wanglab/gogpt-training-data huggingface dataset:
Protein: Caveolae-associated protein 4 (Muscle-related coiled-coil protein) (Muscle-restricted coiled-coil protein) (B1PRL5)
Organism: Rattus norvegicus (Rat)
Function: Modulates the morphology of formed caveolae in cardiomyocytes, but is not required for caveolar formation. Facilitates the recruitment of MAPK1/3 to caveolae within cardiomyocytes and regulates alpha-1 adrenergic receptor-induced hypertrophic responses in cardiomyocytes through MAPK1/3 activation. Contributes to proper membrane localization and stabilization of caveolin-3 (CAV3) in cardiomyocytes (By similarity). Induces RHOA activation and activates NPPA transcription and myofibrillar organization through the Rho/ROCK signaling pathway.
Subcellular location: Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:A2AMM0}. Cytoplasm {ECO:0000250|UniProtKB:A2AMM0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:A2AMM0}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:A2AMM0}. Membrane, caveola {ECO:0000269|PubMed:24567387}. Cell membrane {ECO:0000250|UniProtKB:A2AMM0}. Note=In cardiomyocytes, accumulates in the Z-line of the sarcomere. In vascular smooth muscle cells, detected diffusely throughout the cytoplasm. Localizes in the caveolae in a caveolin-dependent manner. {ECO:0000250|UniProtKB:A2AMM0}.
Interaction partners:
Sequence:
MEHNGSASNAGKIHQNRLSSVTEDEDQDAALTIVTVLDRVATVVDSVQASQKRIEERHREMGNAIKSVQIDLLKLSQSHSNTGYVVNKLFEKTRKVSAHIKDVKARVEKQQVRVTKVETKQEEIMKKNKFRVVIFQEDVPCPASLSVVKDRSLPENEEEAEEVFDPPIDLSSDEEYYVEESRSARLRKSGKEHIDHIKKAFSKENMQKTRQNFDKKVSGIRTRIVTPERRERLRQSGERLRQSGERLRQSGERFKKSISNATPSKEAFKIRSLRKPKDPKAEGQEVDRGMGVDIISGSLALGPIHEFHSDGFSETEKEVTKVGYIPQEGGDPPTPEPLKVTFKPQVRVEDDESLLLELKQSS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q803Z0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSDNGEVEDKPPAPPMRNTSTMIGSSGKDSGPLNHGSKPLPPNPEDKRRKEGFIRSILTGGGDKTNKKKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETSNNQKYMSFTDKGVENFNSSSAVVPKTVSETPAVATVSEDEDEEEDEATPPPVIAPRPENTKSIYTRSVIEPLPPPLSTKDAATSPITNAAADGGSSSNAPSSNTNTTNTTNTTNTTNTTSTSAASSTNAPSTPQTTDKSRKKKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHCNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAVFRDFLNRCLEMDVEKRGSAKELLQHQFLKVAKPLSSLTPLIIAAKEAAKNNR
Protein: ATP-binding cassette, sub-family C member 8 (A0A1B0GT49)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPLAFCGTENHSAAYRVDQGVLNNGCFVDALNVVPHVFLLFITFPILFIGWGSQSSKVHIHHSTWLHFPGHNLRWILTFMLLFVLVCEIAEGILSDGKAK
Protein: Phosphomevalonate kinase (PMKase) (EC 2.7.4.2) (Q9D1G2)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible ATP-dependent phosphorylation of mevalonate 5-phosphate to produce mevalonate diphosphate and ADP, a key step in the mevalonic acid mediated biosynthesis of isopentenyl diphosphate and other polyisoprenoid metabolites.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15126}.
Interaction partners:
- Mevalonate kinase
- Diphosphomevalonate decarboxylase
- Isopentenyl-diphosphate Delta-isomerase 1
- Farnesyl pyrophosphate synthase
- Lanosterol synthase
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Squalene monooxygenase
- Squalene synthase
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
Sequence:
MAPLGASPRLVLLFSGKRKSGKDFVTERLKSRLGGNICALLRLSGPLKEEYAREHGLDFQRLLDASTYKETYRRDMICWGEQKRQADPGFFCRKIVEGVSQPIWLVSDTRRTSDIQWFQEAYGAVIQTVRVVASEQSRQQRGWVFTPGVDDAESECGLDNFGNFDWVIENHGDEQCLEDQLEHLLGFIQAKL
Protein: Protocadherin domain-containing protein (Q9CVI3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MSDAPGDSPRIHLPLNYPPGSPDLGRHYRSNSPLPSIQLQPQSPSASKKHQVVQDLPPANTFVGTGDTTSTGSEQYSDYSYRTNPPKYPSKQVGQPFRLSTPQPPPHPYHGAIWTEVWE
Protein: V-type proton ATPase subunit H (Q38CG7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- V-type proton ATPase subunit C
- Vacuolar proton pump subunit B
- V-type proton ATPase subunit a
- V-type proton ATPase subunit F
- 
- V-type ATPase, C subunit, putative
- V-type proton ATPase subunit
- Vacuolar ATP synthase subunit D, putative
- ATP synthase, putative
- H
Sequence:
MSSTPEVADALFHVRKTGFVDETMTQVLEQLFDCPQHGRVLETYMRGRHEDICMVLIKTLATTHNKSTLGVLLRLFADLARSSTVMGKTLGLCSSVLVDQEDPVQMFLYLATTHSRDRMISDPALYLAATTLRYADPKLNEESLERFFAIVNESLSVNPLQVEAVSFTVHNCAIMAHAKALRHYFFDNKLVQYFPRLLTDTIGDDAASLVQLTYEVLVVTWLLSYEVDGVVSLQEHKMLPHIHRVIQRMQKEKCIRVALMVLWNFVQAERQYMDAVTNPSDATWVSDEIFKLARVNGGKGPSFIAEMVGVGMLKTLTQLARRKFGDEDISELIQDLLNVLENSMETLTSFSEYRGEVLSGSLEWTPVHTCAKFWQSNIMQFEKNGYEVLEALGNIIMNSTNSLTLAVACHDIGEIVRHHPTGRALLQLPQLEGVMARVMELMSHETPEVAKNALLSVQKIMVQRWECI
Protein: Aldehyde dehydrogenase family 7 member B4 (EC 1.2.1.3) (Antiquitin-1) (Turgor-responsive ALDH) (Q9SYG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Alpha-aminoadipic semialdehyde synthase
- Alanine--glyoxylate aminotransferase 2 homolog 2, mitochondrial
- Alanine--glyoxylate aminotransferase 2 homolog 3, mitochondrial
- Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial
- Choline monooxygenase, chloroplastic
- Acetyl-coenzyme A synthetase, chloroplastic/glyoxysomal
- Beta-ureidopropionase
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
- Aldehyde dehydrogenase family 3 member F1
Sequence:
MGSANNEYEFLSEIGLTSHNLGSYVAGKWQANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINYGNELPLAQGINFG
Protein: ADCYAP receptor type I (E9PFU5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAGVVHVSLAALLLLPMAPAMHSDCIFKKEQAMCLEKIQRANELMGFNDSSPGCPGMWDNITCWKPAHVGEMVLVSCPELFRIFNPDQVWETETIGESDFGDSNSLDLSDMGVVSRNCTEDGWSEPFPHYFDACGFDEYESETGDQDYYYLSVKALYTVGYSTSLVTLTTAMVILCRFRKLHCTRNFIHMNLFVSFMLRAISVFIKDWILYAEQDSNHCFISTVECKAVMVFFHYCVVSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTVCVTVWATLRLYFDDTGCWDMNDSTALWWVIKGPVVGSIMVNFVLFIGIIVILVQKLQSPDMGGNESSIYLTNLSPRVPKKAREDPLPVPSDQHSLPFLSCVQKCYCKPQRAQQHSCKMSELSTITLRLARSTLLLIPLFGIHYTVFAFSPENVSKRERLVFELGLGSFQGFVVAVLYCFLNGEVQAEIKRKWRSWKVNRYFAVDFKHRHPSLASSGVNGGTQLSILSKSSSQIRMSGLPADNLAT
Protein: U1 small nuclear ribonucleoprotein A (U1 snRNP protein A) (Q39244)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in nuclear pre-mRNA splicing (By similarity). Seems to not be involved in polyadenylation.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- U1 small nuclear ribonucleoprotein C
- U2 small nuclear ribonucleoprotein A'
- Small nuclear ribonucleoprotein-associated protein
- U1 small nuclear ribonucleoprotein 70 kDa
- Small nuclear ribonucleoprotein-associated protein
- Nuclear protein-like
- Probable small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein SmD3a
- Small nuclear ribonucleoprotein Sm D2
- Probable small nuclear ribonucleoprotein F
Sequence:
MEMQEANQGGGSEVSPNQTIYINNLNEKVKLDELKKSLNAVFSQFGKILEILAFKTFKHKGQAWVVFDNTESASTAIAKMNNFPFYDKEMRIQYAKTKSDVVAKADGTFVPREKRKRHEEKGGGKKKKDQHHDSTQMGMPMNSAYPGVYGAAPPLSQVPYPGGMKPNMPEAPAPPNNILFVQNLPHETTPMVLQMLFCQYQGFKEVRMIEAKPGIAFVEFADEMQSTVAMQGLQGFKIQQNQMLITYAKK
Protein: HTH-type transcriptional activator AllS (P0ACR0)
Organism: Escherichia coli (strain K12)
Function: Positive regulator essential for the expression of allD operon. Binds to the allD promoter.
Interaction partners:
- GDP-L-fucose synthase
- Enterobactin synthase component B
- HTH-type transcriptional repressor AllR
- Type 1 fimbrin D-mannose specific adhesin
- Uncharacterized fimbrial-like protein SfmH
- HTH-type transcriptional regulator TdcA
- Ureidoglycolate lyase
- Allantoinase
- Ureidoglycolate dehydrogenase
Sequence:
MFDPETLRTFIAVAETGSFSKAAERLCKTTATISYRIKLLEENTGVALFFRTTRSVTLTAAGEHLLSQARDWLSWLESMPSELQQVNDGVERQVNIVINNLLYNPQAVAQLLAWLNERYPFTQFHISRQIYMGVWDSLLYEGFSLAIGVTGTEALANTFSLDPLGSVQWRFVMAADHPLANVEEPLTEAQLRRFPAVNIEDSARTLTKRVAWRLPGQKEIIVPDMETKIAAHLAGVGIGFLPKSLCQSMIDNQQLVSRVIPTMRPPSPLSLAWRKFGSGKAVEDIVTLFTQRRPEISGFLEIFGNPRS
Protein: Periplakin (Q9R269)
Organism: Mus musculus (Mouse)
Function: Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling.
Subcellular location: Cell junction, desmosome {ECO:0000269|PubMed:15226441}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O60437}. Cell membrane {ECO:0000269|PubMed:19029034}. Cytoplasm {ECO:0000269|PubMed:19029034}.
Interaction partners:
- Envoplakin
- Kazrin
- Butyrophilin subfamily 1 member A1
- Periaxin
- Ezrin
- Protein-glutamine gamma-glutamyltransferase K
- Plakophilin-1
- Desmoglein-1-alpha
- Desmoglein-1-beta
- Filaggrin
Sequence:
MHSLFRKRNKGKYSPTVQTRSISNKELSDLIEQLQKNADQVERNIVDTEAKMQSDLARMQEGQLPEHRDAALQNVSDSEKLLYVLEADSAIAKHMKHPQGDMIAEDIRQLKERVTNLRGKHKQMYSLAVKEADPRVNWDTLVDEKLDKLSSQSFGTDLPLVDSQVEQHNIFHNEVKAIGPHLAKDKEQNSELQAKYQKLLTASQARQQHLSSLQDYMQRCTNELYWLDQQAKGRMQYDWSDRNLDYPSRRRQYENFINRNLEAKEERINKLHTEGDQLLTAEHPGRNSIEAHMEAVHAEWKEYLNLLICEESHLKYMEDYHQFHKDMKDAQELLRKVDSDLNQKYSPDFKDRYQIELLLRELDDQEKALDKYEDVVRGLQRRGQQVVPLKYRRETPLKPIPVEALCDFESDQGLISRGYSYTLQKNNGESWELTDSTGKKLAAPAVCFIIPPTDPEALALADSLGSQYRSVRQKATGSKHALQQRHEVLRTENPGDASDLQGRQLLAGLDKVASDLDRQEKAITGILRPPLEQGRAIEDSAERAKGLKNITNELLQIEPEKTQCTAECEAFVQALPASGTAPLLKTRVEDTNQKYERLVWLLEAAQEKVDVANRLENSLQRGRELLASYENRLIQDDTMPESGHVLDRKRQELEAMASELQAHKSLLGEVGKNLQVAKQCSSSLASRFQEHCPDLERQEAEVHKLNQRFNNLSQQVERRAQSLQSARAAYDEYCSGYNRVLQFLAKTPSYEPQETDSLGQMETKLKNQKNLLDELASREQEVQKVYADSQQYQQAVKDYELEAEKLRSLLDLENGRNSHVNKRARLQSPAAKVKEEEAALAAKFTEVNAINRQRLQNLEFALNLLRQQPEAGVTHETLQGGKLSSGMEETWKIKKELEEEIERRQQLENEVKSAQEEIQTLKDQGPQESLVRKEVLKKVPDPALEESFQQLQQTLAEEQHKNQLLQEELGALQLRLQALEQETRDGGQEYVVKEVLRIEPDRAQEDEVLQLREELEALRRQKGAREAEVLLLQQRVAALAAEKSRVQEKVTEREVVKLQNDPQLEAEYRRLQEEHQREGTLREKQEEELSFLQAKLRRLEKERAMAEGKITVKEVLKVEKDAAVEREVNDLTRQYEDEAAKARSGQREKTELLRKIWALEEENAKVVVQEKVREIVRPDPKAESEVANLRLELVEQERKFRGAEEQLKSYQSELEALRNRGPQVEVKEVTKEVIKYTTDPETEQELQRLREEIMDKTRLIERCDLEIYQLKQEIQALKDTKPQVQTREVVQEILQFQEDPQTKKEVESLRIQLSEEQKKQVDLEGERASQEEKIKRKEEELAQQRKERVVRQEVVQYEDEPDLRAEVTAFTNSIDAELRQIDKLHVELRRLQHRRAELERQLEELERERQARRAAELEVQRLQQRLAALEQEEAKTGEKVTHTQKVVLQQDPQQTREHALLRAQLEEERHRRQLLEGELEPLRRKLAALEKAEIKEKVVFSESVQVEKGDTEQEIQRLKKSLEEESQSKRELDSEVTRLEAKLSELEFYNSKSSKELDFLREENHKLQLERQNLQLETRRLQSEIEMAATETRDLKNITTIDSGTHLNSRLWSLEKELDDLKKMSKDKDLEIDELQRRLGSVAVKREQRENHLRRSIVVIDPDTGRELSPEEAHRAGLIDWKMFVKLRSQECDWEEISVKGPNGESSVIHDRKSGKKFSIEDALQSGRLTAAQYDRYVNKDMSIQELAVLVSGQK
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (E2CWF1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSGRRPQFSTTERVIKAVPFPPTRRLTLKEVFENGKPKMDVLKNHLVKEGRVEEDVALKIINDGAAILKQEKTMLEVEAPITVCGDVHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTEYFTFKQECRIKYSELVYEACMHTFDCLPLAALLNQQFLCVHGGMSPEITCLDDIRKLDRFAEPPAFGPVCDLLWSDPLEDYGSEKTLEHYTHNTVRGCSYFFSYPAVCEFLQNNSLLSIIRAHEAQDAGYRMYRKNQATGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKGATSVRKEVIRNKIRAIGKMARVFTVLREESENVLILKGLTPTGTLPLGVLSGGKQTIETAKLQAAEEREAIRGFTIAHRIRSFEEARGLDRINERMPPRKEASYHHDAGKTHPHPSKRSDHGKKAL
Protein: Phosphatidylinositol 4-phosphate 5-kinase type-1 beta (PIP5K1-beta) (PtdIns(4)P-5-kinase 1 beta) (EC 2.7.1.68) (Phosphatidylinositol 4-phosphate 5-kinase type I beta) (PIP5KIbeta) (Protein STM-7) (Type I phosphatidylinositol 4-phosphate 5-kinase beta) (O14986)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (By similarity). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of phospholipase PLD2. Together with PIP5K1A, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P70181}. Cell membrane {ECO:0000250|UniProtKB:P70181}. Endomembrane system. Note=Associated with membranes. {ECO:0000250}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol 4-kinase alpha
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Phosphatidylinositol 4-kinase type 2-beta
- Phosphatidylinositol 4-kinase type 2-alpha
- Phosphatidylinositol 4-phosphate 5-kinase-like protein 1
- ADP-ribosylation factor 6
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
Sequence:
MSSAAENGEAAPGKQNEEKTYKKTASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETPQNVPDAKRTGMQKVLYSTAMESIQGPGKSGDGIITENPDTMGGIPAKSHRGEKLLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQALKASPSKKRCNSIAALKATSQEIVSSISQEWKDEKRDLLTEGQSFSSLDEEALGSRHRPDLVPSTPSLFEAASLATTISSSSLYVNEHYPHDRPTLYSNSKGLPSSSTFTLEEGTIYLTAEPNTLEVQDDNASVLDVYL
Protein: Coiled-coil domain-containing protein 85B (A2CEM9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Functions as a transcriptional repressor. May inhibit the activity of CTNNB1 in a TP53-dependent manner and thus regulate cell growth (By similarity). May function in adipocyte differentiation, negatively regulating mitotic clonal expansion (By similarity). Plays a role in cell-cell adhesion and epithelium development through its interaction with proteins of the beta-catenin family (Probable).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15834}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15834}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q15834}.
Interaction partners:
Sequence:
MGSDSEILNRELSKLSDEDLLACTKEELVNRLRKEESDKMSALIQRGRLIKEVNKQLQGHLLEIRELKVINQRLQEENQELRDLCCFLDDDRLKVKKLAREWQLFGHHAAKVMREDLGGYLKKLADLERMQDGLVKENLDLKELCLVLEEECVSRSDSSPGGSTDLNIPCMVARDVGDGSSSTGSVGSPDQLHLVCSPDD
Protein: Glucan 1,3-beta-glucosidase I/II (EC 3.2.1.58) (Exo-1,3-beta-glucanase I/II) (Soluble cell wall protein 6) (P23776)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme hydrolyzes both 1,3-beta- and 1,6-beta-linkages and even has beta-glucosidase activity. It could also function biosynthetically as a transglycosylase.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:9748433}. Secreted {ECO:0000269|PubMed:9748433}.
Interaction partners:
- Glucan 1,3-beta-glucosidase
- Sporulation-specific glucan 1,3-beta-glucosidase
- 1,3-beta-glucan synthase component FKS1
- Invertase 2
- 1,3-beta-glucan synthase component GSC2
- Glucan 1,3-beta-glucosidase 2
- 1,3-beta-glucan synthase component FKS3
- Ergosteryl-beta-glucosidase
- Probable family 17 glucosidase SCW4
Sequence:
MLSLKTLLCTLLTVSSVLATPVPARDPSSIQFVHEENKKRYYDYDHGSLGEPIRGVNIGGWLLLEPYITPSLFEAFRTNDDNDEGIPVDEYHFCQYLGKDLAKSRLQSHWSTFYQEQDFANIASQGFNLVRIPIGYWAFQTLDDDPYVSGLQESYLDQAIGWARNNSLKVWVDLHGAAGSQNGFDNSGLRDSYKFLEDSNLAVTTNVLNYILKKYSAEEYLDTVIGIELINEPLGPVLDMDKMKNDYLAPAYEYLRNNIKSDQVIIIHDAFQPYNYWDDFMTENDGYWGVTIDHHHYQVFASDQLERSIDEHIKVACEWGTGVLNESHWTVCGEFAAALTDCTKWLNSVGFGARYDGSWVNGDQTSSYIGSCANNDDIAYWSDERKENTRRYVEAQLDAFEMRGGWIIWCYKTESSLEWDAQRLMFNGLFPQPLTDRKYPNQCGTISN
Protein: Melanoma-derived growth regulatory protein (Cartilage-derived retinoic acid-sensitive protein) (CD-RAP) (Melanoma inhibitory activity protein) (Q61865)
Organism: Mus musculus (Mouse)
Function: Elicits growth inhibition on melanoma cells in vitro as well as some other neuroectodermal tumors, including gliomas.
Subcellular location: Secreted.
Interaction partners:
- Protein S100-B
Sequence:
MVWSPVLLGIVVLSVFSGPSRADRAMPKLADWKLCADEECSHPISMAVALQDYVAPDCRFLTIYRGQVVYVFSKLKGRGRLFWGGSVQGGYYGDLAARLGYFPSSIVREDLTLKPGKIDMKTDQWDFYCQ
Protein: Fibrinogen gamma chain (P02679)
Organism: Homo sapiens (Human)
Function: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.
Subcellular location: Secreted {ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
Interaction partners:
- Fibrinogen beta chain
- Fibrinogen alpha chain
- Prothrombin
- Integrin beta-3
- Alpha-2-HS-glycoprotein
- Fibronectin
- Heparin cofactor 2
- Albumin
- Fibrinogen-like protein 1
- Coagulation factor XIII B chain
Sequence:
MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL
Protein: Akirin-1 (Q9H9L7)
Organism: Homo sapiens (Human)
Function: Molecular adapter that acts as a bridge between proteins, and which is involved skeletal muscle development (By similarity). Functions as signal transducer for MSTN during skeletal muscle regeneration and myogenesis (By similarity). May regulate chemotaxis of both macrophages and myoblasts by reorganising actin cytoskeleton, leading to more efficient lamellipodia formation via a PI3 kinase dependent pathway (By similarity). In contrast to AKIRIN2, not involved in nuclear import of proteasomes.
Subcellular location: Nucleus {ECO:0000269|PubMed:18066067}.
Interaction partners:
- Akirin-2
Sequence:
MACGATLKRPMEFEAALLSPGSPKRRRCAPLPGPTPGLRPPDAEPPPPFQTQTPPQSLQQPAPPGSERRLPTPEQIFQNIKQEYSRYQRWRHLEVVLNQSEACASESQPHSSALTAPSSPGSSWMKKDQPTFTLRQVGIICERLLKDYEDKIREEYEQILNTKLAEQYESFVKFTHDQIMRRYGTRPTSYVS
Protein: HIST1H2BC protein (Q0D2M2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSGGTKAVTKYTSSK
Protein: tRNA pseudouridine(32) synthase, mitochondrial (EC 5.4.99.28) (tRNA pseudouridine synthase 9) (tRNA pseudouridylate synthase 9) (tRNA-uridine isomerase 9) (Q12069)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for synthesis of pseudouridine from uracil-32 in mitochondrial transfer RNAs.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:15466869}.
Interaction partners:
- Multisubstrate pseudouridine synthase 7
- tRNA pseudouridine synthase 4
- tRNA pseudouridine
- 21S rRNA pseudouridine
- tRNA pseudouridine synthase 1
- tRNA pseudouridine
- tRNA modification GTPase MSS1
Sequence:
MQRNNRLRNLFTVPVIMARQLKRNALSAGLAFAGNATSNEFDEHLQNEVEREREIQKKKKIKRTQSKKSPDLINKSTFQSRTIGSKKEKHRQLDPEYEIVIDGPLRKIKPYHFTYRTFCKERWRDKKLVDVFISEFRDRESEYYKRTIENGDVHINDETADLSTVIRNGDLITHQVHRHEPPVTSRPIKVIFEDDNIMVIDKPSGIPVHPTGRYRFNTITKMLQNNLGFVVNPCNRLDRLTSGLMFLAKTPKGADNIGDQLKAREVTKEYVAKVVGEFPETEVIVEKPLKLIEPRLALNAVCQMDEKGAKHAKTVFNRISYDGKTSIVKCKPLTGRSHQIRVHLQYLGHPIANDPIYSNDEVWGNNLGKGGQADFDIVITKLDEIGKRKPAKSWFHSNGGYGEVLRQEKCSICESDLYTDPGPNDLDLWLHAYLYESTETEEGTEKKKWCYKTEYPEWALRR
Protein: Cytochrome C biogenesis Fc (Q2F961)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MVQLQNFFFFITSMVVPRGTAAPVLLKWFVSRDVPTGASSSNGTIIPIPISLFPFLVYLHSRKFIRSMDRAKSGVLVKASRPILLPDKIGRSSSARNALFRFVPVLHFLIIESMGDLSYLESFCGLLCLQFFRTLFSLPRDRSAKRERALRSKGQTLRPKGNEQQNDKMRCPGHPHIERRVEGFGPVAFPAPPSSSGACLGPPEIGLEALALPTSRLLMAVGHDYYKKVKMNLSISHGGVCIFMLGVLLSNTNKIQFTQRLPLGSELHMGKERCCLRGLDHLHGPTSHSICGNLMIYKPSPTSERFMFEHDESLRADLLPINFPASYENGKLEDFLHRWMKNHEHKNFRFSMFPERRYFFSIRETRSTTEVAIHTNPFTDLYASIGTGSSRTGGWYTTIMKLPFLFSIRIGFLLASSGGSRSLLRQLQKDKLHWN
Protein: Taste receptor type 2 member 4 (T2R4) (Taste receptor type 2 member 8) (T2R8) (Q9JKT3)
Organism: Mus musculus (Mouse)
Function: Gustducin-coupled receptor for denatonium and N(6)-propyl-2-thiouracil implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. In airway epithelial cells, binding of denatonium increases the intracellular calcium ion concentration and stimulates ciliary beat frequency (By similarity).
Subcellular location: Membrane; Multi-pass membrane protein. Cell projection, cilium membrane. Note=In airway epithelial cells, localizes to motile cilia. {ECO:0000250}.
Interaction partners:
- Taste receptor type 2 member 3
- Guanine nucleotide-binding protein G
- Taste receptor type 1 member 3
- Taste receptor type 1 member 2
- Taste receptor type 1 member 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
Sequence:
MLWELYVFVFAASVFLNFVGIIANLFIIVIIIKTWVNSRRIASPDRILFSLAITRFLTLGLFLLNSVYIATNTGRSVYFSTFFLLCWKFLDANSLWLVTILNSLYCVKITNFQHPVFLLLKRTISMKTTSLLLACLLISALTTLLYYMLSQISRFPEHIIGRNDTSFDLSDGILTLVASLVLNSLLQFMLNVTFASLLIHSLRRHIQKMQRNRTSFWNPQTEAHMGAMRLMICFLVLYIPYSIATLLYLPSYMRKNLRAQAICMIITAAYPPGHSVLLIITHHKLKAKAKKIFCFYK