wanglab/gogpt-training-data huggingface dataset:
Protein: Nck-associated protein 1 homolog (Q869Q3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in regulation of actin and microtubule organization. Involved in cell adhesion.
Interaction partners:
- Protein BRICK1
- Protein pirA
- Protein SCAR
- Abl interactor homolog
- Actin-related protein 2
- Rho-related protein racC
- Actin-related protein 2/3 complex subunit 2
- Actin related protein
Sequence:
MAHTNLPEKFQVVIENGENILQRVYNTYKLFQNNKVKPSFFNDEKISKILKNLIAKYPELPENNDKSITGFDLLTSRAKQHLEELEDHYYTITDAYDWKEASFILMQEISSNTVSINFNNNIQLCSKFLDVLVLYGKINYLVSLIPDKKIITAVYAKLFLYTRSASEPTFSKMGRWINDIEQPFKKIQEEFRVLNDAVGHALSSFELTYAKRRVITQLRKDGALNLILKPEDIARPVQDSYRIELAYAGRIQQWILFGYLFAPGTLSTPQSIELLRFTLSECFYLSVFKDISISIHNEFNTLFKNYKSKTINLQKQKKIIKDAAQASTQEAPRKHAERRVYIRQELEAMWNLFRDKPCLLAPKINVLLAALSMAKEEIFWYFRHTDVIPPEKVKKFYNKQNEVREKRISSLLSLVDHLVQLVHTHKKMIQNYYLEYISGADILGLQKVITPQLLQNAGSIVTQAVNTIVNELKSLNANGQDYSFEGFRANWMRLGYLLQSNSCPLKESESKQITSRLNLIYTHSKNVDCLDQLLDEYGNMTQLWSYKEPLFHSFDAAIVDMTCDQPSHSMIYLKLLSQFPNHVANQFYPEEKELIGKECVELANSCLTKITNRIVSIMANTIASTFLSDEQQLADVNAAFPLLQKKKDWKPPKDFVPPIEPASESQFRNRANLEQLRSEEKNAFQLCTALNEFLDITIYDHIFVPREFLREKLGSALKQYMRQSIQPPAPTSSSSQIDINITRLSTYESQLRVFIGVLILVENHVDIDIGDLIRETILTEFYAKALGKSGRVDWFPEGEIEMNELTLHSITSYYVDLVSKKLNTPGVVFSPVKLGFISKAGTPFRAEEHADLTEMRALCDLVGPYGIKVIEREILRFILTTTTSMKEILSLNAANLEEFASNYYKPKAMELLKKFKTTDLDLIVTKSIAIGNALHLRSMIRESMKDVITDNFPYINNAVANAFDQYNRNTFMFPDFLGVDTLALDSGLNVGIADQYLKVILRKVSSEADKRIWELLPVMFSLTFYGNIWKETQYKATIDAHSNNVHVLSKTIIDLLIAFGAINSTTGNEAELFQSFKRFLEISSVNILRMFKGKQGEKFVPNEIQSVIIFLDKFTQQCPLLSKDSLEQYIPYSLIRNMYKDLYEHKNLQKQQSETSEQNF
Protein: SWI/SNF global transcription activator complex subunit SWP82 (P43554)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcription regulatory protein SNF6
- Transcription regulatory protein SNF12
- Actin-related protein 7
- SWI/SNF chromatin-remodeling complex subunit SWI1
- Transcription regulatory protein SNF2
- Actin-like protein ARP9
- SWI/SNF chromatin-remodeling complex subunit SNF5
- SWI/SNF complex subunit SWI3
- Regulator of Ty1 transposition protein 102
- Transcription initiation factor TFIID subunit 14
Sequence:
MLGEDEGNTVLEKGNNPSVKQGEVGAVFIVPKILIREHERVILKQILQILDQDELVQPPLDKFPYKKLELPKYIDELKTRDATNTSYKMIQLDAYGEKKVGSNGELFGGRHYLFNTFTFTAHMGVLLVLLQDVIKVLYQSNATHDEDEFIVQHDQILVMETSEEQTKFLAKNGVIPEESKGSFKYITARSAFVEFGASVIAGGQRIVDDYWESLAKKQNLSSHQRVFKLSTNLISKISLLRPSFQNNRISNANEISANTNNTCTISTSKFESQYPIVTEQPSAEIREAYIENFAKGEHISAIVPGQSISGTLELSAQFRVPRYHSKNSFQQALQMKAMDIPIGRHEELLAQYESQAPDGSASISLPNHIPSVNPSNKPIKRMLSSILDINVSSSKNKKSEENEMIKPMNKGQHKNNTSLNINGWKFESLPLKSAENSGKQQYYRGLPLYEKNTLLERLKQLTPNEIKELEHLHDAVFVNTGLQNVRKVRTKKWKKYWQYKAGIPIGLKRSQLDEFKNKYLKDVLAQTSVTTNFNEITNTDETITTKRVPNPNFLGNCNIKDFKPPYIYSHVNKVPQNVAGDKTAVKLDTEVKNTNANPVVATDPVAAKPDNLANFSNEVAMNN
Protein: Phosphodiesterase (EC 3.1.4.-) (D3ZDI8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- G protein subunit alpha transducin 1
- Rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- G protein subunit alpha transducin 2
- Phosphodiesterase
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanylate kinase
- Retinal guanylyl cyclase 1
- Adenine phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MSLSEEQVRSFLDGNPTFAHQYFEKKLSPENVAGACEGGCLVDCGSLRELCQVEESAALFELVQDMQESVNMERVVFKVLRRLCTILHADRCSLFMYRQRNGVAELATRLFSVQPDSLLEDCLVPPDSEIVFPLDIGIVGHVAQTKKMINVQDVAECPHFSPFADELTDYVTKNILSTPIMNGKDVVAVIMAVNKLDGPCFTSEDEDVFTKYLNFATLNLKIYHLSYLHNCETRRGQVLLWSANKVFEELTDIERQFHKAFYTVRAYLNCDRYSVGLLDMTKEKEFFDVWPVLMGEAQPYSGPRTPDGREIVFYKVIDYILHGKEDIKVIPTPPADHWALTSGLPTYVAESGFICNIMNASADEMFNFQEGPLDESGWVIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDDQDEVLMESLTQFLGWSVLNTDTYDKMNKLENRKDIAQDMVLYHVRCDKDEIQEILPTRDRLGKEPADCEEDELGKILKEELPGPTKFDIYEFHFSDLECTELELVKCGIQMYYELGVVRKFQIPQEVLVRFLFSVSKAYRRITYHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDIDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKFLLAEESLNIYQNLNRRQHEHVIHLMDIAIIATDLALYFKKRTMFQKIVDESKNYEDKKSWVEYLSLETTRKEIVMAMMMTACDLSAITKPWEVQSKVALLVAAEFWEQGDLERTVLDQQPIPMMDRNKAAELPKLQVGFIDFVCTFVYKEFSRFHEEILPMFDRLQNNRKEWKALADEYEAKVKALEEEKKKEEDRVAAKKAGTEICNGGPAPKSSTCCIL
Protein: Phosphomannomutase (PMM) (EC 5.4.2.8) (Phosphoglucomutase) (Q57842)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the formation of mannose-1-P from mannose-6-P. Can also use glucose-6-P.
Interaction partners:
- Diadenylate cyclase
- Putative UTP--glucose-1-phosphate uridylyltransferase
- Uncharacterized protein MJ1631
Sequence:
MFGDLMVFKAYDIRGIYGRELDENFAYSLGKCIGKKFENKKILVGNDVRIGSKELLPYFIVGLKEYADVFYAGTISTPLMYFGTKGKYDLGVILTASHNPPEYTGFKMCDKEAIPLSPIEEIKPIFKKYELTESIKEEAKNLNLDDLKVNIIEEYKKFFLKRCKASDKKIAVDFANGATTIAEKEILNELFDNAVFINDYPDGNFPAHQPDTLKMECLKDIIRAVKKNNCELGLIFDGDGDRLGIVDENGNVLRGDILTAIIAKEILKEKSNAKIVYDLRCSKIVPEIIEKYGGIAIKSRVGHYFIKKLMHEIDAEFAGELSNHFYFKEIGYFESPLLALNYILKAMDEENKSLSELNKEFSKYPHSGEINFRVKDQKYIMEKIKEHFKDCKLEELDGISIYCKNFWFNLRPSNTEPLLRLNLEADDEKTMKEKVEEIKNLIAKLDASL
Protein: Estradiol 17-beta-dehydrogenase 11 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 11) (Dehydrogenase/reductase SDR family member 8) (D6RCD0)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
Interaction partners:
Sequence:
MKFLLDILLLLPLLIVCSLESFVKLFIPKRRKSVTGEIVLITGAGHGIGRLTAYEFAKLKSKLVLWDINKHGLEETAAKCKGLGAKVHTFVVDCSNREDIYSSAKKTTKAFLPAMTKNNHGHIVTVASAAGHVSVPFLLAYCSSKFAAVGFHKTLTDELAALQITGVKTTCLCPNFVNTGFIKNPSTSLGPTLEPEEVVNRLMHGILTEQKMIFIPSSIAFLTTLERILPERFLAVLKRKISVKFDAVIGYKMKAQ
Protein: ADP/ATP translocase 1 (ADP,ATP carrier protein 1) (Adenine nucleotide translocator 1) (ANT 1) (Solute carrier family 25 member 4) (Q05962)
Organism: Rattus norvegicus (Rat)
Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity (By similarity). Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis. Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A4/ANT1 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it (By similarity). Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death (By similarity). It is however unclear if SLC25A4/ANT1 constitutes a pore-forming component of mPTP or regulates it (By similarity). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P12235}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:P12235}; Multi-pass membrane protein {ECO:0000255}. Note=The complex formed with ARL2BP, ARL2 and SLC25A4/ANT1 is expressed in mitochondria (By similarity). May localize to non-mitochondrial membranes (By similarity). {ECO:0000250|UniProtKB:P12235, ECO:0000250|UniProtKB:P48962}.
Interaction partners:
- Non-selective voltage-gated ion channel VDAC3
- Non-selective voltage-gated ion channel VDAC2
- Non-selective voltage-gated ion channel VDAC1
- Creatine kinase S-type
- Creatine kinase U-type, mitochondrial
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- Peptidyl-prolyl cis-trans isomerase D
- Cytochrome c, somatic
- Translocator protein
- ADP/ATP translocase 2
Sequence:
MGDQALSFLKDFLAGGIAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGSSQREFNGLGDCLTKIFKSDGLKGLYQGFSVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQSVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGRKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV
Protein: Tyrosine-protein phosphatase non-receptor type 4 (EC 3.1.3.48) (Protein-tyrosine phosphatase MEG1) (MEG) (PTPase-MEG1) (P29074)
Organism: Homo sapiens (Human)
Function: Phosphatase that plays a role in immunity, learning, synaptic plasticity or cell homeostasis. Regulates neuronal cell homeostasis by protecting neurons against apoptosis. Negatively regulates TLR4-induced interferon beta production by dephosphorylating adapter TICAM2 and inhibiting subsequent TRAM-TRIF interaction. Dephosphorylates also the immunoreceptor tyrosine-based activation motifs/ITAMs of the TCR zeta subunit and thereby negatively regulates TCR-mediated signaling pathway (By similarity). May act at junctions between the membrane and the cytoskeleton.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8910369}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8910369}. Cytoplasm {ECO:0000269|PubMed:20086240, ECO:0000269|PubMed:8910369}.
Interaction partners:
- Glutamate receptor ionotropic, NMDA 2A
- 6-pyruvoyl tetrahydrobiopterin synthase
- TIR domain-containing adapter molecule 2
- Trace amine-associated receptor 1
- Methyl-CpG-binding protein 2
- Mitogen-activated protein kinase 12
- Glutamate receptor ionotropic, delta-2
Sequence:
MTSRFRLPAGRTYNVRASELARDRQHTEVVCNILLLDNTVQAFKVNKHDQGQVLLDVVFKHLDLTEQDYFGLQLADDSTDNPRWLDPNKPIRKQLKRGSPYSLNFRVKFFVSDPNKLQEEYTRYQYFLQIKQDILTGRLPCPSNTAALLASFAVQSELGDYDQSENLSGYLSDYSFIPNQPQDFEKEIAKLHQQHIGLSPAEAEFNYLNTARTLELYGVEFHYARDQSNNEIMIGVMSGGILIYKNRVRMNTFPWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKNLWKACVEHHTFFRLDRPLPPQKNFFAHYFTLGSKFRYCGRTEVQSVQYGKEKANKDRVFARSPSKPLARKLMDWEVVSRNSISDDRLETQSLPSRSPPGTPNHRNSTFTQEGTRLRPSSVGHLVDHMVHTSPSEVFVNQRSPSSTQANSIVLESSPSQETPGDGKPPALPPKQSKKNSWNQIHYSHSQQDLESHINETFDIPSSPEKPTPNGGIPHDNLVLIRMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCERHSGELMLLVRPNAVYDVVEEKLENEPDFQYIPEKAPLDSVHQDDHSLRESMIQLAEGLITGTVLTQFDQLYRKKPGMTMSCAKLPQNISKNRYRDISPYDATRVILKGNEDYINANYINMEIPSSSIINQYIACQGPLPHTCTDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPTGSSSYGCYQVTCHSEEGNTAYIFRKMTLFNQEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCHVRNKRAGKEEPVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEEGFVKPLTTSTNK
Protein: EMAP-like 1 (Echinoderm microtubule-associated protein-like 1 isoform X7) (A0A2R8RMY7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNQHNQRLLLYSSVPFPDDSASATSSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNKKGPTKARPMIAALPLRPTVNNGTVLPKKGGTLPSPSNCKKDNNSPATRSTVKRTSSSEHVGPNNRKDSGVDSKNNRTRAGSTGSNSSGKKTTETKQREPVFSAGMRRVTHCKDEGYVKMYLKGRPITMYMPKDLVDTYCLETKADLPPKKLKLDWVYGYRGRDCRSNLYLLPTGETVYFIASVVVLYNVDEQLQRHYTGHTDDIKCLAVHPDKITIATGQVAGTSSDGKQLAPHVRVWDSVSLNTLHILGNGFFDRALVCLSFSKSNGGSWLCVVDDSNDHMLSVWDWQREDRLAEVKCSNESVFAADFHPTDANIIVTCGKSHLCFWSLEKGSLVKKQGLFEKQEKPKFVLCVTFSENGDAITGDSSGNILVWGKGSNRISLAIQGAHEASVFALCMLRNGTLVSGGKDRKLISWDENFQKIQTVEVPELYGPVRTVAEGRGETVLIGTTKNYVLQGSLNGEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHIYLWDSDSHQPIWTKTLEDSAQSAGFHPSGATVAVGMQTGRWLVLDTESKDLVTVHTDGNEQLSVIRFSPDGNFLAIGSHDNYIYIYAVAENGKKYSRVGKCSGHSSFITHLDWSVDSQYLVSNSGDYEILYWIPSVCKQVVSVETTRDIEWATFTCTLGFHVFGLWPDGSDGTDINAVCSSYAKRLLVTGDDFGKVHLFSFPCSQSRAPSHIYSGHSSHVTNVNFLFDDSHLVSTGGKDMSIMQWRVV
Protein: Phenylcoumaran benzylic ether reductase TP7 (NtPCBER) (EC 1.23.1.-) (Protein TOBACCO PETAL 7) (B6VRE8)
Organism: Nicotiana tabacum (Common tobacco)
Function: Oxidoreductase involved in lignan biosynthesis. Catalyzes the NADPH-dependent reduction of phenylcoumaran benzylic ethers. Converts dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl alcohol (IDDDC), and dihydrodehydrodiconiferyl alcohol (DDDC) to tetrahydrodehydrodiconiferyl alcohol (TDDC).
Interaction partners:
- Quinolinate phosphoribosyltransferase [decarboxylating] 2a, mitochondrial
- Putrescine N-methyltransferase 4.
- Quinolinate synthase, chloroplastic
- Quinolinate synthase, chloroplastic
- S-adenosylmethionine decarboxylase proenzyme
- Putrescine N-methyltransferase 2.
- Putrescine N-methyltransferase 1
- Cytochrome P450 CYP82D47
- Ornithine decarboxylase 1B, chloroplastic
Sequence:
MAEKSKVLIIGGTGYIGKFVVEASAKSGHPTFALVRESTLSDPVKSKIVENFKNLGVTILHGDLYDHESLVKAIKQVDVVISTMGMMQLGDQVKLIAAIKEAGNIKRFFPSEFGMDVDKTNAVEPAKSAFAVKVQIRRAIEAEGIPYTYVSCNCFAGYFLPTMVQPGATVPPRDKVIIPGDGNVKAVFNEEHDIGTYTIKAVDDPRTLNKTLYIKPPKNTLSFNELVAMWEKMIGKTLEKIYIPEEQILKDIETSPMPLPVILAINHATFVKGDQTNFKIEPSFGVEASELYPDVKYTTVEDYLGHFV
Protein: Peptidyl-alpha-hydroxyglycine alpha-amidating lyase 1 (EC 4.3.2.5) (Peptidylamidoglycolate lyase 1) (dPAL1) (Q9V5E1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Peptidyl-alpha-hydroxylglycine alpha-amidating lyase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Mediates the dismutation of the unstable peptidyl(2-hydroxyglycine) intermediate to glyoxylate and the corresponding desglycine peptide amide. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Confined to cell bodies. {ECO:0000269|PubMed:15198673}.
Interaction partners:
- Peptidylglycine alpha-hydroxylating monooxygenase
Sequence:
MKSTDSAKCLGSKSLAICCLLLHLLLCIRPAVSQTQSPQRYLHNVDSNSNNNERLHQILKGSGAGSGATQLNWPQPPKQTVPNVKTELAKLNNTYVYQNAWPANNVKLGAVTAVSFDKAGNVVIFHRVNRVWGQTTFDNRNQYQEKYRGPIRESTILALEPATGKVQYDWGKNFFYMPHGLTVDPEDNVWLTDVAMHQVFKFPPRGGDGKPALTLGDAFQPGSGRKFCKPTSVAVLDNGDFFVADGYCNARILKYSRKGELILFWGQNTFSGISYDVAPQNFFAIPHALTLVPELQLLCAADRENGRVQCFLSSNGTFHSQYHNQLIGDRLFSMAYTPAAGGQLVIVNGPTAELGIHPEHYNEVHGFVLSMRSKQLVSKFGPNNLQFQNPHDVAVTADGNEIYVAELNPMRIHKFVHRSLAKPMSLSASKDSRDSAISQAVGGDQVPAVAVHHPSGKAILVASLMLLFAGSTFALALIFARRRKRGCLPFGARGRRHAWEKSDGFKLGGLLDRDRNGFEKLDQQASDEEQETKTLASAQYA
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2 (Oligosaccharyl transferase subunit OST2) (Oligosaccharyl transferase 16 kDa subunit) (Oligosaccharyl transferase subunit epsilon) (P46964)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000269|PubMed:29301962}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Protein transport protein SEC61
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5
- Protein transport protein SBH2
Sequence:
MAKAPKANTPKVTSTSSAVLTDFQETFKTSKRAYFAQIEKYPKLKLIDTFCFFLVLLGVIQCTFIILIRDNFPFNAFLAGFIICVGQFVLLMSLRLQLCNSFPGISKNRAFAEFIVASLILHFVCLHFIN
Protein: Calsyntenin-3 (Alcadein-beta) (Alc-beta) (Q9BQT9)
Organism: Homo sapiens (Human)
Function: May modulate calcium-mediated postsynaptic signals. Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99JH7}. Note=Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization. {ECO:0000250|UniProtKB:Q99JH7}.; SUBCELLULAR LOCATION: [Isoform CLSTN3beta]: Lipid droplet {ECO:0000250|UniProtKB:Q99JH7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-lipid droplet contact sites through the partitioning of its N-terminal hydrophobic hairpins onto lipid droplets while its C-terminal transmembrane domain remains anchored in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q99JH7}.
Interaction partners:
- Neurexin-1
- Neurexin-2
Sequence:
MTLLLLPLLLASLLASCSCNKANKHKPWIEAEYQGIVMENDNTVLLNPPLFALDKDAPLRYAGEICGFRLHGSGVPFEAVILDKATGEGLIRAKEPVDCEAQKEHTFTIQAYDCGEGPDGANTKKSHKATVHVRVNDVNEFAPVFVERLYRAAVTEGKLYDRILRVEAIDGDCSPQYSQICYYEILTPNTPFLIDNDGNIENTEKLQYSGERLYKFTVTAYDCGKKRAADDAEVEIQVKPTCKPSWQGWNKRIEYAPGAGSLALFPGIRLETCDEPLWNIQATIELQTSHVAKGCDRDNYSERALRKLCGAATGEVDLLPMPGPNANWTAGLSVHYSQDSSLIYWFNGTQAVQVPLGGPSGLGSGPQDSLSDHFTLSFWMKHGVTPNKGKKEEETIVCNTVQNEDGFSHYSLTVHGCRIAFLYWPLLESARPVKFLWKLEQVCDDEWHHYALNLEFPTVTLYTDGISFDPALIHDNGLIHPPRREPALMIGACWTEEKNKEKEKGDNSTDTTQGDPLSIHHYFHGYLAGFSVRSGRLESREVIECLYACREGLDYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYVVVLQPDAPQILLSGTAHFARPAVDFEGTNGVPLFPDLQITCSISHQVEAKKDESWQGTVTDTRMSDEIVHNLDGCEISLVGDDLDPERESLLLDTTSLQQRGLELTNTSAYLTIAGVESITVYEEILRQARYRLRHGAALYTRKFRLSCSEMNGRYSSNEFIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSMIPSAATLIIVVCVGFLVLMVVLGLVRIHSLHRRVSGAGGPPGASSDPKDPDLFWDDSALTIIVNPMESYQNRQSCVTGAVGGQQEDEDSSDSEVADSPSSDERRIIETPPHRY
Protein: C-C motif chemokine 24 (Eosinophil chemotactic protein 2) (Eotaxin-2) (Small-inducible cytokine A24) (Q9JKC0)
Organism: Mus musculus (Mouse)
Function: Chemotactic for resting T-lymphocytes, and eosinophils. Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. Is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line. Binds to CCR3 (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:O00175}.
Interaction partners:
- Probable C-C chemokine receptor type 3
- C-C motif chemokine 5
- C-C motif chemokine 27
- C-C motif chemokine 6
- C-C motif chemokine ligand 26
- Eotaxin
- C-C motif chemokine 28
- C-C motif chemokine 7
- C-X-C chemokine receptor type 3
- Predicted gene, 20878
Sequence:
MAGSATIVAGLLLLVACACCIFPIDSVTIPSSCCTSFISKKIPENRVVSYQLANGSICPKAGVIFITKKGHKICTDPKLLWVQRHIQKLDAKKNQPSKGAKAVRTKFAVQRRRGNSTEV
Protein: Ubiquitin activating E1 enzyme, putative (Q389M1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Autophagocytosis associated protein, putative
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Uncharacterized protein
- Ubiquitin-conjugating enzyme E2, putative
- Ubiquitin-conjugating enzyme E2, putative
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin-conjugating enzyme E2, putative
- Ubiquitin-conjugating enzyme E2, putative
Sequence:
MERLKYLMHDFRIEISFWYELEKRKLHEWRLSEPIIRSPVFGVTSSSSSGIYRSLVSLRAESLSASRVNVTRRLRDETSVSEGDPIDDHSGGTGTSLRCVHTLHDGFIQNFNTAKQLYQLPRRSALWDILKKSLLLPLYTCCKNKREENVTEYSSAEELAWEDVNFSIMALYTYADLKSHRFLYSVAFPVFDLGSPVFVQRRVKGGYTAAGSEFKGVYFPNQFAVDRVHAHLLEKLQKRPENGPNPFIVVRSSAADVKGKGNNDDGCVIFLPFSPKSMEAASNHSMPLIAFLDYSSEGSPGWAVRNIVSALRLAQPLITSFALYCVRNNDVSESVLFHCMCEPLSYTLEEVVEGVSPAKVVGWVDPESDGGASSVHTIDLGPLMSPDKLADASAGLNLTLMKWRALPELNLDRLAQCKALLLGTGTLGCNVARQLLMWGVRHITLVDRGKVSFSNPVRQTLFELSDVNNPREEERNKAIAAAKALKRILPGVNARGVPLTIHMPGHRVDKAREEEVKAEIEALDELIRSHDVVFLLTDSREARWLPTLMATAHCKPTVNVALAFDTYVVMRHGLDPPEGSDKGAKYVRLGCYFCSDSVAPRDSITARTLDQQCTVTRPGLSAIASAIAVELLAQLYNHPLGFACPPYVQSERDATPGVSDSVAGGAVCPLGTIPQQIRGSVAHHNVYTLHGCRYEQCTACSDPIVRSYKDEGSAFVLRCINDPMYIEEVSGVKAFKESCALDSCDGWDDDVDNQ
Protein: Protein PHYTOCHROME KINASE SUBSTRATE 4 (Q9FYE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Modulates phytochrome-mediated control of hypocotyl growth orientation. Involved in PHYA and PHYB signaling. Acts as an inhibitor of asymmetric growth. Not involved in the control of leaf flattening.
Interaction partners:
- Phototropin-1
- Phototropin-2
- Serine/threonine-protein kinase BLUS1
- Root phototropism protein 2
- Thioredoxin-like 3-2, chloroplastic
- F-box/kelch-repeat protein At5g49000
- ABC transporter B family member 19
- Far-red impaired responsive
- Protein PHYTOCHROME KINASE SUBSTRATE 3
- Root phototropism protein 3
Sequence:
MAQTTVTVVATKRDALDPYIKILQNRSNDIDVSFSSYLKPDNNEQQQKENEDTELSIFEARSYFSENGSNDSRCQTRNLSGPRFSSVASAKVSSFTVGQTASSEASWNSQTGLLSNKNRQGSDRDGRRSSKKGPRWFFRRRACPCSSSKSVQVQESKPRIAVPKTGSDRIVSNRIVHSHQTISSPEPIRLTIPSNTVTRSIDYTANKEARAPVSNFSFPTLNETSQLSENPKNPVLNHIKPVRIEPALLPIKPVLNPTSPKGVIIDEEATSDASSDLFEIESFSTQTAARPWAPPVRDSMEETVSEYGYEPSEASVTWSVMTAEPASAVAANFSRIALSSSSTAFSGYDKKRTGLLNCHCEKAVMVNGDKRLVQPVKSVGVQNDVAGKVLCNNGSSKLSVTSRPRQ
Protein: Acyclic carotenoid 1,2-hydratase (EC 4.2.1.131) (Hydroxylycopene hydratase) (Lycopene hydratase) (Q7X3G5)
Organism: Thiocapsa roseopersicina
Function: Involved in the biosynthesis of carotenoids spirilloxanthin. Catalyzes the hydration of lycopene to the corresponding hydroxylated carotenoids 1-HO-lycopene and 1,1'-(HO)2-lycopene. Can also act on geranylgeraniol.
Interaction partners:
- 1-hydroxycarotenoid 3,4-desaturase
- Phytoene dehydrogenase
- Demethylspheroidene O-methyltransferase
- Geranylgeranyl diphosphate synthase, type II
- Geranylgeranyl diphosphate reductase
- Phytoene synthase
- Putative photosynthetic complex assembly protein
- Chlorophyllide reductase subunit Z
- 3-vinyl bacteriochlorophyllide hydratase
- Chlorophyllide a reductase subunit Y
Sequence:
MRAAGILTPGALWAPGPSDTRDERRHDAGRLQPALPGDGRGPLRPGVTRMEGLLHASSVAQQGAGALSGRGERASGSRGTDGGHVGTPGGSDPARGPRFDLRITPGGYLWWYLDALSDDGDHGLTIIAMLGSVFSPYYAWARRRGNPDPLNHCALNVALYGKAGKRWTMTERGRKALRQAPGRLDIGPSHLTWDGTALTIDVNEITAPIPSRVRGRIRVIPAAVNAREFTLDPAERHVWWPIAPISRVEVDLEKPALRWSGHGYLDSNRGEEPLEDAFQCWDWSRANTPSGTTMLYDVTARHGTGASLALRFNASGEVEEFPPPPRVRLPTTGIWRIKRGTQCEAGHQARVVETLEDTPFYARSLVETRLAGETATCVHESLSLDRFASPVVQLMLPFRMPRVGG