wanglab/gogpt-training-data huggingface dataset:
Protein: Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (EC 1.2.1.12) (Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2) (GAPDH-2) (Spermatogenic glyceraldehyde-3-phosphate dehydrogenase) (Q9ESV6)
Organism: Rattus norvegicus (Rat)
Function: May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphoglycerate kinase
- Phosphoglycerate kinase 1
- Fructose-bisphosphate aldolase A
- Triosephosphate isomerase
- Triosephosphate isomerase.
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- Fructose-bisphosphate aldolase C
- Fructose-bisphosphate aldolase B
- Glucose-6-phosphate isomerase
Sequence:
MSRRDVVLTNVTVVQLRRDPCPCPCPCPCPCPCPVIRPPPPPPKVEEPPPPKEEPPPPPPPPPPPQIEPEEPKEAPPPPPPPPPPPPPPPPPPPKPAKELTVGINGFGRIGRLVLRVCMEKGVRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDAPMLVMGVNEKDYNPGSMTVVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGYSHRVVDLLRYMFSREK
Protein: cDNA, FLJ93607 (B2R7U5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004414}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004656}.
Interaction partners:
Sequence:
MIALFNKLLDWFKALFWKEEMELTLVGLQYSGKTTFVNVIASGQFNEDMIPTVGFNMRKITKGNVTIKLWDIGGQPRFRSMWERYCRGVSAIVYMVDAADQEKIEASKNELHNLLDKPQLQGIPVLVLGNKRDLPGALDEKELIEKMNLSAIQDREICCCSISCKEKDNIDITLQWLIQHSKSRRS
Protein: Photosystem II stability/assembly factor HCF136, chloroplastic (O82660)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential for photosystem II (PSII) biogenesis; required for assembly of an early intermediate in PSII assembly that includes D2 (psbD) and cytochrome b559. Has been suggested to be required for chlorophyll a binding.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:9736608}. Note=Restricted to the stromal lamellae (PubMed:9736608). Translocation into the thylakoid lumen occurs via the Tat pathway (Probable) (PubMed:10664464). {ECO:0000269|PubMed:10664464, ECO:0000269|PubMed:9736608, ECO:0000305|PubMed:11719511, ECO:0000305|PubMed:11826309}.
Interaction partners:
- Protein PAM68, chloroplastic
- PsbP-like protein 1, chloroplastic
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Protein HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 244
- Protein HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 173
- Proteasome subunit beta type-1
- Light-harvesting complex-like protein OHP1, chloroplastic
- Oxygen-evolving enhancer protein 1-2, chloroplastic
- Oxygen-evolving enhancer protein 2-1, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic
Sequence:
MASLQLCDGYLLFKPSVSPRFLSQRISHRLIPKASSSPPPSPSPSSSSSSLSFSRRELLYQSAAVSLSLSSIVGPARADEQLSEWERVFLPIDPGVVLLDIAFVPDEPSRGFLLGTRQTLLETKDGGSTWNPRSIPSAEEEDFNYRFNSISFKGKEGWIIGKPAILLYTADAGENWDRIPLSSQLPGDMVFIKATEDKSAEMVTDEGAIYVTSNRGYNWKAAIQETVSATLNRTVSSGISGASYYTGTFSAVNRSPDGRYVAVSSRGNFFLTWEPGQPYWQPHNRAVARRIQNMGWRADGGLWLLVRGGGLYLSKGTGITEEFEEVPVQSRGFGILDVGYRSEEEAWAAGGSGILLRTRNGGKSWNRDKAADNIAANLYAVKFVDDKKGFVLGNDGVLLRYVG
Protein: Myogenin (Class C basic helix-loop-helix protein 3) (bHLHc3) (Myogenic factor 4) (Myf-4) (P15173)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation, cell cycle exit and muscle atrophy. Essential for the development of functional embryonic skeletal fiber muscle differentiation. However is dispensable for postnatal skeletal muscle growth; phosphorylation by CAMK2G inhibits its transcriptional activity in respons to muscle activity. Required for the recruitment of the FACT complex to muscle-specific promoter regions, thus promoting gene expression initiation. During terminal myoblast differentiation, plays a role as a strong activator of transcription at loci with an open chromatin structure previously initiated by MYOD1. Together with MYF5 and MYOD1, co-occupies muscle-specific gene promoter core regions during myogenesis. Cooperates also with myocyte-specific enhancer factor MEF2D and BRG1-dependent recruitment of SWI/SNF chromatin-remodeling enzymes to alter chromatin structure at myogenic late gene promoters. Facilitates cell cycle exit during terminal muscle differentiation through the up-regulation of miR-20a expression, which in turn represses genes involved in cell cycle progression. Binds to the E-box containing (E1) promoter region of the miR-20a gene. Plays also a role in preventing reversal of muscle cell differentiation. Contributes to the atrophy-related gene expression in adult denervated muscles. Induces fibroblasts to differentiate into myoblasts (By similarity).
Subcellular location: Nucleus. Note=Recruited to late myogenic gene promoter regulatory sequences with SMARCA4/BRG1/BAF190A and SWI/SNF chromatin-remodeling enzymes to promote chromatin-remodeling and transcription initiation in developing embryos. {ECO:0000250}.
Interaction partners:
- Transcription factor 12
- Transcription factor E2-alpha
- Myocyte-specific enhancer factor 2C
- Paired box protein Pax-3
- Myocyte-specific enhancer factor 2A
- Paired box protein Pax-7
- Transcription factor 4
- Myocyte-specific enhancer factor 2D
- Serum response factor
- Myogenic factor 6
Sequence:
MELYETSPYFYQEPRFYDGENYLPVHLQGFEPPGYERTELTLSPEAPGPLEDKGLGTPEHCPGQCLPWACKVCKRKSVSVDRRRAATLREKRRLKKVNEAFEALKRSTLLNPNQRLPKVEILRSAIQYIERLQALLSSLNQEERDLRYRGGGGPQPGVPSECSSHSASCSPEWGSALEFSANPGDHLLTADPTDAHNLHSLTSIVDSITVEDVSVAFPDETMPN
Protein: Ferric reduction oxidase 6 (AtFRO6) (EC 1.16.1.7) (Ferric-chelate reductase 6) (Q8RWS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ferric chelate reductase involved in iron uptake by shoot and leaf cells. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nicotianamine synthase 1
- Metal transporter Nramp3
- Vacuolar iron transporter 1
- Nicotianamine synthase 3
- Fe
- Nicotianamine synthase 2
- Solute carrier family 40 member 1
- Nicotianamine synthase
- Fe
- At1g52870/F14G24_14 family protein)
Sequence:
MDDYETPLLSKDSSSSSSVITSSLKWILKVVMSMIFVTWVVFLMMMYPEQLGDDFLTFVSSKTFLGTTGTMFLIFSCPILVISVLASLYLIISGEDKVFTKKKISKFPRFRLWTFPVLVDGPFGVVSAAEFLGIMVFSVFFLWSIYAYTLRNLDLLERFHVLPKNRSILLLEVTGLRLGMIGLLCMVFLFLPISRGSILLRLIDIPFEHATRYHVWLGHITMAFFSLHGLCYVVGWIIQGQLLELIFSWNAIGIAILPGVISLVAGLLMWVTSLHTVRKNYFELFFYTHQLYIVFIVFLALHVGDYMFSIVAGGIFLFILDRFLRFCQSRRTVDVISAKSLPCGTLELVLSKPPNMRYNALSFIFLQVRELSWLQWHPFSVSSSPLDGNHHVAVLIKVLGGWTAKLRDQLSNLYEAENQDQLISPQSYPKITTCVEGPYGHESPYHLAYENLVLVAGGIGITPFFAILSDILHRKRDGKACLPSKVLVVWAIKNSDELSLLSAIDIPSICPFFSKKLNLEIHIYITRQSEPRLEDGMVHKVVHPSVKLPRTNGCSMSVLVGTGDNIWSGLYLIISTIGFISMITLLDIFYIKRYNITTWWYKGLLFVGCMVASVLIFGGLVVVFWHRWEHKTGEVEANGNDKVDLNGEETHNPSAAELKGLAIEEDVQNYTTIRYGTRPAFREIFESLNGKWGSVDVGVIVCGPATLQTTVAKEIRSHSIWRSANHPLFHFNSHSFDL
Protein: UBP1-associated protein 2B (O80678)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein that acts as component of a complex regulating the turnover of mRNAs in the nucleus. Binds with high affinity to RNA molecules that contain U-rich sequences in 3'-UTRs. May function in complex with UBP1 and contribute to the stabilization of mRNAs in the nucleus (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18278441, ECO:0000269|PubMed:18705666}. Note=Relocalizes into nuclear speckles in response to abscisic acid (ABA).
Interaction partners:
- Small nuclear ribonucleoprotein E
- Ubiquitin carboxyl-terminal hydrolase 1
- Small nuclear ribonucleoprotein E
- Ubiquitin-activating enzyme E1 2
- La-related protein 1B
- ARM repeat superfamily protein
- U2 small nuclear ribonucleoprotein A'
- La-related protein 1C
Sequence:
MTKKRKLESESNETSEPTEKQQQQCEKEDPEIRNVDNQRDDDEQVVEQDTLKEMHEEEAKGEDNIEAETSSGSGNQGNEDDDEEEPIEDLLEPFSKDQLLILLKEAAERHRDVANRIRIVADEDLVHRKIFVHGLGWDTKADSLIDAFKQYGEIEDCKCVVDKVSGQSKGYGFILFKSRSGARNALKQPQKKIGTRMTACQLASIGPVQGNPVVAPAQHFNPENVQRKIYVSNVSADIDPQKLLEFFSRFGEIEEGPLGLDKATGRPKGFALFVYRSLESAKKALEEPHKTFEGHVLHCHKANDGPKQVKQHQHNHNSHNQNSRYQRNDNNGYGAPGGHGHFIAGNNQAVQAFNPAIGQALTALLASQGAGLGLNQAFGQALLGTLGTASPGAVGGMPSGYGTQANISPGVYPGYGAQAGYQGGYQTQQPGQGGAGRGQHGAGYGGPYMGR
Protein: PX domain containing serine/threonine kinase like (E9PD56)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAFMEKPPAGKVLLDDTVPLTAAIEASQSLQSHTIAGLSLPLPPKKLIGNMDREFIAERQKGLQNYLNVITTNHILSNCELVKKFLDPNNYSANYTEIALQQVSMFFRSEPKWEVVEPLKDIGWRIRKKYFLMKIKNQPKERLVLSWADLGPDKYLSDKDFQCLIKLLPSCLHPYIYRVTFATANESSALLIRMFNEKGTLKDLIYKAKPKDPFLKKYCNPKKIQGLELQQIKTYGRQILEVLKFLHDKGFPYGHLHASNVMLDGDTCRLLDLENSLLGLPSFYRSYFSQFRKINTLESVDVHCFGHLLYEMTYGRPPDSVPVDSFPPAPSMAVVAVLESTLSCEACKNGMPTISRLLQMPLFSDVLLTTSEKPQFKIPTKLKEALRIAKECIEKRLIEEQKQIHQHRRLTRAQSHHGSEEERKKRKILARKKSKRSALENSEEHSAKYSNSNNSAGSGASSPLTSPSSPTPPSTSVEHAPF
Protein: Nucleosome assembly protein 1-like 5 (Down-regulated in liver malignancy) (Q96NT1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nucleosome assembly protein 1-like 1
- Nucleosome assembly protein 1-like 4
- Nucleolar protein 6
- Malignant T-cell-amplified sequence 2
- Testis-specific Y-encoded-like protein 4
Sequence:
MADSENQGPAEPSQAAAAAEAAAEEVMAEGGAQGGDCDSAAGDPDSAAGQMAEEPQTPAENAPKPKNDFIESLPNSVKCRVLALKKLQKRCDKIEAKFDKEFQALEKKYNDIYKPLLAKIQELTGEMEGCAWTLEGEEEEEEEYEDDEEEGEDEEEEEAAAEAAAGAKHDDAHAEMPDDAKK
Protein: Tektin-5 (Q96M29)
Organism: Homo sapiens (Human)
Function: May be a structural component of the sperm flagellum.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:G5E8A8}.
Interaction partners:
Sequence:
MEFLGTTQTASYCGPKKCCGLTSLPAVQAPVIQECYQPYYLPGYRYLNSWRPSLFYKIANVQTCPDESTSTLRPPTILPTLRSALFSRYSPHDWDQSNQLQVRGAEASRLWASRLTDDSMRLLQDKDQLTHQMQEGTCRNLGQRLSDIGFWKSELSYELDRLLTENQNLETVKRRLECAANEVNCPLQVALECLYHREKRIGIDLVHDNVEKNLIREVDLLKCCQEQMRKLAQRIDIQMRDNRDAQHVLERDLEDKSSAQCIDEKCFNLRNTSDCISFFHGMEKIDGTISVPETWAKFSNDNIKHSQNMRANSIQLREEAEHLFETLSDQMWRQFTDTNLAFNARISEVTDVKNKLQTQLAKTLQEIFQAENTIMLLERSIMAKEGPLKVAQTRLECRTRRPNMELCRDIPQLKLVNEVFTIDDTLQTLKLRLRETQDTLQLLVMTKCRLEHELAIKANTLCIDKEKCMGMRKTFPCTPRLVGHT
Protein: Interferon beta (IFN-beta) (P01575)
Organism: Mus musculus (Mouse)
Function: Type I interferon cytokine that plays a key role in the innate immune response to infection, developing tumors and other inflammatory stimuli. Signals via binding to high-affinity (IFNAR2) and low-affinity (IFNAR1) heterodimeric receptor, activating the canonical Jak-STAT signaling pathway resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response, such as antiviral proteins, regulators of cell proliferation and differentiation, and immunoregulatory proteins (By similarity). Signals mostly via binding to a IFNAR1-IFNAR2 heterodimeric receptor, but can also function with IFNAR1 alone and independently of Jak-STAT pathways. Elicits a wide variety of responses, including antiviral and antibacterial activities, and can regulate the development of B-cells, myelopoiesis and lipopolysaccharide (LPS)-inducible production of tumor necrosis factor. Plays a role in neuronal homeostasis by regulating dopamine turnover and protecting dopaminergic neurons: acts by promoting neuronal autophagy and alpha-synuclein clearance, thereby preventing dopaminergic neuron loss. IFNB1 is more potent than interferon-alpha (IFN-alpha) in inducing the apoptotic and antiproliferative pathways required for control of tumor cell growth.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01574}.
Interaction partners:
- Interferon alpha/beta receptor 1
- Toll-like receptor 4
- Toll-like receptor 3
- Interferon alpha/beta receptor 2
- Interferon regulatory factor 3
- TIR domain-containing adapter molecule 2
- TNF receptor-associated factor 3
- Interferon regulatory factor 7
- Non-receptor tyrosine-protein kinase TYK2
- Interferon gamma receptor 1
Sequence:
MNNRWILHAAFLLCFSTTALSINYKQLQLQERTNIRKCQELLEQLNGKINLTYRADFKIPMEMTEKMQKSYTAFAIQEMLQNVFLVFRNNFSSTGWNETIVVRLLDELHQQTVFLKTVLEEKQEERLTWEMSSTALHLKSYYWRVQRYLKLMKYNSYAWMVVRAEIFRNFLIIRRLTRNFQN
Protein: Protein FAM91A1 (Q658Y4)
Organism: Homo sapiens (Human)
Function: As component of the WDR11 complex acts together with TBC1D23 to facilitate the golgin-mediated capture of vesicles generated using AP-1.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:29084197, ECO:0000269|PubMed:29426865}. Cytoplasmic vesicle {ECO:0000269|PubMed:29426865}. Note=Recruitment to the TGN requires the presence of GOLGA1, GOLGA4 and TBC1D23. {ECO:0000269|PubMed:29084197}.
Interaction partners:
- Protein Njmu-R1
- TBC1 domain family member 23
Sequence:
MNIDVEFHIRHNYPWNKLPANVRQSLGNSQREYEKQVVLYSIRNQLRYRNNLVKHVKKDERRYYEELLKYSRDHLMLYPYHLSDIMVKGLRITPFSYYTGIMEDIMNSEKSYDSLPNFTAADCLRLLGIGRNQYIDLMNQCRSSKKFFRRKTARDLLPIKPVEIAIEAWWVVQAGYITEDDIKICTLPEKCAVDKIIDSGPQLSGSLDYNVVHSLYNKGFIYLDVPISDDSCIAVPPLEGFVMNRVQGDYFETLLYKIFVSIDEHTNVAELANVLEIDLSLVKNAVSMYCRLGFAHKKGQVINLDQLHSSWKNVPSVNRLKSTLDPQKMLLSWDGGESRSPVQEASSATDTDTNSQEDPADTASVSSLSLSTGHTKRIAFLFDSTLTAFLMMGNLSPNLKSHAVTMFEVGKLSDESLDSFLIELEKVQSTGEGEAQRYFDHALTLRNTILFLRHNKDLVAQTAQPDQPNYGFPLDLLRCESLLGLDPATCSRVLNKNYTLLVSMAPLTNEIRPVSSCTPQHIGPAIPEVSSVWFKLYIYHVTGQGPPSLLLSKGTRLRKLPDIFQSYDRLLITSWGHDPGVVPTSNVLTMLNDALTHSAVLIQGHGLHGIGETVHVPFPFDETELQGEFTRVNMGVHKALQILRNRVDLQHLCGYVTMLNASSQLADRKLSDASDERGEPDLASGSDVNGSTESFEMVIEEATIDSATKQTSGATTEADWVPLELCFGIPLFSSELNRKVCRKIAAHGLCRKESLQNLLHSSRKLSLQVLNFVHSFQEGASILDIHTEPSFSSLLSQSSCADMGVPLPAKNLIFKDGVLSEWSGRSPSSLLIANLHLQ
Protein: Dihydropteridine reductase (EC 1.5.1.34) (HDHPR) (Quinoid dihydropteridine reductase) (P11348)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of quinonoid dihydrobiopterin into tetrahydrobiopterin.
Interaction partners:
- Pterin-4-alpha-carbinolamine dehydratase
- Phenylalanine-4-hydroxylase
- Sepiapterin reductase
- Dihydrofolate reductase
- 4a-hydroxytetrahydrobiopterin dehydratase
- Tryptophan 5-hydroxylase 2
- Tyrosine 3-monooxygenase
- Tryptophan 5-hydroxylase 1
- Aldo-keto reductase family 1 member B1
- Aldo-keto reductase family 1 member B7
Sequence:
MAASGEARRVLVYGGRGALGSRCVQAFRARNWWVASIDVVENEEASASVIVKMTDSFTEQADQVTAEVGKLLGDQKVDAILCVAGGWAGGNAKSKSLFKNCDLMWKQSIWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSGMPSGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGNKRPNSGSLIQVVTTDGKTELTPAYF
Protein: ADP-ribosylation factor-like protein 8b (AtARL8b) (ADP-ribosylation factor-like A1D) (AtARLA1D) (Q93Y31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in lysosome motility. May play a role in chromosome segregation.
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q9NVJ2}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NVJ2}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9NVJ2}. Note=Localizes with microtubules at the spindle mid-zone during mitosis. {ECO:0000250|UniProtKB:Q9NVJ2}.
Interaction partners:
- Protein TOM THREE HOMOLOG 1
- Kinesin-like protein KIN-14E
- Tobamovirus multiplication protein 1
- Tobamovirus multiplication protein 3
- Tobamovirus multiplication protein 2B
- N-terminal acetyltransferase B complex catalytic subunit NAA20
- Tobamovirus multiplication protein 2A
Sequence:
MGLWDALLNWLRSLFFKQEMELSLIGLQNAGKTSLVNVVATGGYSEDMIPTVGFNMRKVTKGSVTIKLWDLGGQPRFRSMWERYCRSVSAIVYVVDAADPDNLSVSKSELHDLLSKTSLNGIPLLVLGNKIDKPGALSKEALTDEMGLKSLTDREVCCFMISCKNSTNIDQVIDWLVKHSKSSN
Protein: Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD) (E7FEV5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
- Receptor
- Polyubiquitin-B
- Si:ch211-202a12.4.
- TNF receptor-associated factor 6
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Caspase 8, apoptosis-related cysteine peptidase
- Caspase 22, apoptosis-related cysteine peptidase
- Tumor necrosis factor receptor superfamily, member 1a.
- Inhibitor of nuclear factor kappa B kinase subunit epsilon
Sequence:
MSSTLWSQEKPGGSFRDDWRFYIVVKECTVERPGQKTLRIPRGSLGQACQERNSLGRTIPASKGKRSLRILDQTNVVVSVDERDVMELEEKLAELLFPITNCEERYSLLCNRSRLDRARDINCGSKVRVQLRSGDEPLPGVVRFKGALLPDRALSGIWFGVELLEEGRGQGFTEGSYQGQQLFRCEDECGVFVALDKLELWEDEELEVDRVTLEDNDPEEEGEAPPLEINSRVLVQTREGPERGTVIFCDLLPGNESLGYYVGVDMDNPIGDWDGIIDGKQLCNFASLEHTRLVPICDVMPEYSMQDQRLPKVFACRGGNDKPVSQSKPKSKGLGLQPGSRSKSEFYYTLNGSSVDHPAQSKAKSTWYIDEVGEDPAKSLTDMPPDFNPSSSPSRAPPTTTSLSNDNKFHSLPFSLSRKVGPNGSMSHGPLSLSAGSVMGEQPELLPAATPLQRASSPPQGQPGLEVGSMVEVKENPPLCGVIRWVGLPPGLQESLAGLELEEECVGCTDGTFKGIRYFTCPPKKALFVKLKCCRPDSRFPSLHHSPNPIERCNSIAFGGYLSEVVNENTPPRTENDGLEVMVGKKKGIQGHYNSCYLDSTLFCLFSFSSVLDTVLLRPRSKTDVEYYKETQELLRTEIVNPLRIHGYVCATKIMKLRRILEKVEAASGFTSEEKDPEEFLNILFHHILRVDPLLRLRSAGQKVQDCYFYQIFMDKKDKVMVPTSQQLLEWSFINSDLKFAEAPSCLIIQMPRFGKDFKMFNKIFPSLELDITDLLDDTPRECRICGGLALYECRECYEDYDITPGKIKQFCEKCNTQVHLHPRRKIHRYVKLSVPKELHESVWRQGSYPHQQMELFAVLCIETSHYVAFVKYGSADSAWLFFDSMADRDGGQNGFNIPQVSRCPEVGEYLKMTPEELHALDPKNIQGYARRLLCDAYMCMYQSPTMSLYK
Protein: Flagellar biosynthetic protein FliP (P35528)
Organism: Bacillus subtilis (strain 168)
Function: Plays a role in the flagellum-specific transport system.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Bacterial flagellum basal body {ECO:0000250}.
Interaction partners:
- Flagellar biosynthetic protein FlhB
- Flagellar biosynthetic protein FliR
- Flagellar M-ring protein
- Flagellar motor switch phosphatase FliY
- Flagellum-specific ATP synthase
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliG
- Flagellar biosynthetic protein FliQ
- Probable flagellar assembly protein FliH
- Flagellar biosynthesis protein FlhA
Sequence:
MNEFINIFSSSDPENVSSTVKLLLLLTVFSVAPGILILMTCFTRIVIVLSFVRTSLATQSMPPNQVLIGLALFLTFFIMAPTFSEINKEALTPLMDNKISLDEAYTKAEEPIKEFMSKHTRQKDLALFMNYAKMDKPESLKDIPLTTMVPAFAISELKTAFQIGFMIFIPFLIIDMVVASVLMSMGMMMLPPVMISLPFKILLFVLVDGWYLIVKSLLQSF
Protein: Guanine nucleotide-binding protein subunit beta (Q10282)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Required for adenylate cyclase activation.
Subcellular location: Cell membrane {ECO:0000305|PubMed:11238401}; Peripheral membrane protein {ECO:0000305|PubMed:11238401}; Cytoplasmic side {ECO:0000305|PubMed:11238401}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein alpha-2 subunit
- Uncharacterized protein C16E9.15
- Guanine nucleotide-binding protein alpha-1 subunit
- Pheromone P-factor receptor
- Adenylate cyclase
- Serine/threonine-protein kinase shk1/pak1
- Regulator of G-protein signaling 1
- Guanine nucleotide-binding protein negative regulator 1
- Rho guanine nucleotide exchange factor scd1
Sequence:
MDSGSRVNVNIQGTRVLKNKLGKIPDIDISTDGKYLLSASTNDVLLVWDLHTSNKVAFFEAPSVWIMTCAFSPSTKSIAAGGLNNFCVVYDTSVPDADPVELVGHAGFVSCCKYVDDGHLLTGSGDKTCMFWDIEQAKAISVLKGHEMDIVSLDFLPSNPNLFVTGGCDKLAKLWDLRAAYCCATFPGNTSDINSISFFPSNADFVTGAEDGIARCFDIRASAEIFQYSSPSSSPINSVLFSKSGKLLFIAKDKTCEVWDSISSKTITSLTGHENRISSLALTSDGTMLATGSWDECVRLWSSSG
Protein: B-cell antigen receptor complex-associated protein beta chain (B-cell-specific glycoprotein B29) (Ig-beta) (Immunoglobulin-associated B29 protein) (CD antigen CD79b) (P40259)
Organism: Homo sapiens (Human)
Function: Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Note=Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts. {ECO:0000250}.
Interaction partners:
- B-cell antigen receptor complex-associated protein alpha chain
- Tyrosine-protein kinase Lyn
- Tyrosine-protein kinase SYK
- Immunoglobulin lambda-like polypeptide 1
- Immunoglobulin iota chain
- B-lymphocyte antigen CD19
- C-X-C motif chemokine 9
- Immunoglobulin lambda-like polypeptide 5
- Tyrosine-protein kinase BTK
- Immunoglobulin heavy constant delta
Sequence:
MARLALSPVPSHWMVALLLLLSAEPVPAARSEDRYRNPKGSACSRIWQSPRFIARKRGFTVKMHCYMNSASGNVSWLWKQEMDENPQQLKLEKGRMEESQNESLATLTIQGIRFEDNGIYFCQQKCNNTSEVYQGCGTELRVMGFSTLAQLKQRNTLKDGIIMIQTLLIILFIIVPIFLLLDKDDSKAGMEEDHTYEGLDIDQTATYEDIVTLRTGEVKWSVGEHPGQE
Protein: C-C motif chemokine 23 (CK-beta-8) (CKB-8) (Macrophage inflammatory protein 3) (MIP-3) (Myeloid progenitor inhibitory factor 1) (MPIF-1) (Small-inducible cytokine A23) [Cleaved into: CCL23(19-99); CCL23(22-99); CCL23(27-99); CCL23(30-99)] (P55773)
Organism: Homo sapiens (Human)
Function: Shows chemotactic activity for monocytes, resting T-lymphocytes, and neutrophils, but not for activated lymphocytes. Inhibits proliferation of myeloid progenitor cells in colony formation assays. This protein can bind heparin. Binds CCR1. CCL23(19-99), CCL23(22-99), CCL23(27-99), CCL23(30-99) are more potent chemoattractants than CCL23.
Subcellular location: Secreted.
Interaction partners:
- C-C motif chemokine 21
- C-C chemokine receptor type 1
- C-C motif chemokine 24
- C-C chemokine receptor type 6
- C-C motif chemokine 7
- C-C motif chemokine 2
- C-C motif chemokine 20
- N-formyl peptide receptor 2
- C-C chemokine receptor type 3
- C-C motif chemokine 25
Sequence:
MKVSVAALSCLMLVTALGSQARVTKDAETEFMMSKLPLENPVLLDRFHATSADCCISYTPRSIPCSLLESYFETNSECSKPGVIFLTKKGRRFCANPSDKQVQVCMRMLKLDTRIKTRKN