wanglab/gogpt-training-data huggingface dataset:
Protein: Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (DNA repair protein rad2) (Flap structure-specific endonuclease 1) (P39750)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
Interaction partners:
- Proliferating cell nuclear antigen
- DNA ligase 1
- DNA replication ATP-dependent helicase/nuclease dna2
- DNA ligase 3
- DNA polymerase delta catalytic subunit
- Double-strand break repair protein rad32
- DNA repair protein rhp51
- DNA mismatch repair protein msh6
- DNA polymerase subunit delta-2
- Crossover junction endonuclease mus81
Sequence:
MGIKGLAQVLSEHAPASVKHNDIKNYFGRKVAIDASMSLYQFLIQVRSQDGQQLMNEQGETTSHLMGMFYRTLRIVDNGIKPCFVFDGKPPTLKSGELAKRVARHQKAREDQEETKEVGTAEMVDRFAKRTVKVTRQHNDEAKRLLELMGIPFVNAPCEAEAQCAALARSGKVYAAASEDMDTLCFQAPVLLRHLTFSEQRKEPISEYNIEKALNGLDMSVEQFVDLCILLGCDYCEPIRGVGPARAVELIRQYGTLDRFVKEADRSKYPIPEDWPYEDARRLFLDAEVLPGEEIELKWKSPDADGIIQFLVKEKGFNEDRVKLGINRLEKASKTIPQGRLDSFFKPVPSSPKKPVDTKSKGSAKRKRDSNKGGESKKKR
Protein: DNA replication helicase (EC 3.6.4.-) (P03214)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase elongates using dNTPs. Possesses helicase-like motifs and therefore may act as the helicase subunit of the complex.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04030}.
Interaction partners:
Sequence:
MAEEPRAPEALSSTFMLNMTSDASVRRIVRRIGTLARRRVQQLPDMETFSPEFDPELSEPPFLPFSAYVITGTAGAGKSTSVSCLHHTMDCLVTGATTVAAQNLSQTLRAYCPTVYSAFGFKSRHINMTQRVSSHGRSTDAALEELQRRDLAKYWPVLSDIAAEFRRTKPRGLYSGVSGPAFEVLRDMHQGQLWTTNVIVVDEAGTLSVHILTAVVFCYWFFNAWLRTPLYRRGRIPCIVCVGSPTQTDAFQSSFSHETQVNKIRECDNILTFLVGNPRAATYVDVARNWALFINNKRCTDVQFGHLMKTLEYGLELSPDILAYVDRFVVPRAAIMDPAQYVGWTRLFLSHAEVKTFLTTLHATLKTAGQGRAARGTGGDGGGVTMFTCPVECEVFLDPLAQYKTLVGLPGLTAHTWLQKNYARLGNYSQFADQDMVPVGTEQDEERVKVTYNVTYVKHSSVSVNCKTKKSICGYTGTFGDFMDTLEADSFVEAHGHEQPEYVYSFLARLIYGGIYAFSHGGHSLCENGEYVAELGAVPLPGRTWDPEVTAGMELGELPLEVAWDGERSPAAVFYARVLAPPAANSAPLCSLLNIYNDLRAYFRQCLDVAVRYGGREFRDLPFCTFTNNMLIRDNIEFTSDEPLLHGLLDYASTTENYTLLGYTHLNVFFGIRGKQQPQDAGSSRMPRLMVKDEAGFVCCLEHNTNKLYETIEDKSLNLCSIRDYGISSKLAMTIAKAQGLSLNKVAICFGSHRNIKPGHVYVALSRARHSNCVVMDRNPLSEMITGEGNPASGYIVDALKNSRALLVY
Protein: Multimerin-2 (A6H6E2)
Organism: Mus musculus (Mouse)
Function: Inhibits endothelial cells motility and acts as a negative regulator of angiogenesis; it down-regulates KDR activation by binding VEGFA.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9H8L6}.
Interaction partners:
- Harmonin-binding protein USHBP1
- Roundabout homolog 4
- Adhesion G protein-coupled receptor F5
- C-type lectin domain family 14 member A
- Transcription factor SOX-18
- Claudin-5
- Multimerin-1
Sequence:
MIPTLLLGFGVYLSWGLLGSWAQDPGTKFSHLNRPGMPEGWRLGAEDTSRDPIRRNWCPYQKSRLVTFVAACKTEKFLVHSQQPCPQGAPDCQGVRVMYRVAQKPVYQVQQKVLISVDWRCCPGFQGPDCQDHNPTANPEPTEPSGKLQETWDSMDGFELGHPVPEFNEIKVPQEQQENLLQNLQNDAQSVEDGFPGSWEAPPSNLTDEMTEANLTEFEFPGRTSEHLLQPHIDAFLKAHFSPIWKNFNDSLHSLSQAIRNLSLDVEANHQAIKMIQEGTVARADFQELGAKFEAKVQQNSQRLGQLWQDVEDQLHAQRRSVHHALSDVQAEVSTKLKQLVKAQELPGANGSLVMASAAAAARPEPESLQARLGQLQRNLSALHMVTSQREEELQSTLKNMDSVLKQHAEEIKELYSESDETFDQISKVERQVEELLVNHTGLRELRVILMEKSLIMEENKEEIERQLLELNLTLQHLHAGHADLIKYVKDCNCQRVNSDVDVAPEGHRDVMHTLEETQVSLDEQHQLDGSSLQALQSTVDAMSSAMDAYRGEGERARAERARIRSQLRALDHAVEALKTAANGTRKEIRLLHGSFTALLEDALRHQAVLAALFGEEMIDEMSEEAPRPLPLDYEQIRLALQDAASGLQEQAIGWEDLATRVEALEKAAGGFVEQHPQLAEGLEPSHDSGREEEAMTLAELEQEIRRLSSDVKQIGQCCEASWAASLNSSLEDLHSMLLDTQHGLRQHRQLFHNLFQNFQGLVASNISLDLGKLQAMLSKKDKKQPRGPGESRKRDKKQVVMSTDAHAKGLELWETGSPVAFYAGSSEGATALQMVKFNTTSINVGSSYFPEHGYFRAPKRGVYLFAVSITFGPGPGMGQLVFEGHHRVPVYSTEQRGGSTATTFAMVELQKGERAWFELIQGSATKGSQPGTAFGGFLMFKT
Protein: LIM domain binding 3 (A0A0G2K2C4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000256|ARBA:ARBA00004216}.
Interaction partners:
Sequence:
MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPIQSPLPVIPHQKVVANSPANADYQERFNPSVLKDSALSTHKPIEVKGLGGKATIIHAQYNTPISMYSQDAIMDAIAGQAQAQGSDFSGSLPVKDLAVDSASPVYQAVIKTQSKPEDEADEWARRSSNLQSRSFRILAQMTGTEYMQDPDEEALRRSSTPIEHAPVCTSQATSPLLPASAPSPAAASPIAASPTLATAAAAHAVAASAAGPASSPVENPRPQASAYSPAAATSPAPAAHTSYSEGPAAPAPKPRVVTTASIRPSVYQPVPASPYSPSPGANYSPTPYTPSPAPAYTPSPAPTYTPSPAPTYSPSPAPAYTPSPAPNYNPTPSAAYSGGPSESASRPPWVTDDSFSQKFAPGKSTTSVSKQTLPRGAPAYNPTGPQVTPLARGTFQRAERFPASSRTPLCGHCNNVIRGPFLVAMGRSWHPEEFNCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPICAKCNTKIMGEVMHALRQTWHTTCFICAACKKPFGNSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDKPLCKKHAHAINV
Protein: Par-1, isoform L (EC 2.7.11.-, EC 2.7.11.26) (RE47050p) (Q6NPA6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTAMRTTLQSVPEALPADSVSNGTASNVAAPAAPVSSATNAVPPLAAVSSTTATYATNSISTSSHSVKDQQQQQQQQQHDSANANIVSLPPTTTPVANTNTMMPIVTSSNSATSNSTAATPTPASGAAATGGVGSVSQGPATVSASAANTNHSHQHSHQHHHHVANNMTTDGARLSSNNSAVVASSAINHHHHHTPGSGVAPTVNKNVLSTHSAHPSAIKQRTSSAKGSPNMQMRSSAPMRWRATEEHIGKYKLIKTIGKGNFAKVKLAKHLPTGKEVAIKIIDKTQLNPGSLQKLFREVRIMKMLDHPNIVKLFQVIETEKTLYLIMEYASGGEVFDYLVLHGRMKEKEARVKFRQIVSAVQYCHQKRIIHRDLKAENLLLDSELNIKIADFGFSNEFTPGSKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGSTLRELRERVLRGKYRIPFYMSTDCENLLRKFLVLNPAKRASLETIMGDKWMNMGFEEDELKPYIEPKADLADPKRIEALVAMGYNRSEIEASLSQVRYDDVFATYLLLGRKSTDPESDGSRSGSSLSLRNISGNDAGANAGSASVQSPTHRGVHRSISASSTKPSRRASSGVGPTNAAATVAAATGAVGAVNPSNNYNAAGSAADRASVGSNFKRQNTIDSATIKENTARLAAQNQRPASATQKMLTTADTTLNSPAKPRTATKYDPTNGNRTVSGTSGIIPRRSTTLYEKTSSTEKTNVIPAETNLFDRLRMASAVKSSRHFPRNVPSRSTFHSGQTRARNNTALEYSGTSGASGDSSHPGRMSFFSKLSSRFSKRPNQ
Protein: Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (STAT-induced STAT inhibitor 3) (SSI-3) (O14543)
Organism: Homo sapiens (Human)
Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells (By similarity). Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Tyrosine-protein kinase JAK2
- Tyrosine-protein kinase JAK1
- Non-receptor tyrosine-protein kinase TYK2
- Signal transducer and activator of transcription 3
- Leptin receptor
- Interleukin-6 receptor subunit beta
- Elongin-B
- Signal transducer and activator of transcription 1-alpha/beta
- Insulin receptor substrate 1
- Insulin receptor substrate 2
Sequence:
MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGAPSFPSPPTEPSSEVPEQPSAQPLPGSPPRRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL
Protein: POU domain, class 6, transcription factor 2 (Retina-derived POU domain factor 1) (RPF-1) (P78424)
Organism: Homo sapiens (Human)
Function: Probable transcription factor likely to be involved in early steps in the differentiation of amacrine and ganglion cells. Recognizes and binds to the DNA sequence 5'-ATGCAAAT-3'. Isoform 1 does not bind DNA.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Obscurin
- Wilms tumor protein
- APC membrane recruitment protein 1
Sequence:
MSALLQDPMIAGQVSKPLLSVRSEMNAELRGEDKAATSDSELNEPLLAPVESNDSEDTPSKLFGARGNPALSDPGTPDQHQASQTHPPFPVGPQPLLTAQQLASAVAGVMPGGPPALNQPILIPFNMAGQLGGQQGLVLTLPTANLTNIQGLVAAAAAGGIMTLPLQNLQATSSLNSQLQQLQLQLQQQQQQQQQQPPPSTNQHPQPAPQAPSQSQQQPLQPTPPQQPPPASQQPPAPTSQLQQAPQPQQHQPHSHSQNQNQPSPTQQSSSPPQKPSQSPGHGLPSPLTPPNPLQLVNNPLASQAAAAAAAMSSIASSQAFGNALSSLQGVTGQLVTNAQGQIIGTIPLMPNPGPSSQAASGTQGLQVQPITPQLLTNAQGQIIATVIGNQILPVINTQGITLSPIKPGQQLHQPSQTSVGQAASQGNLLHLAHSQASMSQSPVRQASSSSSSSSSSSALSVGQLVSNPQTAAGEVDGVNLEEIREFAKAFKIRRLSLGLTQTQVGQALSATEGPAYSQSAICRHTILRSHFFLPQEAQENTIASSLTAKLNPGLLYPARFEKLDITPKSAQKIKPVLERWMAEAEARHRAGMQNLTEFIGSEPSKKRKRRTSFTPQALEILNAHFEKNTHPSGQEMTEIAEKLNYDREVVRVWFCNKRQALKNTIKRLKQHEPATAVPLEPLTDSLEENS
Protein: Discoidin domain-containing receptor 2 (Discoidin domain receptor 2) (EC 2.7.10.1) (CD167 antigen-like family member B) (Neurotrophic tyrosine kinase, receptor-related 3) (Receptor protein-tyrosine kinase TKT) (Tyrosine-protein kinase TYRO10) (CD antigen CD167b) (Q62371)
Organism: Mus musculus (Mouse)
Function: Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
Sequence:
MIPIPRMPLVLLLLLLILGSAKAQVNPAICRYPLGMSGGHIPDEDITASSQWSESTAAKYGRLDSEEGDGAWCPEIPVQPDDLKEFLQIDLRTLHFITLVGTQGRHAGGHGIEFAPMYKINYSRDGSRWISWRNRHGKQVLDGNSNPYDVFLKDLEPPIVARFVRLIPVTDHSMNVCMRVELYGCVWLDGLVSYNAPAGQQFVLPGGSIIYLNDSVYDGAVGYSMTEGLGQLTDGVSGLDDFTQTHEYHVWPGYDYVGWRNESATNGFIEIMFEFDRIRNFTTMKVHCNNMFAKGVKIFKEVQCYFRSEASEWEPTAVYFPLVLDDVNPSARFVTVPLHHRMASAIKCQYHFADTWMMFSEITFQSDAAMYNNSGALPTSPMAPTTYDPMLKVDDSNTRILIGCLVAIIFILLAIIVIILWRQFWQKMLEKASRRMLDDEMTVSLSLPSESSMFNNNRSSSPSEQESNSTYDRIFPLRPDYQEPSRLIRKLPEFAPGEEESGCSGVVKPAQPNGPEGVPHYAEADIVNLQGVTGGNTYCVPAVTMDLLSGKDVAVEEFPRKLLAFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITEDPLCMITEYMENGDLNQFLSRHEPLSSCSSDATVSYANLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQVIENTGEFFRDQGRQIYLPQPALCPDSVYKLMLSCWRRETKHRPSFQEIHLLLLQQGAE
Protein: (+)-borneol dehydrogenase 1 (SoBDH1) (EC 1.1.1.198) (A0A8F5SIS3)
Organism: Salvia officinalis (Sage)
Function: Involved in the biosynthesis of monoterpene natural products related to camphor. Catalayzes the oxidation of (+)-borneol to (+)-camphor. Shows absolute selectivity towards (+)-borneol. Catalyzes the oxidation of (+)-isoborneol to (-)-camphor. Shows absolute selectivity towards (+)-isoborneol.
Interaction partners:
Sequence:
MNSSSAVSKRLEGKVAIVTGGASGIGASTVSLFHDHGAKVVIADIQDNLGQTLAGRLGRNISYIHCDVTDENQVRALVDATVAKHGGVDIMFSNAGIVEGPTVSIFDADKGALERLLGINLVGGFLAAKHAARVMSPTKKGCIIFTASACTEVAGISGPGYVASKYGIVGLMKSLAAELGSHGIRANCVSPFGVLTGIAAGDDKTKLMFEGLMSKVGNLKGKILTADDVAKAALYLASDEASYVSGVNLVLDGGYSVVNP
Protein: NMDA receptor synaptonuclear signaling and neuronal migration factor (Juxtasynaptic attractor of caldendrin on dendritic boutons protein) (Jacob protein) (Nasal embryonic luteinizing hormone-releasing hormone factor) (Nasal embryonic LHRH factor) (Q99NF2)
Organism: Mus musculus (Mouse)
Function: Couples NMDA-sensitive glutamate receptor signaling to the nucleus and triggers long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. Part of the cAMP response element-binding protein (CREB) shut-off signaling pathway. Stimulates outgrowth of olfactory axons and migration of gonadotropin-releasing hormone (GnRH) and luteinizing-hormone-releasing hormone (LHRH) neuronal cells.
Subcellular location: Nucleus. Nucleus envelope {ECO:0000250}. Nucleus membrane {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane; Peripheral membrane protein. Cell projection, dendrite {ECO:0000250}. Synapse {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Postsynaptic density {ECO:0000250}. Membrane {ECO:0000250}. Note=Found on the outside of the luteinizing-hormone-releasing hormone (LHRH) cell membrane and axons projecting from the olfactory pit and epithelium. Associates with transcriptionally active chromatin regions. Detected at the nuclear membranes of CA1 neurons. Cortical cytoskeleton. Localized in proximal apical dendrites. Colocalizes with CABP1 in dendrites and dendritic spines. Myristoylation is a prerequisite for extranuclear localization. Translocates from dendrites to the nucleus during NMDA receptor-dependent long-term potentiation (LTP) induction of synaptic transmission at Schaffer collateral/CA1 synapses of hippocampal primary neurons and in an importin-dependent manner (By similarity). {ECO:0000250}.
Interaction partners:
- Prokineticin receptor 2
- Neuromedin-K receptor
- Heparan-sulfate 6-O-sulfotransferase 1
- KiSS-1 receptor
Sequence:
MGAAASRRRALRSEAMSSVAAKVRAARAFGEYLSQSHPENRNGADHLLADAYSGHDGSPEMQPAPQNKRRLSLVSNGRYEGSISDEAVSGKPAIEGPQPHVYTISREPALLPGSEAEAIELAVVKGRRQRERHPHHHSQPLRASPGSSREDISRPCQSWAGSRQGSKECPGCAQLVPGPSSRAFGLEQPPLPEAPGRHKKLERMYSVDGVSDDVPIRTWFPKENLFSFQTATTTMQAISVFRGYAERKRRKRENDSASVIQRNFRKHLRMVGSRRVKAQTFAERRERSFSRSWSDPTPMKADTSHDSRDSSDLQSSHCTLDEACEDLDWDTEKGLEAMACNTEGFLPPKVMLISSKVPKAEYIPTIIRRDDPSIIPILYDHEHATFEDILEEIEKKLNIYHKGAKIWKMLIFCQGGPGHLYLLKNKVATFAKVEKEEDMIHFWKRLSRLMSKVNPEPNVIHIMGCYILGNPNGEKLFQNLRTLMTPYKVTFESPLELSAQGKQMIETYFDFRLYRLWKSRQHSKLLDFDDVL
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2 (A0A8I6AGR8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAVRKKDGGPNVKYYEAADTVTQFDNVRLWLGKNYKKYIQAEPPTNKSLSSLVVQLLQFQEEVFGKHVSNAPLTKLPIKCFLDFKAGGSLCHILAAAYKFKSDQGWRRYDFQNPSRMDRNVEMFMTIEKSLVQNNCLSRPNIFLCPEIEPKLLGKLKDIVKRHQGTISEDKSNASHVVYPAPGNLEEEEWVRPVMKRDKQVLLHWGYYPDSYDTWIPASEIEASVEDAPTPEKPRKVHAKWILDTDTFNEWMNEEDYEVSDDKSPVSRRKKISAKTLTDEVNSPDADRRDKKGGNYKKRKRSPSPSPTPEAKKKNAKKGPSTPYTKSKRGHREEEQEDLTKDMDEPSPVPNVEEVTLPKTVNTKKDSESAPVKGGTMTDLDEQDDESMETTGKDEDENSTGNKGEQTKSADLHEDNVTEQTHHIIVPSYAAWFDYNSVHAIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTACRRNLAGDVCAIMRVHAFLEQWGLINYQVDAESRPTPMGPPPTSHFHVLADTPSGLVPLQPKPPQQGSASQQMLNFPDKGKEKPADMQNFGLRTDMYTKKNIPSKSKAAASATREWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDPYLEDSEASLGPLAYQPIPFSQSGNPVMSTVAFLASVVDPRVASAAAKSALEEFSKMKEEVPTALVEAHVRKVEEAAKVTGKADPAFGLESSGIAGTASDEPERIEESGTEEARAESQAADEKKEPKEPREGGGAVEEEAKEEISEAPKKDEEKGKEADSEKESEKSDGDPIVDPEKDKEPTEGQEEGLKEVAEPEGERKAKVERDIGEGNLSTAAAAALAAAAVKAKHLAAVEERKIKSLVALLVETQMKKLEIKLRHFEELETIMDREREALEYQRQQLLADRQAFHMEQLKYAEMRARQQHFQQMQQQPPPPPPPPPPPALPPGSQPIPPTGAAAPATVHGLAVAPASVASAPPGGGAPPGTLGPSEQIGQAGTTAGPQQPQQAGAPQPGAVPPGVPPPGPHGPSPFPNQQTPPSMMPGAVPGSGHPGVAGNAPLGLPFGLPLPPPAAPSIIPFGSLADSISINLPPPNLHGHHHLPFAPGTIPPPNLPVSMANPLHPNLPATTTMPSSLPLGPGLGSAAAQSPAIVAAVQGSLLPSASPLPDPGTPLPPDPTAPSPGTVTPVPPPQ
