wanglab/gogpt-training-data huggingface dataset:
Protein: Junctophilin-4 (JP-4) (Junctophilin-like 1 protein) (Q96JJ6)
Organism: Homo sapiens (Human)
Function: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH4 is brain-specific and appears to have an active role in certain neurons involved in motor coordination and memory (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Localized predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Triadin
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Aspartyl/asparaginyl beta-hydroxylase
- Ryanodine receptor 1
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Synaptophysin-like protein 2
- Stromal interaction molecule 1
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Junctophilin-3
Sequence:
MSPGGKFDFDDGGCYVGGWEAGRAHGYGVCTGPGAQGEYSGCWAHGFESLGVFTGPGGHSYQGHWQQGKREGLGVERKSRWTYRGEWLGGLKGRSGVWESVSGLRYAGLWKDGFQDGYGTETYSDGGTYQGQWQAGKRHGYGVRQSVPYHQAALLRSPRRTSLDSGHSDPPTPPPPLPLPGDEGGSPASGSRGGFVLAGPGDADGASSRKRTPAAGGFFRRSLLLSGLRAGGRRSSLGSKRGSLRSEVSSEVGSTGPPGSEASGPPAAAPPALIEGSATEVYAGEWRADRRSGFGVSQRSNGLRYEGEWLGNRRHGYGRTTRPDGSREEGKYKRNRLVHGGRVRSLLPLALRRGKVKEKVDRAVEGARRAVSAARQRQEIAAARAADALLKAVAASSVAEKAVEAARMAKLIAQDLQPMLEAPGRRPRQDSEGSDTEPLDEDSPGVYENGLTPSEGSPELPSSPASSRQPWRPPACRSPLPPGGDQGPFSSPKAWPEEWGGAGAQAEELAGYEAEDEAGMQGPGPRDGSPLLGGCSDSSGSLREEEGEDEEPLPPLRAPAGTEPEPIAMLVLRGSSSRGPDAGCLTEELGEPAATERPAQPGAANPLVVGAVALLDLSLAFLFSQLLT
Protein: Galanin receptor type 2 (GAL2-R) (GALR-2) (O43603)
Organism: Homo sapiens (Human)
Function: Receptor for the hormone galanin and GALP. Receptor for the hormone spexin-1. The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Galanin peptides
- Spexin
- Galanin receptor type 1
- Galanin-like peptide
- Galanin receptor type 3
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Free fatty acid receptor 1
- Ligand-gated cation channel ZACN
- Guanine nucleotide-binding protein G
Sequence:
MNVSGCPGAGNASQAGGGGGWHPEAVIVPLLFALIFLVGTVGNTLVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDGWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLSLLFSGPYLSYYRQSQLANLTVCHPAWSAPRRRAMDICTFVFSYLLPVLVLGLTYARTLRYLWRAVDPVAAGSGARRAKRKVTRMILIVAALFCLCWMPHHALILCVWFGQFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRTICAGLLGRAPGRASGRVCAAARGTHSGSVLERESSDLLHMSEAAGALRPCPGASQPCILEPCPGPSWQGPKAGDSILTVDVA
Protein: ALS2 C-terminal-like protein (Q60I27)
Organism: Homo sapiens (Human)
Function: Acts as a guanine nucleotide exchange factor (GEF) for Rab5 GTPase. Regulates the ALS2-mediated endosome dynamics.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15388334, ECO:0000269|PubMed:17239822}. Note=Distributed onto the vesicular compartments in the cytoplasm with strong punctated staining. Colocalizes with RAB5A onto the vesicular/membranous compartments in the cytoplasm, particularly to the leading edges of the cells.
Interaction partners:
- Ras-related protein Rab-5A
- Early endosome antigen 1
Sequence:
MCNPEEAALLRLEEVFSATLAHVNSLVLQPLLPAAPDPSDPWGRECLRLLQQLHKSSQQLWEVTEESLHSLQERLRYPDSTGLESLLLLRGADRVLQAHIEYIESYTSCMVVQAFQKAAKRRSEYWRGQRKALRQLLSGVSSEGSVGASLGQALHQPLAHHVQQYVLLLLSLGDTIGEHHPTRELVVNAVTLFGNLQSFMKQELDQAVATQALWHTLRGRLRDVLCTPAHRLLQDSQDVPVTVAPLRAERVLLFDDALVLLQGHNVHTFDLKLVWVDPGQDGCTFHLLTPEEEFSFCAKDSQGQAVWQWKVTWAVHQALHGKKDFPVLGAGLEPSQPPDCRCAEYTFQAEGRLCQATYEGEWCRGRPHGKGTLKWPDGRNHVGNFCQGLEHGFGIRLLPQASEDKFDCYKCHWREGSMCGYGICEYSTDEVYKGYFQEGLRHGFGVLESGPQAPQPFRYTGHWERGQRSGYGIEEDGDRGERYIGMWQAGQRHGPGVMVTQAGVCYQGTFQADKTVGPGILLSEDDSLYEGTFTRDLTLMGKGKVTFPNGFTLEGSFGSGAGRGLHTQGVLDTAALPPDPSSTCKRQLGVGAFPVESRWQGVYSPFRDFVCAGCPRDLQEALLGFDVQSSRELRRSQDYLSCERTHPEDSVGSMEDILEELLQHREPKALQLYLRKALSNSLHPLGKLLRTLMLTFQATYAGVGANKHLQELAQEEVKQHAQELWAAYRGLLRVALERKGQALEEDEDTETRDLQVHGLVLPLMLPSFYSELFTLYLLLHEREDSFYSQGIANLSLFPDTQLLEFLDVQKHLWPLKDLTLTSNQRYSLVRDKCFLSATECLQKIMTTVDPREKLEVLERTYGEIEGTVSRVLGREYKLPMDDLLPLLIYVVSRARIQHLGAEIHLIRDMMDPNHTGGLYDFLLTALESCYEHIQKEDMRLHRLPGHWHSRELW
Protein: Cytochrome P450 CYP72A616 (PpCYP72A616) (EC 1.14.14.-) (A0A517FNC4)
Organism: Paris polyphylla (Daiswa polyphylla)
Function: Involved in the biosynthesis of spiroketal steroid and saponin natural products from cholesterol such as diosgenin and analogs (e.g. furostanol and spirostanol), plant defense compounds used as main precursors for the industrial production of steroid hormones. During the 5,6-spiroketalization of cholesterol, may catalyze the 27-monohydroxylation of furostanol-type steroid to an intermediate product that undergoes a stereospecific formation of the terminal heterocycle to yield diosgenin.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDSRVLGALAALLAAAAAWVMRAAAEWLWWRPRRLERSLRSQGVDGNLYRFLNGDLKETVRLTKEARAQPISPPSHRFLHRINPLLLRAISHHGKFALTWIGPTPRVSIMDPELVREVLSNKFGHFAKPKAAPIVKLLATGLANYEGEKWVRHRRIINPAFHLEKLKRMLPAFFSCCSELIGRWESLVGCDESREVDVWPELQNLTGDVISRTAFGSSYAEGRRIFQLQSEQAELLIQAVQTVYIPGYRFLPTPKNIRRTKIDKEVRALLRSIIEKRENAMKMGDVHDDLLGLLMEYNLKESEHFNSKNIGMTTEDVIEECKLFYFAGQETTSVLLTWTMILLGMHPSWQDRAREEVSQVFGKNKPDFDGLSRLKTVTMILYEVLRLYPPIIFLTRRTYKPMMLGGITFPPEVQLALPIIFIHHDPEFWGEDAEEFNPDRFADGVSKASKNQMAFFPFGWGPRICIGQGFAMLEAKMGLSMILQRFSFELSPNYSHAPHTKITLQPQHGAQMVLHRL
Protein: Fc receptor-like protein 6 (FcR-like protein 6) (FcRL6) (A1YIY0)
Organism: Mus musculus (Mouse)
Function: Acts as a MHC class II receptor. When stimulated on its own, does not play a role in cytokine production or the release of cytotoxic granules by NK cells and cytotoxic CD8(+) T cells. Does not act as an Fc receptor.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6DN72}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Fc receptor-like A
Sequence:
MLLWMVLLLCESMAEAQELFPNPELTEFTNSETMDVILKCTIKVDPKNPTLQLFYTFYKNNHVIQDRSPHSVFSAEAKEENSGLYQCMVDTEDGLIQKKSGYLDIQFWTPVSHPVLTLQHEATNLAVGDKVEFLCEAHQGSLPIFYSFYINGEILGKPLAPSGRAASLLASVKAEWSTKNYSCEAKNNISREISELKKFPLVVSGTAWIKSNMLPIWLPASLLGGMVIAAVVLMYFFKPCKKHARPETPTLKEPDSFLYVSVDNQRYK
Protein: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase 2) (GlcAT-D) (UDP-glucuronosyltransferase S) (GlcAT-S) (Glucuronosyltransferase S) (Q9Z137)
Organism: Rattus norvegicus (Rat)
Function: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. Substrates include asialo-orosomucoid (ASOR), paragloboside (lacto-N-neotetraosylceramide), Gal-beta-1,4-GlcNAc-beta-1,3-Gal-beta-1,4-Glc-pyridylamine and Gal-beta-1,3-GlcNAc-beta-1,3-Gal-beta-1,4-Glc-pyridylamine.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Carbohydrate sulfotransferase 10
- Beta-1,4-galactosyltransferase
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
- Beta-1,4-galactosyltransferase
- Beta-1,4-galactosyltransferase 3
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 2B37
- UDP-glucuronosyltransferase
- Hematopoietic prostaglandin D synthase
- Solute carrier family 35 member A2
Sequence:
MKSALCNRFFILLPWILIVIIMLDVDPRRPAPQLTSRPYFSPHTVGCGGSRVPLRRSSPGRDAAEKRNESRPQLQPEPRLPTIYAITPTYSRPVQKAELTRLANTFRQVAQLHWILVEDRATRSELVSSFLARAGLPNTHLHVPTPRRYKRPWLPRATEQRNAGLAWLRQRHQHQSAQPGVLFFADDDNTYSLELFQEMRTTRKVSVWPVGLVGGRRYERPLVKNGKVVGWYTGWREDRPFAIDMAGFAVSLQVILSNPKAVFKRRGSQPGMQESDFLKQITTVDELEPKANNCTKVLVWHTRTEKVNLANEPKYHMDTVNIEV
Protein: 5'-AMP-activated protein kinase catalytic subunit alpha-1 (EC 2.7.11.1) (EC 2.7.11.26) (EC 2.7.11.31) (Acetyl-CoA carboxylase kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (Tau-protein kinase PRKAA1) (A0A060VX13)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- AMP-activated protein kinase glycogen-binding domain-containing protein
- 5'-AMP-activated protein kinase subunit beta-1
- Protein kinase, AMP-activated, beta 1 non-catalytic subunit, b
- CBS domain-containing protein
- CBS domain-containing protein
- 5'-AMP-activated protein kinase subunit gamma-1
- 5'-AMP-activated protein kinase subunit gamma-1
- Association with the SNF1 complex
- Association with the SNF1 complex
- calcium/calmodulin-dependent protein kinase
Sequence:
MATTDKQKHEGRVKIGHYILGDTLGVGTFGKVKVGQHELTKHQVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPTDIFMVMEYVSGGELFDYICKNGKLEEKESRRLFQQIISAVDYCHRHMVVHRDLKPENVLLDAQMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFFTPQYLNPSVAALLKHMLQVDPMKRATIKEIREDEWFKDELPKYLFPEDPCYSNNMIDDEALKEVCEKFECTEEEILTCLYSRNHHDPLAVAYHLIIDNRRIMSEAKDFYLASSPPDSFLDDQHLTAAAGLKPHPERMQPFLAGETSPRPRHTLDELNPLKSKHQGVRRAKWHLGIRSQSRPNDIMSEVCRAMKQLDYEWKVVNPYYLRVKRKNPVTGMQTKMSLQLYQVDGRTYLLDFRSIDNDMLEAKSGTATPHQSGSVGNYRTALKNEAAAAAEGGSLASSLTSSVDSTGGDLAPMTAVPRPGSHTIEFFEMCANLIKLLAR
Protein: Transcriptional regulator (B2KUA9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR001705}.
Interaction partners:
Sequence:
MLQACSPSHDWFCDSEPLLFDDEFSMSLMKDLQCIPTPPQSPPMKPGLAKNMSTVDQLELVSELLMEDTDFLQLDWNFTGPASSADDPLSEDCLWRPDGDKQTEDKLSAVLSTSPLLSDIDTQIFAEIAGSTLDCHTAALACQALESEDSPLDSQEQIESTSDYGSLSTGGESSTSDSEEEIDVVTVRRSSTLTRSQHQQQLEDSRREQQRALKRYHFEIQQQHNYAAPRPASPPPPPSPPLKRTRGSGDSQRGLQIPGRSRSLVVRQPVDTEDEEERRRTHNVMERQRRNELKNCFLRLRDNVPELSNNDKASKVVILKRAKESIRNLESENQRLTSKRDKLRERQEQLKARLEQLKRH
Protein: Endophilin-A homolog (Endophilin-1 homolog) (Uncoordinated protein 57) (B1V8A0)
Organism: Caenorhabditis elegans
Function: Involved in synaptic vesicle (SV) recycling in neurons probably by regulating clathrin-mediated endocytosis. By controlling SV endocytosis, regulates the rate of excitatory postsynaptic currents (EPSCs) at neuromuscular junctions and thus locomotion. In a similar manner, involved in necrotic neuronal cell death induced by abnormal hyperactivation of ion channels. Plays a minor role in responses to mechanical stimuli. Plays a minor role in unc-26/synaptojanin localization to synapses.
Subcellular location: Synapse {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:18094048, ECO:0000269|PubMed:21029864}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}. Membrane {ECO:0000305|PubMed:21029864}; Peripheral membrane protein {ECO:0000305|PubMed:21029864}. Note=Localizes to neuromuscular junctions. Co-localizes with snb-1/synaptobrevin and rab-3 but not dyn-1 and apt-4 (PubMed:14622579, PubMed:21029864). Exocytosis promotes dissociation from synaptic vesicles (PubMed:21029864). {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}.
Interaction partners:
- Synaptojanin
- Dynamin
- SH3 domain-containing GRB2-like protein B1
- Receptor tyrosine-protein kinase let-23
- Synaptotagmin-1
- Phosphatidylinositol-binding clathrin assembly protein unc-11
- Synaptobrevin-1
- C2 domain-containing protein
- Putative stoned B-like protein
- Mitogen-activated protein kinase mpk-1
Sequence:
MSLSGLRKQFNKANQYLSETMGAAEPTKLDDVFNEMEKNVDTTYNLITDLVAGTNEYLQPNPATRAKMATQVALSKVRGTTKTSPYPQTEGMLADVMQKYGQQLGDNSDLGKSLNDAAETYRQMADIKYQMEDNVKQNFLDPLTHLQNNELKDVNHHRTKLKGRRLDYDCKKRQQRRDDEMIQAEEKLEESKRLAEMSMFNVLSNDVEQISQLRALIEAQLDFHRQTAQCLENLQQQLGHRIKDAAARPREEHVPLSVLANESRTPRSSFRSPAPSDMSHNSTAAAAFKMPPQNGGGITQAPPSYQGPPPGGLPPPLSQQQKPQCRALFDFDAQSEGELDFKEGTLIELVSQIDENWYEGRVNGKTGLFPVTYVQVLVPLK
Protein: C-type lectin domain-containing protein 38 (O45824)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000303|PubMed:18434533}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Nematode cuticle collagen N-terminal domain-containing protein
Sequence:
MAIFYDDPLERLNQPIKTKSYRKKQVVQRVHVFIFDNWKLILLGILNLIFLIIAIVFAILFFVGSADCAQLPDYTTSPASQLTTSAISSRTSEVQTNAITTTQGTPSNKTSTTTPSTSKVICASGFTLVGTKCGKLVSSNQPRTEADSICKGYGGSTLFSVRNEQETRDMLDFVKDSNIDFLWTGLVCNQTARTSCIWDVKSGTTADYNNFADGFPNVVYGYCIYFIVTGNSAGQWGSEQCSQLMNFVCELPTTIRDPDCKYNYNKNCYIRFDITLTIPQAQRFCNEKGADLVSIHSANENRFILTIYDIHGQILLGGLAPAVDFIVWLDGSPTTYSNLLYFYDTRSCVLMTVARGGPYDGDWYTMNCNVQEFFLCKRAIDF
Protein: Uncharacterized protein (Q38BQ2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAAGDGLLGNQSLVNGGYVTAHNMRCRGTFSMLYHEPFFAAMSVLGAVHVLLAHYSLMLLPPLFSYAPFGMFFFRNTLWMAVFGYPVQGGKPELTILQQSGIGRSFSDTIRGTWRFRDRDAASLFALTTFMLLQLRAWALMGFEPFLPFLSTSNSVVKLNASLNTTDKDLHDGGSRAVNFMQPVMCFLTLFLLVSVVLCKLLSMRSVYKPEFGSLVTSPVWNIIKHRAYNWLHPRIIFMERHLVLPLRAFYCYEKDVVMERYDGYSAVMDCPVAASNHAWFFIAVFCFMVLQWLIFISGWRQARVMLKCPRSDSLGEYISSSAWNLLVHALPCRDPTTIDVTGKSYFWVFMFRYIIPTTTNRLGVWLLHYSLIAAIISTYCFYRQLVAAAIGATRMELANRTATSGNGGLVSIFPPSFVPFKDTNSAAATWTPPEGHCEGMLTIVDDLAAGNVAHRKVGSHCIYADSRFSILNIIYFLLGISGRRWRGAVAVSSFNSPISSVSLLEGPLA
Protein: PH and SEC7 domain-containing protein 2 isoform X2 (Pleckstrin and Sec7 domain-containing 2) (A0A0R4IAG2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004632}.
Interaction partners:
Sequence:
MSQEGQDDPLHTPAETPEGQEEHLENCNGTETETEEPDDGDTENNRNTEEEEEEEEEKVTLDQDDGRNGEIESSCLDPGTENGDICEGGDTQRAEKDSSVTICSLRFENGTEDDSEEQDDEEVIPHEGNLDAFSSTFELSVEEADAEVEDEEREETETRNQDSFSSTFESIVERVAKATVVEEEEEEEEGEEEFDRTKESQDGFSSTFERIVESELLRGGTCYSSLDSLDVLSLTDETDSCVSFEAPLTPLIQQRALMGPEPPELELETVQEGAEGEGEFGTETARDEASSASPLRTTIPGSRSENVLSQPAQWSIPNGFHIELPGNGQSAGMMPNSISDANLTDVLCDSDSELGSVDTLERGSTDTLANGCRVDADAAKRLAKRLFYLEGFKRCDVARHLGKNNEFSQLVASEYLSFFDFTGLSLDRALRNFLKAFPLMGETQERERVLVHFSKRFCHCNPETLTSEDGAHTLTCALMLLNTDLHGHNIGKKMSCQQFISNLDGLDDGKDFPKELLKVLYNSIKNEKLEWAIEEEELRKSLSELVEEQCEAGGKRVVRVTDGSNPFIGIPLLLNATTYKHGVLTRKSHADMDGKRTPRGRRGWKKFYAVLKGMILYLQKDEYKPDKDLSEVDLKNAVRVHHALATRACDYSKRQNVLKLKTSDWRVFLLQAPSEEEMMSWIFRINLVAALFSAPAFPAAIGSMKKFCRPLLPSSTTRLNQEEQLKSHENKLKQVSVELEEHKRSPPELTPKSKESEEYRIKEHYLTYEKCRYETYISLLQAKIRAGSDDLDKIEASLFSGEAKEGHLRKTQSSPSISQGQGVNGRAAHKHIPEHNS
Protein: GH07711p (GM06266p) (Sds22) (Q9VEK8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- E3 ubiquitin-protein ligase PPP1R11
- E3 ubiquitin-protein ligase PPP1R11
- Serine/threonine-protein phosphatase alpha-2 isoform
- Serine/threonine-protein phosphatase beta isoform
- Serine/threonine-protein phosphatase alpha-1 isoform
- Serine/threonine-protein phosphatase
- Phosphatase Herzog
- Aurora kinase B
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase alpha-3 isoform
Sequence:
MGDADRAMNEPEAAKTVSGIQVIPAEDVASIEDIITIDPDCYELDLNHRRIEKLENFEPLTRIERLFLRWNLIKKIENLSSLKTLIELELYDNQITKIENLDDLPHLEVLDISFNRLTKIENLDKLVKLEKVYFVSNRITQIENLDMLTNLTMLELGDNKLKKIENIEMLVNLRQLFLGKNKIAKIENLDTLVNLEILSLQANRIVKIENLEKLANLRELYVSENGVETIENLSENTKLETLDLAKNRLKGIANLEKLELLEELWLNHNGVDDWKDIELLKVNKALQTIYLEYNPLAKDVRYRSKLRDILPQLQKIDATLCKVPGT
Protein: Cell division control protein 12 (Septin) (P32468)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.
Subcellular location: Membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}. Bud neck {ECO:0000269|PubMed:14562095}. Note=Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate.
Interaction partners:
- Seventh homolog of septin 1
- Cell division control protein 10
- Cell division control protein 11
- Cell division control protein 3
- Serine/threonine-protein kinase GIN4
- Probable serine/threonine-protein kinase KCC4
- Probable serine/threonine-protein kinase HSL1
- Bud neck protein 5
- Sporulation-regulated protein 28
- Serine/threonine-protein kinase CLA4
Sequence:
MSAATATAAPVPPPVGISNLPNQRYKIVNEEGGTFTVMLCGESGLGKTTFINTLFQTVLKRADGQQHRQEPIRKTVEIDITRALLEEKHFELRVNVIDTPGFGDNVNNNKAWQPLVDFIDDQHDSYMRQEQQPYRTKKFDLRVHAVLYFIRPTGHGLKPIDIETMKRLSTRANLIPVIAKADTLTAQELQQFKSRIRQVIEAQEIRIFTPPLDADSKEDAKSGSNPDSAAVEHARQLIEAMPFAIVGSEKKFDNGQGTQVVARKYPWGLVEIENDSHCDFRKLRALLLRTYLLDLISTTQEMHYETYRRLRLEGHENTGEGNEDFTLPAIAPARKLSHNPRYKEEENALKKYFTDQVKAEEQRFRQWEQNIVNERIRLNGDLEEIQGKVKKLEEQVKSLQVKKSHLK
Protein: CD276 antigen (4Ig-B7-H3) (B7 homolog 3) (B7-H3) (Costimulatory molecule) (CD antigen CD276) (Q5ZPR3)
Organism: Homo sapiens (Human)
Function: May participate in the regulation of T-cell-mediated immune response. May play a protective role in tumor cells by inhibiting natural-killer mediated cell lysis as well as a role of marker for detection of neuroblastoma cells. May be involved in the development of acute and chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. Could also play a key role in providing the placenta and fetus with a suitable immunological environment throughout pregnancy. Both isoform 1 and isoform 2 appear to be redundant in their ability to modulate CD4 T-cell responses. Isoform 2 is shown to enhance the induction of cytotoxic T-cells and selectively stimulates interferon gamma production in the presence of T-cell receptor signaling.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- T-cell-specific surface glycoprotein CD28
- T-lymphocyte activation antigen CD86
- T-lymphocyte activation antigen CD80
- Cytotoxic T-lymphocyte protein 4
- Trem-like transcript 2 protein
- CD40 ligand
- Tumor necrosis factor receptor superfamily member 9
- Inducible T-cell costimulator
- T-cell surface glycoprotein CD4
- T-cell surface glycoprotein CD8 alpha chain
Sequence:
MLRRRGSPGMGVHVGAALGALWFCLTGALEVQVPEDPVVALVGTDATLCCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFAEGQDQGSAYANRTALFPDLLAQGNASLRLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPYSKPSMTLEPNKDLRPGDTVTITCSSYQGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSILRVVLGANGTYSCLVRNPVLQQDAHSSVTITPQRSPTGAVEVQVPEDPVVALVGTDATLRCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFTEGRDQGSAYANRTALFPDLLAQGNASLRLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPYSKPSMTLEPNKDLRPGDTVTITCSSYRGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSVLRVVLGANGTYSCLVRNPVLQQDAHGSVTITGQPMTFPPEALWVTVGLSVCLIALLVALAFVCWRKIKQSCEEENAGAEDQDGEGEGSKTALQPLKHSDSKEDDGQEIA
Protein: Topoisomerase I damage affected protein 4 (P47153)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized ABC transporter ATP-binding protein/permease YOL075C
- Probable transcription factor TDA9
Sequence:
MNANSTTTAIGLTSPFEKLSFFPHSSNLILAHLHEIIFSFVFYQLAFSVVAPFLNKVVFRKHYTTIRDPLLKIDFNVHTVSMIQAVVSNTVLLPTLTTPMHYNVVTYTDSYSSMVSSLSAGYFIWDLTMCVRYFKLYGLEFTGHAIGSVYVMLLSLRPFCQPWIGRFLIYEASTPFVNINWFIMQCNAKSKNSIPLWFNVVNGLLLMTVFFVVRICWGSIASALLFRQMWKVRDELPKFSAVTMMSLNIFMNLLNVLWFKKMIRIAKKLAKPAPTSKLD
Protein: Protein REDUCED WALL ACETYLATION 2 (EC 2.3.1.-) (Q0WW17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable O-acetyltransferase involved in the acetylation of cell wall polymers (both pectic and nonpectic polysaccharides) and of xylan during secondary wall biosynthesis. Catalyzes the O-acetylation of xyloglucan.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:21673009}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21212300}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Xyloglucan O-acetyltransferase 1
- Xylan O-acetyltransferase 1
- Protein PMR5
- xyloglucan O-acetyltransferase 2
- Protein trichome birefringence-like 31
- Protein trichome birefringence
- Protein trichome birefringence-like 3
- Protein trichome birefringence-like 35
- Protein trichome birefringence-like 32
- Protein trichome birefringence-like 2
Sequence:
MASSSPVTPGLMSVVFGIVPVIVAWLYSEYLHYAKYSVSAKTRHSDVNLVEIAKDFVKEDDKALLIEDGGGLQSASPRAKGPTTHSPLIRFVLLDESFLVENRLTLRAIIEFAVLMVYFYICDRTDVFNSSKKSYNRDLFLFLYFLLIIVSAITSFTIHTDKSPFSGKAIMYLNRHQTEEWKGWMQVLFLMYHYFAAAEYYNAIRVFIACYVWMTGFGNFSYYYIRKDFSLARFAQMMWRLNFLVIFSCIVLNNSYMLYYICPMHTLFTLMVYGALGIMSKYNEMGSVIAAKFFACFVVVIIVWEIPGVFEWIWSPFTLLMGYNDPAKPQLPLLHEWHFRSGLDRYIWIIGMLYAYYHPTVESWMDKLEEAEMKFRVAIKTSVALIALTVGYFWYEYIYKMDKLTYNKYHPYTSWIPITVYICLRNITQSFRGYSLTLLAWLGKITLETYISQFHIWLRSGVPDGQPKLLLSLVPDYPLLNFMLTTSIYVAISYRLFELTNTLKTAFIPTKDDKRLVYNTISALIICTCLYFFSFILITIPQKLV
Protein: Mas-related G-protein coupled receptor member A4 (RF-amide G-protein coupled receptor) (Q91WW2)
Organism: Mus musculus (Mouse)
Function: Orphan receptor. May be a receptor for RFamide-family neuropeptides such as NPFF and NPAF, which are analgesic in vivo. May regulate nociceptor function and/or development, including the sensation or modulation of pain.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11551509}; Multi-pass membrane protein {ECO:0000269|PubMed:11551509}.
Interaction partners:
Sequence:
MAPTTTNPMNETIPGSIDIETLIPNLMIIIFGLVGLTGNVILFWLLGFHLHRNAFLVYILNLALADFLFLLCHIINSTMLLLKVHLPNNILNHCFDIIMTVLYITGLSMLSAISTERCLSVLCPIWYRCRRPEHTSTVLCAVIWFLPLLICILNGYFCHFFGPKYVIDSVCLATNFFIRTYPMFLFIVLCLSTLALLARLFCGAGKTKFTRLFVTIMLTVLVFLLCGLPLGFFWFLVPWINRDFSVLDYILFQTSLVLTSVNSCANPIIYFFVGSFRHRLKHKTLKMVLQSALQDTPETPENMVEMSRSKAEP
Protein: Strn4 protein (B5DF70)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLEYALKQERAKYHKLKFGTDLNQGEKKADLSEQVSNGPVESVTLDNSPLVWKEGRQLLRQYLEEVGYTDTILDMRSKRVRSLLGRSLELNGAGEPVEGAPRASPGPGGLSGGESLLVKQIEEQIKRNAAGKDGKERLGGSVLEQIPFLQNCEDEDSDEDDELDSVQHKKQRVRLPSKALVPEMEDEDEEDDSEDAINEFDFLGSGEDGEGSPDPRRCASEGNPHELESRRVKLQGILADLRDVDGLPPKVTVPPPGTPQPRPHEDVFIMDTIGGGEVSLGDLADLTVTNDNDLSCDLSDSKDAFKKTWNPKFTLRSHYDGIRSLAFHHSQSALLTASEDGTLKLWNLQKAVTAKKNAALDVEPIHAFRAHRGPVLAVTMGSNSEYCYSGGADARIHSWKIPDLNMDPYDGYDPSVLSCVLEGHGDAVWGLAFSPTSQRLASCSADGTIRIWDPSSSGSSCLCTFPMAGEHGIPTSVAFTSTEPAHVVASFRSGDTVLYDLEAGGALLTLESRGSSGPTQINQVVSHPNQPLTITAHDDRGIRFLDNRTGKSVHSMVAHLDAVTCLAVDPNGVFLMSGSHDCSLRLWSLDNKTCVQEITAHRKKHEEAIHAVACHPSKALIASAGADALAKVFV
Protein: diphthine methyl ester synthase (EC 2.1.1.314) (Q8IN02)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 2-
- Eukaryotic translation elongation factor 2
- 2-
- Diphthamide biosynthesis protein 3
- Diphthamide biosynthesis 4, isoform A
- GPI mannosyltransferase 1
- RNA 3'-terminal phosphate cyclase
Sequence:
MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSILGCSLEDMQEFYGRPLLLADRDLVEQGADEILAGAGESDVALLVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAVGCCGLQLYKFGETVSIPYWDETWKPDSFYDKIKLNRLHNMHTLCLLDIKVKEPTPESLMRKRKEYMPPRFMTVAEAAHQLLSIVEKKDSLEKNTVLNEQSLCVGLARVGQESQQIAVGTLLEMRSTDLGGPLHSLIIPAKEMHPLEVEFLQQYAPSIKLDDYNH