wanglab/gogpt-training-data huggingface dataset:
Protein: Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain] (P48740)
Organism: Homo sapiens (Human)
Function: Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development.
Subcellular location: Secreted {ECO:0000269|PubMed:11485744}.
Interaction partners:
Sequence:
MRWLLLYYALCFSLSKASAHTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPFCGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDGTWSNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYTCSAQGVWMNKVLGRSLPTCLPVCGLPKFSRKLMARIFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSLDPEDPTLRDSDLLSPSDFKIILGKHWRLRSDENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVSGWGKQFLQRFPETLMEIEIPIVDHSTCQKAYAPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNRERGQWYLVGTVSWGDDCGKKDRYGVYSYIHHNKDWIQRVTGVRN
Protein: Vomeronasal 2, receptor 120 (E9PX34)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLIFVSVLLFLNFPVASCEPINPGCSLGMADAIFQDGDVLVDCHFVLLTVSIALQKIFHFLRFHLSFPMFIYRIHPNKYQYVIALNFAIEEINKNIHLLPNISLGYDMYSIVQYQATILEHSIRFLTGLKEAIPNYTCRKESKLIAVVTGTSWEFPSRISTILGLYKYPQLTFGPFDPMLSDHVKFPFIYQMAPEDTSLALGMVSLMVHFSWTWVGLIITENEKGIKFLSDLKREMKKNSVCAAFVQMLSLKYRYNWNDLLSTDPAIMGEMVKVFIVFADIDSTLVVIFKASGQVDPWRVWVTTSQWDIASSVRHFILDSFHGTLIFSQHHPEISAFKDFIQTVNPSKYPDDIFLSHIWKMYLNCPFSRVYCKTLKTCSSNGSLALLPWHRFDMDMSEESYHIYNAVYAVAHSLHEMLQEHADVQPVKSRKRLVFSPCRLHPFLKNIQFNNPSGDKVDLSHTGKLETKYDIFNFWNFPQGLGLKVKVGTFSSFLPRNKQFSLSDGMIEWGTKDKQTPLSVCSTSCAPGLMKSPQEGKASCCFDCHPCLENEISNETDSIQCIKCPDDQYANTEQTHCIPKAVTFLAYEDPLGMALACMALCFSALTALVLGVFVKHHETPIVKANNRTLSYILLISLILCFLCSLPFIGLPNMATCILQQMSFGVVFTIAVSTVLAKTVTVVLAFRSTVPGRRMRWILVSPNLIIPICTLIQMVLCAIWLGASAPFVDINAHNERGHITIMCNKGSATAFYCVLGYLGFLAMGTLTVAFWARNLPDIFNEAKFLTFSMLVFCSVWVTFLPVYHSTKGKVMVAVEVFSILASSAGLLGCIFVPKCYIILIRPKNGSFKGLRGTRVCK
Protein: Regulator of telomere elongation helicase 1 homolog (EC 5.6.2.-) (Q93575)
Organism: Caenorhabditis elegans
Function: ATP-dependent DNA helicase implicated in DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065}.
Interaction partners:
- Crossover junction endonuclease MUS81
- RecQ-like DNA helicase blm-1
- ATP-dependent DNA helicase PIF1
- Helicase POLQ-like
- DNA mismatch repair protein S5 domain-containing protein
- Exonuclease 1
- DNA replication ATP-dependent helicase/nuclease DNA2
- RAD51-like protein 1
- GEN1 Holliday junction resolvase homolog
- SAP domain-containing protein
Sequence:
MPPKASNSTEVWINPKLSVKFPFEPYECQRIFMKNVVDVLDRKLDAALESPTGTGKTLSLLCSTLAWVQRQKETKPLDFATWQTSGAGGAEKTDEKLKSAYVPTIFYASRTHSQLEQVVHELNRTEYKWVKTTILGSREHFCINQKVKKIKESNRQAHVCRGLVSKRACHYYNKFDACTTDKMTEFLDKGEAMDIEDFVKLGTQNSLCPYFMSRQRSETAELILLPYNYIIDPKMRRRYKLDLKNSIVIFDEAHNLESICESNASAELTSTSIALCIEELKKVLALLVDEEETARSEADAETGAFGSAKIDLTKKLIENLRTEDLMTVLEKIFSLEEEMDKLFGSSQLKSVPPLSGKASDGEILLETLAKAGFDANSVERLVDVLRDAISYLLSKNEEVALTEKGDGMEKVADFLLSIYSTHAQDVAAAVGEETVKLVDRVDPKTVARNCKLYIQKDKDNEKLTIKYFCFQASISMRMLKMRGVRNVLLASGTLSPIQAFTYNMGLNFGAILENEHALKQVPVLTSIVTRGKRGGLAGSFQNRKNLDYVTGVAEALLRVMEVIPQGILIFFSSYSQMDELVATWKTTKWSSNSNESFWEKMEKTKRVVVEPRAKEELAAIRLRYTQGVSEQHGAALLAVCRGKVSEGIDFCDAESRAVIIIGIPYPPIHDERVVLKKMYLDDLMGRKDTKSERQSSQDWYQMEAFRAVNQAIGRVLRHKDDFGTVVLMDTRYASAKPEMFPKWLRNTISRSDTDGCALKTSRFFKERGHLIENSKTEYIKKQAKQCKSFRQVKQTAASDSKDDIIEITLEDMFSPANMKLEKKEITKLRPPQLIPSTSSVFSLPTNEDELKIKKWEQENDIQCLSSIPLESNKRKFKIETPGPSTSTLTQKSEPPKKKKILLLTRNTLPDEYQKAIEIPTSELLKDMSDDNKKQFATTLRSYKAESIRWDEVFQRFRPIFVPHKADLFIACSNVLRSEDKMKYLKKALESKIHT
Protein: MAP kinase-activated protein kinase 3 (MAPK-activated protein kinase 3) (MAPKAP kinase 3) (MAPKAP-K3) (MAPKAPK-3) (MK-3) (EC 2.7.11.1) (Q3UMW7)
Organism: Mus musculus (Mouse)
Function: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins, such as TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression.
Subcellular location: [Isoform 1]: Nucleus. Cytoplasm. Note=Predominantly located in the nucleus, when activated it translocates to the cytoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Note=Localizes throughout the cell. Degraded in response to osmotic stress.
Interaction partners:
- Mitogen-activated protein kinase 14
- Heat shock protein beta-1
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 12
- MAP kinase-activated protein kinase 2
- Cyclic AMP-dependent transcription factor ATF-4
- Neuronal migration protein doublecortin
- Dual specificity mitogen-activated protein kinase kinase 3
Sequence:
MDGETAGEKGSLVPPPGALGGSALGGAPAPGVRREPKKYAVTDDYQLSKQVLGLGVNGKVLECYHRRSGQKCALKLLYDSPKARQEVDHHWQASGGPHIVRILDVYENMHHGKRCLLIVMECMEGGELFSRIQERGDQAFTEREAAEIMRDIGTAIQFLHSRNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRLGQYSFPNPEWLDVSEDAKQLIRLLLKTDPTERLTIMQFMNHPWINQSMVVPQTPLYTARVLQEDKDHWDDVKEEMTSALATMRVDYDQVKIKDLKTSNNRLLNKRRKKQAGSSSASQGCNNQ
Protein: Monocyte to macrophage differentiation factor (Progestin and adipoQ receptor family member 11) (Progestin and adipoQ receptor family member XI) (Q15546)
Organism: Homo sapiens (Human)
Function: Involved in the dynamics of lysosomal membranes associated with microglial activation following brain lesion.
Subcellular location: Late endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Progestin and adipoQ receptor family member 3
Sequence:
MRFKNRFQRFMNHRAPANGRYKPTCYEHAANCYTHAFLIVPAIVGSALLHRLSDDCWEKITAWIYGMGLCALFIVSTVFHIVSWKKSHLRTVEHCFHMCDRMVIYFFIAASYAPWLNLRELGPLASHMRWFIWLMAAGGTIYVFLYHEKYKVVELFFYLTMGFSPALVVTSMNNTDGLQELACGGLIYCLGVVFFKSDGIIPFAHAIWHLFVATAAAVHYYAIWKYLYRSPTDFMRHL
Protein: Cyclin-C (SRB11 homolog) (hSRB11) (P24863)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Binds to and activates cyclin-dependent kinase CDK8 that phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 18
- Cyclin-dependent kinase 8
- Mediator of RNA polymerase II transcription subunit 12-like protein
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 13-like
- Mediator of RNA polymerase II transcription subunit 13
- Cyclin-dependent kinase 19
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 14
Sequence:
MAGNFWQSSHYLQWILDKQDLLKERQKDLKFLSEEEYWKLQIFFTNVIQALGEHLKLRQQVIATATVYFKRFYARYSLKSIDPVLMAPTCVFLASKVEEFGVVSNTRLIAAATSVLKTRFSYAFPKEFPYRMNHILECEFYLLELMDCCLIVYHPYRPLLQYVQDMGQEDMLLPLAWRIVNDTYRTDLCLLYPPFMIALACLHVACVVQQKDARQWFAELSVDMEKILEIIRVILKLYEQWKNFDERKEMATILSKMPKPKPPPNSEGEQGPNGSQNSSYSQS
Protein: Glycoprotein hormones alpha chain (Anterior pituitary glycoprotein hormones common subunit alpha) (Choriogonadotropin alpha chain) (Chorionic gonadotrophin subunit alpha) (CG-alpha) (Follicle-stimulating hormone alpha chain) (FSH-alpha) (Follitropin alpha chain) (Luteinizing hormone alpha chain) (LSH-alpha) (Lutropin alpha chain) (Thyroid-stimulating hormone alpha chain) (TSH-alpha) (Thyrotropin alpha chain) (P01215)
Organism: Homo sapiens (Human)
Function: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH, follitropin/follicle stimulating hormone/FSH and choriogonadotropin/CG. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways.
Subcellular location: Secreted {ECO:0000269|PubMed:24692546, ECO:0000269|PubMed:2494176}.
Interaction partners:
- Follitropin subunit beta
- Choriogonadotropin subunit beta 3
- Thyrotropin subunit beta
- Follicle-stimulating hormone receptor
- Glycoprotein hormone alpha-2
- Thyrotropin receptor
- Lutropin subunit beta
- Glycoprotein hormone beta-5
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
Sequence:
MDYYRKYAAIFLVTLSVFLHVLHSAPDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS
Protein: Ly49 inhibitory receptor 2 (A0A8I6AAA6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSKQDVPCSTVRFKKSSGLRYQVRPEDTQRPREAGCRVKFPWQLTVIAIGIILSLRLVAVAILVTNSGCDEMHWLCYGIKCYYFIMDKRTWLECKQTCQNYGLSFLKIDDKDELFLQDHIIREKWSRIDNSLFNCDLVAMKSLQKTGNCKYFSMTGLNDDDCGKRHLCICEKGIEKHPTPLCSVNERSRSAL
Protein: Caspase 7 (A0A8I5ZQU7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLSFYYYREEGNSLPVASGGSLVLQRGLLPDGDTRKKKKNASMCPVSTTRDRVPTYLYRMDFEKMGKCIIINNKNFDKATGMDVRNGTDKDAEALFKCFRSLGFEVTVYNDCSCAKMQDLLRRASEEDHSNSACFACVLLSHGEENLIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRNPGKGSWFVQALCSILNEHGKDLEIMQILTRVNDRVARHFESQSDDPRFNEKKQIPCMVSMLTKELYFGR
Protein: FI06402p (PDGF- and VEGF-related factor 3, isoform D) (Q9VM39)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Latrophilin Cirl
- PDGF- and VEGF-receptor related, isoform J
- LD28763p
Sequence:
MHWLVLILVPLVWANSSDLKGAPVMTTVAPTGGHRSPHQQQRLQQLQEAQQLEAHQQHHHHLRHEQHLRAELEGNHQPPIEDVEKKAFLDPQLPMQQHHLRHHNRHHASWEQRVFPSLRHQQHRLSIGPSTAKNLMTTEAPTTRHHGLISNHSRYFDRDGIFPSWAEPRTTRGPNWRQEVDSSDSDEDSDEDDEDDYDEYDEDGDTSNGVDEELARQMPRYSLFTQKLPHIDLKDTDYNAYDQSDELDIVSSSNRNSNKYPSVANPHDKSAGKRNIFDWLFKHDREKEAVKKPHITTTSTTTTTSTTSTVKPTIMRTERPKLQLIDANLKNGGGEEDDSNEDSDSESEEGFSNEQWNKIEHQHHLRQQKHQKELLAMREKSRNTPLIRNIENEVSAAKTLEDNDGHDVENIYARNYVAAKVGQKKEDQLGTPEAVIKARRLHAQKQKSERALAHAHMNQVLKEATCRIPQKRCQLVQQDPSKIYTPHCTILHRCSEDSGCCPSRSQICAAKSTHNVELHFFVKSSKHRSVIEKRTFVNHTECHCIERSTYNEETAMAHYGQSVVRATILSCTCPKSFEKILQDDGQCRCDCSSGNYDCDWLKRGNEHFAMNDRKCIQQGRCKPPTCEFGLYMDKHGRCPKQHEQPSYNAMS
Protein: Cotton fiber protein (Q9FKM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTKSKDGSLLNRLRQAVNKVKFVLSFKINSLWGLVPMLGSSSSSSSLRLSFNDRPGLTAAFTENEPDSTGSSRGALYRTVSYDQSSDEDIDNKAEMFIANFYRQLKIERQISLELKYCQGNNQSFNYRSP
Protein: Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase (EC 2.4.1.256) (Alpha-1,2-glucosyltransferase ALG10-A) (Alpha-2-glucosyltransferase ALG10-A) (Asparagine-linked glycosylation protein 10 homolog A) (Q5BKT4)
Organism: Homo sapiens (Human)
Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5I7T1}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dol-P-Glc:Glc
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
Sequence:
MAQLEGYYFSAALSCTFLVSCLLFSAFSRALREPYMDEIFHLPQAQRYCEGHFSLSQWDPMITTLPGLYLVSIGVIKPAIWIFGWSEHVVCSIGMLRFVNLLFSVGNFYLLYLLFCKVQPRNKAASSIQRVLSTLTLAVFPTLYFFNFLYYTEAGSMFFTLFAYLMCLYGNHKTSAFLGFCGFMFRQTNIIWAVFCAGNVIAQKLTEAWKTELQKKEDRLPPIKGPFAEFRKILQFLLAYSMSFKNLSMLLLLTWPYILLGFLFCAFVVVNGGIVIGDRSSHEACLHFPQLFYFFSFTLFFSFPHLLSPSKIKTFLSLVWKRRILFFVVTLVSVFLVWKFTYAHKYLLADNRHYTFYVWKRVFQRYETVKYLLVPAYIFAGWSIADSLKSKSIFWNLMFFICLFTVIVPQKLLEFRYFILPYVIYRLNIPLPPTSRLICELSCYAVVNFITFFIFLNKTFQWPNSQDIQRFMW
Protein: Secretory carrier-associated membrane protein 2 (Secretory carrier membrane protein 2) (O15127)
Organism: Homo sapiens (Human)
Function: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}. Recycling endosome membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}.
Interaction partners:
- ADP-ribosylation factor 6
- Protein GPR108
Sequence:
MSAFDTNPFADPVDVNPFQDPSVTQLTNAPQGGLAEFNPFSETNAATTVPVTQLPGSSQPAVLQPSVEPTQPTPQAVVSAAQAGLLRQQEELDRKAAELERKERELQNTVANLHVRQNNWPPLPSWCPVKPCFYQDFSTEIPADYQRICKMLYYLWMLHSVTLFLNLLACLAWFSGNSSKGVDFGLSILWFLIFTPCAFLCWYRPIYKAFRSDNSFSFFVFFFVFFCQIGIYIIQLVGIPGLGDSGWIAALSTLDNHSLAISVIMMVVAGFFTLCAVLSVFLLQRVHSLYRRTGASFQQAQEEFSQGIFSSRTFHRAASSAAQGAFQGN
Protein: 8-oxoguanine DNA glycosylase, isoform CRA_e (N-glycosylase/DNA lyase) (E5KPM8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPPWQCI
Protein: 3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) (A0A1D8PQ07)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- 3-hydroxyisobutyryl-CoA hydrolase
- methylmalonate-semialdehyde dehydrogenase
- Aldehyde dehydrogenase domain-containing protein
- Aldehyde dehydrogenase domain-containing protein
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- 4-aminobutyrate aminotransferase
- 4-aminobutyrate aminotransferase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
Sequence:
MLRTSIRAFSTQPRLSTNYGFIGLGLMGQHMARHVYNQLEPSDKLYVYDVDPKHTTQFLTEVTSQTPQNAPLLTPLNSLKDFTTEVDSQLDFIVTMVPEGKHVKSVVSELVGHYKSTGNYDPSIKTTFLDSSTIDIPTSRDVHQLVKSSIPEFDFIDTPVSGGVAGARKGTLSFMLSRETHDDIDPSLTALLSKMGINIFPCGATHGTGLAAKLANNYLLAITNIAAADSFQLAESFGLNLQNYAKLVAVSTGKSWASVDNCPIPGVYPDNNLPSDVNYEGGFITKLTRKDVVLATESAKFNNRFLMLGDIGRHWYDKACEREDIANRDLSVLFEWLGDLKQNEKGDVIDVKRK
Protein: WRKY transcription factor 68 (WRKY DNA-binding protein 68) (Q93WV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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:
Sequence:
MENVGVGMPFYDLGQTRVYPLLSDFHDLSAERYPVGFMDLLGVHRHTPTHTPLMHFPTTPNSSSSEAVNGDDEEEEDGEEQQHKTKKRFKFTKMSRKQTKKKVPKVSFITRSEVLHLDDGYKWRKYGQKPVKDSPFPRNYYRCTTTWCDVKKRVERSFSDPSSVITTYEGQHTHPRPLLIMPKEGSSPSNGSASRAHIGLPTLPPQLLDYNNQQQQAPSSFGTEYINRQEKGINHDDDDDHVVKKSRTRDLLDGAGLVKDHGLLQDVVPSHIIKEEY
Protein: N-acetylglucosamine-1-phosphotransferase subunits alpha/beta (EC 2.7.8.17) (GlcNAc-1-phosphotransferase subunits alpha/beta) (Stealth protein GNPTAB) (UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta) [Cleaved into: N-acetylglucosamine-1-phosphotransferase subunit alpha; N-acetylglucosamine-1-phosphotransferase subunit beta] (Q69ZN6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment.
Subcellular location: [N-acetylglucosamine-1-phosphotransferase subunit alpha]: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q3T906}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q3T906}.; SUBCELLULAR LOCATION: [N-acetylglucosamine-1-phosphotransferase subunit beta]: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q3T906}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q3T906}.
