAQAREKGQAFLDDLILDPKFPGSSLWSIICVMSTSC
Protein: Imidazole glycerol phosphate synthase subunit HisF (EC 4.3.2.10) (IGP synthase cyclase subunit) (IGP synthase subunit HisF) (ImGP synthase subunit HisF) (IGPS subunit HisF) (P60664)
Organism: Escherichia coli (strain K12)
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Subcellular location: Cytoplasm.
Interaction partners:
- Histidine biosynthesis bifunctional protein HisB
- ATP phosphoribosyltransferase
- Histidine biosynthesis bifunctional protein HisIE
- 1-
- Imidazole glycerol phosphate synthase subunit HisH
- Histidinol dehydrogenase
- Histidinol-phosphate aminotransferase
- Tryptophan biosynthesis protein TrpCF
- Bifunctional purine biosynthesis protein PurH
- Adenine phosphoribosyltransferase
Sequence:
MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGGIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAETGKYHVNQYTGDESRTRVTQWETLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQIINIGELKAYLATQGVEIRIC
Protein: Sporulation inhibitor sda (Histidine kinase KinA inhibitor) (Q7WY62)
Organism: Bacillus subtilis (strain 168)
Function: Mediates a developmental checkpoint inhibiting initiation of sporulation (by preventing phosphorylation of spo0A) in response to defects in the replication initiation machinery. Inhibits autophosphorylation of the histidine protein kinase KinA, forming a molecular barricade that prevents productive interaction between the ATP-binding site in the catalytic domain and the phosphorylatable His in the phosphotransfer domain of KinA. Probably also inhibits the activity of KinB, but has relatively little effect on KinC. Has at least one target in vivo in addition to KinA as sda does not require KinA to inhibit sporulation.
Interaction partners:
- Probable phosphatase YqeG
- Uncharacterized protein YwcI
- Chromosomal replication initiator protein DnaA
- Stage 0 sporulation protein A
- Sporulation kinase B
- Uncharacterized protein YycS
Sequence:
MNWVPSMRKLSDELLIESYFKATEMNLNRDFIELIENEIKRRSLGHIISVSS
Protein: ERCC excision repair 8, CSA ubiquitin ligase complex subunit (G3V7B8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- DNA damage-binding protein 1
- DNA excision repair protein ERCC-6
- Cullin-4A
- UV-stimulated scaffold protein A
- E3 ubiquitin-protein ligase RBX1
- DNA damage-binding protein 2
- Cullin-4B
- DNA-directed RNA polymerase II subunit RPB7
- DNA repair endonuclease XPF
- COP1, E3 ubiquitin ligase
Sequence:
MFTSSSFDKTLKVWDTNTLQAADVFNFEETVYSHHMSPAATKHCLVAVGTRGPKVQLCDLKSGSCSHILQGHRQEILAVSWSPRYDYILATASADSRVKLWDVRRASGCLLTLDQHNGKKSQAVESANTAHNGKVNGLCFTSDGLHLLTVGTDNRMRLWNSSSGDNTLMRRMGFRS
Protein: AQP9 protein (Aquaporin 9, isoform CRA_a) (cDNA, FLJ93715, Homo sapiens aquaporin 9 (AQP9), mRNA) (Q6FGT0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MQPEGAEKGKSFKQRLVLKSSLAKETLSEFLGTFILIVLGCGCVAQAILSRGRFGGVITINVGFSMAVAMAIYVAGGVSGGHINPAVSLAMCLFGRMKWFKLPFYVGAQFLGAFVGAATVFGIYYDGLMSFAGGKLLIVGENATAHIFATYPAPYLSLANAFADQVVATMILLIIVFAIFDSRNLGAPRGLEPIAIGLLIIVIASSLGLNSGCAMNPARDLSPRLFTALAGWGFEVFRAGNNFWWIPVVGPLVGAVIGGLIYVLVIEIHHPEPDSVFKAEQSEDKPEKYELSVIM
Protein: Peroxisomal ATPase PEX1 (EC 3.6.4.-) (Peroxin-1) (Peroxisome biogenesis factor 1) (Q5BL07)
Organism: Mus musculus (Mouse)
Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O43933}. Peroxisome membrane {ECO:0000250|UniProtKB:O43933}. Note=Associated with peroxisomal membranes; anchored by PEX26 to peroxisome membranes. {ECO:0000250|UniProtKB:O43933}.
Interaction partners:
- Peroxisomal ATPase PEX6
- Peroxisome assembly protein 26
- Peroxisomal membrane protein PEX13
- Peroxisomal targeting signal 1 receptor
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis factor 10
- UBX domain-containing protein 7
- Peroxisomal targeting signal 2 receptor
- PEX5-related protein
Sequence:
MWSSDRLAGAGSGGAVVTVAFTNARDCFLHLPRRLVAQLHLLQNQAIEVASDHQPTYLSWVEGRHFNDQSENVAEINRQVGQKLGLSSGDQVFLRPCSHVVSCQQVEVEPLSADDWEILELHAISLEQHLLDQIRIVFPKAVVPIWVDQQTYIFIQIVTLMPAAPYGRLETNTKLLIQPKTRQAKESTFPKEGDAHGQVHSYGREQKGLSKELQTRQLHTNSEGITASNGRDPKVPGGPLKPSWWAVLGSMLSFGPDSKQESAWGSLELGAFKNMQSQAAPLEGTFRVCQVQPPSARTTTATSVFHKHCTAHVFPWDQEYFDVEPSFTVTYGKLVKLHSPKQQQDKSKQGVLLPDKEKQLSKSPDHKQISSNRSEEAAEACVLKVVWNGLEELKNATEFTESLELLHRGKVWIPDDLRKRLNIEMHAVVRITPLETTPKIPRSLKLQPRENLPKDVNEETIKTVFSSWVQQSATTMLPLVISKEERIKLEIKDGLREFSLSTVHSQEKEKEEGKTVFVLSSILLQKISVQVLLEPMIKEEQSAEIDFLLPSLTLSSLGGVSALGASAMEHITHSLLGRPLSRQLMALVAGLRNGALLITGGKGSGKSTFAKAICKEAQDTLDARVETVDCKALRGKRLESIQKALEVAFSEAAWRQPSVILLDDLDLIAGLPSVPEQEHSPEAVQSQRLAHALNDMIKEFVSTGSLVALIATSQLQQSLHPSLVSAQGIHTFQCVQHLQPPNPEQRCEILHSVVKNKLGCDISNFPDLDLQCIAKDTEAFVARDFTVLVDRAIHSSLSRQHSSSREDLTLTTSDFQKALRGFLPASLRNVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVVARESGMNFISIKGPELLSKYIGASEQAVRDVFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILTVLSKSLALADDVDLQHVASVTDSFTGADLKALLYNAQLEALQGRLLPSGLPDGGSSSDSDLSLSSMVFLNHSSGSDDSAGDGECGLEQSLLSLEMSEILPDESKFNMYRLYFGSSYESELGNGTPSDLSSHCLSAPSSVTQDLPAAPGKDPLFTQHPVFRTPSQEGCQDLTQEQRDQLRAEISIIKGRYRSQSGEDESLNQPGPIKTTFAISQAHLMTALAHTRPSISEDEGKEFAELYENFQNPKKRKNQSGTVFRTGQKVTLA
Protein: Homeodomain-only protein (Homeobox-only protein) (Odd homeobox protein 1) (mOB1) (Q8R1H0)
Organism: Mus musculus (Mouse)
Function: Atypical homeodomain protein which does not bind DNA and is required to modulate cardiac growth and development. Acts via its interaction with SRF, thereby modulating the expression of SRF-dependent cardiac-specific genes and cardiac development. Prevents SRF-dependent transcription either by inhibiting SRF binding to DNA or by recruiting histone deacetylase (HDAC) proteins that prevent transcription by SRF. Overexpression causes cardiac hypertrophy. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and assists in chaperone-mediated protein refolding (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12297045}. Cytoplasm {ECO:0000269|PubMed:14516659}. Note=According to PubMed:14516659 it is cytoplasmic. {ECO:0000269|PubMed:14516659}.
Interaction partners:
- Histone deacetylase 2
- Leucine-rich repeats and immunoglobulin-like domains protein 1
- Surfactant protein C
- Leucine-rich repeat-containing G-protein coupled receptor 5
- Homeobox protein Nkx-2.1
- 26S proteasome complex subunit SEM1
Sequence:
MSAQTASGPTEDQVEILEYNFNKVNKHPDPTTLCLIAAEAGLTEEQTQKWFKQRLAEWRRSEGLPSECRSVTD
Protein: LD44506p (TBC1 domain family member 22) (Q95RC5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein bS6m
Sequence:
MMDNNVEQLAGKSQTETAESTAAATGTAGAGVAVVTVASGAGPTPGANSSTFWKNSGRRVPGRPSPKRELEKAAAVGVAVGRGAAPGSGMVSTFTEYQKSVSDAWDMGDDEFCIISSTEAAAAAVGAGDAAHFSRQVSQTVALNVIETHSRSNQNHNASRSANESGADLVPVSSSSTDDCKEDRRSLPDSNENRSRLRNYPGRPQLQKISSNCQDSEYETKIEKFQVVLDSPQLDLVALKKISWSGVPRKMRAVSWRLLSKYLPPSSERRMAVLESKRQGYQDLRHNYFRVDSQDETQQDTYRQIHIDVPRMNPQIPLFQQQLVQEMFERILFIWAIRHPASGYVQGINDLVTPFFIVFLQEALTPNTDLEKYDMSTLPEETRNIIEADSFWCLSKFLDCIQDNYIFAQLGIQEKVNQLKDLIQRIDVNLHRHLQAHGVDYLQFSFRWMNNLLTRELPLHCTIRLWDTYLAESDGFALFHLYVCAAFLLHWKEQLMQQNDFQGLMLLLQNLPTHNWSDRQINVLLAEAFRLKFTYADAPKHLETKS
Protein: Sodium/potassium-transporting ATPase subunit alpha (A8QI34)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362084}.
Interaction partners:
- Homeobox protein unc-4
- Sodium/potassium-transporting ATPase subunit beta-1
- Nervana 3, isoform E
- Sodium/potassium-transporting ATPase subunit beta-2
- Polycystin-related Y protein
- GH25158p
- Na/K-ATPase beta subunit isoform 4
- Uncharacterized protein, isoform B
- Uncharacterized protein
- AT04468p
Sequence:
MPPKKKNKEHKINGKEKKKDIQSFKKDVETDNHKIPVDELLERLKTDPNMGLSFVEAKLRLEINGPNILTPQPPTPKWIVFLKTMFGGFAILLWAGSFLCFVGYLIQLQTQHEPPDDNLYLGIALTVLVIVTGLFTYFQVHKSSSIMDSFKNLVPQYATVIREGEINTVTSDEIVKGDIVEVKFGDRVPADIRILEAHGLKVDNSSLTGESEPQVRSTEFTHENPLETKNLAFFSTNVLEGTCRGVVIATGDSTVMGRIANLAAGLDDVQSPISREIQLFIRFITIFAIILGLSFFAISLTLGYEFIDAVVFLIGIIVANVPEGLLVTVTVCLTLTAKRMASKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHLWYDQIIVESDTTESFRGSHFKIEDKSFNALFMCAALCNSAEFKGGQDDIPVFKKDVNGNASEAALLKFTETIFAGIGAFRQKHIKLTEIPFNSTEKYQVSVHEFNSSDGYFIVEMKGAPERILDRCSTIIIQGLSVELTPTLKLEFEEAYLEMGGMGERVLGFADLLLPMSKYPISYEFSADPPNFPLENLRFLGLISLIDPPRAAVPDAVAKCRSAGVRVIMVTGDHPITAKAIARSVGIITTPTAEDIAKQRGVTVLDIDSRQATAIVVHGGELREMKAEELDAVIYYHNEIVFARTSPQQKLIIVEACQRRGEIVAVTGDGVNDSPALKRADIGVAMGISGSDVSKQAADMILLDDNFASIVVGIEEGRIIFDNLKKSIAYTLTSNLPEIVPFLFFVIFDIPLALGTIAILCIDIGTDMLPAISLAYEKAESDIMARMPRDPFEDRLVNKKLILMAYLQIGVIQTVACFFTFFAIMAEHGFPPSRLKGIREDWDSKNVEDLEDGYGQEWTYRERKVLEYTAGTGFFVSIVVTQVFDLLICKTRRNSILQQGMGNHVLNFALVLEFIIACLLCYVPVFEKTLRMYSIKFIWWIYAFPFGLLIFFFDESRRFLIRRNPGGWVEQETYY
Protein: Cell division protein ZapB (P0AF36)
Organism: Escherichia coli (strain K12)
Function: Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18394147}. Note=Localizes to the septum at mid-cell, in a FtsZ-like pattern.
Interaction partners:
- Cell division protein ZapA
- Cell division protein FtsZ
- Macrodomain Ter protein
- Cell division protein ZapC
- Cell division protein ZapD
- Cell division protein FtsN
- Cell division protein FtsA
- Cell division protein ZipA
- Nucleoid occlusion factor SlmA
- Z-ring associated protein G
Sequence:
MTMSLEVFEKLEAKVQQAIDTITLLQMEIEELKEKNNSLSQEVQNAQHQREELERENNHLKEQQNGWQERLQALLGRMEEV
Protein: Pre-mRNA-splicing factor cwf7 (Complexed with cdc5 protein 7) (Splicing factor 27) (Q9USV3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in mRNA splicing.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pre-mRNA-splicing factor cwf10
- Pre-mRNA-splicing factor cwf3
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor prp5
- Pre-mRNA-splicing factor cwf2
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor spp42
- Pre-mRNA-splicing factor cwf15
- Pre-mRNA-splicing factor cwf11
Sequence:
MSYNISLDSLPYFESTYNEEDRSAAAQIVEEELKRSGGLLIKQEEQKKKFQSHRLSDRLENAIVAAGKGEKLAAIDVQRYIQLKPPGTRESLLQSAVVWEYQKSRNDNLYLLEKHGEKAFDSSLEALEVQLELLEKELVNTKKLSQGCNRKRKHYQMEVGARLAEAEVKFGQLLQSSIQCRVATLLS
Protein: X-linked lymphocyte-regulated 4B (B1B0R5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MASKIKGRPPKQPKVTPALPSNDSQQLHENNPGNNLALETCGESSSSHGTGGPKPGPSKKTLNERKRKYGVSVNKTVQNIEWNVDHFLKVQHERRQELYKDYSHQFLTLVMMWNIDVDQIKKQAGKLSDILDEQQKLFQQFQSIHMQKIEEFKELCDRHLKNLQAIKCCRRKAIIEEARKLMDYLEKRVTEE
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (E9PTG1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- AT-rich interaction domain 1A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1
- AT-rich interaction domain 1B
- Protein polybromo-1
- AT-rich interactive domain-containing protein 2
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 3
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
Sequence:
MATPTDPAAMPHPGPSPGPGPSPGPILGPSPGPGPSPGSVHSMMGPSPGPPSVSHPMSTMGSADFPQEGLHQLHKPMDGIHDKGIVEDVHCGSMKGTSMRPPHPGMGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPISGGGPTPPQMPPSQPGTLIPGDLQAMNQPNRGPSPFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQGKRTLPGMQQQQQQQQQQQQQQQQQQPQQPQQPQQQTQAQPQQQQQQQQQPPALVSYNRPSGPGQELLMTAQNTQQKLSAPAPSGRPSPAPPAATQPTATAVPGPSVQQPAPGQPSPVLQLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRIQELESLPGSLPPDLRTKATVELKALRLLNFQRQLRQEVVACMRRDTTLETALNSKAYKRSKRQTLREARMTEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMAEDEEGYRKLIDQKKDRRLAYLLQQTDEYVANLTNLVWEHKQAQAAKEKKKRRRRRKKAEENAEGGEPALGPDGEPIDESSQMSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPRSDSEESESDYEEEDEEEESSRQETEEKILLDPNSEEVSEKDAKQIIETAKQDVDDEYSMQYSARGSQSYYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHKVLRPFLLRRLKKEVESQLPEKVEYVIKCDMSALQKILYRHMQAKGILLTDGSEKDKKGKGGAKTLMNTIMQLRKICNHPYMFQHIEESFAEHLGYSNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEENEEEDEVPDDETLNQMIARREEEFDLFMRMDMDRRREDARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWLRAIEDGNLEEMEEEVRLKKRKRRRNVDKDPVKEDVEKAKKRRGRPPAEKLSPNPPKLTKQMNAIIDTVINYKDRCNVEKVPCNSQLEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKIAKEEESEEESNEEEEEEDEEESEAEAKSVKVKIKLNKKEEKGRDTGKGKKRPNRGKAKPVVSDFDSDEEQDENEQSEASGTDDE
Protein: Calreticulin (CRP55) (Calregulin) (Endoplasmic reticulum resident protein 60) (ERp60) (HACBP) (P15253)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P27797}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P27797}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P27797}. Cell surface {ECO:0000250|UniProtKB:P27797}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P28491}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:Q8K3H7}. Cytolytic granule {ECO:0000250|UniProtKB:P27797}. Note=Also found in cell surface (T cells), cytosol and extracellular matrix. During oocyte maturation and after parthenogenetic activation accumulates in cortical granules. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex (By similarity). In cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation (By similarity). {ECO:0000250|UniProtKB:P27797, ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7}.
Interaction partners:
Sequence:
MLLPVPLLLGLLGLAAAEPVVYFKEQFLDGDGWTERWIESKHKSDFGKFVLSSGKFYGDQEKDKGLQTSQDARFYALSARFEPFSNKGQPLVVQFTVKHEQNIDCGGGYVKLFPAGLDQKDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDANIYAYDSFAVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKTAEKQMKDKQDEEQRLKEEEEEKKRKEEEEAEEDEEDKDDKEDEDEDEEDKDEEEEEAAAGQAKDEL
Protein: Rhophilin-1 (GTP-Rho-binding protein 1) (Q8TCX5)
Organism: Homo sapiens (Human)
Function: Has no enzymatic activity. May serve as a target for Rho, and interact with some cytoskeletal component upon Rho binding or relay a Rho signal to other molecules.
Interaction partners:
- Ropporin-1A
- Transforming protein RhoA
- Rhotekin
- Serine/threonine-protein kinase N1
- Ropporin-1-like protein
- Connector enhancer of kinase suppressor of ras 1
- A-kinase anchor protein 3
- Calcium-binding tyrosine phosphorylation-regulated protein
- Regulator of G-protein signaling 14
Sequence:
MILEERPDGAGAGEESPRLQGCDSLTQIQCGQLQSRRAQIHQQIDKELQMRTGAENLYRATSNNRVRETVALELSYVNSNLQLLKEELEELSGGVDPGRHGSEAVTVPMIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFLTPARSLGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHAPSPDMSAASLCALEQLMMAQAQECVFEGLSPPASMAPQDCLAQLRLAQEAAQVAAEYRLVHRTMAQPPVHDYVPVSWTALVHVKAEYFRSLAHYHVAMALCDGSPATEGELPTHEQVFLQPPTSSKPRGPVLPQELEERRQLGKAHLKRAILGQEEALRLHALCRVLREVDLLRAVISQTLQRSLAKYAELDREDDFCEAAEAPDIQPKTHQKPEARMPRLSQGKGPDIFHRLGPLSVFSAKNRWRLVGPVHLTRGEGGFGLTLRGDSPVLIAAVIPGSQAAAAGLKEGDYIVSVNGQPCRWWRHAEVVTELKAAGEAGASLQVVSLLPSSRLPSLGDRRPVLLGPRGLLRSQREHGCKTPASTWASPRPLLNWSRKAQQGKTGGCPQPCAPVKPAPPSSLKHPGWP
Protein: Histone-lysine N-methyltransferase, H3 lysine-4 specific (EC 2.1.1.354) (COMPASS component SET1) (SET domain-containing protein 1) (Q5ABG1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance, transcription elongation regulation and pathogenesis of invasive candidiasis.
Subcellular location: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
Interaction partners:
- Ash2p
- COMPASS subunit protein
- Swd3p
- Spp1p
- Sdc1p
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- WD-repeat containing protein
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Set6p
- Histone H3.1/H3.2
Sequence:
MSYNNRSGGGASGGYSRRGYHGSHRGGYRTGRSKYPEDRYLVGGMLSLNKGSHYESSDNRYIPNEIGSKSPENRSHRSSTKDGRTPSGLSTPLSSSDKVSTPISIESINGSDRNTGVNNKDSEFPKLSHHSDFTSTIPFSRSINPQKNFMVINDSHTPKTDKGIQSKKIRYNGEGVNHVSDPRIAQSNSNLQKPTKKTKKTPYKQLPQPKFVYNSDSLGPAPMSTIIIWDLPISTSEPFLRNFVSRYGNPLEEMTFITDPTTAVPLGIVTFKFQGNPQKASELAKNFIKTVRQDELKIDGATLKIALNDNENQLLNRKLESAKKKMLQQRLQREQEEEKRRQKLVEEQKKQELLKKKEKEHQESVKKEKSVEHESTIVSTRDKNLVYKPNSTVLSMRHNHKIISSVILPKDLEKYIKSRPYILIRDKYVPTKKISSHDIKRALKKYDWTRVLSDKSGFFIVFNSLNECERCFLNEDNKKFFEYKLVMEMAIPEGFTNNIRENESKSTNDVLDEATNILIKEFQTFLAKDIRERIIAPNILDLLAHDKYPELVEELKSREQAAKPKVLVTNNQLKENALSILEKQRQLFQQRLPSFRMSHDRTQQHKPKRRNSIIPMQHALNFDDDEDSESHSQSESEDEDEDETTASRPLTPVVSTMKRERSSTITSIEDDIELEEREIKKQKVKVPAIEAEIAPESSPEEGEEEEKEEVEIKQEAEEVDIKFQPTEESPRTVYPEIPFSGDFDLNALQHTIKDSEDLLLAQEVLSETTPSGLSNIEYWSWKSKNRKDVQEISQEEEYIEELPESLQSTTGSFKSEGVRKIPEIEKIGYLPHRKRTNKPIKTIQYEDEDEEKPNENTNAVQSSRVNRANNRRFAADITAQIGSESDVLSLNALTKRKKPVTFARSAIHNWGLYAMEPIAAKEMIIEYVGERIRQQVAEHREKSYLKTGIGSSYLFRIDDNTVIDATKKGGIARFINHCCSPSCTAKIIKVEGKKRIVIYALRDIEANEELTYDYKFERETNDEERIRCLCGAPGCKGYLN
Protein: DNA ligase 4 (EC 6.5.1.1) (DNA ligase II) (DNA ligase IV) (Polydeoxyribonucleotide synthase [ATP] 4) (Q08387)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has minor DNA joining activity. Can act on oligo(PDT)/poly(rA) substrate.
Subcellular location: Nucleus {ECO:0000305|PubMed:9271115}.
Interaction partners:
- ATP-dependent DNA helicase II subunit 1
- ATP-dependent DNA helicase II subunit 2
- Non-homologous end-joining factor LIF1
- Non-homologous end-joining protein 1
- DNA repair and recombination protein RAD52
- DNA polymerase IV
- Proliferating cell nuclear antigen
- Exodeoxyribonuclease 1
- Double-strand break repair protein MRE11
- DNA repair protein RAD51
Sequence:
MISALDSIPEPQNFAPSPDFKWLCEELFVKIHEVQINGTAGTGKSRSFKYYEIISNFVEMWRKTVGNNIYPALVLALPYRDRRIYNIKDYVLIRTICSYLKLPKNSATEQRLKDWKQRVGKGGNLSSLLVEEIAKRRAEPSSKAITIDNVNHYLDSLSGDRFASGRGFKSLVKSKPFLHCVENMSFVELKYFFDIVLKNRVIGGQEHKLLNCWHPDAQDYLSVISDLKVVTSKLYDPKVRLKDDDLSIKVGFAFAPQLAKKVNLSYEKICRTLHDDFLVEEKMDGERIQVHYMNYGESIKFFSRRGIDYTYLYGASLSSGTISQHLRFTDSVKECVLDGEMVTFDAKRRVILPFGLVKGSAKEALSFNSINNVDFHPLYMVFDLLYLNGTSLTPLPLHQRKQYLNSILSPLKNIVEIVRSSRCYGVESIKKSLEVAISLGSEGVVLKYYNSSYNVASRNNNWIKVKPEYLEEFGENLDLIVIGRDSGKKDSFMLGLLVLDEEEYKKHQGDSSEIVDHSSQEKHIQNSRRRVKKILSFCSIANGISQEEFKEIDRKTRGHWKRTSEVAPPASILEFGSKIPAEWIDPSESIVLEIKSRSLDNTETNMQKYATNCTLYGGYCKRIRYDKEWTDCYTLNDLYESRTVKSNPSYQAERSQLGLIRKKRKRVLISDSFHQNRKQLPISNIFAGLLFYVLSDYVTEDTGIRITRAELEKTIVEHGGKLIYNVILKRHSIGDVRLISCKTTTECKALIDRGYDILHPNWVLDCIAYKRLILIEPNYCFNVSQKMRAVAEKRVDCLGDSFENDISETKLSSLYKSQLSLPPMGELEIDSEVRRFPLFLFSNRIAYVPRRKISTEDDIIEMKIKLFGGKITDQQSLCNLIIIPYTDPILRKDCMNEVHEKIKEQIKASDTIPKIARVVAPEWVDHSINENCQVPEEDFPVVNY
Protein: Envelope glycoprotein C (P10228)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Major attachment protein that mediates binding of the virus to cell surface heparan sulfate or chondroitin sulfate. Also plays several roles in host immune evasion by inhibiting the host complement cascade activation, and by providing a shield against neutralizing antibodies that interfere with gB-gD, gB-gH/gL or gD-gH/gL interactions (By similarity).
Subcellular location: Virion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAPGRVGLAVVLWSLLWLGAGVSGGSETASTGPTITAGAVTNASEAPTSGSPGSAASPEVTPTSTPNPNNVTQNKTTPTEPASPPTTPKPTSTPKSPPTSTPDPKPKNNTTPAKSGRPTKPPGPVWCDRRDPLARYGSRVQIRCRFRNSTRMEFRLQIWRYSMGPSPPIAPAPDLEEVLTNITAPPGGLLVYDSAPNLTDPHVLWAEGAGPGADPPLYSVTGPLPTQRLIIGEVTPATQGMYYLAWGRMDSPHEYGTWVRVRMFRPPSLTLQPHAVMEGQPFKATCTAAAYYPRNPVEFVWFEDDHQVFNPGQIDTQTHEHPDGFTTVSTVTSEAVGGQVPPRTFTCQMTWHRDSVTFSRRNATGLALVLPRPTITMEFGVRIVVCTAGCVPEGVTFAWFLGDDPSPAAKSAVTAQESCDHPGLATVRSTLPISYDYSEYICRLTGYPAGIPVLEHHGSHQPPPRDPTERQVIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR