wanglab/gogpt-training-data huggingface dataset:
Protein: Immunity factor for SPN (NAD glycohydrolase inhibitor) (SPN immunity factor) (Q2VJ58)
Organism: Streptococcus pyogenes
Interaction partners:
- ADP-ribosyl cyclase / cyclic ADP-ribose hydrolase
- Thiol-activated cytolysin
Sequence:
MYKVPKGLEHYQKMFQKEVTVNDLKKYLIGSDKEYRITRRDSYMGDISDPEVILEYGVYPAFIKGYTQLKANIEEALLEMSNSGQALDIYQAVQTLNAENMLLNYYESLPFYLNRQSILANITKALKDAHIREAMAHYKLGEFAHYQDTMLDMVERTIETF
Protein: Truncated non-functional calcium-binding mitochondrial carrier SAL1-1 (Suppressor of AAC2 lethality) (D6W196)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Calcium-dependent mitochondrial solute carrier.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Bud site selection protein 22
- RNA polymerase I-specific transcription initiation factor RRN11
- Acyl carrier protein, mitochondrial
- Protein SIP4
- Monoglyceride lipase
- Mitochondrial import inner membrane translocase subunit TIM22
- Mitochondrial import inner membrane translocase subunit TIM17
- Adrenodoxin homolog, mitochondrial
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- ADP,ATP carrier protein 2
Sequence:
MLLKNCETDKQRDIRYACLFKELDVKGNGQVTLDNLISAFEKNDHPLKGNDEAIKMLFTAMDVNKDSVVDLSDFKKYASNAESQIWNGFQRIDLDHDGKIGINEINRYLSDLDNQSICNNELNHELSNEKVNKFSRFFEWAFPKRKANIALRGQASHKKNTDNDRSKKTTDSDLYVTYDQWRDFLLLVPRKQGSRLHTAYSYFYLFNEDVDLSSEGDVTLINDFIRGFGFFIAGGISGVISRTCTAPFDRLKVFLIARTDLSSILLNSKTDLLAKNPNADINKISSPLAKAVKSLYRQGGIKAFYVGNGLNVIKVFPESSIKFGSFEVTKKIMTKLEGCRDTKDLSKFSTYIAGGLAGMAAQFSVYPIDTLKFRVQCAPLDTKLKGNNLLFQTAKDMFREGGGQIILQRCHSRYSGHISLCCIRFGDFFCLKKMVYCQTGKDPEPTTRSGHSKQPGCTSNGCIQWNCRSFCCLSNQSFKNKTTSPRNICTSLCV
Protein: RNA2 polyprotein (Genome polyprotein M) (M RNA polyprotein) (Middle component RNA polyprotein) (P2) [Cleaved into: VP58 (P58); Movement protein (MP) (48 kDa protein); Large capsid protein (LCP) (Coat protein VP37) (L subunit) (Large coat protein); Small capsid protein precursor (S subunit); Mature small capsid protein (SCP) (Coat protein VP23) (Small capsid protein, N-terminus part) (Small coat protein, N-terminus part); Small capsid protein C-terminus part (Small coat protein C-terminus part)] (P03599)
Organism: Cowpea mosaic virus (strain SB) (CPMV)
Function: Responsible for viral RNA2 accumulation. May function by recruiting the RNA1-encoded polyprotein that contains the replication protein to RNA2 and enable its replication.
Subcellular location: [VP58]: Host nucleus {ECO:0000269|PubMed:8497075}.; SUBCELLULAR LOCATION: [Movement protein]: Host cell junction, host plasmodesma {ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:27339685}. Note=Assembles in tubules that are embedded within modified plasmodesmata. {ECO:0000269|PubMed:10864669, ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:27339685}.; SUBCELLULAR LOCATION: [Large capsid protein]: Virion {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160, ECO:0000269|PubMed:28373698}.; SUBCELLULAR LOCATION: [Mature small capsid protein]: Virion {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160, ECO:0000269|PubMed:28373698}.
Interaction partners:
Sequence:
MFSFTEAKSKISLWTRSAAPLNNVYLSYSCRCGLGKRKLAGGCCSAPYITCYDSADFRRVQYLYFCLTRYCCLYFFLLLLADWFYKKSSIFFETEFSRGFRTWRKIVKLLYILPKFEMESIMSRGIPSGILEEKAIQFKRAKEGNKPLKDEIPKPEDMYVSHTSKWNVLRKMSQKTVDLSKAAAGMGFINKHMLTGNILAQPTTVLDIPVTKDKTLAMASDFIRKENLKTSAIHIGAIEIIIQSFASPESDLMGGFLLVDSLHTDTANAIRSIFVAPMRGGRPVRVVTFPNTLAPVSCDLNNRFKLICSLPNCDIVQGSQVAEVSVNVAGCATSIEKSHTPSQLYTEEFEKEGAVVVEYLGRQTYCAQPSNLPTEEKLRSLKFDFHVEQPSVLKLSNSCNAHFVKGESLKYSISGKEAENHAVHATVVSREGASAAPKQYDPILGRVLDPRNGNVAFPQMEQNLFALSLDDTSSVRGSLLDTKFAQTRVLLSKAMAGGDVLLDEYLYDVVNGQDFRATVAFLRTHVITGKIKVTATTNISDNSGCCLMLAINSGVRGKYSTDVYTICSQDSMTWNPGCKKNFSFTFNPNPCGDSWSAEMISRSRVRMTVICVSGWTLSPTTDVIAKLDWSIVNEKCEPTIYHLADCQNWLPLNRWMGKLTFPQGVTSEVRRMPLSIGGGAGATQAFLANMPNSWISMWRYFRGELHFEVTKMSSPYIKATVTFLIAFGNLSDAFGFYESFPHRIVQFAEVEEKCTLVFSQQEFVTAWSTQVNPRTTLEADGCPYLYAIIHDSTTGTISGDFNLGVKLVGIKDFCGIGSNPGIDGSRLLGAIAQGPVCAEASDVYSPCMIASTPPAPFSDVTAVTFDLINGKITPVGDDNWNTHIYNPPIMNVLRTAAWKSGTIHVQLNVRGAGVKRADWDGQVFVYLRQSMNPESYDARTFVISQPGSAMLNFSFDIIGPNSGFEFAESPWANQTTWYLECVATNPRQIQQFEVNMRFDPNFRVAGNILMPPFPLSTETPPLLKFRFRDIERSKRSVMVGHTATAA
Protein: Noggin (Q13253)
Organism: Homo sapiens (Human)
Function: Inhibitor of bone morphogenetic proteins (BMP) signaling which is required for growth and patterning of the neural tube and somite. Essential for cartilage morphogenesis and joint formation. Inhibits chondrocyte differentiation through its interaction with GDF5 and, probably, GDF6.
Subcellular location: Secreted.
Interaction partners:
- Bone morphogenetic protein 4
- Bone morphogenetic protein 2
- Bone morphogenetic protein 7
- Growth/differentiation factor 5
- Bone morphogenetic protein 6
- Bone morphogenetic protein 5
- Growth/differentiation factor 6
- Growth/differentiation factor 7
- Sonic hedgehog protein
- R-spondin-1
Sequence:
MERCPSLGVTLYALVVVLGLRATPAGGQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPPEDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGGQRCGWIPIQYPIISECKCSC
Protein: Pre-B-cell leukemia transcription factor 1 (Homeobox protein PBX1) (Homeobox protein PRL) (P40424)
Organism: Homo sapiens (Human)
Function: Transcription factor which binds the DNA sequence 5'-TGATTGAT-3' as part of a heterodimer with HOX proteins such as HOXA1, HOXA5, HOXB7 and HOXB8. Binds to the DNA sequence 5'-TGATTGAC-3' in complex with a nuclear factor which is not a class I HOX protein. Has also been shown to bind the DNA sequence 5'-ATCAATCAA-3' cooperatively with HOXA5, HOXB7, HOXB8, HOXC8 and HOXD4. Acts as a transcriptional activator of PF4 in complex with MEIS1. Also activates transcription of SOX3 in complex with MEIS1 by binding to the 5'-TGATTGAC-3' consensus sequence (By similarity). In natural killer cells, binds to the NFIL3 promoter and acts as a transcriptional activator of NFIL3, promoting natural killer cell development (By similarity). Plays a role in the cAMP-dependent regulation of CYP17A1 gene expression via its cAMP-regulatory sequence (CRS1) (By similarity). Probably in complex with MEIS2, involved in transcriptional regulation by KLF4. Acts as a transcriptional activator of NKX2-5 and a transcriptional repressor of CDKN2B (By similarity). Together with NKX2-5, required for spleen development through a mechanism that involves CDKN2B repression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:28270404}.
Interaction partners:
- Homeobox protein PKNOX1
- Homeobox protein Meis1
- Homeobox protein Hox-B1
- Homeobox protein Hox-A9
- Homeobox protein Meis2
- Transcription factor E2-alpha
- Homeobox domain-containing protein
- Pancreas/duodenum homeobox protein 1
- Homeobox protein PKNOX2
- Homeobox protein Hox-B8
Sequence:
MDEQPRLMHSHAGVGMAGHPGLSQHLQDGAGGTEGEGGRKQDIGDILQQIMTITDQSLDEAQARKHALNCHRMKPALFNVLCEIKEKTVLSIRGAQEEEPTDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGAGSDNSVEHSDYRAKLSQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVSIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFNKQATEILNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAAKTAVTATNVSAHGSQANSPSTPNSAGSSSSFNMSNSGDLFMSVQSLNGDSYQGAQVGANVQSQVDTLRHVISQTGGYSDGLAASQMYSPQGISANGGWQDATTPSSVTSPTEGPGSVHSDTSN
Protein: Ras GTPase-activating-like protein IQGAP3 (Q86VI3)
Organism: Homo sapiens (Human)
Interaction partners:
- Cell division control protein 42 homolog
- Ras GTPase-activating-like protein IQGAP1
- Ras-related C3 botulinum toxin substrate 3
- Ras GTPase-activating-like protein IQGAP2
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 1
- Anillin
- Calmodulin-1
- Kinesin-like protein KIF20A
- Calmodulin-1
Sequence:
MERRAAGPGWAAYERLTAEEMDEQRRQNVAYQYLCRLEEAKRWMEACLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEQLRYQATGLHFRHTDNINFWLSAIAHIGLPSTFFPETTDIYDKKNMPRVVYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELSNMASELAKYGLQLPAFSKIGGILANELSVDEAAVHAAVLAINEAVERGVVEDTLAALQNPSALLENLREPLAAVYQEMLAQAKMEKAANARNHDDRESQDIYDHYLTQAEIQGNINHVNVHGALEVVDDALERQSPEALLKALQDPALALRGVRRDFADWYLEQLNSDREQKAQELGLVELLEKEEVQAGVAAANTKGDQEQAMLHAVQRINKAIRRRVAADTVKELMCPEAQLPPVYPVASSMYQLELAVLQQQQGELGQEELFVAVEMLSAVVLINRALEARDASGFWSSLVNPATGLAEVEGENAQRYFDALLKLRQERGMGEDFLSWNDLQATVSQVNAQTQEETDRVLAVSLINEALDKGSPEKTLSALLLPAAGLDDVSLPVAPRYHLLLVAAKRQKAQVTGDPGAVLWLEEIRQGVVRANQDTNTAQRMALGVAAINQAIKEGKAAQTERVLRNPAVALRGVVPDCANGYQRALESAMAKKQRPADTAFWVQHDMKDGTAYYFHLQTFQGIWEQPPGCPLNTSHLTREEIQSAVTKVTAAYDRQQLWKANVGFVIQLQARLRGFLVRQKFAEHSHFLRTWLPAVIKIQAHWRGYRQRKIYLEWLQYFKANLDAIIKIQAWARMWAARRQYLRRLHYFQKNVNSIVKIQAFFRARKAQDDYRILVHAPHPPLSVVRRFAHLLNQSQQDFLAEAELLKLQEEVVRKIRSNQQLEQDLNIMDIKIGLLVKNRITLQEVVSHCKKLTKRNKEQLSDMMVLDKQKGLKSLSKEKRQKLEAYQHLFYLLQTQPIYLAKLIFQMPQNKTTKFMEAVIFSLYNYASSRREAYLLLQLFKTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVLSVHTDPVHLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKATLAEKFPDATDSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGALAAPQRHALGAVAQLLQHAAAGKAFSGQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYITVGELVNTHRLLLEHQDCIAPDHQDPLHELLEDLGELPTIPDLIGESIAADGHTDLSKLEVSLTLTNKFEGLEADADDSNTRSLLLSTKQLLADIIQFHPGDTLKEILSLSASREQEAAHKQLMSRRQACTAQTPEPLRRHRSLTAHSLLPLAEKQRRVLRNLRRLEALGLVSARNGYQGLVDELAKDIRNQHRHRHRRKAELVKLQATLQGLSTKTTFYEEQGDYYSQYIRACLDHLAPDSKSSGKGKKQPSLHYTAAQLLEKGVLVEIEDLPASHFRNVIFDITPGDEAGKFEVNAKFLGVDMERFQLHYQDLLQLQYEGVAVMKLFNKAKVNVNLLIFLLNKKFLRK
Protein: L-cysteine S-thiosulfotransferase subunit SoxA (EC 2.8.5.2) (Cytochrome c551 subunit diheme) (Protein SoxA) (SoxAX cytochrome complex subunit A) (Sulfur oxidizing protein A) (Thiosulfate-oxidizing multienzyme system protein SoxA) (TOMES protein SoxA) (O33434)
Organism: Paracoccus pantotrophus (Thiosphaera pantotropha)
Function: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
Subcellular location: Periplasm {ECO:0000269|PubMed:10940005, ECO:0000305|PubMed:17547421}.
Interaction partners:
- Sulfur compound chelating protein SoxZ.
- Monoheme cytochrome SoxX
- Thiosulfate-binding protein SoxY.
- Sulfur dehydrogenase subunit SoxD.
- Sulfate thiol esterase SoxB
- Sulfur dehydrogenase subunit SoxC.
- Sulfane dehydrogenase subunit SoxC.
- Cytochrome c.
- Cytochrome c.
- Thiosulfate/3-mercaptopyruvate sulfurtransferase.
Sequence:
MPRFTKTKGTLAATALGLALAGAAFADPVEDGLVIETDSGPVEIVTKTAPPAFLADTFDTIYSGWHFRDDSTRDLERDDFDNPAMVFVDRGLDKWNAAMGVNGESCASCHQGPESMAGLRAVMPRVDEHTGKLMIMEDYVNACVTERMGLEKWGVTSDNMKDMLSLISLQSRGMAVNVKIDGPAAPYWEHGKEIYYTRYGQLEMSCANCHEDNAGNMIRADHLSQGQINGFPTYRLKDSGMVTAQHRFVGCVRDTRAETFKAGSDDFKALELYVASRGNGLSVEGVSVRH
Protein: Phytochelatin synthase (Q38AN4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGNGQINARASTEEHLRKWEAALAALEKVSNSGRRAMERDRVYYGGAEDARSGNEEVLEGSMRGACRSSQVSFSTTAGGSESSCTEHQPPRRQNQTPNENNGRSWGTNQSGNTSNINNAEQSRTGSLVGQHRSRQQVVEIRKARMAFFKSYEVQRDYEHKAIMECGHFGAAAVALSYLLGGARGCRDRKKCVTMEDIFFAVHLPLHYLHSGVQTLQVMSDILREFIDVDNRFKNEYGLSVVHFDISPVVGQVELGRNEVGDRQTCMQLHEFTKAIANDSEEQIQAVRIVNYDPYVLQQETFVDNFVDGDDDVSALADSIRVGLRDQERQYSKNNNGVYAVIVEVRCVVELMVTLAEGIVDDQLHVRLFEVPAAALFKAMTVPLENERARGFMRIFRKDSVPVMSHDEVQSMFSPELAGGNVLGTTSMGTHASAISGHTSPHIIAVAWAMHLLGGDRASAHGHGNGLPVSDIVRTMKFPAEVLIDSTLPLGEVFKYAREYIRLTERNYDVSIYPILTNTSREDAVPTISVFELESILTDVKNANKDPDAPEHVMVIMYNANVAHNVLYVSNTPQWCVLSGYDEESQVVSLIDAHPKKFMKLWTCSLERLHRAMTSNGYLIFSKRTAASTHVGLSHDETWCDSLPLGHESQAPRVGALRRVDPTVQRYLALLRDQDALGVTRREVMRTLCFPSLPLSPTMIALTLTELGCPTTFEDVIVALPFEISSLMLRYFTLESMAVCLTTYVEHVGLNVSVKAYHTDRRNGNKARVTVEEFEQIMEECLADRGKALVMLFNTNEIEVFGDSRPFGSTGLVVGYNKATGGVTVMDTNPNRYFRTWSVCLHTLFRAMHDADTVHRRCGFLKVSHCTTLPAPSFPLEYSRETPLRMLPLRNIFHVSPSPHFQALSCAFTQLGFFYSPEEIFYEAYLQTMNRQRRRGTQAFAWRDVDVSLSVINKQIDTVFLAQICRMFLESRNSTRGSSDSQIDEHNDEEWLVHVEVMEDVTEGNIDSILRDATRRENNNTVLLLNYDTAIAHDVVGFGRSAALIKAYNPDTKSVLLWEAEHTVFGMFWTVDVPKFIEIGNLMDKGRSPYGLVKFEKVKRKLSGRRTLMKHLDAHEGGSPSKGFDDVPSGPMALRRNREMMTRFLFSPQESPDRRR
Protein: Phosphoinositide 3-kinase regulatory subunit 5 (PI3-kinase regulatory subunit 5) (IB PI3-kinase p101 subunit) (PI3-kinase p101 subunit) (Phosphatidylinositol 4,5-bisphosphate 3-kinase regulatory subunit) (PtdIns-3-kinase regulatory subunit) (PtdIns-3-kinase p101) (p101-PI3K) (O02696)
Organism: Sus scrofa (Pig)
Function: Regulatory subunit of the PI3K gamma complex. Required for recruitment of the catalytic subunit to the plasma membrane via interaction with beta-gamma G protein dimers. Required for G protein-mediated activation of PIK3CG.
Subcellular location: Nucleus {ECO:0000269|PubMed:12507995, ECO:0000269|PubMed:15611065}. Cytoplasm {ECO:0000269|PubMed:12507995, ECO:0000269|PubMed:15611065}. Cell membrane {ECO:0000269|PubMed:12507995, ECO:0000269|PubMed:15611065}; Peripheral membrane protein {ECO:0000305|PubMed:12507995}. Note=Predominantly localized in the nucleus in absence of PIK3CG/p120 (PubMed:12507995, PubMed:15611065). Colocalizes with PIK3CG/p120 in the cytoplasm (PubMed:12507995, PubMed:15611065). Translocated to the plasma membrane in a beta-gamma G protein-dependent manner (PubMed:12507995, PubMed:15611065). {ECO:0000269|PubMed:12507995, ECO:0000269|PubMed:15611065}.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Uncharacterized protein.
- non-specific serine/threonine protein kinase
- Tyrosine-protein kinase.
- Non-specific serine/threonine protein kinase
- protein kinase C
- GTPase NRas
- Guanine nucleotide-binding protein G
Sequence:
MQPGATTCTEDRIQHALERCLHGLSLSRRSTSWSAGLCLNCWSLQELVSRDPGHFLILLEQILQKTREVQEKGTYDLLAPLALLFYSTVLCTPHFPPDSDLLLKAARTYHRFLTWPVPYCSICQELLTFIDAELKAPGISYQRLVRAEQGLSTRSHRSSTVTVLLLNPVEVQAEFLDVADKLSTPGPSPHSAYITLLLHAFQATFGAHCDLSGLHRRLQSKTLAELEAIFTETAEAQELASGIGDAAEARQWLRTKLQAVGEKAGFPGVLDTAKPGKLRTIPIPVARCYTYSWNQDSFDILQEILLKEQELLQPEILDDEEDEDEEDEEEDLDADGHCAERDSVLSTGSAASHASTLSLASSQASGPTLSRQLLTSFVSGLSDGVDSGYMEDIEESAYERPRRPGGHERRGHRRPGQKFNRIYKLFKSTSQMVLRRDSRSLEGSPDSGPPLRRAGSLCSPLDSPTLPPSRAQGSRSLPQPKLSPQLPGWLLAPASRHQRRRPFLSGDEDPKASTLRVVVFGSDRISGKVVRAYSNLRRLENNRPLLTRFFKLQFFYVPVKRSRGTGTPTSPAPRSQTPPLPTDAPRHPGPAELGAAPWEESTNDISHYLGMLDPWYERNVLGLMHLPPEVLCQSLKAEPRPLEGSPAQLPILADMLLYYCRFAARPVLLQVYQTELTFITGEKTTEIFIHSLELGHSAATRAIKASGPGSKRLGIDGDREAVPLTLQIIYSKGAISGRSRWSNMEKLCTSVNLSKACRQQEELDSSTEALTLNLTEVVKRQTPKSKKGFNQISTSQIKVDKVQIIGSNSCPFAVCLDQDERKILQSVIRCEVSPCYKPEKSSLCPPPQRPSYPPAPATPDLCSLLCLPIMTFSGALP
Protein: Long-wave-sensitive opsin 1 (Red cone photoreceptor pigment) (Red-sensitive opsin) (ROP) (P04000)
Organism: Homo sapiens (Human)
Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Testis-specific protein TEX28
- Nyctalopin
- FERM domain-containing protein 7
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MAQQWSLQRLAGRHPQDSYEDSTQSSIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSVWMIFVVTASVFTNGLVLAATMKFKKLRHPLNWILVNLAVADLAETVIASTISIVNQVSGYFVLGHPMCVLEGYTVSLCGITGLWSLAIISWERWMVVCKPFGNVRFDAKLAIVGIAFSWIWAAVWTAPPIFGWSRYWPHGLKTSCGPDVFSGSSYPGVQSYMIVLMVTCCIIPLAIIMLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMIFAYCVCWGPYTFFACFAAANPGYAFHPLMAALPAYFAKSATIYNPVIYVFMNRQFRNCILQLFGKKVDDGSELSSASKTEVSSVSSVSPA
Protein: Sp7 transcription factor (Specificity protein 7 beta) (Q6IMK1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLTAACSKFGGSSPLRDSTALGKGGTKKPYTDLSAPKTMGDAYPAPFSSTNGLLSPAGSPPAPASGYANDYPPFPHSFPGPTGAQDPGLLVPKGHSSSDCLPSVYTSLDMSHPYGSWYKAGIHAGISPGPGNTPTPWWDMHPGGNWLGGGQGQGDGLQGTLSTGPAQPPLNPQLPTYPSDFAPLNPAPYPAPHLLQPGPQHVLPQDVYKPKAVGNSGQLEGSGAGKPPRGAGTGGSGGYAGSGAGRSTCDCPNCQELERLGAAAAGLRKKPIHSCHIPGCGKVYGKASHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELERHVRTHTREKKFTCLLCSKRFTRSDHLSKHQRTHGEPGPGPPPSGPKELGEGRSVGEEEANQPPRSSTSPAPPEKAPGGSPEQSNLLEI
Protein: Disintegrin and metalloproteinase domain-containing protein 30 (ADAM 30) (EC 3.4.24.-) (Q9UKF2)
Organism: Homo sapiens (Human)
Function: Plays a role in lysosomal amyloid precursor protein (APP) processing by cleaving and activating CTSD/cathepsin D which leads to APP degradation.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:27333034}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 2
- Disintegrin and metalloproteinase domain-containing protein 20
- Disintegrin and metalloproteinase domain-containing protein 21
- Hyaluronidase PH-20
Sequence:
MRSVQIFLSQCRLLLLLVPTMLLKSLGEDVIFHPEGEFDSYEVTIPEKLSFRGEVQGVVSPVSYLLQLKGKKHVLHLWPKRLLLPRHLRVFSFTEHGELLEDHPYIPKDCNYMGSVKESLDSKATISTCMGGLRGVFNIDAKHYQIEPLKASPSFEHVVYLLKKEQFGNQVCGLSDDEIEWQMAPYENKARLRDFPGSYKHPKYLELILLFDQSRYRFVNNNLSQVIHDAILLTGIMDTYFQDVRMRIHLKALEVWTDFNKIRVGYPELAEVLGRFVIYKKSVLNARLSSDWAHLYLQRKYNDALAWSFGKVCSLEYAGSVSTLLDTNILAPATWSAHELGHAVGMSHDEQYCQCRGRLNCIMGSGRTGFSNCSYISFFKHISSGATCLNNIPGLGYVLKRCGNKIVEDNEECDCGSTEECQKDRCCQSNCKLQPGANCSIGLCCHDCRFRPSGYVCRQEGNECDLAEYCDGNSSSCPNDVYKQDGTPCKYEGRCFRKGCRSRYMQCQSIFGPDAMEAPSECYDAVNLIGDQFGNCEITGIRNFKKCESANSICGRLQCINVETIPDLPEHTTIISTHLQAENLMCWGTGYHLSMKPMGIPDLGMINDGTSCGEGRVCFKKNCVNSSVLQFDCLPEKCNTRGVCNNRKNCHCMYGWAPPFCEEVGYGGSIDSGPPGLLRGAIPSSIWVVSIIMFRLILLILSVVFVFFRQVIGNHLKPKQEKMPLSKAKTEQEESKTKTVQEESKTKTGQEESEAKTGQEESKAKTGQEESKANIESKRPKAKSVKKQKK
Protein: Myopalladin (145 kDa sarcomeric protein) (Q86TC9)
Organism: Homo sapiens (Human)
Function: Component of the sarcomere that tethers together nebulin (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin, at the Z lines.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11309420}. Nucleus {ECO:0000269|PubMed:11309420}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:11309420}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11309420, ECO:0000269|PubMed:28017374}. Note=Bound to sarcomere both at the Z-line periphery and in the central I-band region. {ECO:0000269|PubMed:11309420}.
Interaction partners:
- Nebulin
- Ankyrin repeat domain-containing protein 1
- Nebulette
- Alpha-actinin-2
- Tropomodulin-4
- Telethonin
- Cysteine and glycine-rich protein 3
- Calpain-3
- Ankyrin repeat domain-containing protein 23
- Tropomodulin-1
Sequence:
MQDDSIEASTSISQLLRESYLAETRHRGNNERSRAEPSSNPCHFGSPSGAAEGGGGQDDLPDLSAFLSQEELDESVNLARLAINYDPLEKADETQARKRLSPDQMKHSPNLSFEPNFCQDNPRSPTSSKESPQEAKRPQYCSETQSKKVFLNKAADFIEELSSLFKSHSSKRIRPRACKNHKSKLESQNKVMQENSSSFSDLSERRERSSVPIPIPADTRDNEVNHALEQQEAKRREAEQAASEAAGGDTTPGSSPSSLYYEEPLGQPPRFTQKLRSREVPEGTRVQLDCIVVGIPPPQVRWYCEGKELENSPDIHIVQAGNLHSLTIAEAFEEDTGRYSCFASNIYGTDSTSAEIYIEGVSSSDSEGDPNKEEMNRIQKPNEVSSPPTTSAVIPPAVPQAQHLVAQPRVATIQQCQSPTNYLQGLDGKPIIAAPVFTKMLQNLSASEGQLVVFECRVKGAPSPKVEWYREGTLIEDSPDFRILQKKPRSMAEPEEICTLVIAEVFAEDSGCFTCTASNKYGTVSSIAQLHVRGNEDLSNNGSLHSANSTTNLAAIEPQPSPPHSEPPSVEQPPKPKLEGVLVNHNEPRSSSRIGLRVHFNLPEDDKGSEASSEAGVVTTRQTRPDSFQERFNGQATKTPEPSSPVKEPPPVLAKPKLDSTQLQQLHNQVLLEQHQLQNPPPSSPKEFPFSMTVLNSNAPPAVTTSSKQVKAPSSQTFSLARPKYFFPSTNTTAATVAPSSSPVFTLSSTPQTIQRTVSKESLLVSHPSVQTKSPGGLSIQNEPLPPGPTEPTPPPFTFSIPSGNQFQPRCVSPIPVSPTSRIQNPVAFLSSVLPSLPAIPPTNAMGLPRSAPSMPSQGLAKKNTKSPQPVNDDNIRETKNAVIRDLGKKITFSDVRPNQQEYKISSFEQRLMNEIEFRLERTPVDESDDEIQHDEIPTGKCIAPIFDKRLKHFRVTEGSPVTFTCKIVGIPVPKVYWFKDGKQISKRNEHCKMRREGDGTCSLHIESTTSDDDGNYTIMAANPQGRISCSGHLMVQSLPIRSRLTSAGQSHRGRSRVQERDKEPLQERFFRPHFLQAPGDMVAHEGRLCRLDCKVSGLPPPELTWLLNGQPVLPDASHKMLVRETGVHSLLIDPLTQRDAGTYKCIATNKTGQNSFSLELSVVAKEVKKAPVILEKLQNCGVPEGHPVRLECRVIGMPPPVFYWKKDNETIPCTRERISMHQDTTGYACLLIQPAKKSDAGWYTLSAKNEAGIVSCTARLDIYAQWHHQIPPPMSVRPSGSRYGSLTSKGLDIFSAFSSMESTMVYSCSSRSVVESDEL
Protein: Protein phosphatase 1 regulatory subunit 14B (Phosphatase holoenzyme inhibitor 1) (PHI-1) (Ubiquitous PKC-potentiated PP1 inhibitor) (Q8K3F3)
Organism: Rattus norvegicus (Rat)
Function: Inhibitor of PPP1CA. Has over 50-fold higher inhibitory activity when phosphorylated (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MADSGPAGGAALAAPAPGPGSGSTGPRVYFQSPPGAAGEGPGGADDDGPVRRQGKVTVKYDRKELRKRLNLEEWILEQLTRLYDCQEEEIPELEIDVDELLDMESDDTRAARVKELLVDCYKPTEAFISGLLDKIRGMQKLSTPQKK
Protein: Glycosyltransferase (Transferring glycosyl group transferase (DUF604)) (F4HU33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSRLIFLILAILFSLQFVFYPLNFISSSSQPLIKFSVSPVVSGSGSVHEPDQTELKHVVFGIAASAKFWKHRKDYVKLWWKPNGEMNGVVWLDQHINQNDNVSKTLPPIRISSDTSRFQYRYPKGLRSAIRITRIVSETVRLLNGTELEKNVRWIVMGDDDTVFFPENLVKVLRKYDHNQFYYIGSSSESHIQNLKFSYGMAYGGGGFAISYPLAKALEKMQDRCIQRYSELYGSDDRIHACMSELGVPLTKEVGFHQIDLYGKLLGLLSAHPLAPLVSIHHLDLVDPVFPNMGRVNAMRRFMVPAKLDSPSLAQQSICYDADHRWTVSVSWGYTVQIIRGVLSAREMVIPTRTFIDWYKQADERSYAFNTRPIAKSACQRPRVYYLSNALPDLALRRTASEYVRWYDMWEPECDWDMSDPSEFERVIVYKKPDPDRWNKHRAPRRDCCRVLPTTKNGTMVIDVGACKDDEFAEFLVK
Protein: Protocadherin alpha 2 (B5AK96)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
GEVRTKGELDYEERTSYEIQVIASDKGTPAMSGHCKISVKLVDINDNTPEVSITSLSLPVQENAPLGAVIALISVSDRDSGVNGQVTCSLSPHVPFKLVSTFKNYYSLVLDSALDREATADYKVMVTARDGGSPSLRATASVSVEVADVNDNAPVFAQPEYTVFVKENNPPGAHIFTVSAMDADAQENALVSYSLVERRVGERLLSSYVSVHAESGKVFALQPLDHEELELLQFQVTARDAGVPALGSNVTLQVFVLDENDNAPLLLPQGAVGVGGSVSELVPRSVGSGHVVTKVRAVDADSGYNAWLSYELQSTVGMRSLFRVGLYTGEISTTRALDEVDAPRQRLLVLVKDHGEPSLTATATVLVSLVENSQAPKTSSRALVDAAGQEASLVTVNVYLVIAICAVSSLLVLTLLLYTALRCSAMPTDGACAPGRPMLVCSSAVGSWSYSQQRRQRVCSGEGPPKTDLMAFSPSLSQGPESAEERQPPLEAEYLGKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEETKKKKKKKK