wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-binding cassette sub-family F member 3 (Q8K268)
Organism: Mus musculus (Mouse)
Function: Displays an antiviral effect against flaviviruses such as west Nile virus (WNV) in the presence of OAS1B.
Interaction partners:
- Stalled ribosome sensor GCN1
- Large ribosomal subunit protein bL20m
- Actin-related protein 8
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein bL33m
- Small ribosomal subunit protein uS3
Sequence:
MATCADILRSEFPEIDGQVFDYVTGVLHSGSADFESVDDLVEAVGELLQEVSGDSKDDAGIRAVCQRMYNTLRLAEPQNQGNSQVLLDAPIQLSKIMENYDCDTKLPGLLKREQSSTVNAKKLEKAEARLKAKQEKRSEKETLKTSNPLVLEEASASQAGSRKESRLESSGKNKSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLHVEQEVAGDDTPALQSVLESDTVREDLLRQERELSLRIAAGRAEGSEAAQLAEIYGKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKPVDKESEVVLKFPDGFEKFSPPILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFPGLPEEEYRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSVTRVEGGFDQYRALLQEQFRREGFL
Protein: Replicative DNA helicase DnaB (EC 5.6.2.3) (DNA 5'-3' helicase DnaB) (O83097)
Organism: Treponema pallidum (strain Nichols)
Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
Interaction partners:
- DNA primase
- Elongation factor Tu
- Large ribosomal subunit protein bL9
- DNA polymerase III subunit gamma/tau
- Single-stranded DNA-binding protein
- Chromosomal replication initiator protein DnaA
- DNA topoisomerase 1
- Uncharacterized protein TP_0059
- Beta sliding clamp
- Replication restart protein PriA
Sequence:
MPGMPNPTQELKGKIPPHNLEAERAVLGAVLLDDSALSTATEQLSASSFYSAAHQRIFQALVELSDLGQRPDILVLSEHLRSCEALDFVGGSAYVASLTDAVPSAANVEYYTRIVCDAAMRRSLLKVARIITAEAFNDTVSGNIVLETAQREIYDLTNARRVATFKLLKNLIPDLVNTIETRYRNQSDLVGIATGLTALDNLTGGFQNSELIVIGARPSMGKTALAMTMASNIAIRQRIPTAFFSLEMSNLLLMQRLIAAESGVSATNLRKGLLQLSDFGRIQNAAGEMYDAPLYIVDVPNMKLLDLRAVARRLCVQEKIQIIFVDYLGLIVADNPFAPRYEQFAAISQSLKSLARELDIPIVALSQVGRPAEGSAPNLADIRGSGAIEQDADVVMFLHRDRNETETQLILAKQRNGPIGTVELEFQASFTRFVCKSP
Protein: Uncharacterized protein slr1608 (P73001)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Glutaminase
Sequence:
MLIPFLFKLTLPLASGIALSSCGTLPEADLGTAAGNQTSSEPTNSVEIVQANQPEIKAVPVIDGLEHPWGMAWLPNGDILITERPGRLRIVRDGVLDPEAIAGVVAVSTVSAQQLFASQQGGLLDIALHPRFAENRFVYFTYSHGTQQANRTRVARAVFDGEKLTDWQVIFEVGQTKPGGQHFGSRLTWLPDETLLVSIGDGGNPPVELEGDFIRQQAQNRASHLGKIIRINDDGTVPADNPFRNDPKAAPEVWSYGHRNIQGLAYDPVTQKVWATEHGSRGGDELNLIQKGKNYGWPVVSFSKEYSTDQPVAPATSRPDMVDPLQIWTPAIAPSGLTIYNGDRHPEWQGTIFAGGLVDRGIRHLRLDENNQIIDETTISIGQRVRDVRQGPDGHVYVLTDQNNGQLLRLES
Protein: Eukaryotic translation initiation factor 2 subunit alpha homolog (Q9SIZ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.
Interaction partners:
- protein-synthesizing GTPase
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor 2 subunit beta
- Translation initiation factor eIF2B subunit gamma
- eIF-2-alpha kinase GCN2
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit E
- protein-synthesizing GTPase
- Eukaryotic translation initiation factor 3 subunit I
Sequence:
MASQTPNLECRMYEAKYPEVDMAVMIQVKNIADMGAYVSLLEYNNIEGMILFSELSRRRIRSVSSLIKVGRIEPVMVLRVDKEKGYIDLSKRRVSEEDIQTCEERYNKSKLVHSIMRHVAETLSIDLEDLYVNIGWPLYRRHGHAFEAFKILVTDPDSVLGPLTREIKEVGPDGQEVTKVVPAVTEEVKDALVKNIRRRMTPQPMKIRADIELKCFQFDGVVHIKEAMKNAEAAGNEDCPVKIKLVAPPLYVLTTQTLDKEQGIEILNKAIAACTETIETHKGKLVVKEGARAVSERDEKMLTEHMAKLRLDNEEMSGDEDSGDEEEDTGMGEVDLDAGAGIIE
Protein: Delta-sarcoglycan (Delta-SG) (35 kDa dystrophin-associated glycoprotein) (35DAG) (Q92629)
Organism: Homo sapiens (Human)
Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Subcellular location: Cell membrane, sarcolemma; Single-pass type II membrane protein. Cytoplasm, cytoskeleton.
Interaction partners:
- Alpha-sarcoglycan
- Dystroglycan 1
- Beta-sarcoglycan
- Sarcospan
- Dystrophin
- Epsilon-sarcoglycan
- Gamma-sarcoglycan
- Caveolin-3
- Filamin-C
- Alpha-1-syntrophin
Sequence:
MPQEQYTHHRSTMPGSVGPQVYKVGIYGWRKRCLYFFVLLLMILILVNLAMTIWILKVMNFTIDGMGNLRITEKGLKLEGDSEFLQPLYAKEIQSRPGNALYFKSARNVTVNILNDQTKVLTQLITGPKAVEAYGKKFEVKTVSGKLLFSADNNEVVVGAERLRVLGAEGTVFPKSIETPNVRADPFKELRLESPTRSLVMEAPKGVEINAEAGNMEATCRTELRLESKDGEIKLDAAKIRLPRLPHGSYTPTGTRQKVFEICVCANGRLFLSQAGAGSTCQINTSVCL
Protein: Bisdemethoxycurcumin synthase (EC 2.3.1.211) (Curcuminoid synthase) (Q8LIL0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Plant-specific type III polyketide synthase (PKS) that catalyzes the one-pot formation of the C6-C7-C6 diarylheptanoid scaffold of bisdemethoxycurcumin by the condensation of two molecules of 4-coumaroyl-CoA and one molecule of malonyl-CoA.
Interaction partners:
- 4-coumarate--CoA ligase
- 4-coumarate--CoA ligase-like 9
- Chalcone--flavanone isomerase
- Agmatine hydroxycinnamoyltransferase 1
- Chalcone-flavonone isomerase family protein
- Chalcone-flavonone isomerase family protein
- 4-coumarate--CoA ligase-like 1
- Os11g0205400 protein
- 4-coumarate--CoA ligase-like 2
- 4-coumarate--CoA ligase-like 3
Sequence:
MAPTTTMGSALYPLGEMRRSQRADGLAAVLAIGTANPPNCVTQEEFPDFYFRVTNSDHLTALKDKFKRICQEMGVQRRYLHHTEEMLSAHPEFVDRDAPSLDARLDIAADAVPELAAEAAKKAIAEWGRPAADITHLVVTTNSGAHVPGVDFRLVPLLGLRPSVRRTMLHLNGCFAGCAALRLAKDLAENSRGARVLVVAAELTLMYFTGPDEGCFRTLLVQGLFGDGAAAVIVGADADDVERPLFEIVSAAQTIIPESDHALNMRFTERRLDGVLGRQVPGLIGDNVERCLLDMFGPLLGGDGGGGWNDLFWAVHPGSSTIMDQVDAALGLEPGKLAASRRVLSDYGNMSGATVIFALDELRRQRKEAAAAGEWPELGVMMAFGPGMTVDAMLLHATSHVN
Protein: Spore coat protein SP65 (Spore coat protein E) (Q9NAX4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Forms a triad with cellulose and pspB that is essential for spore outer layer formation.
Subcellular location: Spore wall {ECO:0000269|PubMed:17416892}. Note=Depends on pspB for incorporation into the coat. Accumulates initially in vesicles distinct from prespore vesicles (PSVs).
Interaction partners:
- Uncharacterized protein
- Nuclear pore protein
- ATP-dependent RNA helicase ddx19
- Nuclear pore complex protein
- Uncharacterized protein
- Nucleoporin 133
- mRNA export factor GLE1
- Nuclear pore protein
- Nuclear pore complex protein nup85
- Uncharacterized protein
Sequence:
MKVLLLLVCLVFAYVNASYDACYNVVCPSNYQCRAEGDQAYCVPEHHEYGCDRHSCGRGYECVERWDSFCCKPIHHRPHPHPRPPHPHPRPTNCDYTSCPREFDCHVINRNVTACLPDNHVCRDFQCPVGTHCFNGERGPHCVSDTHYPNLCRVTKCSYDFTCKMVRGNPTCLRNHDGISTHSPTHTPTHSPTTSPTHCPSCTELAPFCHSAGLVCRTILNPSCVSAVRGIINTRSCCTYIAVCASNSTSTTGATTGATTPTSTTGAATTAAATTTTATSTTGAATTAPATTTTTSTTGAATTAPATTTTSTTGAATTAPATTTTTATTIVGVTTANSVGGLTTTRATTVAGVTTANSVGGLTTAGITTVAGATTGNSVGGLTTARATTVADVTTANSVGGLTTAGVTTVAGATTGNSVGGLTTARATTVADVTTANSVGGLTTSRATTIAGATTANSIGGLTN
Protein: Peroxisome proliferator-activated receptor gamma (E2IH99)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MVDTRRAAWSLLSFGLGTLDLAEMDNKMNSFDMETLSTLDYPYLPSLEYSHNSPHHHSPDRSHSFNHSPDRSQSFNHSPDRNHSINHSPDRSYSYNHRSDRSHSFNHSPDRSHSFNHSPDRSQSFNHSPDRNHSINHSPDRSHSYNHRSDRSHSFNHSPDRSHSFNHSPDRSHSFNHRSDRSHSFNHSPDKSHSYNYTYSGNQNASSPLNIDCRVCGDKASGFHYGVHACEGCKGFFRRTVRLKLVYDHCELHCRIHKKSRNKCQYCRFQKCLLVGMSHDAIRFGRMPQVEREKLQAEFMDVDPRNPESAELRALSRQLCLSYHRHFPLTKSKAKAILSGKTHGNSPFVIHDMKSLTAGQYFINCRQLPVLERQRSVLPPEEPAGELELSVFRRIQIRSAEAVQEVTEFAKSIPGFTELDMNDQVILLKYGVIEVMTTMLAPLMNKDGTLFAYGQIFMTREFLKSLRKPFCEMMEPKFEFAVKFNVLELDDSDMALFFAVIILSGDRPGLVNVKPIEDLQETVLQALELQLKTIHPDCPQLFAKLLQKMTDLRQLVANHVRLIHLLKKQELEVCLHPLLQEIMRDLY
Protein: Seipin (J3KQ12)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MSTEKVDQKEEAGEKEVCGDQIKGPDKEEEPPAAASHGQGWRPGGRAARNARPEPGARHPALPAMVNDPPVPALLWAQEVGQVLAGRARRLLLQFGVLFCTILLLLWVSVFLYGSFYYSYMPTVSHLSPVHFYYRTDCDSSTTSLCSFPVANVSLTKGGRDRVLMYGQPYRVTLELELPESPVNQDLGMFLVTISCYTRGGRIISTSSRSVMLHYRSDLLQMLDTLVFSSLLLFGFAEQKQLLEVELYADYRENSYVPTTGAIIEIHSKRIQLYGAYLRIHAHFTGLRYLLYNFPMTCAFIGVASNFTFLSVIVLFSYMQWVWGGIWPRHRFSLQVNIRKRDNSRKEVQRRISAHQPGAGPEGQEESTPQSDVTEDGESPEDPSGTEGQLSEEEKPDQQPLSGEEELEPEASDGSGSWEDAALLTEANLPAPAPASASAPVLETLGSSEPAGGALRQRPTCSSS
Protein: Ephrin A3 (A0A0G2JV56)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- receptor protein-tyrosine kinase
- Ephrin type-A receptor 2
- Ephrin type-A receptor 1
- Ephrin type-A receptor 3
- Ephrin type-A receptor 8
- Ephrin type-A receptor 7
- Ephrin type-A receptor 10
- Ephrin type-A receptor 5
- Ras GTPase-activating protein 1
- Tyrosine-protein kinase Fyn
Sequence:
MAAAPLLLLLLLVPVPLLPLLAQGPGGALGNRHAVYWNSSNQHLRREGYTVQVNVNDYLDIYCPHYNSSGPGGGAEQYVLYMVNLSGYRTCNASQGSKRWECNRQHASHSPIKFSEKFQRYSAFSLGYEFHAGQEYYYISTPTHNLHWKCLRMKVFVCCASTSHSGEKPVPTLPQFTMGPNVKINVLEDFEGENPQVPKLEKSISGTSPKREHLPLAVGIAFFLMTLLAS
Protein: Dysbindin protein homolog (Biogenesis of lysosome-related organelles complex 1 subunit 8) (BLOC-1 subunit 8) (Q9XWQ1)
Organism: Caenorhabditis elegans
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in gut granule biogenesis.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- SNAPIN protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Glycolipid transfer protein domain-containing protein
- CCM gene homolog
- mitogen-activated protein kinase kinase
- Dual specificity mitogen-activated protein kinase kinase mek-2
Sequence:
MDMLNTLRDTLSSVQAELSTGVEKLRMNVSANIVAQQKVSTESVNEILNTSAGNELLQNFQNLITEVEENGAEGGRLANLCSTRMGRCQQMCKEKADAVMEIDEFLRNSVEFDKKIREINAQISKLTRFCNQTEQAMTYLEALCEVAHTEGEVDLIRQQAKSAATIVQIECESPSVLTSALRSRPEDAVKAQQEEVMLEEFLSSKNMQLP
Protein: Meiosis induction protein kinase IME2/SME1 (EC 2.7.11.1) (P32581)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein kinase which is essential for the initiation of meiosis and sporulation.
Interaction partners:
- Meiosis-specific transcription factor NDT80
- Suppressor of mar1-1 protein
- DNA replication licensing factor MCM2
- Cell division control protein 6
- Origin recognition complex subunit 6
- Origin recognition complex subunit 3
- DNA replication licensing factor MCM3
- Minichromosome maintenance protein 5
- Origin recognition complex subunit 1
- DNA replication licensing factor MCM6
Sequence:
MVEKRSRQSSSSGSEFSVPPDVDNPPLSIPLKTLSDRYQLIEKLGAGSFGCVTLAKAQFPLSNILGKQHDIRGTLMDQPKNGHQNYITKTQGVVAIKTMMTKLHTLQDYTRVREIKFILAIPANDHLIQIFEVFIDSENYQLHIVMECMEQNLYQMMKHRRRRVFSIPSLKSILSQILAGLKHIHEHNFFHRDLKPENILITPSTQYFEKEYMNQIGYQDNYVIKLADFGLARHVENKNPYTAYVSTRWYRSPEILLRSGYYSKPLDIWAFGCVAVEVTVFRALFPGANEIDQIWKILEVLGTPIKRSDFVNTNHITAPPPGGFWDDASNLVHKLNLKLPYVEGSSLDHLLSSSQLSDLSEVVKKCLRWDPNERATAQELCEMPFFENTVASQVDARGNVTNTEQALIFAGINPVATNTKPIYFNSSTKLPAETESNDIDISNNDHDSHAMCSPTLNQEKLTLVEFLNEFVEEDNDDHSIPDVGTDSTISDSIDETELSKEIRNNLALCQLPDEEVLDHSLSNIRQLTNDIEIINKDEADNMEQLFFDLEIPEKDEFQRKQPFNEHADIDEDIVLPYVNNSNYTHTDRSHHRGDNVLGDASLGDSFNSMPDFTPRNFLIPTLKKSREKFEPHLSNSNQHFGNVTF
Protein: G kinase-anchoring protein 1 (cGMP-dependent protein kinase-anchoring protein of 42 kDa) (Q5VSY0)
Organism: Homo sapiens (Human)
Function: Regulates insulin-dependent IRS1 tyrosine phosphorylation in adipocytes by modulating the availability of IRS1 to IR tyrosine kinase. Its association with IRS1 is required for insulin-induced translocation of SLC2A4 to the cell membrane. Involved in TNF-induced impairment of insulin-dependent IRS1 tyrosine phosphorylation.
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:Q9JMB0}.
Interaction partners:
- cGMP-dependent protein kinase 1
Sequence:
MASAVLSSVPTTASRFALLQVDSGSGSDSEPGKGKGRNTGKSQTLGSKSTTNEKKREKRRKKKEQQQSEANELRNLAFKKIPQKSSHAVCNAQHDLPLSNPVQKDSREENWQEWRQRDEQLTSEMFEADLEKALLLSKLEYEEHKKEYEDAENTSTQSKVMNKKDKRKNHQGKDRPLTVSLKDFHSEDHISKKTEELSSSQTLSHDGGFFNRLEDDVHKILIREKRREQLTEYNGTDNCTAHEHNQEVVLKDGRIERLKLELERKDAEIQKLKNVITQWEAKYKEVKARNAQLLKMLQEGEMKDKAEILLQVDESQSIKNELTIQVTSLHAALEQERSKVKVLQAELAKYQGGRKGKRNSESDQCR
Protein: peptidyl-tRNA hydrolase (EC 3.1.1.29) (J3KQ48)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMPSKSLVMEYLAHPSTLGLAVGVACGMCLGWSLRVCFGMLPKSKTSKTHTDTESEASILGDSGEYKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQDAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY
Protein: Glypican-1 (G1MQ88)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}. Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
MLRSSGVKSFPFQREHLRICPQGYTCCTSEMEENFANKSRSEFEAMMKEAGRSVQTILTAQYRSFDNYFQDLLNKSEKALYDTFPSLYGELYTQNTKVFKDLYSELRRYYRGSNINLEEALNEFWTRLLERLFKLMNAQYHITDEYLDCMVKHAEQHKPFGEVPRDLKVKATRAFIVARSYAQGFLVGSDVVKKVSQVSLSHECTRAVMKLMYCPHCRGMASVKPCSNYCLNVVKGCLANQADLNTEWKYLMDALVAVADRIDGPYNVDTVIGTIHMRISEAISNLQENKDSITAKVFQGCGNPKISTKGSSSEDKKRRGKVTLEAKSSAVALEMLVLDAKGNLTALKSYWVTLPGVLCSKKVMASAAADDKCWNGMTKGSYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLGNANMGNDVDFQDASDDMSGSGSGDSCPDDVCGKRLSKSPSTRQPETHAIPKQSGHGVIGASSRSLPSAFLLFLLGASIAVQHLWR
Protein: NUF2 component of NDC80 kinetochore complex (E9PQC4)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
METLSFPRYNVAEIVIHIRNKILTGADGKNLTKNDLYPNPKPEVLHMIYMRALQIVYGIRLEHFYMMPVNSEVMYPHLMEGFLPFSNLVTHLDSFLPICRVNDFETADILCPKAKRTSRFLSGIINFIHFREACRETYMEFLWQYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQEGNSQKKSNISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARSLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYERVTTINQEIQKIKLGIQQLKDAAEREKLKSQEIFLNLKTALEKYHDGIEKAAEDSYAKIDEKTAELKRKMFKMST
Protein: Transcriptional regulator SlyA (B1JJ73)
Organism: Yersinia pseudotuberculosis serotype O:3 (strain YPIII)
Function: Transcription regulator that can specifically activate or repress expression of target genes.
Interaction partners:
Sequence:
MESTLGSDLARLVRVWRALIDHRLKPLELTQTHWVTLYNINRLPPEQSQIQLAKAIGIEQPSLVRTLDQLEEKGLITRHTCANDRRAKRIKLTEQSSPIIEQVDGVICSTRKEILGGISSDEIAVLSGLIDKLEKNIIQLQTK
Protein: Intercellular adhesion molecule 3 (ICAM-3) (CDw50) (ICAM-R) (CD antigen CD50) (P32942)
Organism: Homo sapiens (Human)
Function: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM3 is also a ligand for integrin alpha-D/beta-2. In association with integrin alpha-L/beta-2, contributes to apoptotic neutrophil phagocytosis by macrophages.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- CD209 antigen
- Integrin beta-2
- Integrin alpha-L
- C-type lectin domain family 4 member M
- Intercellular adhesion molecule 2
- Intercellular adhesion molecule 1
- Moesin
- Inter-alpha-trypsin inhibitor heavy chain H4
- Vascular cell adhesion protein 1
- Syncytin-1
Sequence:
MATMVPSVLWPRACWTLLVCCLLTPGVQGQEFLLRVEPQNPVLSAGGSLFVNCSTDCPSSEKIALETSLSKELVASGMGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVYRLPERVELAPLPPWQPVGQNFTLRCQVEDGSPRTSLTVVLLRWEEELSRQPAVEEPAEVTATVLASRDDHGAPFSCRTELDMQPQGLGLFVNTSAPRQLRTFVLPVTPPRLVAPRFLEVETSWPVDCTLDGLFPASEAQVYLALGDQMLNATVMNHGDTLTATATATARADQEGAREIVCNVTLGGERREARENLTVFSFLGPIVNLSEPTAHEGSTVTVSCMAGARVQVTLDGVPAAAPGQPAQLQLNATESDDGRSFFCSATLEVDGEFLHRNSSVQLRVLYGPKIDRATCPQHLKWKDKTRHVLQCQARGNPYPELRCLKEGSSREVPVGIPFFVNVTHNGTYQCQASSSRGKYTLVVVMDIEAGSSHFVPVFVAVLLTLGVVTIVLALMYVFREHQRSGSYHVREESTYLPLTSMQPTEAMGEEPSRAE
Protein: Caspase a (EC 3.4.22.36) [Cleaved into: Caspase a subunit p20; Caspase a subunit p10] (Q9I9L7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Thiol protease which cleaves IL-1 beta (il1b), releasing the mature cytokine which is involved in a variety of inflammatory processes, and mediates apoptosis. Component of the NLRP1 inflammasome, which plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, recruited to the NLRP1 inflammasome in its precursor form. Its subsequent activation causes the cleavage of pro-il1b into the midformed il1b, which then evetually leads to il1b maturation and secretion in the extracellular milieu. Required for the development of the cartilaginous pharyngeal skeleton.
Subcellular location: Inflammasome {ECO:0000269|PubMed:30150286}. Cytoplasm {ECO:0000269|PubMed:12464617, ECO:0000269|PubMed:30150286}. Note=Co-localizes with pycard, nlrp1 and caspb in the cytoplasm (PubMed:30150286). Co-localizes with pycard at large cytoplasmic aggregates, known as specks (PubMed:12464617, PubMed:30150286). {ECO:0000269|PubMed:12464617, ECO:0000269|PubMed:30150286}.
Interaction partners:
- Apoptosis-associated speck-like protein containing a CARD
- Interleukin-1.
- NACHT, LRR and PYD domains-containing protein 1 homolog
- Caspase 8, apoptosis-related cysteine peptidase
- Caspase 22, apoptosis-related cysteine peptidase
- Caspase b,-like
- NACHT domain-containing protein.
- Nucleotide-binding oligomerization domain-containing 1.
- Myeloid differentiation primary response protein MyD88
- NOD2a protein
Sequence:
MAKSIKDHLQDALSNIGADNLRRFQSRLGDRKQEPRVRKSTIEKLKDEIDLVDLLVNTFTSDAVSVTVDILRGIKCNAVAEELLENTGQGGVSQPEPPVPEPIPKDPAQLKELKVTPCSQQFKNKILREKGQETYEIKDKSVRKRLALLINNVDFDDKAMKRSGSEKDEENMEKLLKELDYQVVKRPNLSAKEMDEAIRDFAQREEHKYSDSAFVVIMSHGKRDAIMGVHYHRTNNPSDSFPVDNVYRRLNSENCPALRDKPKVILIQACRGGEHGRVWASDGEPDEPIEIEDDDFVHKEKDFISLMSCTPDTKSYRHVQNGTFYVQTLVDVFIKCAHEDHIEELFRKVLRRFEHPNMIGNFKQMACKDRATLPKLFYLFPGL
Protein: BARP protein (Q38CV3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSITFNNLWLLLTVLCTSGIRAHHVWNDCFADGNHPPVDEIPVLCRVAEQLRGLPDTISSAVETAAAASSKAFEAKVQAEEAVELAESKGLNVTKAKEAAVRATLAAEAAATAASNVEINAANIAAVPWSQRRQDVGLQELALCDNVDKDVREAAAKCTKKADNVTAQSLSAALEALENLYTDVNTRETLRREDVEFHTELKSLEEHVEEAVRAQKQAEDAAADAIKIAGTNTGPVVNSVASPEGSVLLLMAGLFLGSVL
Protein: Phosphatidylinositol 3-kinase catalytic subunit type 3 (EC 2.7.1.137) (Q9W1M7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ras-related protein Rab5
- non-specific serine/threonine protein kinase
- Beclin-1-like protein
- Autophagy-related 14
- UV radiation resistance-associated gene protein
- Autophagy-related 1, isoform B
- Autophagy-related protein 13 homolog
- Autophagy protein 5
- Autophagy protein 12-like
- RB1-inducible coiled-coil protein 1
Sequence:
MDQPDDHFRYIHSSSLHERVQIKVGTLEGKKRQPDYEKLLEDPILRFSGLYSEEHPSFQVRLQVFNQGRPYCLPVTSSYKAFGKRWSWNEWVTLPLQFSDLPRSAMLVLTILDCSGAGQTTVIGGTSISMFGKDGMFRQGMYDLRVWLGVEGDGNFPSRTPGKGKESSKSQMQRLGKLAKKHRNGQVQKVDWLDRLTFREIEVINEREKRMSDYMFLMIEFPAIVVDDMYNYAVVYFEPEGDVKYKLPAKPKLVSVPDSEIQMENLVERKHHRLARSERSGISDRDAKPTASIRDQLHTIVYRYPPTYVLSSEEQDLVWKFRFYLSSHKKALTKFLKCINWKLEDEVTQALWMLANWAPMDVEDALELLSPTFTHPQVRKYAVSRLAQAPDEDLLLYLLQLVQALKYEDPRHIVHLHGCIFPERDVVRSILDDNGSLLDQSSLSDLSATSSGLHGSVIPANQRAASVLAAIKSDKSVSPGSAGGSGSGGQGSVALPNPSAPATPGSSSLPCDSNSNALMLAEGISFGSVPANLCTFLIQRACTNATLANYFYWYLSIEVEEVESVRKQDERAHDMYAMVLKMFLKVLENGNFNLRGIFYNLRKQRRFIDELVKLVKLVAKEPGNRNKKTEKFQKLLAEQDMFKVNFTNFEPIPFPLDPEIYITKIVPMRTSLFKSALMPAKLTFVTSIAHHEYAAIFKHGDDLRQDQLILQMITLMDKLLRRENLDLKLTPYKVLATSSKHGFLQYVDSCTVAEVLAREGNIHNFFRKHHPCDNGPYGISAEVMDTYIKSCAGYCVITYLLGVGDRHLDNLLLTTNGKLFHIDFGYILGRDPKPMPPPMKLSKEMVEAMGGISSEHHHEFRKQCYTAYLHLRRHANVMLNLFSLMVDATVPDIALEPDKAVKKVEENLQLGLTDEEAVQHLQSLLDVSITAVMPALVEQIHRFTQYWRK
Protein: Mitogen-activated protein kinase 6 (MAP kinase 6) (MAPK 6) (EC 2.7.11.24) (Extracellular signal-regulated kinase 3) (ERK-3) (MAP kinase isoform p97) (p97-MAPK) (Q16659)
Organism: Homo sapiens (Human)
Function: Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK3/MAPK6 is phosphorylated at Ser-189 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6. May promote entry in the cell cycle (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates to the cytoplasm following interaction with MAPKAPK5. {ECO:0000250}.
Interaction partners:
- MAP kinase-activated protein kinase 5
- Neuralized-like protein 4
- G1/S-specific cyclin-D3
- Septin-7
- Ubiquitin-protein ligase E3A
- E3 ubiquitin-protein ligase HERC2
- Transcription factor Jun
- Mitogen-activated protein kinase 4
- Nuclear receptor coactivator 3
- Kalirin
Sequence:
MAEKFESLMNIHGFDLGSRYMDLKPLGCGGNGLVFSAVDNDCDKRVAIKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVFEILGPSGSQLTDDVGSLTELNSVYIVQEYMETDLANVLEQGPLLEEHARLFMYQLLRGLKYIHSANVLHRDLKPANLFINTEDLVLKIGDFGLARIMDPHYSHKGHLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKTLFAGAHELEQMQLILESIPVVHEEDRQELLSVIPVYIRNDMTEPHKPLTQLLPGISREALDFLEQILTFSPMDRLTAEEALSHPYMSIYSFPMDEPISSHPFHIEDEVDDILLMDETHSHIYNWERYHDCQFSEHDWPVHNNFDIDEVQLDPRALSDVTDEEEVQVDPRKYLDGDREKYLEDPAFDTNYSTEPCWQYSDHHENKYCDLECSHTCNYKTRSSSYLDNLVWRESEVNHYYEPKLIIDLSNWKEQSKEKSDKKGKSKCERNGLVKAQIALEEASQQLAGKEREKNQGFDFDSFIAGTIQLSSQHEPTDVVDKLNDLNSSVSQLELKSLISKSVSQEKQEKGMANLAQLEALYQSSWDSQFVSGGEDCFFINQFCEVRKDEQVEKENTYTSYLDKFFSRKEDTEMLETEPVEDGKLGERGHEEGFLNNSGEFLFNKQLESIGIPQFHSPVGSPLKSIQATLTPSAMKSSPQIPHQTYSSILKHLN
Protein: Polyribonucleotide nucleotidyltransferase (EC 2.7.7.8) (Polynucleotide phosphorylase) (PNPase) (Q3IJ73)
Organism: Pseudoalteromonas translucida (strain TAC 125)
Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
Interaction partners:
- Ribonuclease E
- Transcription termination/antitermination protein NusA
- Transcription termination factor Rho
- Translation initiation factor IF-2
- tRNA pseudouridine synthase B
- Poly
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS4
Sequence:
MQAIIKEFQLGQHTVTLETGAIARQADGAVLASIGDTSVLVTVVGKREAQPGQDFFPLTVNYQERMYAAGRIPGGFLKREGRPNDGETLIARLIDRPIRPLFPSGFVNEVQVIATVVSVNPEIQPDMVALIGTSAALAISGIPFSGPIGATRVGYIDGEYVLNPTLKELEESKLDLVVAGTDNAVLMVESEADVLAEDIMLGAVVYGHEQAQAIITAIKEFKAEAGKPTWDWTAPAKNVSLEEKVASIAADKVGEAYRITDKVARKEALGVAKDEVVAVLTSELAEGESLDKQEIGKIFGSLEKKIVRGRIAAGEKRIDGREPDMIRALDVMTGVLPRTHGSAIFTRGETQALVTATLGTERDSQLIDDLTGTHKNHFMLNYNFPPFCVGETGFVGSPKRREIGHGNLAKRGIAAVMPTLTEFPYSIRVVSEITESNGSSSMASVCGTSLALMNAGVPIKASVAGIAMGLVKEDDKFVVLSDILGDEDHLGDMDFKVAGTAGGITALQMDIKIEGITQEIMQIALKQAKAARLHILEVMDKAISAPSEELSQFAPRIYTMKIPQKKIAEVIGKGGATIRQLTEETGTTIEIGDDGTIKIAATDGESAANAISRIEQLTAELEVGTIYEGKVVRIVDFGAFVNILPGKDGLVHISQISTERVNNVTDHLSEGQEVKVKVLEVDRQGRVRLSIKEAMESAAPAADAPTDA