wanglab/gogpt-training-data huggingface dataset:
Protein: DNA repair and recombination protein RAD54-like (EC 3.6.4.12) (F1Q8K0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks. Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby changing the homology search from the diffusion-based mechanism to a motor-guided mechanism. Also plays an essential role in RAD51-mediated synaptic complex formation which consists of three strands encased in a protein filament formed once homology is recognized. Once DNA strand exchange occured, dissociates RAD51 from nucleoprotein filaments formed on dsDNA (By similarity).
Interaction partners:
- DNA repair protein RAD51 homolog
- WRN RecQ-like helicase.
- DNA repair and recombination protein RAD54B isoform X1
- Protein VAC14 homolog
- BLM RecQ-like helicase.
- DNA repair protein RAD52 homolog
- Exonuclease 1
- FA complementation group M.
- Helicase ATP-binding domain-containing protein.
- Structure-specific endonuclease subunit MUS81
Sequence:
MRRSLAPSQVAKRKQGPDSDDEEDWEPDMEPQCKRDCREKYISPYRKPLTPLTNRPFCADGNEHEAFIRKILSKPFKIPIPNYTGVLGLRALGLRRAGVRKALHDPFEDGALVLYEPPVISAHDLIKADKEKLPVHVVVDPVLSKVLRPHQREGVKFLWDCVTGRRIENSYGCIMADEMGLGKTLQCITLIWTLLKQSPDCKPEIDKVIVVSPSSLVRNWYNEVGKWLGGRVQPVAIDGGSKDEIDSKLVNFISQQGMRIPTPILIISYETFRLHAEVLHKGKVGLVICDEGHRLKNSDNQTYLALNSMNAQRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAQEFKKRFEIPILKGRDADASDKDRAAGEQKLQELISIVNRCLIRRTSDILSKYLPVKIEQVVCCNLTPLQKELYKLFLKQAKPVESLQTGKISVSSLSSITSLKKLCNHPALIYEKCLTGEEGFDGALDLFPQNYSTKAVEPQLSGKMLVLDYILAMTRTTTSDKVVLVSNYTQTLDLFEKLCRNRRYLYVRLDGTMSIKKRAKIVERFNNPSSPEFIFMLSSKAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSTGTIEEKILQRQAHKKALSSCVVDEEQDVERHFSLGELRELFSLNEKTLSDTHDRFRCRRCVNGRQVRPPPDDSDCTCDLSNWHHCADKRGLRDPVLQASWDAAVSFVFHQRSHEDQRGVV
Protein: Conserved protein (O05436)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable peptidoglycan biosynthesis protein MviN
- Putative mutator protein MutT4
- ECF RNA polymerase sigma factor SigM
- Anti-sigma-M factor RsmA
- Pullulanase
- NYN domain-containing protein
- Uncharacterized membrane protein Rv3835
- Probable conserved proline rich membrane protein
- Probable conserved transmembrane alanine rich protein
- Probable conserved transmembrane protein
Sequence:
MTALQLGWAALARVTSAIGVVAGLGMALTVPSAAPHALAGEPSPTPFVQVRIDQVTPDVVTTSSEPHVTVSGTVTNTGDRPVRDVMVRLEHAAAVTSSTALRTSLDGGTDQYQPAADFLTVAPELDRGQEAGFTLSAPLRSLTRPSLAVNQPGIYPVLVNVNGTPDYGAPARLDNARFLLPVVGVPPDQATDFGSAVAPETTAPVWITMLWPLADRPRLAPGAPGGTVPVRLVDDDLANSLANGGRLDILLSAAEFATNREVDPDGAVGRALCLAIDPDLLITVNAMTGGYVVSDSPDGAAQLPGTPTHPGTGQAAASSWLDRLRTLVHRTCVTPLPFAQADLDALQRVNDPRLSAIATISPADIVDRILDVSSTRGATVLPDGPLTGRAINLLSTHGNTVAVAAADFSPEEQQGSSQIGSALLPATAPRRLSPRVVAAPFDPAVGAALAAAGTNPTVPTYLDPSLFVRIAHESITARRQDALGAMLWRSLEPNAAPRTQILVPPASWSLASDDAQVILTALATAIRSGLAVPRPLPAVIADAAARTEPPEPPGAYSAARGRFNDDITTQIGGQVARLWKLTSALTIDDRTGLTGVQYTAPLREDMLRALSQSLPPDTRNGLAQQRLAVVGKTIDDLFGAVTIVNPGGSYTLATEHSPLPLALHNGLAVPIRVRLQVDAPPGMTVADVGQIELPPGYLPLRVPIEVNFTQRVAVDVSLRTPDGVALGEPVRLSVHSNAYGKVLFAITLSAAAVLVTLAGRRLWHRFRGQPDRADLDRPDLPTGKHAPQRRAVASRDDEKHRV
Protein: Neurotrophin-3 (NT-3) (HDNF) (Nerve growth factor 2) (NGF-2) (Neurotrophic factor) (P20181)
Organism: Mus musculus (Mouse)
Function: Seems to promote the survival of visceral and proprioceptive sensory neurons.
Subcellular location: Secreted.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 16
- BDNF/NT-3 growth factors receptor
- High affinity nerve growth factor receptor
- NT-3 growth factor receptor
- Neurotrophic factor BDNF precursor form
- Glial cell line-derived neurotrophic factor
- Ciliary neurotrophic factor
- Platelet-derived growth factor receptor alpha
- Insulin-like growth factor 1
- Sortilin
Sequence:
MSILFYVIFLAYLRGIQGNSMDQRSLPEDSLNSLIIKLIQADILKNKLSKQMVDVKENYQSTLPKAEAPREPEQGEATRSEFQPMIATDTELLRQQRRYNSPRVLLSDSTPLEPPPLYLMEDYVGNPVVANRTSPRRKRYAEHKSHRGEYSVCDSESLWVTDKSSAIDIRGHQVTVLGEIKTGNSPVKQYFYETRCKEARPVKNGCRGIDDKHWNSQCKTSQTYVRALTSENNKLVGWRWIRIDTSCVCALSRKIGRT
Protein: Photosystem I reaction center subunit VIII (PSI-I) (P12186)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May help in the organization of the PsaL subunit.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Photosystem I reaction center subunit IX
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I reaction center subunit VI, chloroplastic
- Chlorophyll a-b binding protein
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I reaction center subunit V, chloroplastic
- Chlorophyll a-b binding protein
- Photosystem I reaction center subunit XI, chloroplastic
- Os07g0435300 protein
- Chlorophyll a-b binding protein
Sequence:
MMDFNLPSIFVPLVGLVFPAIAMASLFLYVQKNKIV
Protein: Unconventional myosin-Id (Unconventional myosin Myr 4) (F1PRN2)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Unconventional myosin that functions as actin-based motor protein with ATPase activity (By similarity). Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes. Required for normal planar cell polarity in ciliated tracheal cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement in the trachea. Required for normal, polarized cilia organization in brain ependymal epithelial cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q63357}. Perikaryon {ECO:0000250|UniProtKB:Q63357}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63357}. Early endosome {ECO:0000269|PubMed:11208135}. Cytoplasm, cell cortex {ECO:0000269|PubMed:11208135}. Note=Colocalizes with the actin cytoskeleton in the cell cortex close to the apical cell membrane (PubMed:11208135). Colocalizes with cytoplasmic puncta that are reminiscent of transport vesicles (By similarity). {ECO:0000250|UniProtKB:Q63357, ECO:0000269|PubMed:11208135}.
Interaction partners:
- Myosin XVA.
Sequence:
MAEQESLEFGKADFVLMDTVSMPEFMANLRLRFEKGRIYTFIGEVVVSVNPYKALNIYGRDTIEQYKGRELYERPPHLFAIADAAYKAMKRRSKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIVQQPGERSFHSFYQLLQGGSEQMLRSLHLQKSLSSYNYIHVGAQLKSSINDAAEFKVVADAMKVIGFKPEETQTVYKILAAILHLGNLKFMVDGDTPLIENGKVVSIIAELLSTKTDMVEKALLYRTVATGRDIIDKQHTEQEASYGRDAFAKAIYERLFCWIVTRINDIIEVKNYDTTIHGKNTVIGVLDIYGFEIFDNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIIAILDDACMNVGKVTDEMFLEALNSKLGKHGHFSSRKLCASDKILEFDRDFRIRHYAGDVVYSVIGFIDKNKDTLFQDFKRLLYNSSNPVLKNMWPEGKLSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIEHCGFQDDVAYGKTKIFIRTPRTLFTLEELRAQMLIRIVLFLQKVWRGTLARMRYKRTKAALTIIRYYRHYKVKSYIQEVARRFHGVKTMKDHGKHVKWPTPPKVLRRFEEALQAIFNRWRASQLIKSLPASDLPQVRAKVAAMEMLKGQRADLGLQRAWEGNYLASKPDTPQTSGTFVPVANELKRKDKYMNVLFSCHVRKVNRFSKVEDRAIFVTDRHLYKMDPTKQYKVMKTIPLYNLTGLSVSNGKDQLVVFHTKDNKDLIVCLFSKQPTHESRIGELVGVLVNHFKSEKRHLQVNVTNPVQCSLHGKKCTVSVETRLNQPEPDFTKNRSGFILSVPGN
Protein: Potassium-transporting ATPase potassium-binding subunit (ATP phosphohydrolase [potassium-transporting] A chain) (Potassium-binding and translocating subunit A) (Potassium-translocating ATPase A chain) (P03959)
Organism: Escherichia coli (strain K12)
Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00275, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0000269|PubMed:7896809}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00275, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0000269|PubMed:7896809}.
Interaction partners:
- Potassium-transporting ATPase KdpC subunit
- Potassium-transporting ATPase ATP-binding subunit
- Potassium-transporting ATPase KdpF subunit
- Sensor protein KdpD
- KDP operon transcriptional regulatory protein KdpE
- Low affinity potassium transport system protein Kup
- Maltose/maltodextrin import ATP-binding protein MalK
- Iron
- Maltose/maltodextrin transport system permease protein MalG
- Spermidine/putrescine import ATP-binding protein PotA
Sequence:
MAAQGFLLIATFLLVLMVLARPLGSGLARLINDIPLPGTTGVERVLFRALGVSDREMNWKQYLCAILGLNMLGLAVLFFMLLGQHYLPLNPQQLPGLSWDLALNTAVSFVTNTNWQSYSGETTLSYFSQMAGLTVQNFLSAASGIAVIFALIRAFTRQSMSTLGNAWVDLLRITLWVLVPVALLIALFFIQQGALQNFLPYQAVNTVEGAQQLLPMGPVASQEAIKMLGTNGGGFFNANSSHPFENPTALTNFVQMLAIFLIPTALCFAFGEVMGDRRQGRMLLWAMSVIFVICVGVVMWAEVQGNPHLLALGTDSSINMEGKESRFGVLVSSLFAVVTTAASCGAVIAMHDSFTALGGMVPMWLMQIGEVVFGGVGSGLYGMMLFVLLAVFIAGLMIGRTPEYLGKKIDVREMKLTALAILVTPTLVLMGAALAMMTDAGRSAMLNPGPHGFSEVLYAVSSAANNNGSAFAGLSANSPFWNCLLAFCMFVGRFGVIIPVMAIAGSLVSKKSQAASSGTLPTHGPLFVGLLIGTVLLVGALTFIPALALGPVAEYLS
Protein: Interferon regulatory factor 8 (A0A8I6AJP7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSLAQMSPKPAPLCAPLIFLSVGSRIALTHRDVIPKSVFFPRMCDRNGGRRLRQWLIEQIDSSMYPGLIWESEEKTLFRIPWKHAGKQDYNQEVDASIFKAWAVFKGKFKEGDKAEPATWKTRLRCALNKSPDFEEVTDRSQLDISEPYKVYRIVPEEEQKCKLGVAPAGCMSDVTEMECGRSEIEELIKEPSVDEYMGIAKRSPSPPEACRSQILPDWWAQQPNAGLPLVTGYTAYDAHHSALSQMVINFYYGGKLVGQATTTSLEGCRLSLSQPGLPKLYGPDGLEPVCFPAADTIPSERQRQVTRKLFGHLERGVLLHSNRKGVFVKRLCQGRVFCSGNAVVCKGRPNKLERDEVVQVFDTNMFLRDLQQFYATQSRLPDSRVVLCFGEEFPDTAPLRSKLILVQVEQLYARQMVEEAGKSCGAGSLMPALEEPQPDQAFRMFPDICTSHQRPFFRENQQITV
Protein: DNL-type zinc finger protein (Hsp70-escort protein 1) (HEP1) (mtHsp70-escort protein) (Q9D113)
Organism: Mus musculus (Mouse)
Function: May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Stress-70 protein, mitochondrial
Sequence:
MLRTALSRMPTLLRSVRTRDSGPRRLWDLGARLKTAERLRGWAWGWASGWRSSSSAPGSGRAAALGRVEADHYQLVYTCKVCGTRSSKRISKLAYHQGVVIVTCPGCQNHHIIADNLSWFSDLKGKRNIEEILAARGEEVRRVSGDGALELILEAAVPPDTPEGDEDPPNPGKMGQS
Protein: RxLR effector protein Avh52 (Avirulence homolog protein 52) (G4ZSG0)
Organism: Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines)
Function: Effector that suppresses plant defense responses during the early stages of pathogen infection. Suppresses cell death induced by effectors and PAMPs in plant hosts. Interacts with host acetyltransferase TAP1 and causes TAP1 relocation into the nucleus where it acetylates histones H2A and H3 during early infection, thereby promoting susceptibility of host plant to P.sojae.
Subcellular location: Secreted {ECO:0000269|PubMed:30346270}. Host nucleus {ECO:0000269|PubMed:30346270}.
Interaction partners:
- RxLR effector protein Avh238
Sequence:
MRLTSILVLVIAATFHTTGTALTLTKDSKAGIANGDSPASGDFIDANSARLLRRVEKDKVDYEQDEQRSFGALKDAVKKLNPVTAVKKFFKQRAKRKKVIQTARDADNNLAWAMKEVYKAAN
Protein: Protein krasavietz (Eukaryotic translation initiation factor 5C domain-containing protein) (Decp) (eIF5C domain-containing protein) (Protein extra bases) (Q9VNE2)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in memory formation.
Interaction partners:
Sequence:
MSQKTERPVLSGQRIKTRKRDEREKYDPTGFRDAVIAGLEKTEGDLEQISKYLDSAGNKLDYRRYGEVLFDILIAGGLLVPGGSISQDGEKPRTSYCIFDAPESMESMRNHEQVFVKLIRRYKYLEKMFEEEMGKVLLFVKGFTPSERIKLARMTALWLVNGSVPPNVLLVLNNEHLIKDGIALEFLLELFQTFKQEKGIAYLIQALKKGGLESKLMDFFPPNKRTEEYFKQVFLDKELNEIVKLHKAQASQEAKRELQQALIDDINDEKPYNEITSDIKDFSQRTNIPDHEIIVIIWSTIMSLGEWNKKEELVTDQAVRHLKNYCPLLQAFASTDRSELALILKVQEFCYENMNFMKAFQKIILLFYKTEVLSEEIILRWYKEGHSNKGKMHFLEQMRKFVEWLQSAEEESESEDEQKNGE
Protein: Uncharacterized HTH-type transcriptional regulator YcjW (P77615)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Putative ABC transporter periplasmic-binding protein YcjN
- Kojibiose phosphorylase
- Inner membrane ABC transporter permease protein YcjO
- D-glucoside 3-dehydrogenase
- Inner membrane ABC transporter permease protein YcjP
- D-guloside 3-dehydrogenase
- Beta-phosphoglucomutase
- 3-dehydro-D-guloside 4-epimerase
- Glucosylglycerate phosphorylase
- Outer membrane porin G
Sequence:
MSPTIYDIARVAGVSKSTVSRVLNKQTNISPEAREKVLRAIEELQYQPNKLARALTSSGFDAIMVISTRSTKTTAGNPFFSEVLHAITAKAEEEGFDVILQTSHNPAEDLQKCESKIKQKMIKGIIMLSSPADESFFAQLDKYDIPVVVIGKVEGQYAHVYSVDTDNFGDSIALTDALIESGHQNIACLHAPLDVHVSVDRVNGYKQSLAAHNIAVRDEWIVDGGYTHETALKAARQLLSQSPLPEAVFATDSLKLMSIYRAAAEKNIAIPQQLAVVGYSNETLSFILTPAPGGIDVPTQELGQQSCELLFRLISGKPSPQNITVATHMTLK
Protein: Tetratricopeptide repeat protein 8 (TPR repeat protein 8) (Bardet-Biedl syndrome 8 protein) (Q8TAM2)
Organism: Homo sapiens (Human)
Function: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17574030}. Cell projection, cilium membrane {ECO:0000269|PubMed:17574030}. Cytoplasm {ECO:0000269|PubMed:22072986}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:17574030}. Cell projection, cilium {ECO:0000250|UniProtKB:Q8VD72}.
Interaction partners:
- BBSome complex member BBS2
- BBSome complex member BBS4
- BBSome complex member BBS5
- BBSome complex member BBS1
- BBSome complex member BBS7
- Protein PTHB1
- Leucine zipper transcription factor-like protein 1
- Chaperonin-containing T-complex member BBS12
- BBSome complex assembly protein BBS10
- Rab-3A-interacting protein
Sequence:
MSSEMEPLLLAWSYFRRRKFQLCADLCTQMLEKSPYDQEPDPELPVHQAAWILKARALTEMVYIDEIDVDQEGIAEMMLDENAIAQVPRPGTSLKLPGTNQTGGPSQAVRPITQAGRPITGFLRPSTQSGRPGTMEQAIRTPRTAYTARPITSSSGRFVRLGTASMLTSPDGPFINLSRLNLTKYSQKPKLAKALFEYIFHHENDVKTIHLEDVVLHLGIYPFLLRNKNHIEKNALDLAALSTEHSQYKDWWWKVQIGKCYYRLGMYREAEKQFKSALKQQEMVDTFLYLAKVYVSLDQPVTALNLFKQGLDKFPGEVTLLCGIARIYEEMNNMSSAAEYYKEVLKQDNTHVEAIACIGSNHFYSDQPEIALRFYRRLLQMGIYNGQLFNNLGLCCFYAQQYDMTLTSFERALSLAENEEEAADVWYNLGHVAVGIGDTNLAHQCFRLALVNNNNHAEAYNNLAVLEMRKGHVEQARALLQTASSLAPHMYEPHFNFATISDKIGDLQRSYVAAQKSEAAFPDHVDTQHLIKQLRQHFAML
Protein: 17.8 kDa class I heat shock protein (17.8 kDa heat shock protein) (AtHsp17.8) (Q9LNW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cytosolic mediator for sorting and targeting of nascent chloroplast outer envelope membrane (OEM) proteins to the chloroplast. Functions as a AKR2A cofactor to facilitates the targeting of OEP7 to chloroplasts.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Heat shock 70 kDa protein 4
- Ankyrin repeat domain-containing protein 2A
- Heat shock protein 90-1
- Heat shock 70 kDa protein 5
- Chaperone protein ClpB4, mitochondrial
- 14.7 kDa heat shock protein
- Heat stress transcription factor A-2
- Outer envelope membrane protein 7
- Heat shock 70 kDa protein 8
- Chaperone protein ClpB1
Sequence:
MSLIPSFFGNNRRSNSIFDPFSLDVWDPFKELQFPSSLSGETSAITNARVDWKETAEAHVFKADLPGMKKEEVKVEIEDDSVLKISGERHVEKEEKQDTWHRVERSSGQFSRKFKLPENVKMDQVKASMENGVLTVTVPKVEEAKKKAQVKSIDISG
Protein: adenylate cyclase (EC 4.6.1.1) (M9PD54)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDVELEEEEERICLRTAEEGQLANMDDDKLVSDEVHLRQLSATPSSAFSLQHSRGSDTKEEAPPEGGTMGGKSAAPREEGEPDERVVLRRAVDKGAIALAQIDDLKLEGDDDDEAVVNGEEVDGLGLSNPAAQTTDDEQITVNGTGAAATSSVAADAASSEDAASTAMATPDMSKIPRLPGDGAQMEDNGSGDLPPSLRASTTSILSNLRKKQQGGPLRGGVAKQTPLRVQSVRIVEAKRAYGPKRRTESCSIFGNSNFEHDLESGNSLASIPGQSQRPLNNEMYSAFKSGNVVKGILCPSLTNSFKQSSLERSYLTYTHRQRQKSLIIVNVVDFVLKIVLAFVWIMRRSELGPIESDDGTSMATAITWSVCCGIANMAICFLGYWRCFANNYLHWAAVCTWVLFNIQGFVGQGVGFADREYLVWYILFVIFVPYAMLPLPLKWCVVGGTITASCHLAVITIIKLQHGEATINPECVLFQIFANFILYTAINVAGMYTKYLTDRGQRLAFIETHKAMEHKKESEKELQRTQKLLDSILPNIVNNQIRSEMYKGTDPTVETQFNKLYVYPMDNVSILFADIKGFTELASKTSAQQLVKILNDLFARFDRIAEDNHCLRVKLLGDCYYCVSQFESDNWKTRPDHAVCSVETGLHMIKAIKDVRLHTHVDLNMRIGIHSGSVMCGVLGNKKWHFDVWSNDVIIANHMESGGIPGRVHISEATLKCLNDAYEVEPGNGGCRDNHLKMLNVKTYLIKRTEPLRPKRRFGTRSSAHLAGSVATAAPPCATPTALPKSISASGSGSIGGVTATGNDGASIDGRSLEYAATIAVPAQQPTQLLQQQQKKNISLNSLPNVVEGVAMDSRRIRNGCGVMGGAGGTGGGGTGPCGMSTVSSPTAMMSAPLEVQLRPRNGACSIQNLAEAIDGKGLIIEDESTTDWIPEIPFKNLNSPEDGLNRADSILVDTKEDHRVSVAVLDEEIDEFIEQNIQINSNKEIRREYLNPWTLKFKDKSQEQKFCQLREDMFRSNMLCVFVIWIFMVLCQVIIIPRCTRLIICLSVGTVILTFCCVLVMAEEFPGLPRCLKTNSAKLVHQRQRRTLFICGVIVSMCMLSAIGLVLCPSSTYIGTADEHSRFLRMVSPYSNISMTEKEFKLNVYLSATIHHNITISTPASGGPTPLVDITSSGPSDEFVRSTLNALTLNLTPPLPQSHRPYTLTTNGHSVSLSNLSYSDASVMQSSSDVEGQCAHPEYLVFTWVLCLVSLATALKLYYLVKALMALAMVAFYTTLIMMKFGSGDSFSLVELSRLGMPLGVQMLILLISFLVMVCYHARLVEVTSRLDFIWKEQAERELTNMKSNRALNDTLIKNILPDHVATYYLSDEHTDELYSKMHNLCGVMFASIPNFQDFYSEDIDNGKACIRILNEIICDFDELLEEPRFASVEKIKTVGATYMAAAGLNHEHLRLRGETSEDSVCDLVEFAFAMKQKLEEINGDAFNNFQLRVGICSGPLVSGVIGARKPVYDIWGNTVNVASRMDSTGENWRVQVPENTAELLCSRGYTCVKRGEIAVKGKGMMTTFYVHPKGISESQLISPVRMPAGIPLAQTPNLQRQTSHHGSFSAVVFGMLQASKRSTAIAGTPTGTPSPQIRRGHRGSTFSSVRLSQKSTTVNPVRRNTTRVRGRSYRQKKSSSNNSIVTQASSSYMPSFRRIDQIETTISKSHNDAL
Protein: Antigen presenting cell lectin-like receptor A2 (C-type lectin domain family 4, member b1) (Dendritic cell immuno-activating receptor alpha isoform) (Q7TS58)
Organism: Mus musculus (Mouse)
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit gamma
- C-type lectin domain family 6 member A
- E3 ubiquitin-protein ligase CBL-B
- Antigen presenting cell lectin-like receptor A1
Sequence:
MVQERQLQGKAVSWSLRLWSAAVISILLLSTCFIASCVVTYQFSMDKPNRRLSELDRYHSLTCFSEGNMVSDKVWSCCPKDWKLFGSHCYLVPTVFSSASWNKSEENCSRMGAHLVVIHSQEEQDFITGILDIHAAYFIGLWDTGHRQWQWVDQTPYEESVTFWHNGEPSSDNEKCVTVYYRRNIGWGWNDISCNLKQKSVCQMKKINL
Protein: Endoplasmin (EC 3.6.4.-) (Heat shock 108 kDa protein) (HSP 108) (HSP108) (Heat shock protein 90 kDa beta member 1) (Transferrin-binding protein) (P08110)
Organism: Gallus gallus (Chicken)
Function: Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). Has ATPase activity (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P14625}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P41148}.
Interaction partners:
- Calreticulin.
- Protein disulfide isomerase family A member 6
- Endoplasmic reticulum chaperone BiP
- Hypoxia up-regulated protein 1
- Protein disulfide-isomerase A4
- DnaJ homolog subfamily B member 11
- Calreticulin.
- Protein disulfide-isomerase A3
- Uncharacterized protein.
- Heat shock protein HSP 90-alpha
Sequence:
MKSAWALALACTLLLAASVTAEEVDVDATVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIKEIREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTVKIKCDKEKNMLHVTDTGIGMTKEELIKNLGTIAKSGTSEFLNKMTEMQDDSQSTSELIGQFGVGFYSAFLVADRVIVTSKHNNDTQHIWESDSNEFSVIDDPRGNTLGRGTTITLVLKEEASDYLELDTVKNLVKKYSQFINFPIYVWSSKTETVEEPVEEEEAKEEKEETDDNEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKTFSKEHDDPMAYIHFTAEGEVTFKSILFVPNSAPRGLFDEYGSKKSDFIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIAEEKYNDTFWKEFGTNVKLGVIEDHSNRTRLAKLLRFQSSHHESNLTSLDQYVERMKEKQDKIYFMAGASRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFEESEKSKESREALEKEFEPLLNWMKDKALKDKIEKAVLSQRLTQSPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIKDMLRRVKENEDDKTVSDLAVVLFETATLRSGYMLPDTKEYGDRIERMLRLSLNIDLDAKVEEEPEEPEDAAEEAEQDEEEVDADAEDSETQKESTDVKDEL
Protein: RUNX family transcription factor 2 (I3L0L0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASNSLFSTVTPCQQNFFWDPSTSRRFSPPSSSLQPGKMSDVSPVVAAQQQQQQQQQQQQQQQQQQQQQQQEAAAAAAAAAAAAAAAAAVPRLRPPHDNRTMVEIIADHPAELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGEVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKVTVDGPREPRRHRQKLDDSKPSLFSDRLSDLGRIPHPSMRVGVPPQNPRPSLNSAPSPFNPQGQSQITDPRQAQSSPPWSYDQSYPSYLSQMTSPSIHSTTPLSSTRGTGLPAITDVPRRISDSEPSTLDSQSSTTLFLSSEEPGPSTAALPSPSSSSCEPQAFSPGPPALPPLLPPLPAASAPPGPGASRRTGRYSVVASSPEAAPRLVDWLPGCPSTISPSTRGDDKERPPPVLAPAEGPERSRAPRPSTAGREEGTVDAGTSPPPRARPAAAASLEAHVGDILVELRTMNGHLDSIARALTKLASSLGPQPEPLPDVSDAN
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (Alpha-enolase) (Eno) (Q97QS2)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed at the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to the degradation of the extracellular matrix and transmigration of the bacteria.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11442827, ECO:0000269|PubMed:12435062}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000305|PubMed:11442827}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11442827, ECO:0000269|PubMed:12435062}. Secreted, capsule {ECO:0000269|PubMed:11442827}. Secreted, cell wall {ECO:0000269|PubMed:11442827}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface; in encapsulated strains it is on the exterior of the capsule (ATCC 11733), in unencapsulated strains it is on the cell wall (R6x) (PubMed:11442827, PubMed:12435062). Extraneously added enolase binds to bacterial cells (PubMed:11442827). The export of enolase might depend on secA2 (By similarity). Once secreted, it remains attached to the cell surface, probably in complex with plasminogen (PubMed:11442827, PubMed:12435062). Detected by antisera of human patients infected with pneumococcal disease (PubMed:12435062). {ECO:0000250|UniProtKB:A0A0H3GN27, ECO:0000269|PubMed:11442827, ECO:0000269|PubMed:12435062}.
Interaction partners:
Sequence:
MSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPSGASTGEHEAVELRDGDKSRYGGLGTQKAVDNVNNIIAEAIIGYDVRDQQAIDRAMIALDGTPNKGKLGANAILGVSIAVARAAADYLEIPLYSYLGGFNTKVLPTPMMNIINGGSHSDAPIAFQEFMILPVGAPTFKEALRYGAEIFHALKKILKSRGLETAVGDEGGFAPRFEGTEDGVETILAAIEAAGYVPGKDVFIGFDCASSEFYDKERKVYDYTKFEGEGAAVRTSAEQIDYLEELVNKYPIITIEDGMDENDWDGWKALTERLGKKVQLVGDDFFVTNTDYLARGIQEGAANSILIKVNQIGTLTETFEAIEMAKEAGYTAVVSHRSGETEDSTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDQLGEVAEYRGLKSFYNLKK