wanglab/gogpt-training-data huggingface dataset:
Protein: Spore wall and anchoring disk complex protein EnP1 (Host cell adhesion protein EnP1) (A7TZU4)
Organism: Encephalitozoon intestinalis (Microsporidian parasite)
Function: Spore wall protein involved in the adhesion to host cells surface glycoaminoglycans (GAGs). Microsporidian spore adherence is an integral part of activation and host cell infection.
Subcellular location: Spore wall {ECO:0000269|PubMed:17557882}. Spore, perispore {ECO:0000269|PubMed:17557882}. Note=Also localizes at the anchoring disk complex which consists of the polar sac and the anchoring disk, playing a crucial role in the rupture of the spore wall and the subsequent release of the polar tube following activation.
Interaction partners:
Sequence:
MKLLGLLISAFGAINALKIKALYLSCDYELRPYNAVIDSQCMAFALNGSNIHEAIRYLNAMNIDKAYVLYWNDHDLHQNPMVLHKNGALAPFDRYTNTAKHVLCVEACSCPGPQSRPVVCPENNGASVSSPCPPCGQGNNTTVCDKVVVNPQPVKPLPAPCTPCAPCESSSSEKSESKECMTFPRICKKKCGPRHGRSPKKVEIVKSQKTYTFDIERYKRRGDVVVRVCSQDCKDKFEKFVLTKTGEIRKGKDKKCIPEPLPECLQCPKNLYKLKSGIEAKVCSEVCMYINSKCEIFVLIGDCDFYKVVMNERRRKQSSFHLKKIRGQKLRELIRQGLFGVEFSPLKC
Protein: A-type potassium channel modulatory protein DPP6 (DPPX) (Dipeptidyl aminopeptidase-like protein 6) (Dipeptidyl aminopeptidase-related protein) (Dipeptidyl peptidase 6) (Dipeptidyl peptidase IV-like protein) (Dipeptidyl peptidase VI) (DPP VI) (Q9Z218)
Organism: Mus musculus (Mouse)
Function: Promotes cell surface expression of the potassium channel KCND2. Modulates the activity and gating characteristics of the potassium channel KCND2. Has no dipeptidyl aminopeptidase activity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22311982}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- A-type voltage-gated potassium channel KCND3
- A-type potassium channel modulatory protein KCNIP1
- Voltage-gated potassium channel KCNC1
- Major prion protein
- A-type voltage-gated potassium channel KCND2
- IgLON family member 5
- Potassium voltage-gated channel subfamily A member 4
- A-type potassium channel modulatory protein KCNIP2
- Contactin-associated protein-like 2
- Leucine-rich glioma-inactivated protein 1
Sequence:
MNQTAGASNNVRCPPGKGHKELVGSNPPQRNWKGIAIALLVILVICSLIVTSVILLTPAEDTSLSQKKKVTVEDLFSEDFKIHDPEAKWISNKEFIYRERKGSVILRNVETNNSTVLIEGKKIESLRAIRYEISPDKEYVLFSYNVEPVYQHSHTGYYVLSKIPHGDPQSLDPPEVSNAKLQYAGWGPKGQQLIFIFENNIYYCAHVGKQAIRVVSTGKEGVIYNGLSDWLYEEEILKSHIAHWWSPDGTRLAYATINDSRVPLMELPTYTGSVYPTVKPYHYPKAGSENPSISLHVIGLNGPTHDLEMMPPDDPRMREYYITMVKWATSTKVAVTWLNRAQNVSILTLCDATTGVCTKKHEDESEAWLHRQNEEPVFSKDGRKFFFVRAIPQGGRGKFYHITVSSSQPNSSNDNIQSITSGDWDVTKILSYDEKRNKIYFLSTEDLPRRRHLYSANTVDDFNRQCLSCDLVENCTYVSASFSHNMDFFLLKCEGPGVPTVTVHNTTDKRRMFDLEANEEVQKAINDRQMPKIEYRKIEVEDYSLPMQILKPATFTDTAHYPLLLVVDGTPGSQSVTERFEVTWETVLVSSHGAVVVKCDGRGSGFQGTKLLQEVRRRLGFLEEKDQMEAVRTMLKEQYIDKTRVAVFGKDYGGYLSTYILPAKGENQGQTFTCGSALSPITDFKLYASAFSERYLGLHGLDNRAYEMTKLAHRVSALEDQQFLIIHATADEKIHFQHTAELITQLIKGKANYSLQIYPDESHYFHSVALKQHLSRSIIGFFVECFRVQDKLPTATAKEEEEED
Protein: TorCAD operon transcriptional regulatory protein TorR (P38684)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system TorS/TorR involved in the anaerobic utilization of trimethylamine-N-oxide (TMAO). Phosphorylated TorR activates the transcription of the torCAD operon by binding to four decameric boxes located in the torCAD promoter. Box1, 2 and 4 contain the DNA sequence 5'-CTGTTCATAT-3' and box3 contains the DNA sequence 5'-CCGTTCATCC-3'. Phosphorylated as well as unphosphorylated TorR negatively regulates its own expression by binding to box1 and 2.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor protein TorS
- Periplasmic protein TorT
- Cytochrome c-type protein TorC
- Response regulator inhibitor for tor operon
- Trimethylamine-N-oxide reductase 1
- Aerobic respiration control sensor protein ArcB
- Chaperone protein TorD
- Sensor histidine kinase HprS
- Sensor protein BasS
- Nitrate/nitrite response regulator protein NarP
Sequence:
MPHHIVIVEDEPVTQARLQSYFTQEGYTVSVTASGAGLREIMQNQSVDLILLDINLPDENGLMLTRALRERSTVGIILVTGRSDRIDRIVGLEMGADDYVTKPLELRELVVRVKNLLWRIDLARQAQPHTQDNCYRFAGYCLNVSRHTLERDGEPIKLTRAEYEMLVAFVTNPGEILSRERLLRMLSARRVENPDLRTVDVLIRRLRHKLSADLLVTQHGEGYFLAADVC
Protein: Mitochondrial RNA-splicing protein MRS4 (P23500)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: MRS4 suppresses a mitochondrial splice defect in the first intron of the COB gene. It may act as a carrier, exerting its suppressor activity via modulation of solute concentrations in the mitochondrion (possibly of cations). Not essential.
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- Protein CCC1
- Frataxin homolog, mitochondrial
- Iron transporter SMF3
- Asparagine--tRNA ligase, mitochondrial
- Magnesium transporter MRS2, mitochondrial
- Iron transport multicopper oxidase FET3
- Iron-regulated transcriptional activator AFT2
- Iron-regulated transcriptional activator AFT1
- tRNA
- Mitochondrial pyrimidine nucleotide transporter RIM2
Sequence:
MNTSELSIAEEIDYEALPSHAPLHSQLLAGAFAGIMEHSLMFPIDALKTRVQAAGLNKAASTGMISQISKISTMEGSMALWKGVQSVILGAGPAHAVYFGTYEFCKARLISPEDMQTHQPMKTALSGTIATIAADALMNPFDTVKQRLQLDTNLRVWNVTKQIYQNEGFAAFYYSYPTTLAMNIPFAAFNFMIYESASKFFNPQNSYNPLIHCLCGGISGATCAALTTPLDCIKTVLQVRGSETVSIEIMKDANTFGRASRAILEVHGWKGFWRGLKPRIVANIPATAISWTAYECAKHFLMKN
Protein: Ras-related C3 botulinum toxin substrate 3 (EC 3.6.5.2) (p21-Rac3) (P60764)
Organism: Mus musculus (Mouse)
Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P60763}. Endomembrane system {ECO:0000250|UniProtKB:P60763}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P60763}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60763}. Cell membrane {ECO:0000250|UniProtKB:P60763}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60763}. Note=Membrane-associated when activated. Colocalizes with NRBP to endomembranes and at the cell periphery in lamellipodia. Colocalized with CIB1 in the perinuclear area and at the cell periphery. {ECO:0000250|UniProtKB:P60763}.
Interaction partners:
- Rho guanine nucleotide exchange factor TIAM1
- Proto-oncogene vav
- Plexin-A1
- Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
- Dedicator of cytokinesis protein 1
- Dedicator of cytokinesis protein 2
- BAR/IMD domain-containing adapter protein 2
- Guanine nucleotide exchange factor VAV2
- Actin nucleation-promoting factor WASL
- Rho guanine nucleotide exchange factor 7
Sequence:
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDLRDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKPGKKCTVF
Protein: Exported serine/threonine protein kinase (EC 2.7.11.1) (Q8IBR9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Gametocyte-specific protein
- EF-hand domain-containing protein
- LCCL/lectin adhesive-like protein 1
- Nucleoporin NUP116/NSP116, putative
- Uncharacterized protein
- Autophagy protein 5
- Uncharacterized protein
- Merozoite surface protein 1
- Protein transport protein USE1, putative
- Spindle assembly abnormal protein 6, putative
Sequence:
MNNRKGKTRNFKKQIKSNMNKEKCEIINDIHSSNVEIENRDNKRNEIINYRKEKHPCSNLSNMTLNPSSYHVSNPINSHNVNVYSSSNNIMNFRKYINDDSSNDITKQSNLSSIESHTMNLNNLYNFNNICNEINSYGFKSNPLDNTKVQNMNSSYCNQMKYSDYYQHKPCLCHRRGILNTSNSSENQINSSDVCSLHKNDYTKISMNFPNASSSVNVDSNVYNSNITAPCVMNSNPMNYNNGKWGSDIINMMQTTNMNNLKINDLNLNEINKINFQDSDLSICSHGTSKSKKHKSDYSTVPYNILSNNMKPNHFTSNSVPSNNILSNNMIPNNIALNNMSSSSIISNNMASCNIPLNNMISNDGISNNIILSNLLLKSLSNKHTSNNMVSNDMLNNMPNNMLNNMSNIMSNNMSNNMSNNMLNNMSNNMSSNMSSNMARNVSNNMSSNFISSNLSNSFISNNMSSNLFLKSLISNNFIPDHLIPNNSNSKNIISNNVNLNNFVSNNFTSNHMEYNNRKNKNLIASSKVNTLNNENMNSLSEKLNPLILSSSHSIHNENQVFNNLHFSEHMQKDNEEIKNDKVIKHMQEEQIKKTPEAYLLNNYYLMFQQKLENQQSYTKNMKTDDPIKFNDIIINQQNICNSSMKNYNNINEEKNKMCSHENITENMNISTIKNNDDKQIVVSKRSSNVLRQMIDFPSVNDKIQNESFANTRRKAREMNIQNDICSEAYKSETIKDRLRSRARKKGLEGVVGGRTTEANSQSLSKYDFLLNKNTIPNNTINLRNKKESKQNAQINNSKETCYHIIEDIDSNVNEQITKDIDMNEIKSSLKVDENMMRFLCADEKKEEMNQNHEQENILDCANKKVFNKNGSSRRKRNNEIKNKKHEEGKDKEDKNLNDKDMEKTNVEENDIEEENITEENITEENVTEENITEENVTEENITEENITEENVTEENEDKNSDDKNVEERNCRASAHGRRFIQTRSRYKQLYNEKHRINKNMHNKQINKMSQINNRNRNMNNMDEEKKSSTDICDHSREMENDENEENVELDNIKELNGIINKENIENDENIKPDMKKNKEKVNVITNERNKRKREKTKCTDEKNDQGKDNTHEHMVEKKVKLEEDSEEMERNTNNNKINYDKNNNDEKNNNTDCTNCTYCEDNIKENNIIFLNGNVENIDNDKNKLVSETVECTNDINEKKKIGEQIACTNNDKMLYSVNVINDDFNMKNVVEFLSHNDVAIKKELNYLNIENKIHEREYILDNKKTLHIDNKKNKDIYYNIAKSGIDENMINSNLFDNYDNKNNVRDLPRDLYSSTDGTMDIIINKKKKIWLNIGCINYMDNFVGKGSYGSVRKVLYNIDLNNEYLKFYMDKINDVKFLKVLTHTCHMKKGLKYLVDKYDIASDSDCVSYWNDYYLELKDHVDDEKYEEITKETKNVQKVQDEKNKDNEKSINKNTNKLNEKELVILESDLMLNNKLDNCLCCHKKRYFELAVKEIDISRKGNEFQFLREQELLCHFNCNVIKPLSTKIGHLKDKQNYEILMHCATGDLRKLLQNLLYHRKKEYEKKKKVNKILKLIHILFGRKYHCFESLYNFECIGLCYKKLKNMKMKINNNTIEIKNPEFDYIYENVKEYNCGLTESECKFLFFQIASGISFIQTCYQSNIVRLTDIKLQNILVFTDSYNIYNPLKWHLCISDFGCSAMEYATYYLENSKNFMNVYKTLLNQWKYEFKNQLSSYFQGTVYTMAPEGLCYDHNGNYRQSKYNQLIYFYEQNFGDIEKRFEELQKPPISIKHTMHNLKVLNINCNVNFTFLNNHLQKYNNEQDEKTIQESTDTIKKEKNTLTCKKINMDNETNGTNYKNYKNKNNMSENLNIPSESSSTNNSSTNNYNNSNNTSASTQYSPFDIRCDSWSLGIILADLAKCGVNSYEYMIMDNYREEDNLFNEKMEILNNIILKDLNVLEDDEMFYIKYIMDYYDIVSLQWGDEIIQNERIKHNVHMHKKIDTNESKNKNNNNEINRDNAYNIYDKHKKNHADNNNNNNNIIISTNTDETNKENKKVHVKSCNKKTPHNSDMCPNNIRSSSNTVGMVFNKNEIYLNSLKKDDEKVHVENSESFTQHYKSLILKYKKYIKNDKFIQIKNEYVHYYKIYKKYLNEENMRRYLLLALLLMNNNISYKRCNEIQSFAKVELTIKNIGSGIFKFRNKKEKENYIKEFKMNVQNDMMNPNKDYWHSRLTNKYLACILKDICHDDFYNRMKKIKKSFNKYELPLNYSDEYWDLLTNLLNYVPSERLLACEVLGHDFFSEHNEKIHNIIKENNHERYVELFKDETFCDTLLKNYKQEKKEKNYISRPFFQDLRKKLDGVYKEDQKKNIQSDYKLKLKKCSIPLEIIRNKIILNKQNSEEKCHNNDNCYIIDTTNNSNINNNNNNNNCSNNVLRHNKKSDIFNKNIVNQINNNKTIKYIILMYEIIIKNMKKKCGMCNDIKNCLNYKHIINKIKNLENLILNFQLSKKNIICDHKKKIKIPMLYLSNVCNNIYYFLNDYSIFEEFKNLDIFMNIHLPFEHLSLPLCDEKTFRNKNFANFYFKPIYYYSLPYKIIHAWYTGPAHIYFNHPYIPDFIKLICLREKNVLRRKEIIFWYDEDIVLNNILKIKDILKCSNDFLCTPYVSHLIGKQLILRKYFITKFFNDKMKLYIDN
Protein: DELTA-stichotoxin-She4b (DELTA-SHTX-She4b) (Cytolysin III) (Sticholysin II) (St II) (St-II) (StII) (StnII) (Sticholysin-2) (STCH2) (P07845)
Organism: Stichodactyla helianthus (Sun anemone) (Stoichactis helianthus)
Function: Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and cytolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers. Cytolytic effects include red blood cells hemolysis, platelet aggregation and lysis, cytotoxic and cytostatic effects on fibroblasts. Lethality in mammals has been ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia, and inotropic effects.
Subcellular location: Secreted. Nematocyst {ECO:0000269|PubMed:16432881}. Target cell membrane {ECO:0000269|PubMed:17573423}. Note=Forms an alpha-helical membrane channel in the prey. {ECO:0000269|PubMed:17573423}.
Interaction partners:
Sequence:
ALAGTIIAGASLTFQVLDKVLEELGKVSRKIAVGIDNESGGTWTALNAYFRSGTTDVILPEFVPNTKALLYSGRKDTGPVATGAVAAFAYYMSSGNTLGVMFSVPFDYNWYSNWWDVKIYSGKRRADQGMYEDLYYGNPYRGDNGWHEKNLGYGLRMKGIMTSAGEAKMQIKISR
Protein: RE08710p (Q9VHF7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE65433p
- Trypsin iota
- FI02848p
- GH20109p
- trypsin
- Acyl-CoA binding protein 5
- Jonah 25Biii
- Zinc carboxypeptidase A 1
- Serine protease 3
- Uncharacterized protein, isoform A
Sequence:
MSRNQDLCLAVFALLTTAGISHGAPQMGRVVNGTDSSVEKYPFVISMRGSSGSHSCGGSIISKQFVMTAAHCTDGRKASDLSVQYGVTKINATGPNVVRVKKIIQHEDYNPYNNYANDISLLLVEEPFEFDGVTVAPVKLPELAFATPQTDAGGEGVLIGWGLNATGGYIQSTLQEVELKVYSDEECTERHGGRTDPRYHICGGVDEGGKGQCSGDSGGPLIYNGQQVGIVSWSIKPCTVAPYPGVYCKVSQYVDWIKKSQIILA
Protein: HMG box-containing protein 1 (HMG box transcription factor 1) (High mobility group box transcription factor 1) (Q62661)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'-TTCATTCATTCA-3'. Binding to the histone H1.0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4 (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
- Paired amphipathic helix protein Sin3a
Sequence:
MVWEVKTNQRPHAVQRLLLVMDERATGVSDSLELLQCNENVPSSPGYNSCDEHMELDDLPELQAVQSDPTQSAIYQLSSDVSHQEYPRPSWSQNTSDIPENTHREDEVDWLTELANIATSPQSPLMQCSFYNRSSPVHIIATSKSLHSYARPPPVSSAKSGPAFPHDHWKEETPVRHERANSESESGIFCMSSLSDDDDLGWCNSWPSTVWHCFLKGTRLCFHKESKKEWQDVEDFARAASCDEEEIQMGTHKGYGSDGLKLLSHEESVSFGESVLKLTFDPGTVEDGLLTVECKLDHPFYVKNKGWSSFYPSLTVVQHGIPCCEIHIGDVCLPPGHPDAINFDDSGVFDTFKSYDFTPMDSSAVYVLSSMARQRRASLSCGGPGTGQEFAGSEFSKSCGSPGSSQLSSSSLYTKAVKSHSSGTVSATSPNKCKRPMNAFMLFAKKYRVEYTQMYPGKDNRAISVILGDRWKKMKNEERRMYTLEAKALAEEQKRLNPDCWKRKRTNSGSQQH
Protein: Complement C8 gamma chain (A0A8I6A1Y6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MWTSGLCFLWHWTVDSDLEQCTPPPPCPITYCHRTAMLSPGAVLFFTLILMASSLGQRTRKPYGSTSPISTIQAQANFNAQQFAGTWLLVAVGSACRFLQEQGHRAEATTLHIAPQGAAMAASTFRKLDGICWQVRQLYGITGVPGRFLLQAPRARGPVHVVVAETDYQSFAILYLEQARRLSVKLYTRTLPVSDSALNAFEERVRGANLTEDQIFFFPKYGFCETADQFHILNGECQQGRAVGWRG
Protein: Vinculin (Metavinculin) (B3DI32)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004278}. Cell projection, podosome {ECO:0000256|ARBA:ARBA00004188}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MPVFHTKTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTSPVAAVQAAVSNLVRVGKETVQTTEDKIMKRDMPSAFIKVENACAKLVEAAQMLRTDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLITYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVTSMNTVKELLPVLISAIKIFVTTKCTKSHGVEEALKNRNYTFDKMTAEINEIIRVLQLTSWDEDAWANKKDTEAMKRALALIESKMGQAKGWLRDPNALPGDPGEHALRQILDEAGKVGELCAGKERREILGTAKTLGQMTDQVSDVRARGQGATPMGMQKAQQVAQGLDILVGKVENAARKLEALTNAKQAIAKRIDNAQSWLADPNGGPEGEENIRALLAEAKRIADLCEDPKERDDILRSIGEIAGLTARLVELRRIGKGDTPEARALAKQIGTALQNLQAKTNRAVANMRPAKAAVTLEGKMEQALRWINNPGVDDHGVGQAAIRGLIAEGRRLASSLPGPYRQELLAKCEQVEQLMMQLADLAARGEGESPQARAVAAHLLEAIKDLKAKMQEAMTQEVSDVFSDTTTPIKLLAVAATAPLEAPNREEVFEERASNFENHASRLGATAEKAAAVGTANKSTVEGIQAAVKSARDLTPQVTSAARILLKNPGNQAAYEHFDTMKNQWIDNIEKMTSLVDEAIDTKSLLDASEEAIKKDIDKCRVAMANVQPQMLVAGATSIARRANRVLLVAKREVENSEDPKFRELVKAASDELGRTISPMVMAAKGVAGNIQDPGLQKGFLDSGYRILAAVGKVREAFQPQELDFPPPPPDLDQLHVNDDQAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEMVSEPMMVAARSLHDEARKWSSKPEVPDEGFEAAEAEVDIDDEDEFTDNEDDYEPELLLMSSNQPVNQPILAAAQSLHQEARKWSSKGNDIIGAAKRMALLMAEMSRLVRGGSGNKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISEEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ
Protein: Interleukin-22 (IL-22) (IL-10-related T-cell-derived-inducible factor) (IL-TIF) (IL-TIF alpha) (Interleukin-22a) (IL-22a) (Q9JJY9)
Organism: Mus musculus (Mouse)
Function: Cytokine that plays a critical role in modulating tissue responses during inflammation. Plays an essential role in the regeneration of epithelial cells to maintain barrier function after injury and for the prevention of further tissue damage. Unlike most of the cytokines, has no effect on immune cells. Signals through a heterodimeric receptor composed of two subunits, the specific receptor IL22RA1 which is present on non-immune cells in many organs and the shared subunit IL10RB. Ligation of IL22RA1 with IL22 induces activation of the tyrosine kinases JAK1 and TYK2, which in turn activates STAT3. In turn, promotes cell survival and proliferation through STAT3, ERK1/2 and PI3K/AKT pathways.
Subcellular location: Secreted.
Interaction partners:
- Interleukin-22 receptor subunit alpha-1
- Interleukin-10 receptor subunit beta
- Interleukin-22 receptor subunit alpha-2
- Interleukin-22b
- Interleukin-17A
- Interleukin-23 receptor
- Interleukin-20 receptor subunit alpha
- Interleukin-17F
- Interleukin-10
- Interferon gamma
Sequence:
MAVLQKSMSFSLMGTLAASCLLLIALWAQEANALPVNTRCKLEVSNFQQPYIVNRTFMLAKEASLADNNTDVRLIGEKLFRGVSAKDQCYLMKQVLNFTLEDVLLPQSDRFQPYMQEVVPFLTKLSNQLSSCHISGDDQNIQKNVRRLKETVKKLGESGEIKAIGELDLLFMSLRNACV
Protein: ATP synthase subunit alpha (EC 7.1.2.2) (ATP synthase F1 sector subunit alpha) (F-ATPase subunit alpha) (P05036)
Organism: Rhodospirillum rubrum
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
Interaction partners:
Sequence:
MEIRAAEISAILKEQIANFGTEAESAEVGQVLSVGDGIARVYGLDNVQAGEMVEFANGVKGMALNLESDNVGIVIFGEDRGIKEGDVVKRTQTIVDVPVGKGLLGRVVDGLGNPIDGKGDLVDVERKRAEVKAPGIIPRKSVHEPVQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAVILDTILNQKAVNDKAKDDSEKLFCVYVAVGQKRSTVAQVVKVLADHGALDYTIVVAATASEPAPLQFLAPYTGCTMGEFFRDNGMHAVIFYDDLTKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDDNGAGSLTALPVIETQANDVSAYIPTNVISITDGQIFLETDLFFKGIRPAVNVGLSVSRVGSSAQIKAMKQVAGSIKLELAQYREMAAFAQFASDLDPATQKLLARGARLTELLKQAQYSPLAVEEQVCVIYAGTRGYLDKLKTTDVVRYEASLLGALRTSGADLLESIRTGKALSKEIEQKLVKFLDDFGKKFA
Protein: Endophilin-B1 (SH3 domain-containing GRB2-like protein B1) (Q6AYE2)
Organism: Rattus norvegicus (Rat)
Function: May be required for normal outer mitochondrial membrane dynamics. Required for coatomer-mediated retrograde transport in certain cells. May recruit other proteins to membranes with high curvature. May promote membrane fusion. Involved in activation of caspase-dependent apoptosis by promoting BAX/BAK1 activation. Involved in caspase-independent apoptosis during nutrition starvation and involved in the regulation of autophagy. Activates lipid kinase activity of PIK3C3 during autophagy probably by associating with the PI3K complex II (PI3KC3-C2). Associated with PI3KC3-C2 during autophagy may regulate the trafficking of ATG9A from the Golgi complex to the peripheral cytoplasm for the formation of autophagosomes by inducing Golgi membrane tubulation and fragmentation. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11604418}. Golgi apparatus membrane {ECO:0000269|PubMed:11604418}; Peripheral membrane protein {ECO:0000269|PubMed:11604418}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9JK48, ECO:0000250|UniProtKB:Q9Y371}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JK48, ECO:0000250|UniProtKB:Q9Y371}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9Y371}. Midbody {ECO:0000250|UniProtKB:Q9Y371}. Note=Association with the Golgi apparatus depends on the cell type. Following starvation colocalizes with ATG5 and LC3 autophagy-related protein(s)on autophagosomal membranes. {ECO:0000250|UniProtKB:Q9JK48, ECO:0000250|UniProtKB:Q9Y371, ECO:0000269|PubMed:11604418}.
Interaction partners:
- UV radiation resistance associated
- Beclin-1
- Activating molecule in BECN1-regulated autophagy protein 1
- Beclin 1-associated autophagy-related key regulator
- Endophilin-B2
- Phosphatidylinositol 3-kinase catalytic subunit type 3
Sequence:
MNIMDFNVKKLAADAGTFLSRAVQFTEEKLGQAEKTELDAHLENLLSKAECTKVWTEKIMKQTEVLLQPNPNARIEEFVYEKLDRKAPSRINNPELLGQYMIDAGTEFGPGTAYGNALIKCGETQKRIGTADRELIQTSALNFLTPLRNFIEGDYKTIAKERKLLQNKRLDLDAAKTRLKKAKAAETKSSSEQELRITQSEFDRQAEITRLLLEGISSTHAHHLRCLNDFVEAQMTYYAQCYQYMLDLQKQLGSFPSNYVSNNNQTSGTPVPYTLSNTIGPSAVASTGSLVITCPPNLSDLKDSSSTRKARVLYDYDAANSTELSLLADEVITVFSVVGMDSDWLMGERGNQKGKVPITYLELLN
Protein: Tenascin C (A0A8I6AIS3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MGAVTWLLPGIFLALFALTPEGGVLKKVIRHKRESGLNLTLPEENQPVVFNHIYNIKLPMGSQCSVDLESTSGEKDLSPTPESSGSFQEHTVDGENQIVFTHRINIPRRACGCAAAPDVKELLSRLEELEMLVSSLREQCTMGTGCCLQPAEGRLDSRPFCSGRGNFSAEGCGCVCEPGWKGPNCSEPECPGNCNLRGQCLDGQCICDQGFTGEDCSQLACPNDCNDQGKCVNGVCVCFEGYAGLDCGLEVCPVPCSEEHGMCVDGRCVCKDGFAGEDCNEPLCFNNCNNRGRCVENECVCDEGFTGEDCSELICPNDCFDRGRCINGTCYCEEGFTGEDCGELTCPNNCQGHGQCEEGQCVCNEGFAGADCSEKRCPADCHHHGRCLNGQCECDDGFTGADCGELQCPNGCSGHGRCVNGQCVCDEGYTGEDCSQRRCPNDCHNRGHCVQGKCICEQGFKGFDCSEMSCPNDCHQHGRCVNGMCICDDDYTGEDCRDRRCPRDCSQRGRCVDGQCICEDGFTGSDCAELSCPGDCHGHGRCVNGQCICHEGFTGKDCKEQRCPSDCHGQGRCEDGQCICHEGFTGLDCGQRSCPNDCSNQGQCVAGRCICNEGYTGVDCSEVSPPKDLIVTEVTEETVNLAWDNEMRVTEYLIMYTPTHADGLEMQFRVPGDQTSTTIRELEPGVEYFIHVFAILENKRSIPVSARVATYLPAPEGLKFKSIKETSVEVEWDPLDIAFETWEIIFRNMNKEDEGEITKSLRRPETSYRQTGLAPGQEYEISLHIVKNNTRGPGLKKVTTTRLDAPSQIEVRDITDTTALITWSKPLAEIDSIELSYGIKDVPGDRTTIDLTHEDNQYSIGNLKPDTEYEVSLISRRVDMASNPAKETFITGLDAPRNLRRVSQTDNSITLEWRNVKADIDSYRIKYAPISGGDHAEIDVPKSQQATTKTTLTGLRPGTEYGVGVSAVKGDKEGDPATINAATEIDAPRDLQVSETTQDSLTLFWKTPLAKFDRYRLNYSLPTGQSIEIQLPKDATSHVLTDLEPGQEYTVLLTAEKGRHKSKPARVKASTAMGSPKEIMFSDITENAATVSWRAPTAQVESFRITYVPVTGGPPSMVTVDGTDTETRLVRLTPGVEYHVSVIAMKGFEESDPVSGSLITALDGPSGLLTANITDSEALAMWQPAIATVDSYVISYTGERVPEITRTVSGNTVEFELHDLEPATEYTLSVFAEKGHQKSSTIATKFTTDLDSPRELTATEVQSETALLTWRPPRASVTGYLLVYESVDGTVKEVIVGPDTTSYSLADLSPSTHYTARIQALSGSLRSKLIQTIFTTIGLLYPFPRDCSQAMLNGDTTSGLYTIYINGDKTQALEVYCDMTSDGGGWIVFLRRKNGREDFYRNWKAYAAGFGDRREEFWLGLDNLSKITAQGQYELRVDLQDHGESAYAVYDRFSVGDAKSRYKLKVEGYSGTAGDSMNYHNGRSFSTYDKDTDSAITNCALSYKGAFWYKNCHRVNLMGRYGDNNHSQGVNWFHWKGHEYSIQFAEMKLRPSNFRNLEGRRKRA
Protein: Uncharacterized oxidoreductase Rv0484c (EC 1.-.-.-) (P9WGR5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- Ribonuclease Z
- Bifunctional oligoribonuclease and PAP phosphatase NrnA
- Linear primary-alkylsulfatase
- Formylglycine-generating enzyme
- Transcriptional regulator Rv0485
- Possible penicillin-binding protein
Sequence:
MTTIGTRKRVAVVTGASSGIGEATARTLAAQGFHVVAVARRADRITALANQIGGTAIVADVTDDAAVEALARALSRVDVLVNNAGGAKGLQFVADADLEHWRWMWDTNVLGTLRVTRALLPKLIDSGDGLIVTVTSIAAIEVYDGGAGYTAAKHAQGALHRTLRGELLGKPVRLTEIAPGAVETEFSLVRFDGDQQRADAVYAGMTPLVAADVAEVIGFVATRPSHVNLDQIVIRPRDQASASRRATHPVR
Protein: Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial (Glu-AdT subunit B) (EC 6.3.5.-) (Cytochrome oxidase assembly factor PET112 homolog) (PET112-like) (D6REA0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03147}.
Interaction partners:
Sequence:
MAAPMLRWGCRGRRWAFARVDGGSCHRRGAPTGSTSNQIRGESSVAQQPLHTAQKTRKGEHKWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHYFYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKQSQVIPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAEGQLRVDANISVHHPGEPLGVRTEVKNLNSIRFLAKAIDYEIQRQINELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATSLPAGADPQQVINIDQIRETLPELPSVTREKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRAEPKKVTSWVLNTFLGYLKQQNLAVSESPVTPSALAELLDLLDSRTISSSAAKQVFEELWKREGKTPGQIVSEKQLELMQDQGALEQLCHSVMEAHPQVVMDVKNRNPRAINKLIGLVRKATQSRADPVMIKEILEKKLSL
Protein: Transcription cofactor vestigial-like protein 4b (Vestigial like 4 (Drosophila)) (Q6NV03)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLFTKMDLLNYQYLDKMNNNIGILCYEGDAALRGESRMQSLSSAVSNHRTGPPPISPSKRKHSAEQADDDIDCNSEHVAKMSRLFAAQLGKPANGDYRKDPRERSRSPIERMAAPSMSLVGGHHLYMPSLALDQPLALTKNMDSSRSMGISPTASPVERQQNRPSVITCAPANNRNCNLSHCTGSHNGCSPGLNASYRRASNSNTACDPVIEEHFRRSLGKNYKEPEPVTNSVSITGSVDDHFAKALGETWLQIKAKGGSSSPDASPNTHMVNHNHSPSLVS