Interaction partners:
- N-acetylglucosamine-1-phosphotransferase subunit gamma
- N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
- Synaptonemal complex protein 3
Sequence:
MLLKLLQRQTYTCLSHRYGLYVCFVGVVVTIVSAFQFGEVVLEWSRDQYHVLFDSYRDNIAGKSFQNRLCLPMPIDVVYTWVNGTDLELLKELQQVREHMEEEQRAMRETLGKNTTEPTKKSEKQLECLLTHCIKVPMLVLDPPLPANCTLKDLPTLYPSFHAASDMFNVAKPKNPSTNVSVVVFDTTKDVEDAHAGPFKGGSKQMVWRAYLTTDKEAPGLVLMQGLAFLSGFPPTFKETSQLKTKLPEKLSSKIKLLRLYSEASVALLKLNNPKGFQELNKQTKKNMTIDGKELTISPAYLLWDLSAISQSKQDEDVSASRFEDNEELRYSLRSIERHAPWVRNIFIVTNGQIPSWLNLDNPRVTIVTHQDIFQNLSHLPTFSSPAIESHIHRIEGLSQKFIYLNDDVMFGKDVWPDDFYSHSKGQKVYLTWPVPNCAEGCPGSWIKDGYCDKACNNSACDWDGGDCSGNTAGNRFVAGGGGTGNIGAGQHWQFGGGINTISYCNQGCANSWLADKFCDQACNVLSCGFDAGDCGQDHFHELYKVTLLPNQTHYVVPKGEYLSYFSFANIARRGVEGTYSDNPIIRHASIANKWKTIHLIMHSGMNATTIYFNLTLQNANDEEFKIQIAVEVDTREAPKLNSTTQKAYESLVSPVTPLPQADVPFEDVPKEKRFPKIRRHDVNATGRFQEEVKIPRVNISLLPKEAQVRLSNLDLQLERGDITLKGYNLSKSALLRSFLGNSLDTKIKPQARTDETKGNLEVPQENPSHRRPHGFAGEHRSERWTAPAETVTVKGRDHALNPPPVLETNARLAQPTLGVTVSKENLSPLIVPPESHLPKEEESDRAEGNAVPVKELVPGRRLQQNYPGFLPWEKKKYFQDLLDEEESLKTQLAYFTDSKHTGRQLKDTFADSLRYVNKILNSKFGFTSRKVPAHMPHMIDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPLNISQVFHEVDTDQSGVLSDREIRTLATRIHDLPLSLQDLTGLEHMLINCSKMLPANITQLNNIPPTQEAYYDPNLPPVTKSLVTNCKPVTDKIHKAYKDKNKYRFEIMGEEEIAFKMIRTNVSHVVGQLDDIRKNPRKFVCLNDNIDHNHKDARTVKAVLRDFYESMFPIPSQFELPREYRNRFLHMHELQEWRAYRDKLKFWTHCVLATLIIFTIFSFFAEQIIALKRKIFPRRRIHKEASPDRIRV
Protein: Signal peptidase complex subunit 2 (Microsomal signal peptidase subunit 2) (Q04969)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Signal peptidase complex catalytic subunit SEC11
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 3
- Endoplasmic reticulum chaperone BiP
- Translocation protein SEC62
- Protein transport protein SBH1
- Endoplasmic reticulum vesicle protein 25
- Protein transport protein SBH2
- Kinetochore protein SPC25
- Transcriptional activator HAC1
Sequence:
MSSAKPINVYSIPELNQALDEALPSVFARLNYERSYALLDAKLYIGYSIAVVAGLSFFLDKKFERDQIVTYQKLLVGAYFVLSLLFWYFSRFIEKGTVYVGKRRGTKEEIYVKTKFEKNEPLYLVELVQKKKGENSKKELKAKLEVNKVFNESGYLQNDAYFKWFSEQHNVLDTKKNE
Protein: Hemerythrin HHE cation binding domain subfamily (A0A0H2UNW3)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MTDERIHILRDILLELHNGASPESVQDRFDATFTGVSAIEISLMEHELMNSDSGVTFEDVMELCDVHANLFKNAIKGVEVSDTEHPGHPVRVFKEENLALRAALIRIRRLLDTYESMEDEEMLAEMRKGLVRQMGLVGQFDIHYQRKEELFFPIMERYGHDSPPKVMWGVDDQIRELFQTALTTAKSLPEVSISSVKEAFEAFATEFESMIFKEESILLMILLESFTQDDWLQIAEESDAYGYAIIRPSEKWVPERQSFIEEKIAEEPVQLDTAEGQVQQVIDTPEGHFTITFTPKEKEAVLDRHSQQAFGNGYLSVEQANLILNHLPMEITFVNKEDIFQYYNDNTPADEMIFKRTPSQVGRNVELCHPPKYLDKVKTIMKGLREGSKDKYEMWFKSESRGKFVHITYAAVHDEDGEFQGVLEYVQDIQPYREIDTDYFRGLE