wanglab/gogpt-training-data huggingface dataset:
Protein: Down syndrome cell adhesion molecule 1, isoform BR (A0A0B4K828)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVAQYYDTDVNKAYVIRGNAAVLKCEIPSFVADFVSVVSWHTDQNEDFLPGSEYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVSAKGPTFASDMKSYTFVRHFGQSFALLCQAQAYPVPLIRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVAPQISPFSFGDEPLNRGEVASVNCVVPKGDLPLDIYWTLNSALIVNGEMGFTLVRLNKRTSSLNVDSLEAVHRGSYKCIANNSAGYAEYVSTLDVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Cell division inhibitor SulA (Q9HZJ8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division (By similarity).
Interaction partners:
- Cell division protein FtsZ
- LexA repressor
- DNA repair protein RecN
- YebG family protein
- Tol-Pal system protein TolA
- Uncharacterized protein PA1624
- Transmembrane protein
- Peptide chain release factor RF-3
- SPOR domain-containing protein
- Flagellar protein FlgN
Sequence:
MQTSHSLPSAQLPLFQEAFWASNGAPLLDDVIDSPSSASIEEPAAFSELSLSGLPGHCLTLLAPILRELSEEQDARWLTLIAPPASLTHEWLRRAGLNRERILLLQAKDNAAALALSCEALRLGRSHTVVSWLEPLSRAARKQLSRAAQLGQAQSLNIRLG
Protein: RING-type domain-containing protein (Q38FD4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Polyubiquitin, putative
Sequence:
MSVTGFGDVVVSFDAEGVVVVGLTYERSNATQWLLLPEIPVEVPLVKVLRDLEESGASRQRSPGRMRGEGVKGDVCLPDSEVGSPCNACGVNNIRSDCCISVARVGHIPERNRAYCLLLELSSSSDAADVQRDLLHVEWANGPLCAPQFLQSVGRIMRVEHEGRDAACVSNCAGWRTQVSTDNAEDVCLRVLCSVSCGVDGASSRRQLESEKEISSVALRRDAPLAPIEEFCPICREEIASGRTCVVTMCTHVFHLVCLMKHLEDVSSYCPLCRFSMSSLETKCNACGTCQDLWSCLVCGWVGCGKGRHGHSIRHFHSTGHSCAVQNSTSRIWNYRASTFLHHQLAMELGYEDDARAERAAAQEEGRSALSVRHSGEKPRVSASSYWRSRWWWDEKEEEAAQELNGDYVREYYLRVMEELMQEQADYFEGRTMVEGENAAVPIGTWKKLQSAERRQRRSLASRYIAGLRRIALHSQMAVNNFVKQEVLWRDSLREELLLQSHTNQGLNARISSLGANIDKARQRGEQQVALKEEELRDLQGRLESLMRDLE
Protein: Photosystem II reaction center protein J (PSII-J) (Q2LIN4)
Organism: Oryza sp. IRGC 105360
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01305}; Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01305}.
Interaction partners:
Sequence:
MADTTGRIPLWLIGTVTGIAVIGLIGVFFYGSYSGLGSSL
Protein: Sodium channel modifier 1 (Q9BWG6)
Organism: Homo sapiens (Human)
Function: Plays a role in alternative splicing of pre-mRNAs, possibly by contributing to the selection of non-consensus donor sites.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:17656373}. Nucleus speckle {ECO:0000269|PubMed:17656373}. Note=Colocalizes with LUC7L2 and SNRNP70 in nuclear speckles. {ECO:0000250|UniProtKB:Q8K136}.
Interaction partners:
- Armadillo repeat-containing protein 7
- Putative RNA-binding protein Luc7-like 2
- Luc7-like protein
- Splicing factor 3B subunit 3
- Splicing factor 3B subunit 1
- Small nuclear ribonucleoprotein Sm D2
- E3 ubiquitin-protein ligase RNF113A
- Splicing factor 3B subunit 2
- Pre-mRNA-processing-splicing factor 8
- Cell division cycle 5-like protein
Sequence:
MSFKREGDDWSQLNVLKKRRVGDLLASYIPEDEALMLRDGRFACAICPHRPVLDTLAMLTAHRAGKKHLSSLQLFYGKKQPGKERKQNPKHQNELRREETKAEAPLLTQTRLITQSALHRAPHYNSCCRRKYRPEAPGPSVSLSPMPPSEVKLQSGKISREPEPAAGPQAEESATVSAPAPMSPTRRRALDHYLTLRSSGWIPDGRGRWVKDENVEFDSDEEEPPDLPLD
Protein: Metallo-beta-lactamase domain-containing protein 1 (EC 3.1.27.-) (Endoribonuclease MBLAC1) (A4D2B0)
Organism: Homo sapiens (Human)
Function: Endoribonuclease that catalyzes the hydrolysis of histone-coding pre-mRNA 3'-end. Involved in histone pre-mRNA processing during the S-phase of the cell cycle, which is required for entering/progressing through S-phase. Cleaves histone pre-mRNA at a major and a minor cleavage site after the 5'-ACCCA-3' and the 5'-ACCCACA-3' sequence, respectively, and located downstream of the stem-loop. May require the presence of the HDE element located at the histone pre-RNA 3'-end to avoid non-specific cleavage.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:30507380}. Nucleus {ECO:0000269|PubMed:30507380}. Note=Localizes in the nucleus during early S-phase of the cell cycle. {ECO:0000269|PubMed:30507380}.
Interaction partners:
Sequence:
MRTEPLCGASPLLVPGDPYSVVVLLQGYAEPEGVGDAVRADGSVTLVLPQTRGPASSHRESPRGSGGAEAALEEAARGPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSHDFCLPGGRYLPHGLGEGQPLRLGPGLEVWATPGHGGQRDVSVVVAGTALGTVVVAGDVFERDGDEDSWQALSEDPAAQERSRKRVLVVADVVVPGHGPPFRVLREASQPETEGGGNSQQEPVVGDEEPALH
Protein: 3-methyl-2-oxobutanoate hydroxymethyltransferase 1, mitochondrial (EC 2.1.2.11) (Ketopantoate hydroxymethyltransferase 1) (O82357)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14675432}.
Interaction partners:
- Pantoate--beta-alanine ligase
- Putative 2-dehydropantoate 2-reductase
- Dihydroxy-acid dehydratase, chloroplastic
- Branched-chain-amino-acid aminotransferase 3, chloroplastic
- Branched-chain-amino-acid aminotransferase 6
- Putative branched-chain-amino-acid aminotransferase 7
- Branched-chain-amino-acid aminotransferase 1, mitochondrial
- Branched-chain-amino-acid aminotransferase 2, chloroplastic
- Branched-chain-amino-acid aminotransferase 5, chloroplastic
- Pantothenate kinase 2
Sequence:
MASSLTRNCSRFSKAISVRFMSNLPENTVYGGPKPQNPNQRVTLTHLRQKHRRGEPITVVTAYDYPSAVHLDTAGIDVCLVGDSASMVVHGHDTTLPISLDEMLVHCRAVARGAKRPLLVGDLPFGTYESSSSQAVDTAVRVLKEGGMDAIKLEGGSASRITAAKAIVEAGIAVIGHVGLTPQAISVLGGFRPQGRNIASAVKVVETAMALQEAGCFSVVLECVPPPVAAAATSALKIPTIGIGAGPFCSGQVLVYHDLLGMMQHPHHAKVTPKFCKQYANVGEVINKALMEYKEEVSKKVFPGPSHSPYKITASELDGFLTELQKLGFDKAASAAALAAENMEPSK
Protein: UPF0234 protein YajQ (P0A8E7)
Organism: Escherichia coli (strain K12)
Function: Binds nucleotides, may bind tRNA.
Interaction partners:
Sequence:
MPSFDIVSEVDLQEARNAVDNASREVESRFDFRNVEASFELNDASKTIKVLSESDFQVNQLLDILRAKLLKRGIEGSSLDVPENIVHSGKTWFVEAKLKQGIESATQKKIVKMIKDSKLKVQAQIQGDEIRVTGKSRDDLQAVMAMVRGGDLGQPFQFKNFRD
Protein: Cytoplasmic dynein 1 intermediate chain 2 (Cytoplasmic dynein intermediate chain 2) (Dynein intermediate chain 2, cytosolic) (DH IC-2) (O88487)
Organism: Mus musculus (Mouse)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function (By similarity). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (By similarity). The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28619825}. Cytoplasm {ECO:0000269|PubMed:28619825}. Note=Detected in the cytoplasm of pachytene spermatocytes. Localizes to the manchette in elongating spermatids. {ECO:0000269|PubMed:28619825}.
Interaction partners:
- Cytoplasmic dynein 1 light intermediate chain 2
- Cytoplasmic dynein 1 heavy chain 1
- Cytoplasmic dynein 1 light intermediate chain 1
- Dynein light chain 1, cytoplasmic
- Dynein light chain roadblock-type 1
- Dynactin subunit 1
- Dynein light chain 2, cytoplasmic
- Dynactin subunit 2
- Dynein light chain
- Cytoplasmic dynein 2 light intermediate chain 1
Sequence:
MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAAVSVQEESDLEKKRREAEALLQSMGLTTDSPIVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRRGPIKLGMAKITQVDFPPREIVTYTKETQTPVTAQPKEDEEEEDDVATPKPPVEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEEAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (Q6FKY1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00560}. Mitochondrion {ECO:0000250|UniProtKB:P00560}.
Interaction partners:
- Triosephosphate isomerase
- Phosphoglycerate mutase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Phosphoglycerate mutase
- Enolase 1
- mRNA 3'-end-processing protein RNA14
- Enolase 2
Sequence:
MSLSSKLTVQDLELKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHNPRYVVLASHLGRPNGERNEKYSLAPVAEELQSLLGKPVTFLNDCVGSEVDSAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASAEDVAKFRKELCSLADVYINDAFGTAHRAHSSMVGFDLPQRAAGFLLTKELQYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFTFKKVLENAEIGDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFVIADAFSADANTKIVSDKEGIPAGWQGLDNGPESRKLFAATIAKAKTIVWNGPPGVFEFEKFASGTKAMLDEVVKSSTSGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELLEGKELPGVAFLSEKN
Protein: Flavin-containing monooxygenase (EC 1.-.-.-) (G5EBJ9)
Organism: Caenorhabditis elegans
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|PIRNR:PIRNR000332}. Microsome membrane {ECO:0000256|ARBA:ARBA00004524}.
Interaction partners:
- Serine/threonine-protein phosphatase C23G10.1
- C-type lectin domain-containing protein
- C-type lectin domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
- VWFA domain-containing protein
- Invertebrate-type lysozyme 3
- Zinc transporter Slc39a7
- Nematode cuticle collagen N-terminal domain-containing protein
Sequence:
MGNKRVAVIGAGASGLPSIRHGLLYGFDVTCFEASDDIGGLWRYKSHETNESSVMKTTVINTSKEMTAYSDFTPQENLANFMHNNEMLNYFKSYAEHHGLMKHIKLRHRVLNIERSKNYDNDGTWKVIYQTPEEKTLEEIFDGVLVCSGHHAIPHWPKPFPGQNEFKGRIVHSHDYKDHKGYEDKVVVVVGIGNSGIDVAVEQSRIAKQVYLVTRRGTWLIPKLETRGLPFDIIMNTRFFSLYKLFPQAMLNSLVEYRINQRIDHDLYGLKPAHRVFSAHPSLNDELPNRIANGTVRIKPNIKKFDGYAIHFEDGTIVPHVDEVVMSTGFSFEFNLIEHGKLVPVSENEVDLFKYMFPVATSDHNSLCIIGLIQPFGSIMPVSEQQARVFFANMVSGNNLIPKKSQMSEDVLNKKEAMAQQFVKSRRHTIQVDYIPYMDELAELIGCQVPLLRTLFTDPVLGLRLFFGPNAGYCYRLAGPHTWNGARNAILTIDQRVRMATTTKPEPTNYTVPLVISSIILLLVIYFVM
Protein: Small ribosomal subunit protein mS40 (28S ribosomal protein S18-2, mitochondrial) (28S ribosomal protein S18b, mitochondrial) (B0S7P4)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MAASVLNTVLRRLPMLSLFRGSHRVQVPLQTLCTKAPSEEDSLSSVPISPYKDEPWKYLESEEYQERYGSRPVWADYRRNHKGGVPPQRTRKTCIRRNKVVGNPCPICRDHKLHVDFRNVKLLEQFVCAHTGIIFYAPYTGVCVKQHKRLTQAIQKARDHGLLIYHIPQVEPRDLDFSTSHGAVSATPPAPTLVSGDPWYPWYNWKQPPERELSRLRRLYQGHLQEESGPPPESMPKMPPRTPAEASSTGQTGPQSAL
Protein: RNA-binding protein MEX3B (RING finger and KH domain-containing protein 3) (Q69Z36)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Note=Predominantly expressed in the cytoplasm and shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. Localization to P-bodies is dependent on 14-3-3 (By similarity). {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase DZIP3
- Snurportin-1
Sequence:
MPSSLFADLERNGSGGGGGGGGGGGGGGSGGGETLDDQRALQLALDQLSLLGLDSDEGASLYDSEPRKKSVNMTECVPVPSSEHVAEIVGRQGGSGRDGDRRGFSISPTPSLEPWLPGCKIKALRAKTNTYIKTPVRGEEPVFVVTGRKEDVAMARREIISAAEHFSMIRASRNKNTALNGAVPGPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEAHIALRTGGIIELTDENDFHANGTDVGFDLHHGSGGSGPGSLWSKPTPSITPTPGRKPFSSYRNDSSSSLGSASTDSYFGGGTSGSAAATSRLADYSPPSPALSFAHNGNNNNNGNGYTYTAGEASVPSPDGGPELQPTFDPAPAPPPGTPLLWAQFERSPGGGSAAPVSSSCSSSASSSASSSSVVFPGGGASSTPSNANLGLLVHRRLHPGTSCPRLSPPLHMATGAGEHHLARRVRSDPGGGGLAYAAYANGLGTQLPGLPSSDTSGSSSSSSSSSSSSSSSSGLRRKGSRDCSVCFESEVIAALVPCGHNLFCMECANRICEKSEPECPVCHTAVTQAIRIFS
Protein: Uncharacterized protein YgiM (P0ADT8)
Organism: Escherichia coli (strain K12)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Multifunctional CCA protein
- Uncharacterized protein YfeK
- Anti-sigma-E factor RseA
- Uncharacterized protein YggN
- ECF RNA polymerase sigma-E factor
Sequence:
MPKLRLIGLTLLALSATAVSHAEETRYVSDELNTWVRSGPGDHYRLVGTVNAGEEVTLLQTDANTNYAQVKDSSGRTAWIPLKQLSTEPSLRSRVPDLENQVKTLTDKLTNIDNTWNQRTAEMQQKVAQSDSVINGLKEENQKLKNELIVAQKKVDAASVQLDDKQRTIIMQWFMYGGGVLGLGLLLGLVLPHLIPSRKRKDRWMN
Protein: Protocadherin beta-9 (PCDH-beta-9) (Protocadherin-3H) (Q9Y5E1)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MKTRGFSFPRQRQVLFLFLFWGVSLAGSGFGRYSVTEETEKGSFVVNLAKDLGLAEGELAARGTRVVSDDNKQYLLLDSHTGNLLTNEKLDREKLCGPKEPCMLYFQILMDDPFQIYRAELRVRDINDHSPVFRHKEMVLKISENTAEGTAFRLERAQDPDEGHNSIQNYTISSNSFFHIKISGSDEGMIYPELVLDKALDREEQEELSLTLTALDGGSPSRSGTSTIRIVVLDVNDNVPQFAQALYETQAPENSPVGSLIVKVSAGDADSGVNAEVSYSFFDASEDILTTFQINPFSGEIFLRELLDYELVNSYKINIQAMDGGGLSARCTVLIKVLDSNDNPPELIISSLSNSVAENSPGIVLAVFKIKDRDSGENGKTICYVQDNLPFFLKPSVDNFYILMTEGALDRESKAEYNITITVTDLGTPRLKTEHSITLQVSDVNDNAPAFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQDPHLPLASLVSINADNGHLFALRSLDYEALQAFDFRVGASDRGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPAQAQADLLTVYLVVALASVSSLFLLSVLLFVAVRLCRRSRAASVGRCSVPEGPFPGHLVDVSGTGTLFQSYQYEVCLTGGSETGEFKFLKPITPHLPPHRGGKEIEENSTLPNSFGFNY
Protein: Adenosine deaminase (EC 3.5.4.4) (Adenosine aminohydrolase) (Q920P6)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion. Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion. Enhances CD4+ T-cell differentiation and proliferation. Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change. Stimulates plasminogen activation. Plays a role in male fertility. Plays a protective role in early postimplantation embryonic development.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P00813}; Peripheral membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:P00813}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:19900420, ECO:0000269|PubMed:8783262}. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:P00813}. Note=Colocalized with DPP4 at the cell surface. {ECO:0000250|UniProtKB:P00813}.
Interaction partners:
- Dipeptidyl peptidase 4
- Adenosine kinase
- Purine nucleoside phosphorylase
- 5'-nucleotidase
- Deoxycytidine kinase
- 5',3'-nucleotidase, mitochondrial
- Cytosolic purine 5'-nucleotidase
- Adenine phosphoribosyltransferase
- Double-stranded RNA-specific adenosine deaminase
- 5'-nucleotidase
Sequence:
MAQTPAFNKPKVELHVHLDGAIKPETILYYGKKRGIDLPADTVEGLRNIIGMDKPLSLPDFLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVDPIPWNQAEGDLTPDEVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSPEVLELCKKYHQKTVVAMDLAGDETIEGSSLFPGHVEAYEGAVKDGIHRTVHAGEVGSAEVVREAVDILKTERVGHGYHTIEDEALYNRLLKENMHFEVCPWSSYLTGAWNPKTTHAVVRFKDDQANYSLNSDDPLIFKSTVDTDYQMVKKDMGFTEEEFKRLNINAAKSSFLPEDEKKELLERLYKEYQ
Protein: coproporphyrinogen oxidase (EC 1.3.3.3) (Q05AK3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTSLALCTINSSTRSIARLCRVSHSAHGTADVHSFVARYSTLRNCSASLPRGKCSFIKTGTRQMCQSSPRRISLGRYGKGVFLAAGAAAVTGVLAAGVSHFQRAEMATKISRVEEEDGDIRERCKSFMSPPVTDIKLLEQRKDEMSTRMEMLIMETQSAFCRALEQVDGGSFRVDRWSRKEGGGGISCVMQDGKIFEKAGVNVSVVYGNLTEEAARQMRSRGKILKGKDGKLPFRAMGVSSVIHPKNPHIPTVHFNYRYFEIEEADGTKQWWFGGGTDLTPVYIDLEDATHFHKTLKEACDKHHPKYYPDFKKWCDNYFYIRHRGETRGIGGIFFDDLDSPDQDEVFNFVRSCAKTVVPCYLPIVYKHLNDSFTPEEKDWQQVRRGRYVEFNLVYDRGVKFGLATPGSRIESILMSLPLTARWEYMHEPTKGTKEAEMLEILRNPKQWI
Protein: Uncharacterized protein, isoform J (M9PBG0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVTICSLSAALSCNIAYRFPIYEMEHLDLAGYLGHTPQSWNTLGTFQDQDAVYLSSSRQMLEPILEETSEDEERARSSLIVSLDRRSTLWSSTESETGSVLRIETIKDIDAVSERDFVCPPKRPRRSHDLNSGQISEDCVQLRRPMPYDPEYHNSFERFLALEACARDSFGSQGQRSSIGSRRGGTFEDFYSDRDSSHSLSRSSSLVQFESLERQLTLQEQHQSMNSLGNSSPSLTCESGASTRARTRDSSPESRKGSAPTLSLLKRYESSDCSHLHQTYYELNNLNFEYKQQQELLSRSLREAELKSDLESSSSSSSSSDSSGHSLLSSCLVPGDAVATERGKQDGTNSRRIPPNSAENLSEDSGYCEPRTLKREKSKSIPKNFEKLCEEEEELLLLEEGAPHSRDFKDEHDLCQTEIEQTADTAALACSPSSINSSPERASSESESASPLPSPTGSASTSSAASFTWLHNSLPDIREPRGPLSVEINNSKPKTNGSVLATTRQNSGSTRSSSSADSCDGISLLGPTHSLNELQVLERRRRPRHIRPSQRNCHSNSSSEELEELDNLFVACHTPPRIRRSCSWNERARKVVGVASAGYLNASYQNLTLLNYTDNWLPAEILQKNHKRSPAEEMSKQSSNTCGNYEHMICKGNFLLDEISKVYDKNVSILTDKPVLDTKLPAPVECDLNEPIECSKVQHVQLNIKPPPRQKRLTQQPPAAMTFNGLVKTFDQDPTNLRTSYTQSLEQCHLDEQETAKPASYPPSAISQRFLPKRRFQSQTSAAKQRSLVSSTPNLAASDDGQPESEYDIYVSSAHASMHQLPQTTTLPKPLGILLPAGSRHSFGKEVSFCPVVSKYCWQEQSSEEPTEDQFHSSEGEQGPPSDDELMDPTLVHNTRENENIAALFEPEPEQAHRLREPAIAQKFTGFHTNALLSASTHAEKNLSCEESANVKNKANLATPDCRDQRTEAKTTLEPEPALSSTVSLKPCAVANSSCREETPSDAINEPASATARPLSLPILSEPPTNRAHRILYSSQQLRRYEPKASPINKMPPANELSPQAAAVARTDEKHPTSRSLFSRFTHGLRFSLRRKKKQQQQEPSQVKESPKELRQSPEESQPVDFVHIPLKPPRSSQCGRLDDTIVSETSSGHVHSWQQQEQLGKTSTLQKVTGKPPLPKMPPRSGILTHAPQETTGETVNCHRTEALPSVEREHCNQLTGQLVAKVQAQRMRDTGLSSQIVVAEETHTVNRLAGHGDATRPTVVTAVPVSVAPVAEVDKMGLIETNLDTHETVISGKTRSLMDITCNPLSMPHKRYIVKRLNVNSVAYDVDELDAEVKPSPGGMASVRRPHKSMEFLLDKENQKNILPPENELQKSHDHNPGALSEHQLRVQASLQRLNIPDWFRHYNKGPEKAADGENACTSATGGGYRPGNFTRKRAQESGRWQGLNSKTTSLSSLGSQRSDRSPLLMSPSAHSHHGGQSSYSCGSTTIHGPAPVQIGMGATRWSTSHLNSTQMSPGASQRGSFTRGAPINSSFISVASGSGLLRNSYRQPYLGWRSTEKLSQRTPHERLANSLLTQRTAPPSTRAGNETRTLHSVSTEIQSSIKEVTSAIVHFVNDQQQSQHPRSRSTSPNSSFVLSNSRCWLESSFVGTRTLDSPQTPVIDNSPPELARKQQQLHPHQVHLDVGLSPVVSAGQLPHRMNGINRIGNGGGESAIQV
Protein: Triggering receptor expressed on myeloid cells 1 (TREM-1) (CD antigen CD354) (Q9JKE2)
Organism: Mus musculus (Mouse)
Function: Cell surface receptor that plays important roles in innate and adaptive immunity by amplifying inflammatory responses. Upon activation by various ligands such as PGLYRP1, HMGB1 or HSP70, multimerizes and forms a complex with transmembrane adapter TYROBP/DAP12. In turn, initiates a SYK-mediated cascade of tyrosine phosphorylation, activating multiple downstream mediators such as BTK, MAPK1, MAPK3 or phospholipase C-gamma. This cascade promotes the neutrophil- and macrophage-mediated release of pro-inflammatory cytokines and/or chemokines, as well as their migration and thereby amplifies inflammatory responses that are triggered by bacterial and fungal infections. By also promoting the amplification of inflammatory signals that are initially triggered by Toll-like receptor (TLR) and NOD-like receptor engagement, plays a major role in the pathophysiology of acute and chronic inflammatory diseases of different etiologies including septic shock and atherosclerosis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9NP99}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9NP99}. Note=Recruited to lipid rafts when activated. {ECO:0000250|UniProtKB:Q9NP99}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- High mobility group protein B1
- Triggering receptor expressed on myeloid cells 2
- Transcription initiation factor IIA subunit 2
- Peptidoglycan recognition protein 1
- Trem-like transcript 1 protein
- Trem-like transcript 2 protein
- C-type lectin domain family 5 member A
- Interleukin-1 beta
- Cold-inducible RNA-binding protein
Sequence:
MRKAGLWGLLCVFFVSEVKAAIVLEEERYDLVEGQTLTVKCPFNIMKYANSQKAWQRLPDGKEPLTLVVTQRPFTRPSEVHMGKFTLKHDPSEAMLQVQMTDLQVTDSGLYRCVIYHPPNDPVVLFHPVRLVVTKGSSDVFTPVIIPITRLTERPILITTKYSPSDTTTTRSLPKPTAVVSSPGLGVTIINGTDADSVSTSSVTISVICGLLSKSLVFIILFIVTKRTFG
Protein: Potassium channel subfamily K member 13 (Tandem pore domain halothane-inhibited potassium channel 1) (THIK-1) (Q9HB14)
Organism: Homo sapiens (Human)
Function: Potassium channel displaying weak inward rectification in symmetrical K(+) solution.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium channel subfamily K member 18
- Potassium channel subfamily K member 12
- Potassium channel subfamily K member 6
- Potassium channel subfamily K member 4
- Keratin, type II cytoskeletal 2 oral
- Potassium channel subfamily K member 7
Sequence:
MAGRGFSWGPGHLNEDNARFLLLAALIVLYLLGGAAVFSALELAHERQAKQRWEERLANFSRGHNLSRDELRGFLRHYEEATRAGIRVDNVRPRWDFTGAFYFVGTVVSTIGFGMTTPATVGGKIFLIFYGLVGCSSTILFFNLFLERLITIIAYIMKSCHQRQLRRRGALPQESLKDAGQCEVDSLAGWKPSVYYVMLILCTASILISCCASAMYTPIEGWSYFDSLYFCFVAFSTIGFGDLVSSQNAHYESQGLYRFANFVFILMGVCCIYSLFNVISILIKQSLNWILRKMDSGCCPQCQRGLLRSRRNVVMPGSVRNRCNISIETDGVAESDTDGRRLSGEMISMKDLLAANKASLAILQKQLSEMANGCPHQTSTLARDNEFSGGVGAFAIMNNRLAETSGDR