wanglab/gogpt-training-data huggingface dataset:
Protein: MAM domain-containing glycosylphosphatidylinositol anchor protein 2 (MAM domain-containing protein 1) (P60755)
Organism: Mus musculus (Mouse)
Function: May be involved in cell-cell interactions.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Neuroligin-2
- Neuroligin-1
- Neuroligin-3
Sequence:
MDLVYGLVWLLTVLLEGISGQGVYAPPTVRIVHSGLACNIEEERYSERVYTIREGETLELTCLVTGHPRPQIRWTKTAGSASDRFQDSSVFNETLRITNIQRHQGGRYYCKAENGLGSPAIKSIRVDVYYLDDPVVTVHQSIGEAKEQFYYERTVFLRCVANSNPPVRYSWRRGQEVLLQGSDKGVEIYEPFFTQGETKILKLKNLRPQDYANYSCIASVRNVCNIPDKMVSFRLSNKTASPSIKLLVDDPIVVNPGEAITLVCVTTGGEPTPSLTWVRSFGTLPEKIVLNGGTLTIPAITSDDAGTYSCIANNNVGNPAKKSTNIIVRALKKGRFWITPDPYHKDDNIQIGREVKISCQVEAVPSEELTFSWFKNGRPLRSSERMVITQTDPDVSPGTTNLDIIDLKFTDFGTYTCVASLKGGGISDISIDVNISSSTVPPNLTVPQEKSPLVTREGDTIELQCQVTGKPKPIILWSRADKEVAMPDGTMQMESYDGTLRIVNVSREMSGMYRCQTSQYNGFNVKPREALVQLIVQYPPAVEPAFLEIRQGQDRSVTMSCRVLRAYPIRVLTYEWRLGNKLLRTGQFDSQEYTEYPLKSLSNENYGVYNCSIINEAGAGRCSFLVTGKAYAPEFYYDTYNPVWQNRHRVYSYSLQWTQMNPDAVDRIVAYRLGIRQAGQQRWWEQEIKINGNIQKGELITYNLTELIKPEAYEVRLTPLTKFGEGDSTIRVIKYTGEFHCGFEDGNICLFTQDDTDNFDWTKQSTATRNTKYTPNTGPSADRSGSKEGFYMYIETSRPRLEGEKARLLSPVFSIAPKNPYGPTNSAYCFSFFYHMYGQHIGVLNVYLRLKGQTTIENPLWSSSGNKGQRWNEAHVNIYPITSFQLIFEGIRGPGIEGDIAIDDVSIAEGECAKQDLPTKNSVDGAVGILVHIWLFPVIILISILSPRR
Protein: Survival protein SurE-like phosphatase/nucleotidase domain-containing protein (G8BD63)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
Sequence:
MQFLTQSILLFLATAVIAKNIILSNDDGWQATNIRATYYKLKEAGHEVWLVAPVSQRSGFGGKFDIPTSPTLQTDGEFKYPPAGSPSWGHEEDDDHIWYFNGTPASSIAFGLQYVIPEKFNNVSIDLVVAGPNEGTNLSPGMFTLSGTVGATYNSVYRGYPAVAFSGSNSNNSFFKDSLDLDDANEPSTIYANKVTEFVNQLFKTQGDNSRALPLGVGLNVNFPKVGYENESCTDPAWVFTRLTGQYASGADLKFNASSNSFVWAQTSWQALTVCNNGDCSLPSENLVVEHTKCATSVSVFAIDYDANLGITNQVEGLLDPLFKKD
Protein: Alpha-1,2-mannosyltransferase alg9 (EC 2.4.1.259) (EC 2.4.1.261) (Asparagine-linked glycosylation protein 9) (Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase) (Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase) (Q9P7Q9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Probable Dol-P-Man:Man
- Dol-P-Man:Man
- Dolichyl-phosphate beta-glucosyltransferase
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- GPI transamidase component gaa1
- GPI mannosyltransferase 4
- GPI ethanolamine phosphate transferase 3
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- GPI-anchor transamidase
- Dolichol-phosphate mannosyltransferase
Sequence:
MPSKAPRKSLSVSFVWTFSILAVLRLTSASFRVIDDCDEVYNYWEPLHYLLYGYGLQTWEYSPEYAIRSWFYIALHAVPGFLARGLGLSRLHVFYFIRGVLACFSAFCETNLILAVARNFNRAVALHLTSVLFVNSGMWSASTSFLPSSFAMNMVTLALSAQLSPPSTKRTVKVVSFITIGAVIGWPFSAALSIPFILLELVDLKGRFRHLFCRWFKAIFVALLITGICITVDSLFYHRIQFVAWNIVKYNVLAKDGRGPDIYGTEPWWYYFANLSLQHNIVLWFAMACGPLVLLAAFTNWINLDSFLDLSSVISPFYIWLFIFIIQPHKEERFMYPIYPVLCLAAAIGLDMSLKLMIQILSSINETVRSKFPVRFVVLCVYAIIGCLSIARILAIQNYNAPMIIYPAISFLETDNNVTTNVCVGKEWYRYPSTFFLPDNSRLKFVKSEFDGILPGEFVESNSTWWNREGYYQIPEHMNEFNNEEPTRYTSLESCDFLIDLEFDHSKATVNEPIYSKSDGWIPVMVYPFIDTKQTPFMGRAFAVPFIEPKWGRYEILVKKPVKIDFSNLRRASKQQA
Protein: AKT serine/threonine kinase 2 (J3QLS6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKL
Protein: Ciliary microtubule associated protein 1A (Outer dense fiber of sperm tails protein 3) (Outer dense fiber protein 3) (Sperm tail protein SHIPPO 1) (Q920N1)
Organism: Mus musculus (Mouse)
Function: Outer dense fibers are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail. May help to maintain the passive elastic structures and elastic recoil of the sperm tail.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11870087}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:11870087, ECO:0000269|PubMed:37295417}. Note=Expressed in the cytoplasmic lobe of spermatids. {ECO:0000269|PubMed:11870087}.
Interaction partners:
- Outer dense fiber protein 4
Sequence:
MAEEVWMGTWRPHRPRGPIMALYSSPGPKYLIPPTTGFVKHTPTKLRAPAYSFRGAPMLLAENCSPGPRYSVNPKILKTGKDLGPAYSILGRYHTKTLLTPGPGDYFPEKSTKYVFDSAPSHSISARTKTFRVDSTPGPAAYMLPVVMGPHTVGKVSQPSFSIKGRSKLGSFSDDLHKTPGPAAYRQTEVQVTKFKAPQYTMAARVEPPGDKTLKPGPGAHSPEKVTLNKPCAPTVTFGIKHSDYMTPLVVDVE
Protein: Magnesium transporter NIPA1 (Non-imprinted in Prader-Willi/Angelman syndrome region protein 1 homolog) (Q8BHK1)
Organism: Mus musculus (Mouse)
Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17166836}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:17166836}. Note=Recruited to the cell membrane in response to low extracellular magnesium.
Interaction partners:
- Gamma-tubulin complex component 5
- Cytoplasmic FMR1-interacting protein 1
- Atlastin-1
- Receptor expression-enhancing protein 1
- Spartin
- Maspardin
- Spastin
Sequence:
MGTAAAAAAAGEGARGPSPAAVSLGLGVAVVSSLVNGSTFVLQKKGIVRAKRRGTSYLTDIVWWAGTIAMAVGQIGNFLAYTAVPTVLVTPLGALGVPFGSILASYLLKEKLNILGKLGCLLSCAGSVVLIIHSPKSESVTTQAELEEKLTNPVFVGYLCIVLLMLLLLIFWIAPAHGPTNIMVYISICSLLGSFTVPSTKGIGLAAQDILHNNPSSQRALCLCLVLLAVLGCSIIVQFRYINKALECFDSSVFGAIYYVVFTTLVLLASAILFREWSNVGLVDFLGMACGFTTVSVGIVLIQVFKEFNFNLGEMNKSNMKTD
Protein: Protein BOP2 (Bypass of PAM1 protein 2) (Q06150)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized protein YDR246W-A
- Ubiquitin-like protein MDY2
- Solute carrier RCH1
- Oxidoreductase-like protein SRL4
- Increased recombination centers protein 6
- Uncharacterized protein YDR366C
Sequence:
MVAALTYLPTELIQRIFEFTVVETDSQYWLYNLVALIDFSVSSRGGGSITEDFLTNYVRKNLMVLDLTCEATQDSILRAEYGFLKRLLPYIDMDAQYIRVVDLETNADKAQNLKAEKLIVIFDEFSDLKLIETFFPLANSNSNIIEFVFCVRNIKSSFYSPLEKLHIANIVADIDINTLYLDFVDSNIYSDQNFFGIFDPDIFQLINKNYRNFFSKTNEKGKKRPPICKKICFPFVETLNLDYMALDSFFNSILHKLTTKIKTFERNNEFDVDKNLNLNSTTTVAALIIKSILQQFFNNFHISFPNLVTLNFIKMSTYPNNNEITQCCNFIDLSSYVLNKCLSENISINFLFQLHSLKNWSMPKIKEFTGHKFKYDETTFSGSPERYIKSLRGNIKILQEMAINETNDGTCYFRVKLIPEGVEKTQIINWIPFTSSFSDDTFKQRHHLKRPMICLKNNSLRSLTVKIIRIEKCSSIRIQGFYLPNLQELFINNTLCDTTQHQKQASNDMSCIEFTSWNELPQCKKLGFAQLEDDSNYVLNISNLQDHLPNLDLRESFPTFFDIRQKFVVV
Protein: Probable asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (Glutamine-dependent asparagine synthetase) (Q54MB4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- asparaginase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Putative isoaspartyl peptidase/L-asparaginase
- Multifunctional protein pyr1-3
- Adenylosuccinate synthetase
- Asparagine synthetase
- Sumo-conjugating enzyme ubc9
- RING-type domain-containing protein
- Type-1 glutamine synthetase 2
Sequence:
MCGILAILNSLEEASKLRKKALSLSSRLRHRGPDWNGIYQSSDSILTHERLAIVGLENGAQPLLNEDETIALTVNGEIYNHEKLREDLVATGKHTFKTHSDCEPILHLYEDKGDDFVHMLDGDFAFVVYNKKANSFLAARDPIGVVPLYIGWHKDGSIWFSSEMKAIKDDCYKFQPFPPGHYFSSKTKEFVRYYKPNWIMGDSPSGVLKSEEQVLPAIKEAFEQAVVSRMMSDVPYGVLLSGGLDSSLVASIVSRHAEQRVEDHEKSRAWWPRIHSFCIGLKDAPDLKAARDVADYLQTVHHEYHFTVQEGIDALPDVIKHLETYDVTTIRASTPMYFLSRKIKAMGVKMVLSGEGSDEIFGGYLYFHNAPDANEFHVECCRRIKALHSFDCLRANKSTAAWGVEVRVPFLDQRFLDVAMNIDPSHKVCHDDQGKKRMEKYILRKAFETKEGEKPYLPSSVLWRQKEQFSDGVGYSWIDGLKENAENEVSDEEFAKRESYFPDDTPTTKEAFLYRKMFEAIYPGKECMETVQRWIPTWGASQDPSGRAQKVHLSTTE
Protein: Protein ENL (YEATS domain-containing protein 1) (Q03111)
Organism: Homo sapiens (Human)
Function: Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically recognizes and binds acetylated and crotonylated histones, with a preference for histones that are crotonylated. Has a slightly higher affinity for binding histone H3 crotonylated at 'Lys-27' (H3K27cr) than 'Lys-20' (H3K9cr20).
Subcellular location: Nucleus.
Interaction partners:
- Cyclin-T1
- RNA polymerase II elongation factor ELL2
- AF4/FMR2 family member 1
- Cyclin-dependent kinase 9
- Protein AF-9
- AF4/FMR2 family member 4
- RNA polymerase II elongation factor ELL
- RNA polymerase II elongation factor ELL3
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- ELL-associated factor 1
Sequence:
MDNQCTVQVRLELGHRAQLRKKPTTEGFTHDWMVFVRGPEQCDIQHFVEKVVFWLHDSFPKPRRVCKEPPYKVEESGYAGFIMPIEVHFKNKEEPRKVCFTYDLFLNLEGNPPVNHLRCEKLTFNNPTTEFRYKLLRAGGVMVMPEGADTVSRPSPDYPMLPTIPLSAFSDPKKTKPSHGSKDANKESSKTSKPHKVTKEHRERPRKDSESKSSSKELEREQAKSSKDTSRKLGEGRLPKEEKAPPPKAAFKEPKMALKETKLESTSPKGGPPPPPPPPPRASSKRPATADSPKPSAKKQKKSSSKGSRSAPGTSPRTSSSSSFSDKKPAKDKSSTRGEKVKAESEPREAKKALEVEESNSEDEASFKSESAQSSPSNSSSSSDSSSDSDFEPSQNHSQGPLRSMVEDLQSEESDEDDSSSGEEAAGKTNPGRDSRLSFSDSESDNSADSSLPSREPPPPQKPPPPNSKVSGRRSPESCSKPEKILKKGTYDKAYTDELVELHRRLMALRERNVLQQIVNLIEETGHFNVTNTTFDFDLFSLDETTVRKLQSCLEAVAT
Protein: Secretogranin-2 (Chromogranin-C) (Secretogranin II) (SgII) [Cleaved into: Secretoneurin (SN); Manserin] (P10362)
Organism: Rattus norvegicus (Rat)
Function: Neuroendocrine protein of the granin family that regulates the biogenesis of secretory granules.
Subcellular location: Secreted. Note=Neuroendocrine and endocrine secretory granules.
Interaction partners:
- Secretogranin-1
- Chromogranin-A
- Secretogranin-3
- Carboxypeptidase E
- Neurosecretory protein VGF
- Neuroendocrine protein 7B2
Sequence:
MTESKAYRFGAVLLLIHLIFLVPGTEAASFQRNQLLQKEPDLRLENVQKFPSPEMIRALEYIEKLRQQAHREESSPDYNPYQGISVPLQLKENGEESHLAESSRDVLSEDEWMRIILEALRQAENEPPSALKENKPYALNLEKNFPVDTPDDYETQQWPERKLKHMRFPLMYEENSRENPFKRTNEIVEEQYTPQSLATLESVFQELGKLTGPSNQKRERVDEEQKLYTDDEDDVYKTNNIAYEDVVGGEDWSPMEEKIETQTQEEVRDSKENTEKNEQINEEMKRSGHLGLPDEGNRKESKDQLSEDASKVITYLRRLVNAVGSGRSQSGQNGDRAARLLERPLDSQSIYQLIEISRNLQIPPEDLIEMLKAGEKPNGLVEPEQDLELAVDLDDIPEADIDRPDMFQSKTLSKGGYPKAPGRGMMEALPDGLSVEDILNVLGMENVANQKSPYFPNQYSRDKALLRLPYGPGKSRANQIPKVAWIPDVESRQAPYDNLNDKDQELGEYLARMLVKYPELMNTNQLKRVPSPGSSEDDLQEEEQLEQAIKEHLGQGSSQEMEKLAKVSKRIPAGSLKNEDTPNRQYLDEDMLLKVLEYLNQEQAEQGREHLAKRAMENM
Protein: 40S ribosomal protein S24 (Q9W229)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 40S ribosomal protein S27
- 60S ribosomal protein L27
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein eS10A
- FI01658p
Sequence:
MSGTTATIRTRKFMTNRLLARKQMVCDVLHPGLSSVNKTEIREKLAAMYKVTPDVVFAFGFRTNFGGGRSTGFALIYDTLDFAKKFEPKYRLARHGLFEQKKQTRKQRKERRNRMKKVRGTAKAKIGTGKK
Protein: Acyl-CoA 6-desaturase (EC 1.14.19.3) (Delta(6) fatty acid desaturase) (D6D) (Delta(6) desaturase) (Delta-6 desaturase) (Fatty acid desaturase 2) (O95864)
Organism: Homo sapiens (Human)
Function: Involved in the biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors, acting as a fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 6 of the fatty acyl chain. Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleate (GLA) (18:3n-6) and stearidonate (18:4n-3), respectively. Subsequently, in the biosynthetic pathway of HUFA n-3 series, it desaturates tetracosapentaenoate (24:5n-3) to tetracosahexaenoate (24:6n-3), which is then converted to docosahexaenoate (DHA)(22:6n-3), an important lipid for nervous system function (By similarity). Desaturates hexadecanate (palmitate) to produce 6Z-hexadecenoate (sapienate), a fatty acid unique to humans and major component of human sebum, that has been implicated in the development of acne and may have potent antibacterial activity. It can also desaturate (11E)-octadecenoate (trans-vaccenoate, the predominant trans fatty acid in human milk) at carbon 6 generating (6Z,11E)-octadecadienoate (By similarity). In addition to Delta-6 activity, this enzyme exhibits Delta-8 activity with slight biases toward n-3 fatty acyl-CoA substrates (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Stearoyl-CoA desaturase
- Phospholipase A and acyltransferase 3
- Very long chain fatty acid elongase 5
- Very long chain fatty acid elongase 2
- Cytosolic phospholipase A2
- Group 10 secretory phospholipase A2
- 85/88 kDa calcium-independent phospholipase A2
- Fatty acid synthase
- Phospholipase A2, membrane associated
- Very long chain fatty acid elongase 6
Sequence:
MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQHPGGQRVIGHYAGEDATDAFRAFHPDLEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVLGEWQPIEYGKKKLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIVHKNWVDLAWAVSYYIRFFITYIPFYGILGALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAYRDWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGKLWLDAYLHK
Protein: DnaJ homolog subfamily C member 3 (Endoplasmic reticulum DNA J domain-containing protein 6) (ER-resident protein ERdj6) (ERdj6) (Interferon-induced, double-stranded RNA-activated protein kinase inhibitor) (Protein kinase inhibitor of 58 kDa) (Protein kinase inhibitor p58) (Q13217)
Organism: Homo sapiens (Human)
Function: Involved in the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. Acts as a negative regulator of the EIF2AK4/GCN2 kinase activity by preventing the phosphorylation of eIF-2-alpha at 'Ser-52' and hence attenuating general protein synthesis under ER stress, hypothermic and amino acid starving stress conditions (By similarity). Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity.
Subcellular location: Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Interferon-induced, double-stranded RNA-activated protein kinase
- Endoplasmic reticulum chaperone BiP
- DnaJ homolog subfamily B member 1
- X-box-binding protein 1
- Protein disulfide-isomerase A6
- Hypoxia up-regulated protein 1
- Endoplasmin
- Heat shock 70 kDa protein 4
- 52 kDa repressor of the inhibitor of the protein kinase
- DnaJ homolog subfamily B member 11
Sequence:
MVAPGSVTSRLGSVFPFLLVLVDLQYEGAECGVNADVEKHLELGKKLLAAGQLADALSQFHAAVDGDPDNYIAYYRRATVFLAMGKSKAALPDLTKVIQLKMDFTAARLQRGHLLLKQGKLDEAEDDFKKVLKSNPSENEEKEAQSQLIKSDEMQRLRSQALNAFGSGDYTAAIAFLDKILEVCVWDAELRELRAECFIKEGEPRKAISDLKAASKLKNDNTEAFYKISTLYYQLGDHELSLSEVRECLKLDQDHKRCFAHYKQVKKLNKLIESAEELIRDGRYTDATSKYESVMKTEPSIAEYTVRSKERICHCFSKDEKPVEAIRVCSEVLQMEPDNVNALKDRAEAYLIEEMYDEAIQDYETAQEHNENDQQIREGLEKAQRLLKQSQKRDYYKILGVKRNAKKQEIIKAYRKLALQWHPDNFQNEEEKKKAEKKFIDIAAAKEVLSDPEMRKKFDDGEDPLDAESQQGGGGNPFHRSWNSWQGFNPFSSGGPFRFKFHFN
Protein: RE10833p (Trivet, isoform A) (Q9VAX3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLAMPTLMMPATAQMTLSAAHGKPYETKLLAIHQTHLQQQQQQQAPAPPQQQQQVQQSQQQAPNGKQQSQQMTIVTTQQQQQQQHPQSQSPHQQQQSQQQAAAAAAAAAAAAHHQQQQAVAAAVCAAQQQAVVVQQQQQQQYQIHSQQQSPQQQQVLCISPKQEQFHIFVGDLSSEIETQQLREAFTPFGEISDCRVVRDPQTLKSKGYGFVSFIKKSEAESAITAMNGQWLGSRSIRTNWATRKPPASKENIKPLTFDEVYNQSSPSNCTVYVGGVNSALTALSEEVLQKTFAPYGAIQEIRVFKDKGYAFVRFSTKEAATHAIVGVHNTEINAQPVKCSWGKESGDPNNAQTIATQALNSAAAAAAGFPYGVGAAAAAAAYGQQLAATGCWYSPTPTYPASSATAAAVTPAAASAAAVQNQFLQGIQGYHFGQYGGYQQGYMGMGVQIPATWQGVTQAQISPAQQLATGVAGTAIPQAAGVVAYPIQQFQVSPQVYPLLLQAQ
Protein: Putative aga operon transcriptional repressor (P0ACK2)
Organism: Escherichia coli (strain K12)
Function: Probable repressor for the aga operon for N-acetyl galactosamine transport and metabolism.
Interaction partners:
- D-tagatose-1,6-bisphosphate aldolase subunit KbaZ
- Putative D-galactosamine-6-phosphate deaminase AgaS
Sequence:
MSNTDASGEKRVTGTSERREQIIQRLRQQGSVQVNDLSALYGVSTVTIRNDLAFLEKQGIAVRAYGGALICDSTTPSVEPSVEDKSALNTAMKRSVAKAAVELIQPGHRVILDSGTTTFEIARLMRKHTDVIAMTNGMNVANALLEAEGVELLMTGGHLRRQSQSFYGDQAEQSLQNYHFDMLFLGVDAIDLERGVSTHNEDEARLNRRMCEVAERIIVVTDSSKFNRSSLHKIIDTQRIDMIIVDEGIPADSLEGLRKAGVEVILVGE
Protein: Sodium-dependent phosphate transport protein 2A (Sodium-phosphate transport protein 2A) (Na(+)-dependent phosphate cotransporter 2A) (NaPi-3) (Sodium/phosphate cotransporter 2A) (Na(+)/Pi cotransporter 2A) (NaPi-2a) (Solute carrier family 34 member 1) (Q06495)
Organism: Homo sapiens (Human)
Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. The cotransport has a Na(+):Pi stoichiometry of 3:1 and is electrogenic (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:26047794}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:20335586}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at the brush border membranes of the proximal tubules. Internalized from the cell surface upon PTH stimulation. {ECO:0000250|UniProtKB:Q06496, ECO:0000250|UniProtKB:Q60825}.
Interaction partners:
- Na
- Sodium-dependent phosphate transport protein 2C
- Sodium-dependent phosphate transport protein 1
- Fibroblast growth factor 23
- Sodium-dependent phosphate transport protein 2B
- Phosphate-regulating neutral endopeptidase PHEX
- Parathyroid hormone
- 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
- Probable small intestine urate exporter
- Na
Sequence:
MLSYGERLGSPAVSPLPVRGGHVMRGTAFAYVPSPQVLHRIPGTSAYAFPSLGPVALAEHTCPCGEVLERHEPLPAKLALEEEQKPESRLVPKLRQAGAMLLKVPLMLTFLYLFVCSLDMLSSAFQLAGGKVAGDIFKDNAILSNPVAGLVVGILVTVLVQSSSTSTSIIVSMVSSGLLEVSSAIPIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHITRLVVASFNIHGGRDAPDLLKIITEPFTKLIIQLDESVITSIATGDESLRNHSLIQIWCHPDSLQAPTSMSRAEANSSQTLGNATMEKCNHIFVDTGLPDLAVGLILLAGSLVLLCTCLILLVKMLNSLLKGQVAKVIQKVINTDFPAPFTWVTGYFAMVVGASMTFVVQSSSVFTSAITPLIGLGVISIERAYPLTLGSNIGTTTTAILAALASPREKLSSAFQIALCHFFFNISGILLWYPVPCTRLPIRMAKALGKRTAKYRWFAVLYLLVCFLLLPSLVFGISMAGWQVMVGVGTPFGALLAFVVLINVLQSRSPGHLPKWLQTWDFLPRWMHSLKPLDHLITRATLCCARPEPRSPPLPPRVFLEELPPATPSPRLALPAHHNATRL
Protein: E3 ubiquitin-protein ligase MGRN1 (EC 2.3.2.27) (Mahogunin RING finger protein 1) (RING-type E3 ubiquitin transferase MGRN1) (Q5XIQ4)
Organism: Rattus norvegicus (Rat)
Function: E3 ubiquitin-protein ligase. Mediates TSG101 monoubiquitination at multiple sites. Plays a role in the regulation of endosome-to-lysosome trafficking. Impairs MC1R- and MC4R-signaling by competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP production. Does not inhibit ADRB2-signaling. Does not promote MC1R ubiquitination. Acts also as a negative regulator of hedgehog signaling (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000250}. Early endosome {ECO:0000250}. Note=The endosomal localization is dependent on the interaction with TSG101. {ECO:0000250}.
Interaction partners:
- Protein smoothened
- Multiple epidermal growth factor-like domains protein 8
- Attractin
Sequence:
MGSILSRRIAGVEDIDIQANSAYRYPPKSAGNYFASHFFMGGEKFDTPHPEGYLFGENMDLNFLGSRPVQFPYVTPAPHEPVKTLRSLVNIRKDSLRLVRYKDDTDSPTEDGEKPRVLYSLEFTFDADARVAITIYCQAVEEFVNGMTVYSCKNPSLQSETVHYKRGVSQQFSLPSFKIDFSEWKDDELNFDLDRGVFPVVIQAVVDEGDVVEVTGHAHVLLAAFEKHVDGSFSVKPLKQKQIVDRVSYLLQEIYGIENKNNQETKPSDDENSDNSSECVVCLSDLRDTLILPCRHLCLCTSCADTLRYQANNCPICRLPFRALLQIRAVRKKPGALSPISFSPVLAQSVDHDEHSNSDSVPPGYEPISLLEALNGLRAVSPAIPSAPLYEEITYSGISDGLSQASCPLAGLDRIIENGIQKGKTQSKSPDSTLRSPSSPIHEEDEEKLSEDPEAPLPPSGVELVLQESSSPESFGTEEVGEPSLKQGSRVPSIDDVLQDGSPQHHGCSQPVPPADIYLPALGPESCSVGIEE
Protein: Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (MAP3K gamma protein kinase) (AtMAP3Kgamma) (Q9C5H5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mitogen-activated protein kinase (MAPK) involved in the transduction of signal between the host cell surface chitin receptor complex CERK1-LYK5 and the intracellular MAPK cascade that leads to chitin-induced immunity. Phosphorylates and activates MAPK targets (e.g. MKK4, MKK5, and possibly MKK2) when phosphorylated by PBL27 after elicitation by chitin. Required for resistance to the fungus A.brassicicola.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27679653}. Cytoplasm, cytosol {ECO:0000269|PubMed:27679653}.
Interaction partners:
- Serine/threonine-protein kinase BSK1
Sequence:
MRWLPQISFSSPSSSPSSSLKPVASYSESPDPDRNQDRDRFHRRLFRFNRGRLTRQRKLRHLTDDDVLLGERRASTSSSTFDSGLTRSPSAFTAVPRSPSAVPLPLPLPLPEVAGIRNAANARGLDDRDRDPERLISDRTSSGPPLTSVNGGFARDSRKATENSSYQDFSPRNRNGYWVNIPTMSAPTSPYMSPVPSPQRKSTGHDLPFFYLPPKSNQAWSAPDMPLDTSGLPPPAFYDITAFSTDNSPIHSPQPRSPRKQIRSPQPSRPSSPLHSVDSSAPPRDSVSSPLHPRLSTDVTNGRRDCCNVHPLPLPPGATCSSSSAASVPSPQAPLKLDSFPMNSQWKKGKLIGRGTFGSVYVASNSETGALCAMKEVELFPDDPKSAECIKQLEQEIKLLSNLQHPNIVQYFGSETVEDRFFIYLEYVHPGSINKYIRDHCGTMTESVVRNFTRHILSGLAYLHNKKTVHRDIKGANLLVDASGVVKLADFGMAKHLTGQRADLSLKGSPYWMAPELMQAVMQKDSNPDLAFAVDIWSLGCTIIEMFTGKPPWSEFEGAAAMFKVMRDSPPIPESMSPEGKDFLRLCFQRNPAERPTASMLLEHRFLKNSLQPTSPSNSDVSQLFNGMNITEPSSRREKPNFKLDQVPRARNMTSSESESGQQQQQQQYRSPDLTGTVNRLSPRSTLEAIPSPCPSQRPKPSSSDRRRTGVTSDHL
Protein: Cadherin-24 (Q86UP0)
Organism: Homo sapiens (Human)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Cadherin-24 mediate strong cell-cell adhesion.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Cadherin-12
- Catenin delta-1
- Catenin beta-1
Sequence:
MWGLVRLLLAWLGGWGCMGRLAAPARAWAGSREHPGPALLRTRRSWVWNQFFVIEEYAGPEPVLIGKLHSDVDRGEGRTKYLLTGEGAGTVFVIDEATGNIHVTKSLDREEKAQYVLLAQAVDRASNRPLEPPSEFIIKVQDINDNPPIFPLGPYHATVPEMSNVGTSVIQVTAHDADDPSYGNSAKLVYTVLDGLPFFSVDPQTGVVRTAIPNMDRETQEEFLVVIQAKDMGGHMGGLSGSTTVTVTLSDVNDNPPKFPQSLYQFSVVETAGPGTLVGRLRAQDPDLGDNALMAYSILDGEGSEAFSISTDLQGRDGLLTVRKPLDFESQRSYSFRVEATNTLIDPAYLRRGPFKDVASVRVAVQDAPEPPAFTQAAYHLTVPENKAPGTLVGQISAADLDSPASPIRYSILPHSDPERCFSIQPEEGTIHTAAPLDREARAWHNLTVLATELGWSWGPERGWVPLLVAEWSAPAAPPQRSPVGSAVGIPQDSSAQASRVQVAIQTLDENDNAPQLAEPYDTFVCDSAAPGQLIQVIRALDRDEVGNSSHVSFQGPLGPDANFTVQDNRDGSASLLLPSRPAPPRHAPYLVPIELWDWGQPALSSTATVTVSVCRCQPDGSVASCWPEAHLSAAGLSTGALLAIITCVGALLALVVLFVALRRQKQEALMVLEEEDVRENIITYDDEGGGEEDTEAFDITALQNPDGAAPPAPGPPARRDVLPRARVSRQPRPPGPADVAQLLALRLREADEDPGVPPYDSVQVYGYEGRGSSCGSLSSLGSGSEAGGAPGPAEPLDDWGPLFRTLAELYGAKEPPAP
Protein: Homeobox protein Six3 (O73708)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MVFRSPLELYPSHFFLPNFADRPLLLASSAPSTRSPEDLSMFQLPTLNFSPEQVASVCETLEETGDIERLGRFLWSLPVAPGACEAINKHESILRARAVVAFHTGNFRDLYHILENHKFTKDSHGKLQAMWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRSLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHQAIGQNGMRSLSESGCAPRSSAESPSTAASPTTSVSSMTERVDTGTSILSVTSSDSECDV