Protein: Transcriptional activator hap2 (P24488)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Global regulator of respiratory functions in yeast cells. It belongs to a complex that binds to the sequence CCAAT located upstream of genes involved in mitochondrial electron transport.
Subcellular location: Nucleus.
Interaction partners:
- Transcriptional activator hap5
- Transcriptional activator hap3
- CCAAT-binding factor complex subunit php4
- Iron-sensing transcriptional repressor
- DNA polymerase epsilon subunit C
- Zinc finger protein rst2
- Monothiol glutaredoxin-4
- Uncharacterized bolA-like protein C8C9.11
- Monothiol glutaredoxin-3
Sequence:
MNPYEPVEGLYVNAKQYHRILKRREARAKLEERLRGVQTTKKPYLHESRHKHAMRRPRGPGGRFLTADKVSKLRAQEAAEAAANGGSTGDDVNATNANDATVPATVSSEVTHTSEGYADSNDSRPSSISNSSESPAPINSATASMSPANNTSGNNITSPNVRGELDMSGNIAMSGGPTNTASTSGPVPHDMTVLPQTDSNTSNLMSSGSQLGSFATASTNGNNSTTTTTSSAAHPGSFHKGTNDYSSTLAGNEHSAFPGLDVYHDDSVSAGAAFIPHNPMDSIDHLDVNDPTATGLPVLPASDIDPLNLTGNTQDSMIIGQQTYPSHGSSGTMK
Protein: Somatotropin (Growth hormone) (P01244)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
Subcellular location: Secreted.
Interaction partners:
- Prolactin
- Growth hormone receptor
- Prolactin-6A1
- Appetite-regulating hormone
- Somatoliberin
- Leptin
- Erythropoietin
- Pro-opiomelanocortin
- Granulocyte colony-stimulating factor
- Ciliary neurotrophic factor
Sequence:
MAADSQTPWLLTFSLLCLLWPQEAGAFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKEEAQQRTDMELLRFSLLLIQSWLGPVQFLSRIFTNSLMFGTSDRVYEKLKDLEEGIQALMQELEDGSPRIGQILKQTYDKFDANMRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFAESSCAF
Protein: Proteasome subunit alpha 2 (20S proteasome alpha subunit 2) (Proteasome core protein PrcA 2) (Q53084)
Organism: Rhodococcus erythropolis (Arthrobacter picolinophilus)
Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
Interaction partners:
- Proteasome subunit beta 2
- Proteasome-associated ATPase
- Prokaryotic ubiquitin-like protein Pup 2
- Hypothetical protein
- Pup--protein ligase 2
- Pup deamidase/depupylase
- Glycerol kinase
- Glycerol kinase
- AAA family ATPase
Sequence:
MTMPYYASAEQIMRDRSELARKGIARGRSVVVLTYRDGVLFVAENPSRALHKVSELYDRLGFAAVGKYNEFENLRRAGIVHADMRGYSYDRRDVTGRSLANAYAQTLGTIFTEQPKPYEVEICVAEIGRFGSSTPAQLYRITYDGSIADEQEFVVMGGTTEPIVTAMRESYQRDLDLESAVRLAVGALQKGGPAPAGTTEAEPRTLDVSALEVAVLDSNRPRRAFKRIAGSSLEEMLPTPAATEDAPPANGDAPS
Protein: Cellular communication network factor 6 (CCN family member 6) (WNT1-inducible-signaling pathway protein 3) (WISP-3) (O95389)
Organism: Homo sapiens (Human)
Function: Plays a role in mitochondrial electron transport and mitochondrial respiration. Through its regulation of the mitochondrial function may play a role in normal postnatal skeletal growth and cartilage homeostasis.
Subcellular location: Secreted {ECO:0000269|PubMed:27252383}. Mitochondrion {ECO:0000269|PubMed:27252383}. Note=Associated with membranes. {ECO:0000269|PubMed:27252383}.
Interaction partners:
- Proto-oncogene Wnt-1
Sequence:
MQGLLFSTLLLAGLAQFCCRVQGTGPLDTTPEGRPGEVSDAPQRKQFCHWPCKCPQQKPRCPPGVSLVRDGCGCCKICAKQPGEICNEADLCDPHKGLYCDYSVDRPRYETGVCAYLVAVGCEFNQVHYHNGQVFQPNPLFSCLCVSGAIGCTPLFIPKLAGSHCSGAKGGKKSDQSNCSLEPLLQQLSTSYKTMPAYRNLPLIWKKKCLVQATKWTPCSRTCGMGISNRVTNENSNCEMRKEKRLCYIQPCDSNILKTIKIPKGKTCQPTFQLSKAEKFVFSGCSSTQSYKPTFCGICLDKRCCIPNKSKMITIQFDCPNEGSFKWKMLWITSCVCQRNCREPGDIFSELKIL
Protein: Basic membrane protein A (Immunodominant antigen P39) (Probable substrate-binding protein BmpA) (Q45010)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Not known; immunogenic protein.
Subcellular location: Cell inner membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Ribose/galactose ABC transporter, permease protein
- Sugar ABC transporter, ATP-binding protein
- Flagellar filament 41 kDa core protein
- Ribose/galactose ABC transporter, permease protein
- Chaperonin GroEL
- Basic membrane protein C
- Small ribosomal subunit protein uS12
Sequence:
MNKILLLILLESIVFLSCSGKGSLGSEIPKVSLIIDGTFDDKSFNESALNGVKKVKEEFKIELVLKESSSNSYLSDLEGLKDAGSDLIWLIGYRFSDVAKVAALQNPDMKYAIIDPIYSNDPIPANLVGMTFRAQEGAFLTGYIAAKLSKTGKIGFLGGIEGEIVDAFRYGYEAGAKYANKDIKISTQYIGSFADLEAGRSVATRMYSDEIDIIHHAAGLGGIGAIEVAKELGSGHYIIGVDEDQAYLAPDNVITSTTKDVGRALNIFTSNHLKTNTFEGGKLINYGLKEGVVGFVRNPKMISFELEKEIDNLSSKIINKEIIVPSNKESYEKFLKEFI
Protein: Down syndrome cell adhesion molecule 1, isoform T (Q0E9I6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVAQYYDTDVNKAYVIRGNAAVLKCEIPSFVADFVSVVSWHTDQNEDFLPGSEYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGSVAPKVNKNDEFSHDRIAIGGMVALRCPAQSFPVPVYRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVAPQISPFSFGDEPLNRGEVASVNCVVPKGDLPLDIYWTLNSALIVNGEMGFTLVRLNKRTSSLNVDSLEAVHRGSYKCIANNSAGYAEYVSTLDVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV