wanglab/gogpt-training-data huggingface dataset:
Protein: Serine hydroxymethyltransferase (EC 2.1.2.1) (B7Z0X1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADQKLLQTPLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRELFNLDDEKWGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTPTKKISATSIFFESMPYKVNPETGIIDYDKLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPRAGVIFFRKGVRSTKANGDKVLYDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLISRGYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKSAMNPSGIRLGTPALTTRGLAEQDIEQVVAFIDAALKVGVQAAKLAGSPKITDYHKTLAENVELKAQVDEIRKNVAQFSRKFPLPGLETL
Protein: Kinesin-like protein costa (Kinesin-like protein costal2) (O16844)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulates cubitus interruptus (ci) processing by recruiting multiple kinases to promote its efficient phosphorylation. Scaffolds multiple kinases and ci into proximity to promote its hyperphosphorylation, which then targets it for SCFSlimb/proteasome-mediated processing to generate its repressor form. Hh signaling inhibits ci phosphorylation by interfering with the cos-ci-kinases complex formation. Negatively regulates hh-signaling pathways during various processes, including photoreceptor differentiation. May negatively regulate a hh-signaling pathway which functions in the intestinal immune response to bacterial uracil by activating the Duox-dependent production of reactive oxygen species (ROS).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9244298}.
Interaction partners:
- Suppressor of fused homolog
- Protein smoothened
- Serine/threonine-protein kinase fused
- Transcriptional activator cubitus interruptus
- cAMP-dependent protein kinase catalytic subunit 1
- cAMP-dependent protein kinase catalytic subunit 2
- Protein patched
- Protein hedgehog
- Casein kinase I isoform alpha
- Protein kinase shaggy
Sequence:
MEIPIQVAVRIFPHRELKDLLRSFGPTEPKKDAQAVDEGADSKDSEAQVPAAEKDNPSISETDPNGNAEQDSAADSKTIPDANGNDSGQKDYPDSAYCVQAIPISASALGLPSALPGGDPMDSIAAGLIQVGPHTVPVTHALPSSSSQEQVYHQTVFPLITLFLEGFDASVVTYGQRGQGKSYTLYGNVQDPTLTDSTEGVVQLCVRDIFSHISLHPERTYAINVGFVEICGGDVCDLLGMGNIHCTNVDAVFHWLQVGLSARQSLPAHTLFTLTLEQQWVSKEGLLQHRLSTASFSDLCGTERCGDQPPGRPLDAGLCMLEQVISTLTDPGLMYGVNGNIPYGQTTLTTLLKDSFGGRAQTLVILCVSPLEEHLPETLGNLQFAFKVQCVRNFVIMNTYSDDNTMIVQPAEPVPESNSSAGPLSQAGPGDNFGLQFAASQWSKLVTNAEGLFSKLIDSKLITEVEKEQIEEWLFLKQECEECLSSTEAMRQQKQLVPILEAEEPEDVNSEAANSESPNSDNENDTDNESHRPDLDDKIESLMEEFRDKTDALILEKHAEYLSKHPKAVMQSQDREIEAQPPEENGDDRKVSIGSRRRSVQPGASLSTAELAMLNRVASQQPPPPIDPESVVDPLESSSGEGIRQAALAAAAATAPIEQLQKKLRKLVAEIEGKQRQLREIEETIQVKQNIIAELVKNSDTRSHAKQRFHKKRAKLEAECDKAKKQLGKALVQGRDQSEIERWTTIIGHLERRLEDLSSMKHIAGESGQKVKKLQQSVGESRKQADDLQKKLRKECKLRCQMEAELAKLRESRETGKELVKAQGSPEQQGRQLKAVQARITHLNHILREKSDNLEEQPGPEQQETLRHEIRNLRGTRDLLLEERCHLDRKLKRDKVLTQKEERKLLECDEAIEAIDAAIEFKNEMITGHRSIDTSDRIQREKGEQMLMARLNRLSTEEMRTLLYKYFTKVIDLRDSSRKLELQLVQLERERDAWEWKERVLSNAVRQARLEGERNAVLLQRQHEMKLTLMLRHMAEETSASSASYGERALAPACVAPPVQASSDFDYDHFYKGGGNPSKALIKAPKPMPTGSALDKYKDKEQRSGRNIFAKFHVLTRYASAAAAGSSGSTAEESTALIESTTTATATTTSTTTTGAVGKVKDKALVSFRPEQLKRLMPAPTATKVTRQKNKIIIQDASRRN
Protein: Tryptophan 5-hydroxylase 1 (EC 1.14.16.4) (Tryptophan 5-monooxygenase 1) (P17752)
Organism: Homo sapiens (Human)
Function: Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis.
Interaction partners:
- Pterin-4-alpha-carbinolamine dehydratase
- Aromatic-L-amino-acid decarboxylase
- Pterin-4-alpha-carbinolamine dehydratase 2
- Dihydropteridine reductase
- Tryptophan 2,3-dioxygenase
- Tryptophan 5-hydroxylase 2
- Indoleamine 2,3-dioxygenase 1
- Indoleamine 2,3-dioxygenase 2
- Sodium-dependent serotonin transporter
- Sepiapterin reductase
Sequence:
MIEDNKENKDHSLERGRASLIFSLKNEVGGLIKALKIFQEKHVNLLHIESRKSKRRNSEFEIFVDCDINREQLNDIFHLLKSHTNVLSVNLPDNFTLKEDGMETVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQELNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTIKRPFGVKYNPYTRSIQILKDTKSITSAMNELQHDLDVVSDALAKVSRKPSI
Protein: Protein kinase C and casein kinase substrate in neurons protein 1 (Syndapin-1) (Q4V920)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Binds to membranes via its F-BAR domain and mediates membrane tubulation. Plays a role in cellular transport processes by recruiting dynamins to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with cobl, and by recruiting cobl to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission (By similarity). Required for normal embryonic development, including normal development of laterality, normal body size and shape, as well as normal brain and heart development. Required for normal development of stereocilia and kinocilia in sensory hair cells of neuromasts in the posterior lateral line organ, and thus also for balance keeping and normal swimming behavior.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23203810}. Cytoplasm, cytosol {ECO:0000269|PubMed:23203810}. Cell membrane {ECO:0000269|PubMed:23203810}; Peripheral membrane protein {ECO:0000269|PubMed:23203810}; Cytoplasmic side {ECO:0000269|PubMed:23203810}. Cell projection {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Synapse {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Detected in axons. In primary neuronal cultures, present at a high level in presynaptic nerve terminals and in the cell body. Detected at vesicular structures in neuron cell bodies and neurites (By similarity). Detected at the apical surface of cells at the basis of forming cilia, but not in the cilia themselves. {ECO:0000250}.
Interaction partners:
- Ig-like domain-containing protein.
- EH domain-containing protein 1b
Sequence:
MSGAYDESAMSDETTDSFWEVGNYKRTVKRIEDGHRLCNDMMSCIQERAKIEKAYSQQLTDWSKRWRQLVERGPQYGTLERAWLAVMTEAEKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQMMGGFKETKEADEGFRKAQKPWAKKLKELETAKKTYHMACKEEKIASAREANSKGEASVTTDQQKKLQEKVDKCKNDVQKAKEKYEKSLDELNKCTPQYMENMEVVFDQCQQFEEKRLNFLREVLLDTKRHLNLTESQSYATVYRELERTIVSASAQEDLKWFSSVHGPGMHMNWPQFEEFNPDLSHAISKKEKVKRNHDGVTLTQVTHGAEHGTPQTGDRGSVSSYEKNQQYSAEWSDDEQPPTAAQSASETNGGNPFEEDSKGVRVRALYDYEGQEQDELTFKAGDELTKLEDEDEQGWCKGRLDSGQLGLYPANYVEPV
Protein: CUGBP Elav-like family member 4 (CELF-4) (Bruno-like protein 4) (CUG-BP- and ETR-3-like factor 4) (RNA-binding protein BRUNOL-4) (Q7TSY6)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein implicated in the regulation of pre-mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Promotes exclusion of both the smooth muscle (SM) and non-muscle (NM) exons in actinin pre-mRNAs. Activates the splicing of MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MYIKMATLANGQADNASLSTNGLGSSPGSAGHMNGLSHSPGNPSTIPMKDHDAIKLFIGQIPRNLDEKDLKPLFEEFGKIYELTVLKDRFTGMHKGCAFLTYCERESALKAQSALHEQKTLPGMNRPIQVKPADSESRGGSSCLRQPPSQDRKLFVGMLNKQQSEDDVRRLFEAFGNIEECTILRGPDGNSKGCAFVKYSSHAEAQAAINALHGSQTMPGASSSLVVKFADTDKERTMRRMQQMAGQMGMFNPMAIPFGAYGAYAQALMQQQAALMASVAQGGYLNPMAAFAAAQMQQMAALNMNGLAAAPMTPTSGGSTPPGITAPAVPSIPSPIGVNGFTGLPPQANGQPAAEAVFANGIHPYPAQSPTAADPLQQAYAGVQQYAGPAAYPAAYGQISQAFPQPPPMIPQQQREGPEGCNLLIYHLPQEFGDAELMQMFLPFGFVSFDNPASAQTAIQAMNGFQIGMKRLKVQLKRPKDANRPY
Protein: Large ribosomal subunit protein bL36m (54S ribosomal protein rtc6, mitochondrial) (O94690)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor Tu
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL32m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL19m
Sequence:
MASLGRKFFAVGVLSRVFPSAFNAQKGLLKNASMFLTPAFRLSPSLLPWNFSRGFKVKASVKKRCSSCYFVRRKGRLYVLCKKHPRHKTRQG
Protein: NF-kappa-B inhibitor-like protein 1 (Inhibitor of kappa B-like protein) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 1) (Q5STV6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASTSRRQRRERRFRRYLSAGRLVRAQALLQRHPGLDVDAGQPPPLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQGPDAYTDFFLPLLSRCPSAMGIKNKDGETPGQILGWGPPWDSAEEEEEDDASKEREWRQKLQGELEDEWQEVMGRFEGDASHETQEPESFSAWSDRLAREHAQKCQQQQREAEGSRRPPRAEGSSQSWRQQEEEQRLFRERARAKEEELRESRARRAQEALGDREPKPTRAGPREEHPRGAGRGSLWRFGDVPWPCPGGGDPEAMAAALVARGPPLEEQGALRRYLRVQQVRWHPDRFLQRFRSQIETWELGRVMGAVTALSQALNRHAEALK
Protein: Ran-binding protein 1 homolog b (Q8RWG8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250}.
Interaction partners:
- GTP-binding nuclear protein Ran-3
- RAN GTPase-activating protein 1
- GTP-binding nuclear protein Ran-2
- F2O10.4 protein
- Nuclear pore complex protein NUP155
- RAN GTPase-activating protein 2
- Nuclear pore complex protein NUP54
- Ras-related protein RABH1e
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP205
Sequence:
MASISNEPERENRDEEETGANEDEDTGAQVAPIVRLEEVAVTTGEEDEDTILDLKSKLYRFDKDGSQWKERGAGTVKFLKHRVSGKIRLVMRQSKTLKICANHLVGSGMSVQEHAGNDKSCVWHARDFSDGELKDELFCIRFASVENCKAFMQKFKEVAESEEEKEESKDASDTAGLLEKLTVEEKESEKKPVEKAEENKKSEAVEEKKTEESVPSA
Protein: MHC class I-like protein MILL2 (MHC class I-like located near the leukocyte receptor complex 2) (Q8HWE5)
Organism: Mus musculus (Mouse)
Function: Binds to heparan sulfate proteoglycans on the surface of fibroblast (NIH-3T3) cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16920948}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:16920948}.
Interaction partners:
- NKG2-D type II integral membrane protein
- Beta-2-microglobulin
- Natural cytotoxicity triggering receptor 1
- UL16 binding protein 1
- Killer cell lectin-like receptor subfamily C, member 1
- CD226 antigen
- Myeloid cell surface antigen CD33
- Natural killer cells antigen CD94
- Transferrin receptor protein 1
- Hematopoietic progenitor cell antigen CD34
Sequence:
MKASSGKPREFRPAVLLLILGLLLRDSRGSSIQGFLADVEVHGSSRLTRTHTLRYNVRAHSLEGSEKTQLLVLIYVDEELFLKYNGDSRETEPLGCWIKGHGGNETCARETNNLLKVEEKLRGMMAEVINQKSQEEGLHTLQATLGCELLSNGSTRGFWHLGYDGQNFLTFDQKTLTWTVDGPSTQQNKMFWKTHAPRADLVKTFLDDICPAHLQRYLASLRNGLQDTGPPMVTVTCRNYPVGRVTLTCRAFNLYTREATLVWLQDGKPVQQKTFRSETILPSGDGTYQARVSIRVLPGQEPQFSCNLRHGNHSIMQTAVSGHAAEDSQDVASSATASAGSALPVVLAVALARAN
Protein: Phosphatidylinositol transfer protein 2 (PtdIns transfer protein 2) (DdPITP2) (Q9NCL7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10769190}. Golgi apparatus {ECO:0000269|PubMed:10769190}.
Interaction partners:
Sequence:
MLIKEYRMVLPLTVEEYQIAQLYMVAKKSKESTKGGEGIEIIKNEPFDNEKGKGQYTEKIIYLANSLPRFAAAILPSSALKIEEKAWNAYPYCKTEYSCPFFGEKLVLSIESMHLPGRGEVENALKCDAETLKQRHVDFIDIANDQPKEYIKEEDPKIFKSVKTERGPLDDPKWRDKVEPVMTCYKLVHAEFKYWGFQTKVENVIQDTGVRDVLLKAHRALFCWIDEWFGLTIEDIRKIEEETKAELAKKLEENKAANK
Protein: Homeodomain-only protein (Q8AYB8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Atypical homeodomain protein which does not bind DNA and is required to modulate cardiac growth and development. May act via an interaction with SRF, leading to modulate the expression of SRF-dependent cardiac-specific genes and cardiac development. May act as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and assist in chaperone-mediated protein refolding (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8R1H0}. Cytoplasm {ECO:0000250|UniProtKB:Q8R1H0}.
Interaction partners:
- Chloride intracellular channel protein
- Leucine-rich repeats and immunoglobulin-like domains 1.
Sequence:
MSANGNAALGVRLTEDQVKVLEENFTKVSKHPDETTLMLIAAECGLSEEQTAVWFRMRNAQWRKAEGLPAELGSVKD
Protein: ARM repeat superfamily protein (F4I8B3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEKRLRSSLKTSSEEFLSSAVKLTLKSSKPSLKTIINAVKPSSDLSSSLPLALHNSILHHTESFQKLLDEVNNNNTYIPSPSNSPPTKRHRGTTGTSPDSDLDQRKHQILASLQILSYVLHLCLLNPKNAFPTSDLLPAAQALHNNLRLFESDSVLCLEIAGVCECWWKEGLVGRESLISQSLPFLLSRSLTLKKKVDVHRVYMLREAFTLFDFEDESIEDLRMLLMRCVVSPLYVKTEDGQRFVSFAFGLSRQLMKSGLAVVKAQIPLGSKSVLEGFGGILFRAWKEVELDLKGEIEDGFLQGIIDSAIHASSSAFAASLRRVLGGFISQRTSQGVEKLLFTLAEPMIFRSLQVANSNVRLNALHLLLDLFPMEDPDATKEAKDTLLDKQFYLLEKLLSDECPDVRSVAVEGLSRVFYLFWEVIPSATITKVLTKIFDDMSHESCSEVRLSTVNGITYLLANPQSHGILKVILPRLGHLMLDSVTSVRVAMVDLLLLIRDVRAFQFNTVVSLDVLLSVLASDQTHVAKGIARLLIPSYFPSRKRAEEACQRCRTLINRNPKAGARFCEFLVSLGATVKSVLHLVGFFLNSVLSGDKLLENQTEGLLRAAYYLCKDLVADSGCMASLKELLPGEKLKSLLAFAPTAQAQSSVIDIITMVSPDIVSEVLEDCMNLVVNCGGLPSDAGRQTELRSVHKLLLSSNAFCDLIGTFTSIMQKTAYRCQINFGYEVERKNLQSMKRKKSKSSGKSSVRWKHVSGKNAISFEEDYLVAVGIAWQIKDLLTTEDARKSILESDIEELLLSLKVVSHTSILQATCCEYMDVNPDIMDQTMDHILVCTDELFQAGDIGTPGTTSPEANLSKKPTTSNGNQPKRRNRNARDDASEGSKEGGVLNKVKMLTAIFKFFVESTEMGLASNFQASMFKFSSAYLKYVISIFNDHSTGKLEFEDADMKEMILCTKSSTSYAGKFINLVMRHATEASRPLFESFDLANDLLDLFTMVEKSLGSAYASRIVSALNPWIPDLVLALGPCFINNDSEESSYTSSFNHIKLCFPSWLLTCAKIELHEINKEDVTETSGFLALKKLRNTIFTLVKGNTKVLDAIGYVLLLCLAVCIEKRDYSTALGLLHLVCVKLVGSEDREWKELDTMLVLLPRIYPIIEREIGEGRDEDEVKTLEAARELLQPVWMYHVYETGRFHMMDEEEE
Protein: Phosphoserine aminotransferase, chloroplastic (PSAT) (EC 2.6.1.52) (Phosphohydroxythreonine aminotransferase) (P52877)
Organism: Spinacia oleracea (Spinach)
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:Q96255}.
Interaction partners:
Sequence:
MAMAATSSTQTNLFLKAPFNPQQNCQQTHFLPLNFKIRNPISRITCSATPTATAVSTTTKIDQRSEERVFNFAAGPAVLPENVLQKAQSELLNWRGSGMSVMEMSHRGKEFTSIIDKAEADLRTLLNIPSDYTVLFLQGGASTQFSAIPLNLCTPDSAVDYIVTGSWGDKAAKEAAKYAAVSSIWSGKSDNYVRIPNFDGSEFVQNSQARYLHICANETIYGVEFKKYPVPANPDGFLVADMSSNFCSKPVDVTKFGLIYAGAQKNVGPSGVTIVIVRNDLIGNAQKMTPVMLDYKIHADNKSLYNTPPCYGIYMCGLVFEDLLNQGGLVEVEKKNKAKAQVLYDAIDESNGFYKCPVEKSVRSLMNVPFTLEKSELEGDFIKEAAKEKMVALKGHRSVGGMRASIYNAMPLAGVEKLVAFMKEFQAKHA
Protein: Oxysterol-binding protein homolog 2 (Oxysterol-binding protein-related protein 2) (ORP 2) (OSBP-related protein 2) (Q12451)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis. Binds and transports sterol. Plays a role in the positive regulation of vesicular transport of ceramide from the ER to the Golgi, negatively regulating COPII-mediated ER export of cargos.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11408574, ECO:0000269|PubMed:12727870, ECO:0000269|PubMed:20008566}; Peripheral membrane protein {ECO:0000269|PubMed:11408574, ECO:0000269|PubMed:12727870}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20008566}. Note=Cell periphery, enriched in small buds of G1 phase cells and near the bud-neck region of S phase cells. Enriched on regions of the ER in close proximity with the plasma membrane (PM), which may represent PM-ER membrane contact sites (MCS) (PubMed:20008566). {ECO:0000269|PubMed:20008566}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein SCS2
- Vesicle-associated membrane protein-associated protein SCS22
- Myosin-5
- Protein MSS51, mitochondrial
- Phosphatidylinositol 4-kinase STT4
- Phosphatidylinositol-3-phosphatase SAC1
- Oxysterol-binding protein homolog 1
- Phosphatidylinositol 4-kinase PIK1
- Oxysterol-binding protein homolog 3
- ADP-ribosylation factor 1
Sequence:
MSREDLSIAEDLNQVSKPLLKVKLLEVLGQGDFKHLKALVDNEFQPKDDPSVQQVLNLILHYAVQVAPILLIKEIVAHWVDQVGDEKSSSKSDDGIHLDLNYQDENGNTPLHLAAAQSRSDVISFLLSQKSINDCVKNKAHQQPLDMCKDLNVAQMIQLKRDDYFLETVHSLRAAMNKRDFSKLDSIWKNPRNLNLLDINGIDPETGTTLLYEYSQKKDIEMCQWLLKHGAEATVKDGKGRSPLDLVKNIKLPAKPSNNVTPEIKLKNLLEKNLREQAIVHEDVASSKPPTYKGFLKKWTNFAHGYKLRWFILSGDGNLSYYKDQSHVDRPRGTLKVSTCRLHIDSSEKLNFELLGGITGTTRWRLKGNHPIETTRWVNAIQSAIRFAKDKEILNKKKAVPPSLALKNKSPALISHSKTQGSLPEASQYYQHTLHKEVIQPSSVSLYRRPSNNLSVVSSEIQLNDNLTESGKRFVSKMIENRLDGSKTPVGVHTGSALQRVRSSNTLKSNRSMQSGSGVASPIDKVPNGANLSQSNTTTGSTASLSDNNYIDNFEGDEANSDDEEEDLGINFDRDEEYIKAQYGPYKEKLDMYEQAISIELSSLIELIEQEEPSPEVWLTIKKSLINTSTIFGKLKDLTYKRDKRLVDMVSKQGDVNNVWVQSVKELEMELSNKTERLASIDKERRGLKKILHKKLLESHATAGNKESLENDKEQESDTTASTLGQIAKFISATKEEDEASDADEFYDAAELVDEVTELTEAHPEISTAAAPKHAPPPVPNETDNDSQYVQDEKSKIESNVEKTSQKFEKQNNLVTEDEPKTDQSLKNFKAEDKESQVKEKTKEIASSVIGEKTIVAVTTVQKRKEEYLLKEGSYLGYEDGIRKRLSMDKDDRPKISLWAVLKSMVGKDMTRMTLPVTFNEPTSLLQRVAEDLEYSELLDQAATFEDSTLRTLYVAAFTASSYASTTKRVAKPFNPLLGETFEYSRPDKQYRFFTEQVSHHPPISATWTESPRWDFWGESFVDTKFNGRSFNVKHLGLWHIKLRPNDNEKEELYTWKKPNNTVIGILIGNPQVDNHGEVNVVNHTTGDHCKLYFKARGWRSSGAYEITGEVYNKKKQKVWILGGHWNEAIFAKKVVKDGDLSLEKTRTAASAGNGPTDDGTKFLIWKANDRPEEPFNLTPFAITLNAPQPHLLPWLPPTDTRLRPDQRAMEDGRYDEAGDEKFRVEEKQRAARRKREENNLEYHPQWFVRDTHPITKAKYWRYTGKYWVKRRDHDLKDCGDIF
Protein: Erbb2 interacting protein (A0A8I5ZN42)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTTKRSLFVRLVPCRCLRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTVVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRLTKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLREFWMDGNRLTFIPGFIGSLRQLTYLDVSKNNIEMVEEGISTCENLQDFLLSSNSLQQLPETIGSLKNVTTLKIDENQLMYLPDSIGGLRSIEELDCSFNEIEALPSSIGQLTNIRTFAADHNYLQQLPPEIGNWKNVTVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSDNQSKPLIPLQKETDSETQKMVLTNYMFPQQPRTEDVMFISDNESFNPALWEEQRKQRAQVAFECDEDKDEREAPPREGNLKRYPTPYPDELKNMVKTVQTIVHRLKDEETNEESGRDLKQHEDQQVVNKDKGVKPSESITTKSKLDEREKYMNSVPKTSEPEAETNAGNSPVTTNRKSSGNMKHLVNHDDVFEESEELSSDEEMKMAEMRPPLIETSINQPKVVALSNNKKDDAKDTDSLSDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTALCSPAKQIPIDSNSKIRQEDENFNSLLQNGVNLNNSPEEKFKINDKKDFKLPEYDLNIEEQLVLIEKDVDSKATSEDSHQLDHINMNLNKLVTNNIFQPEIMERSKMQDIVLGTGFLSIHSKSEAEHIENGNKFLNSESINKVNGLSEDTAQSPGRIEPQNTSPADVGISKSTEDLSPQRSGPAGSVVKSHSITNMETGGLKIYDILSDDGPQPPGATVKVASTMDGKNIVRSKSATLLYDQPLQVFTASSSSSELLSGTKAVFKFDSNHNPEDPDIIRASIVPGPQSIPQLYGPPQYNVQYSGSAAMKDTLWHPKQNPQIDPVSFPPQRLPRSESAENHSYTKHSANMNFSNHNNVRANTAYHLHQRLAPTRHGEMWAVSPNDRLVPAVSRTTVQRQSSVSSTASVNLGDPGPTRRTEGDYLSYRELHSMGRTPVTSGSQRPLSARAFSIDGPSTSRPQSARPSISEIPERTMSVSDFNYSRTSPSKRPNARVGSEHSLLDPPGKSKVPHDWREQVLRHIEAKKLEKVTEHEFFYSLYEFTFLRIGSSFVFNQ
Protein: S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) (SAMDC) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase beta chain; S-adenosylmethionine decarboxylase alpha chain] (P0A7F6)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
Interaction partners:
- Polyamine aminopropyltransferase
- S-adenosylmethionine synthase
- DNA-cytosine methyltransferase
- Agmatinase
- Constitutive ornithine decarboxylase
- Inducible ornithine decarboxylase
- Biosynthetic arginine decarboxylase
Sequence:
MKKLKLHGFNNLTKSLSFCIYDICYAKTAEERDGYIAYIDELYNANRLTEILSETCSIIGANILNIARQDYEPQGASVTILVSEEPVDPKLIDKTEHPGPLPETVVAHLDKSHICVHTYPESHPEGGLCTFRADIEVSTCGVISPLKALNYLIHQLESDIVTIDYRVRGFTRDINGMKHFIDHEINSIQNFMSDDMKALYDMVDVNVYQENIFHTKMLLKEFDLKHYMFHTKPEDLTDSERQEITAALWKEMREIYYGRNMPAV
Protein: H/ACA ribonucleoprotein complex subunit CBF5 (EC 5.4.99.-) (Centromere-binding factor 5) (H/ACA snoRNP protein CBF5) (Small nucleolar RNP protein CBF5) (rRNA pseudouridine synthase) (O43100)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P33322}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit NOP10
- H/ACA ribonucleoprotein complex subunit
- Small nuclear ribonucleoprotein complex protein Nhp2, putative
- rRNA 2'-O-methyltransferase fibrillarin
- Nucleolar protein 58
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- Nucleolar protein 56
- Uncharacterized protein
- H/ACA ribonucleoprotein complex subunit 2
- ATP-dependent RNA helicase has1
Sequence:
MAKEVDYTIKPEATASNINTEDWPLLLKNYDKLMVRTGHFTPIPAGSSPLKRDLKSYINSGVINLDKPSNPSSHEVVAWMKRILRAEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCVIRLHDKIPGGEAQFKRALETLTGALFQRPPLISAVKRQLRIRTIHESKLYEFDNERHLGVFWVSCEAGTYIRTLCVHLGLLLGVGAHMQELRRVRSGAMSENEGMVTLHDVLDAQWLYDNQRDESYLRKVIKPLESLLTTYKRIVVKDSAVNAVCYGAKLMIPGLLRFEAGIELGEEVVLMTTKGEAIAIGIAQMSTVELSTCDHGVVAKVKRCIMERDLYPRRWGLGPVALEKKKLKSSGKLDKYGRANEATPAKWKSEYKDYSAPDGDSSQQAVDVVAKEEASPKEEPSLEANESKMDIDDAQDDEDKKKRKRHEGETPEERAERKRKKKEKKEKKERRKSKQEKDDSDDSD
Protein: Beta-1,3-galactosyltransferase 5 (Beta-1,3-GalTase 5) (Beta3Gal-T5) (Beta3GalT5) (b3Gal-T5) (EC 2.4.1.-) (Beta-3-Gx-T5) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 5) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 5) (Q9Y2C3)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of Gal to GlcNAc-based acceptors with a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc structure. Can use glycolipid LC3Cer as an efficient acceptor.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Galactoside alpha-
- Galactoside alpha-
- Beta-1,4-galactosyltransferase 4
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
- Beta-1,4-galactosyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 3
Sequence:
MAFPKMRLMYICLLVLGALCLYFSMYSLNPFKEQSFVYKKDGNFLKLPDTDCRQTPPFLVLLVTSSHKQLAERMAIRQTWGKERMVKGKQLKTFFLLGTTSSAAETKEVDQESQRHGDIIQKDFLDVYYNLTLKTMMGIEWVHRFCPQAAFVMKTDSDMFINVDYLTELLLKKNRTTRFFTGFLKLNEFPIRQPFSKWFVSKSEYPWDRYPPFCSGTGYVFSGDVASQVYNVSKSVPYIKLEDVFVGLCLERLNIRLEELHSQPTFFPGGLRFSVCLFRRIVACHFIKPRTLLDYWQALENSRGEDCPPV
Protein: Intermediate transcription factor 3 small subunit (VITF-3 32 kDa subunit) (VITF-3 small subunit) (P68720)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: Acts with RNA polymerase to initiate transcription from intermediate gene promoters.
Interaction partners:
Sequence:
MFEPVPDLNLEASVELGEVNIDQTTPMIKENSGFISRSRRLFAHRSKDDERKLALRFFLQRLYFLDHREIHYLFRCVDAVKDVTITKKNNIIVAPYIALLTIASKGCKLTETMIEAFFPELYNEHSKKFKFNSQVSIIQEKLGYQFGNYHVYDFEPYYSTVALAIRDEHSSGIFNIRQESYLVSSLSEITYRFYLINLKSDLVQWSASTGAVINQMVNTVLITVYEKLQLVIENDSQFTCSLAVESKLPIKLLKDRNELFTKFINELKKTSSFKISKRDKDTLLKYFT