wanglab/gogpt-training-data huggingface dataset:
Protein: RecQ-like DNA helicase Blm (EC 5.6.2.4) (Bloom syndrome helicase ortholog) (Bloom syndrome protein homolog) (Dmblm) (DNA 3'-5' helicase BLM) (Mutagen-sensitive protein 309) (RecQ helicase homolog) (Q9VGI8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA topoisomerase 3-alpha
- Replication protein A 70 kDa DNA-binding subunit
- DEAD-box ATP-dependent DNA helicase Fancm
- GEO08380p1
- DNA repair protein Rad51 homolog
- Mlh1, isoform A
- DNA topoisomerase 3-beta
- Crossover junction endonuclease MUS81
- DNA repair endonuclease XPF
- CG9273 protein
Sequence:
MSKKPVAQRKQLTLSSFIGLDGNSQSQPKSRAASVRSKPPAVYNPIFLDASSSDDETTEISSQSNNGTIATKKSSRDPRTAKLKKHTYLDLSVSPLAKLSAKKYARDSPKKPTSLDLSVSPLAELLAKKSDRDSPKKPVQNENSYTYRGLSESPVENKSIGDTLRKPPQKERKTSIVWLSDSPEKKVTQNERKILDSPLQRFSFEDFPNKENGNRHHLLTLPDSPPPPQPVKKPEKTMWQNETKTIQDKDSPANPLVSNNLASISTLLDSSRAPNTYKGSSRNLFEDSPEKSGSGEQGYKLGSAKENEIPTKPATASLERNSVTSSPSPAAPLKPRYSVAFDNSLADYLKDLAQNDNFSIDPNKQNTETLKSTLGFFRNTYVELMEKYCSLIDQIPAMHFNEIAGFQPNTFLKLKVMRQKFKARTQLVQNSLDKKESQLKAEQEALEKEEIEMQAEQAQQTVLSSSSPEKSRPIMPLPKVQEIKDEKIPNRNQLIHDLCGEPDNFSPPSSPRDTQLIPKRQQLINDLCGEPDDFSPPSKQNDPHLLRKCEELVHDLCEEPDDYLAQSMMLDGDLEEEQLNGPTQGTTTSGMDDDEDDLEGLLAEIEDEHQKMQGRRSEFNGYSYKELEAVKVKEKHKETPINISLDDDGFPEYDEAMFEQMHSQAAANKSRVSSAGPSTSKSVVPTKQTSALHSQKLSGNFHANVHNDGITGEFDGQKFEHSTRLMHGLSYSFGLKSFRPNQLQVINATLLGNDCFVLMPTGGGKSLCYQLPAILTEGVTIVISPLKSLIFDQINKLASLDICAKSLSGEQKMADVMAIYRDLESQPPMVKLLYVTPEKISSSARFQDTLDTLNSNNYISRFVIDEAHCVSQWGHDFRPDYKKLGVLKKRFPNVPTIALTATATPRVRLDILAQLNLKNCKWFLSSFNRSNLRYRVLPKKGVSTLDDISRYIRSKPQHFSGIIYCLSRKECDETSKKMCKDGVRAVSYHAGLTDTDRESRQKDWLTGKMRVICATVAFGMGIDKPDVRFVLHYSLPKSIEGYYQEAGRAGRDGDVADCILYYNYSDMLRIKKMLDSDKALQYNVKKIHVDNLYRIVGYCENLTDCRRAQQLDYFGEHFTSEQCLENRETACDNCINKRAYKAVDALEHARKAARAVKDLCSGRSRFTLLHIADVLKGSKIKKIIDFNHHKTPHHGVLKDWDKNDVHRLLRKMVIDGFLREDLIFTNDFPQAYLYLGNNISKLMEGTPNFEFAVTKNAKEAKAAVGSVSDGATSSTADGQSGMREIHERCYTDLLDLCRTIASQRNVTMASIMNIQALKSMAETLPITEKDMCSIPHVTKANFDKYGAKLLEITSNYASEKLLMQAVLDEEEEQAAAKQRPSTSGWNNESVDWDMAVASQGNANTSGASGFNSFRAGKRKKIYKSGASKRYKTSTTSPAARKTTSARGRGGRAGAKRAESSASSASGWKSKKTGNSFGFDLMPLPGSK
Protein: Olfactory receptor 96 (Olfactory receptor MOR121-1) (Olfactory receptor Olfr96) (Olfactory receptor family 11 subfamily A member 4) (Q8VFE3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Beta-adrenergic receptor kinase 1
Sequence:
MGILSTGNQTVTEFVLLGFHEVPGLHLLFFSVFTILYASIITGNMLIAVVVVSSQRLHTPMYFFLVNLSFIEIVYTSTVVPKMLEGFLQEATISVAGCLLQFFVFGSLATDECFLLAVMAYDRYLAICHPLRYPHLMGPQWCLGLVLTVWLSGFMVDGLVVALMAQLRFCGPNLVDHFYCDFSPLMVLACSDTQVAQVTTFVLSVVFLTVPFGLVLISYAQIVVTVLRVPSGTRRTKAFSTCSSHLAVVSTFYGTLMVLYIVPSAVHSQLLSKVIALLYTVVTPIFNPVIYTLRNQEVQQALRRLLYCKPTEM
Protein: adenylate cyclase (EC 4.6.1.1) (Q9VK52)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Ras-like protein 1
- cAMP-dependent protein kinase catalytic subunit 1
- cAMP-dependent protein kinase catalytic subunit 2
- IP06402p
- Bis
- LD28489p
- Inosine triphosphate pyrophosphatase
- Molybdenum cofactor biosynthesis protein 1
- GTP cyclohydrolase 1
- 3',5'-cyclic-AMP phosphodiesterase, isoform I
Sequence:
MYKKTAYAPRKCYLDYTDERLWERGYLKAKCKELCLEEEYKKYQIRLMISYLTVFFPLFIFVVVGCELCPWIFSEQKKLIYYESLTAIVVLVAVPGILSINFFESFVLRHRWIMVFSSILSAYIVVLVDIFQILVFHFKYHWPLNTLYDVFVLCMIYMFLPIPSIRGAALLATSVSLMYIGLFIYFLKSDDEDISEVVHDLDTICVDIFHYLGFNLMGIFFRIMNDTMVRSSFLDRHQFLKEEMWLRQARQQESMLLDSILPPQIAKPIQQSIKERIMLSETDSDRIVVNARRTENFMAIQIHPDVSILYADVVNYTHLTTTLTVEKLVKVLHDLYGRFDMAASTFKVQRIKFLGDCYYCVAGLGEADPDHARMAVSLGISMIANIQEVRAHRALDIDMRIGVHSGTLLAGVIGQAKLQYDIWGPDVDIANRLEATGKPGYVHVSGRTLSSLNVAEYTVFPGTEVAQSDPILQKQPMTTYLLTAAPSRNSVRSVDAVHSYAEIDINALGASRKSPILRPTLMSDELREEFKKMPVGGFNIRSPCCRDNSNDEKVNHGLGMFCVAFKDSSLEWSYLHKPDFILKYSVLLAWGIGCCLIYIQIVNDKFTICVECIVIDMVVFTFLTSLLFISWFKKVCWWRCVENDSRKYGRVSCKLFKIWERIQHSFVLRVTIYMSIVASYYLLISTILLNCDKNQYELDVINSKLYHYDIVTDNCFNPWVFTDMISLIVGVSYTFARIPFALKMLITCCATVAYLVIVFFQYSFIFEHSATTTPFMKAELAHCLRVCMMLLTMYAKERQSEFNTKINFKINQDLQGKQKAADITNKSIIILLTNILPSHVVEVYLDSVANHELYYENYKMVSVMFAMLINFQMDLPSLRVLNDIITEFDRLLNAYKEYYVVEKIKVVGCTYMAACGLDFTLAKSKFGSRTHASYSSELEQVLYRKESKGTENDHDEVAFIMTTFALDLMRVLSVCNKAYAGRPFDRALSTGEICIGISTGEIMAGVVGASQPHYDIWGNPVNMASRMESTGLPGHIHVTQETANILEQFDIMCMYRGMTFVKGRGEIPTYFVGIDDNLKFLPSNVKKNNMSKRFSILSSLVPVHSRSTTSSEYI
Protein: Succinylglutamate desuccinylase (EC 3.5.1.96) (O50177)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
Interaction partners:
- N-succinylglutamate 5-semialdehyde dehydrogenase
- N-succinylarginine dihydrolase
- Arginine N-succinyltransferase subunit beta
- Arginine N-succinyltransferase subunit alpha
- NAD-specific glutamate dehydrogenase
- Succinylornithine transaminase/acetylornithine aminotransferase
- Topoisomerase II
- Gamma-glutamyl phosphate reductase
- Bifunctional protein PutA
- Arginine/ornithine transport ATP-binding protein AotP
Sequence:
MLALGKLLDLTLAGREPTEKIQLTADGTRLHWLAEGALEVTPIGARDNGVDLLLSAGIHGNETAPIELLERLIRKVAAGTLKPAARVLFLFGNPEAIRRGERYVEQDMNRLFNGRHEEGSGNEAFRAAELERLAQVFFSKTERVHLHYDLHTAIRGSKIEQFALYPWAEGRQHSRSELARLRDAGIEAVLLQNKPGITFSAYTYGQLGAEAFTLELGKARPFGENQEVNLERLERSLELLIDGSEEQPDGSRLDGLKLFSVSREVIKHSDHFRLHLDDDVANFTELSPGYLLAEDIGGTRWVVDEVGARIIFPNPRVKNGLRAGILVVPAKL
Protein: Uncharacterized oxidoreductase F53C11.3 (EC 1.-.-.-) (Q93761)
Organism: Caenorhabditis elegans
Interaction partners:
- Fatty acid synthase
- Probable 2,4-dienoyl-CoA reductase decr-1.2 [
Sequence:
MAHCLHPEKFFPVVKSVALPPGSLNGKVALVTGGGTGLGKAIATTFAHLGASVAIAARRLDVLEKTADEIRSSTGGVCEPFQMDVKDPAKVAKAFDAVEKKLGHTPDILINNAAGNFIMATERLSPNAYGTIIDIVLKGTLHVTTELGRRCIQQKRGASVLSITTLYAQSGAPFVVPSAVSKAGVENMTKSLASEWAKHGLRFNAIAPGPIPTEGAFGRLFAGELKDSGDAMKASVPVGRLGHPEEIANLAAFMSSDFMSWMNGAIIDFDGGQQHIHHGSHMGQFLHEWDNEKWEETENLIRGRTGKEKKSKL
Protein: Transcriptional repressor (LexA family) (Q72P22)
Organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Interaction partners:
Sequence:
MNRQRSRRNELHPTQKKLLELLKRWKDEPRTIRELMEALDLKYPNLVYHHIEQLENKGYLKRNPNNPKDYEIVSDPEESNIVYLNRYGEAQCGPNGTILDGDPVERIPLSRKMLPFSSSDGFIVKARGNSMIPRIKDGDLVIAKKASDANDKALIVCVQNGKVLIKQLRKSETGILLLSLNDEFDPITINPDKDDFKIEGEVKLILSYT
Protein: Carboxypeptidase N catalytic chain precursor (EC 3.4.17.3) (Carboxypeptidase N, polypeptide 1) (Q6NY94)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLSGSSLIWIGALLLGLEASLTGASDFQHHGYEEMVRALFAVQSECPYITRIYSIGRSTEGRHLYVLEFSDNPGIHETLEPEFKYVGNMHGNEVLGRELLIYLSQFLCEEYRAGNERITRLIHDTRIHILPSMNPDGYEVAARQGPEFNGYLVGRGNSKEVDLNRNFPDLNALMYYYEKHNGQNHHLPLPDNWELQVEPETLAVIKWMQNYNFVLSANLHGGAVVANYPFDKSREPRLRGKTTYSATTDDKIFRKLAKTYSYAHSWMHKGWNCGDYFDEGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPATALANEWLANREALVSYMEQVHHGIKGMVYDENNNAISNAVISVAGISHDITSGTLGDYFRLLLPGTYTVTASAPGYQPSTSTVTVGPAEAIQLHFTLRAQPKGTNLNVKPYLNKKGLSTAKIPPTNLGPR
Protein: Cyclin-dependent kinase 17 (EC 2.7.11.22) (Cell division protein kinase 17) (PCTAIRE-motif protein kinase) (Q8I7M8)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase, which, in association with cyy-1, regulates the trafficking of synaptic vesicles in the DA9 motor neuron and probably also in the DD motor neurons and in RIA interneurons.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20510931}. Cell projection, dendrite {ECO:0000269|PubMed:20510931}. Cell projection, axon {ECO:0000269|PubMed:20510931}. Note=Evenly distributed in the dendrite, the axon and the cell body of the DA motor neuron. {ECO:0000269|PubMed:20510931}.
Interaction partners:
- Cyclin-Y
- Cyclin-dependent kinase 5 activator 1
- Cell division control protein
- WD repeat-containing protein fzy-1
- Fizzy-related protein homolog
Sequence:
MTAYSPADSNAEARLLSGGSDPISDTENLLDLAYEVGTSSSDNTRYDRESENDEEEIGVGWEDTTSSSLNKRMCKSATFHDFCDDSEYSRRPVTTLHEEDFDEEEEDEFEDASDRRNLDEDDVEYEDEDDEDDIVVEEEEITPEDIEHSPTGVTTQTTPPSNNTSKSKKKKKRKSDEEDGLRKMKKSSTFASFLNMFVSRRRSGRDSGERLMSRSTCMLRPSISLSVVQESMILGSDGESVEVSPCTSDQTPTGVPPRYIVNVKMRQKTARKWSEEEIQKRLSLPADLRLPVAVVDKLNRTPTLDQPLTRKNRRASLSEIGFGKLETYEKLDKLGEGTYATVFRGRSILTNKFVALKEIRLEQEEGAPCTAIREVSLLRNLRHANVVTLHDIIHTDRLLTLVFEYVDRDLKQYMDSCNNAMQMNNIRLFLYQLLRGLAYCHQRRVLHRDLKPQNLLITAKGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSTDYSTHIDMWGVGCILFEMIAGRALFPGGTPTEQLGLIFRTLGSPRPDRHPTICEKPTFYPYANRHYNPDPLCRQIPRIDAHGFELLMKFLQYEGKDRVSAAEAVKHPFLRTIAVKCCHLRDEQSVLEADGIHIERELLASDHHHSSRRHHRGTLVKDKYRMHSSHHT
Protein: Glycosyltransferase 8 domain-containing protein 1 (EC 2.4.1.-) (Q68CQ7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSFRKVNIIILVLAVALFLLVLHHNFLSLSSLLRNEVTDSGIVGPQPIDFVPNALRHAVDGRQEEIPVVIAASEDRLGGAIAAINSIQHNTRSNVIFYIVTLNNTADHLRSWLNSDSLKSIRYKIVNFDPKLLEGKVKEDPDQGESMKPLTFARFYLPILVPSAKKAIYMDDDVIVQGDILALYNTALKPGHAAAFSEDCDSASTKVVIRGAGNQYNYIGYLDYKKERIRKLSMKASTCSFNPGVFVANLTEWKRQNITNQLEKWMKLNVEEGLYSRTLAGSITTPPLLIVFYQQHSTIDPMWNVRHLGSSAGKRYSPQFVKAAKLLHWNGHLKPWGRTASYTDVWEKWYIPDPTGKFNLIRRYTEISNIK
Protein: Maltose/maltodextrin transport system permease protein MalF (P02916)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:18456666}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:18456666}; Periplasmic side {ECO:0000269|PubMed:18456666}. Note=A substantial portion of it protrudes into the periplasmic space; inserts in an SRP- and Sec-dependent, YidC-independent fashion into the membrane.
Interaction partners:
- Maltose/maltodextrin import ATP-binding protein MalK
- Maltose/maltodextrin transport system permease protein MalG
- Maltose/maltodextrin-binding periplasmic protein
- Maltoporin
- Maltose operon periplasmic protein
- sn-glycerol-3-phosphate import ATP-binding protein UgpC
- sn-glycerol-3-phosphate transport system permease protein UgpE
- PTS system glucose-specific EIIA component
- Inner membrane ABC transporter permease protein YcjP
- sn-glycerol-3-phosphate transport system permease protein UgpA
Sequence:
MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANRKAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTYNFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNRQALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSITADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGMVLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGVKPAWFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLPLLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIAFEGGGGQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD
Protein: Excisionase (P03699)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Part of the excision complex necessary for the excision of prophage from the host genome by site-specific recombination at the att site.
Interaction partners:
Sequence:
MYLTLQEWNARQRRPRSLETVRRWVRECRIFPPPVKDGREYLFHESAVKVDLNRPVTGGLLKRIRNGKKAKS
Protein: Large ribosomal subunit protein mL65 (28S ribosomal protein S30, mitochondrial) (MRP-S30) (S30mt) (P82924)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279123}.
Interaction partners:
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS29
- MRPL41 protein
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS31
- Large ribosomal subunit protein mL37
- Small ribosomal subunit protein bS1m
- Small ribosomal subunit protein uS7m
Sequence:
MAATRCWRFVLRSPGLSLHTAAEATVTAPEVTGSDVKAAPVARYPPIVASLTADSKAARQRRVERWQATVHAAKSVDEKLRILTKMQFMKYVVYPQTFALNADRWYQSFTKTVFLSGLPPPQAQPDREPAQVVDLAALRAAVCDCLLQEHFFLRRKKRAPIYQERYAVASPFLDQLVPSLTGLLSAYNPVLAAAALDCNRPVHFYWLRGEEIIPGGHRKGRVDAVRYQINDKPHNQIRISRQLPEFVPLDYSVPVEVPVKNCKPDKLPLFKRQYENAIFIGTKTADPLCYGHTQFHLLPDKLKRERLLKQNCADQIEVIFRANAIASLFAWTGAQAMYQGFWSEADVTRPFVSQGVITDGKYFSFFCYQLNTLALTAQADQNNPRKNICWGTQSMPLYETIEDNDVKGFNDDVLLQLVHFLLNRPEEDKAQLLVN
Protein: S-methyltransferase (Q1WMA5)
Organism: Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Interaction partners:
Sequence:
MSSHEEKPSSNKEDDDHSSYALQLVFSGALPMVLNAVIKLNVFEIIAKAGPGAKLSPSQIVSQMPTKNPEAPVVLDRMLRMLASYSVLTCSVVDFSHGSGQRVYGLSPVSKYFVKNENGGCFGPLLDLLQDKVLTDIWYELAPAVLEGGTAFNRAYNMHIFKYTGINQKFNETFNTATINHAKVIVQEILKNYKGFENLKTLVDVGGGLGVTLDLITSKYPNLKGINYDLPHVTQNAPTYPGVVHVGGDMFESVPKGDAIFMKWILHDWDDEHCLKLLKNCYKALPENGKVIAVDAILPMNPDNSSSTKHISQVDLFTLVLYHPGGKERTENEFLALVAEAGFGGIRKVCVCCDLWVMEFYK
Protein: L-2-aminoadipate reductase (EC 1.2.1.31) (EC 1.2.1.95) (Alpha-aminoadipate reductase) (Alpha-AR) (L-aminoadipate-semialdehyde dehydrogenase) (P40976)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Saccharopine dehydrogenase [NADP
- Oxalate--CoA ligase
- Putative acyl carrier protein, mitochondrial
- Aromatic amino acid aminotransferase C56E4.03
- Aromatic amino acid aminotransferase C1773.13
- Aromatic amino acid aminotransferase C569.07
- Orotidine 5'-phosphate decarboxylase
- 3-isopropylmalate dehydrogenase
- Phosphoribosylaminoimidazole carboxylase
- L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
Sequence:
MSQTAPSDTEYNQRLERWSERLKSQTISHLPTDYSRPVPSRLVEAVFERTLPEDAKTALIKVYVAAQAKGILVTPFNILLTIFIILVSRMTGDEDISIGTSSENAIPFVLRTFIQPSDSFLDLLAKVCDLEKEGSSDAVDFSDLINFLNAKLSKKDDPRKTLVHLRFYNAPDAPSENFLSTTGLDVDLTVLVSVKKPSDQLTSLRSQFTFPDLQLKLIYNQLLFSESRVNIVADQLLKLVVSASKDVTGPIGALDLMTPTQMNVLPDPTVDLDWSGYRGAIQDIFASNAAKFPDRECIVVTPSVTIDAPVTSYTYRQIDESSNILAHHLVKNGIERGDVVMVYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQIIYLSVAKPRALVVLEDAGVLSPTVVEYVEKSLELKTYVPALKLAKDGSLTGGSVSKGADDILQHVLHLKSEQTGVVVGPDSTPTLSFTSGSEGIPKGVKGRHFSLAYYFDWMAQEFNLSESDRFTMLSGIAHDPIQRDIFTPLFLGASLIVPTAEDIGTPGQLAQWANKYKVTVTHLTPAMGQLLAAQADEPIPSLHHAFFVGDILTKRDCLRLQVLANNVNVVNMYGTTETQRSVSYFVVPARSQDQTFLESQKDVIPAGRGMKNVQLLVINRFDTNKICGIGEVGEIYLRAGGLAEGYLGNDELTSKKFLKSWFADPSKFVDRTPENAPWKPYWFGIRDRMYRSGDLGRYLPTGNVECSGRADDQIKIRGFRIELGEINTHLSRHPNVRENITLVRRDKDEEPTLVAYIVPQGLNKDDFDSATESEDIVVNGLKKYRKLIHDIREYLKTKLPSYAIPSVIVPLHKMPLNPNGKIDKPALPFPDTSQLAAASRSHSKHGVDETLTATERDIRDIWLRIIPHATDVNKKASFFDIGGHSILATRLIFELRKKFAVNVPLGLVFSEPTIEGLAKEIERMKSGEMISVMDIGKEETREPEIEYGKDALDLVDLIPKEFPTSKDLGIDEPKTVFLTGANGYLGVFILRDLMTRSSNLKVIALVRASSEEHGLKRLKDSCTAYGVWDESWAQKISVVNGDLALENWGIEERKWNKLTEVVDYVIHNGALVHWVYPYSKLRGPNVMGTITALKLCSLGKGKSLSFVSSTSTVDTEYYVNLSNEITSKGGNGIPESDPLQGSSKDLHTGYGQSKWVSEYLVRQAGLRGLRGVVVRPGYILGDSKSGAINTDDFLVRMVKGCIELGLYPNINNTVNMVPADHVARVVTASAFHPEQGVIVAHVTSHPRLRFNQFLGTLSTFGFNTKLSEYVNWRIALERFVINESHDSALYPLLHFVLDNLPANTKAPELDDTNTREILKRDASWTNVDVSNGAAILEHEMGLYLSYLVAIGFLPKPTLEGKKLPEVKINEATLEKLASAGGRGGAPTH
Protein: IS1167, transposase (A0A0H2UQB1)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MEQLHFITKLLDIKDPNIQILDIINKDTHKEIIAKLDYDAPSCPECGNQLKKYDFQKPSKIPYLETTGMPTRILLRKRRFKCYHCSKMMVAETSIVKKNHQIPRIINQKIAQKLIEKISMTDIAHQLSISTSTVIRKLNDFHFKHDFSCLPEIMSWDEYAFTKGKMSFIAQDFNNLNIITVLEGRTQAIIRNHFLKYDRAVRCRVKIITMDMFSPYYDLARQLFPCAKIVLDRFHIVQHLSRAMSRVRVQIMNQLDRKSHEYKAIKRYWKLIQQDSRKLSDKHFYRPTFRMHLTNKEILNKLLSYSQDLKHHYQLYQLLLFHFQNKEPEKFFGLIEDNLKQVHPLFQTVFKTFLKDKEKIVNALQLHYSNAKLEATNNLIKLIKRNAFGFRNFENFKKRIFIALNIKKERTKFVLSRA
Protein: DNA repair protein RAD51 homolog 1 (P70099)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q06609}. Chromosome {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. Recruited at sites of DNA damage following interaction with TOPBP1 in S-phase. Colocalizes with ERCC5/XPG to nuclear foci in S phase. Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner. {ECO:0000250|UniProtKB:Q06609}.
Interaction partners:
Sequence:
MAMQMQLEANADTSVEEESFGPQPISRLEQCGISANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFTADPKKPIGGNIIAHASTTRLYLRKGRGETRICKVYDSPCLPEAEAMFAINADGVGDAKD
Protein: Ubiquitin carboxyl-terminal hydrolase creB (EC 3.4.19.12) (Carbon catabolite repression protein B) (Deubiquitinating enzyme creB) (Ubiquitin thioesterase creB) (Ubiquitin-hydrolyzing enzyme creB) (Ubiquitin-specific-processing protease creB) (Q96V54)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Ubiquitin thioesterase component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Deubiquitinates the creA catabolic repressor and the quinate permease qutD. Also plays a role in response to carbon starvation and the control of extracellular proteases activity.
Interaction partners:
- Catabolite repression protein creC
- DNA-binding protein creA
- WD repeat protein
- HECT-type ubiquitin ligase-interacting protein creD
- RNA polymerase I specific transcription initiation factor Rrn7, putative
- E3 ubiquitin-protein ligase RSP5
- Ubiquitin-like domain-containing protein
- B-zip transcription factor
- AN1-type domain-containing protein
- Polyubiquitin
Sequence:
MGSFLKSFRKDVGSAAPSVGAPPAKKEPQPLPMTPLEKMLTELGPIRGDGSDKFYGMENFGNTCYCNSILQCLYYSVPFREAVLNYPKRTPIEDLEAALAKALRYQDPNARLEAEALAEKQKAANSPRPGQPPNPQQKPEDKDSPEYKKKLALQTLPLLETTDNSVSYGIPESLFSSLKDMFESIVGSQSRIGIIRPQHFLEVLRRENEMFRTAMHQDAHEFLNLLLNEVVVDVEKAAAKLLESPQPASDVSDSVIPSSSSGSRTPNTTRWVHELFEGLLTSETQCLTCEKASQRDEVFLDLSVDLEQHSSVTSCLRKFSAEEMLCERNKFHCDNCGGLQEAEKRMKIKRLPRILALHLKRFKYTEDLQRLQKLFHRVVYPYHLRLFNTTDDAEDPDRLYELYAVVVHIGGGPYHGHYVSIIKTQDRGWLLFDDEMVEPVDKNYVRNFFGDKPGLACAYVLFYQETTMEAVMKEQEQENTEPPVEVNASTLKQNGFSSSATLAHAHSASQVPTYEDHDRFTGLKRAPTAPQLSTHPEHTTTDSESLPSPAPDPAPLTSLPPIPPIPETPPAPLTSRKSDLQSKKERVKEEKERKAAEKEKEKQRRKEIETRLKDRQRREDDDLKAALEASKVSKEDEDRRNHAENGTSKKNAGGLGRFRSLSQRLSTKESRTSLSRIPPLPNGNHTLSKVPDESEQTHPKSPTPPAPLSRPASQPLNDDLLGSPRADTLAVPTEQEHIKNSKHDRSSHGKWRSFSLRKKSFNILSS
Protein: Integrin subunit beta 1 binding protein 1 (C9J5T5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGV
Protein: Outer-membrane lipoprotein LolB (P61320)
Organism: Escherichia coli (strain K12)
Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability.
Subcellular location: Cell outer membrane; Lipid-anchor.
Interaction partners:
- Outer-membrane lipoprotein carrier protein
- Lipoprotein-releasing system transmembrane protein LolE
- Lipoprotein-releasing system ATP-binding protein LolD
- Lipoprotein-releasing system transmembrane protein LolC
- Outer membrane protein assembly factor BamD
- Cell division topological specificity factor
- Peptidoglycan-associated lipoprotein
- Cold shock-like protein CspC
- DNA topoisomerase 4 subunit A
- LPS-assembly protein LptD
Sequence:
MPLPDFRLIRLLPLAALVLTACSVTTPKGPGKSPDSPQWRQHQQDVRNLNQYQTRGAFAYISDQQKVYARFFWQQTGQDRYRLLLTNPLGSTELELNAQPGNVQLVDNKGQRYTADDAEEMIGKLTGMPIPLNSLRQWILGLPGDATDYKLDDQYRLSEITYSQNGKNWKVVYGGYDTKTQPAMPANMELTDGGQRIKLKMDNWIVK
Protein: TSET complex member tstB (Protein TSAUCER) (Q54TB8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Protein SGT1 homolog
- Luminal-binding protein 1
- CS domain-containing protein
- Activator of 90 kDa heat shock protein ATPase homolog
- Heat shock factor-type DNA-binding domain-containing protein
- RapGAP/RanGAP domain-containing protein
- Uncharacterized protein
- DEX1 C-terminal beta-sandwich domain-containing protein
- 60 kDa heat shock protein, mitochondrial
- Luminal-binding protein 2
Sequence:
MSELSESGSYNSYNSLSAGSPLPLQEIFNGAETKCQSHYLQSRINTNYEQVKQQLKESAEKKNSSKIYSSLQHLTYYKVEKDLLETILRIIDITDDKKTLRLAYYFLGEISQFKHLINNSTEIKNITTIFNKEMQHKDISRKVVSLKTTASVAPNDVLIDANILDVISGILRKVGEDPDKTQKKKGFFTRATTDLGRERSLLQYSCFVACRNRYKNNPSLFMPIVEGIKCVDPVGARHAVSLTLNYALENPSTVAATTKRFIPLLKANKGKEAVYLVDPFARRNFIKLCGHLAATPSPIGNVITMENKDFFQSLCQSVMDAHLSVAFYAINVLSRFSWPTLESAHIDAIQFDSELPHFESLAFQTSLIVGICNKMRIGFNTYSIGAYSNYSMQHGHHHLHHYHQGGSGTVGGSVPSSSSSSSSSSNITTSALSSGSSSNSSLSSQQLLLVQQQQQQLLHQQSNPFLHLACKLISVLSQSYVKYSYPKDSTTQQPIIGDWSFDEKQYQHQSVYPYHHNLSPFTGLPNPISNNNNSSNNTKDQSTTTTTSTTSSSSNSIHPFSSLTQLILNLLNISPSISIRIQALKALVWLCPSNLDQSKLYLETFRSQLRDPYHPTHLFKELFLELYKRIIATPILSPMILELVYDWIDIIPSKCDTSLVCEIWKTIVEFGKVFANEKLLASIFKILDRIVHPDFRVLAMEIQKDIIKFLGEYSNQITFEQPSRFEQCKSRSGSNQQQHLSNMSLNSIIQRLQQYSIFSPWQIRLESIDSLAKIAFQSSTVVKVHIYNFLTLLPNESHGWTTVKSNTSIIVNTLDQLLTCRAKWLPLFKSSDLSQNQIKDLKNDHTNLCLQIGLFFDQLSFDYLPLGIESKKYLGSK