wanglab/gogpt-training-data huggingface dataset:
Protein: Ganglioside-induced differentiation-associated protein 1 (GDAP1) (O88741)
Organism: Mus musculus (Mouse)
Function: Regulates the mitochondrial network by promoting mitochondrial fission.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8TB36}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TB36}. Cytoplasm {ECO:0000269|PubMed:16172208}.
Interaction partners:
- Mitochondrial fission 1 protein
- Mitofusin-2
- SH3 domain and tetratricopeptide repeat-containing protein 2
- Peroxisomal membrane protein 11B
Sequence:
MARRQDEARAGVPLRVEGPPDKEVHLILYHWTHSFSSQKVRLVIAEKALKCEEHDVSLPLSEHNEPWFMRLNSAGEVPVLVHGENIICEATQIIDYLEQTFLDERTPRLMPDEGSMYYPRVQHYRELLDSLPMDAYTHGCILHPELTVDSMIPAYATTRIRSQIGNTESELKKLAEENPDLQEAYIAKQKRLKSKLLDHDNVKYLKKILDELEKVLDQVETELQRRNEETPEEGNQPWLCGESFTLADVSLAVTLHRLKFLGFARRNWGHGKRPNLETYYERVLKRKTFNKVLGHVNNILISAVLPTAFRVAKKRAPKVLGSTLVVGLLVGMGYFAFMLFRRRLGSMILALRPRPNYF
Protein: Uncharacterized protein (Q385K2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMTQNVKQVQVGKHSFPLYSHPAIRETAGTEAYVERVVQKHQNSPRVRNSVNYVARKLRQIGAMKTLNPEEHQVGEETSCAKSARTDRKHSYSPSPFEGRIPAALKSAKRNSEVCKTPMGKLQAPCSPTVCGYPLPYPRSLSHNLFNVIQDTRRKGKTNTEQSELKNEGDPLTLSPIVPKVDTSPATESKGRRREEKPLAHEGQLLKHKLDVWRDLFLASAAQQLAASGHPRSRRDDAGNVFYSNISCYLKEGCIVKSEDTDLRTGPRDHLRVQGAYLSHLAPEAFANLHVTLDGNTFVLRNVQRTSPTIKQISEELCEERGIRLLPTAMQKKVAYLVSQVSTSTKERAGTISGKKGLATSKWKHTNSLQTCKHSLNMELPEVTYRSRVLSTIREGAYGSPFQKGCKM
Protein: Genome polyprotein (K7Y1A2)
Organism: Hepacivirus hominis
Subcellular location: Host endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004291}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004291}. Virion membrane {ECO:0000256|ARBA:ARBA00004182}.
Interaction partners:
Sequence:
APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGACWTVYHGAGTRTIASPKGPVIQMYTNVDLDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVESLETTMRSPVFTDNSTPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSITVPHPNIEEVALSTTGEIPFYGKAIPLETIKGGRHLIFCHSKKKCDELAAKLVALGVNAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYRFAAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLTRLKPTLHGPTPLLYRLGAVQNEITLTHPITKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPAIIPDREVLYREFDEMEECSQHLPYIEQG
Protein: E3 ubiquitin-protein ligase RNF19A (EC 2.3.2.31) (Double ring-finger protein) (Dorfin) (RING finger protein 19A) (p38) (Q9NV58)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11237715, ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12750386, ECO:0000269|PubMed:15456787}. Note=Present in the hyaline inclusion bodies specifically found in motor neurons from amyotrophic lateral sclerosis patients. Present in the Lewy bodies specifically found in neurons from Parkinson disease patients.
Interaction partners:
- Superoxide dismutase
- NACHT, LRR and PYD domains-containing protein 11
- Ubiquitin/ISG15-conjugating enzyme E2 L6
- Synphilin-1
Sequence:
MQEQEIGFISKYNEGLCVNTDPVSILTSILDMSLHRQMGSDRDLQSSASSVSLPSVKKAPKKRRISIGSLFRRKKDNKRKSRELNGGVDGIASIESIHSEMCTDKNSIFSTNTSSDNGLTSISKQIGDFIECPLCLLRHSKDRFPDIMTCHHRSCVDCLRQYLRIEISESRVNISCPECTERFNPHDIRLILSDDVLMEKYEEFMLRRWLVADPDCRWCPAPDCGYAVIAFGCASCPKLTCGREGCGTEFCYHCKQIWHPNQTCDAARQERAQSLRLRTIRSSSISYSQESGAAADDIKPCPRCAAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCTFWGKKPWSRKKKILWQLGTLVGAPVGIALIAGIAIPAMIIGIPVYVGRKIHNRYEGKDVSKHKRNLAIAGGVTLSVIVSPVVAAVTVGIGVPIMLAYVYGVVPISLCRSGGCGVSAGNGKGVRIEFDDENDINVGGTNTAVDTTSVAEARHNPSIGEGSVGGLTGSLSASGSHMDRIGAIRDNLSETASTMALAGASITGSLSGSAMVNCFNRLEVQADVQKERYSLSGESGTVSLGTVSDNASTKAMAGSILNSYIPLDKEGNSMEVQVDIESKPSKFRHNSGSSSVDDGSATRSHAGGSSSGLPEGKSSATKWSKEATAGKKSKSGKLRKKGNMKINETREDMDAQLLEQQSTNSSEFEAPSLSDSMPSVADSHSSHFSEFSCSDLESMKTSCSHGSSDYHTRFATVNILPEVENDRLENSPHQCSISVVTQTASCSEVSQLNHIAEEHGNNGIKPNVDLYFGDALKETNNNHSHQTMELKVAIQTEI
Protein: Uncharacterized protein (Q57WY2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGDAFTKYATGSNSCISPRTAGGDSNYGSPPPNSKAPAMPSYRTETAVIPPSTPRVKGACHDNDVKEVEPPTATQQLQKVRQMFRRLDSHNDGMEEALIGLRSRIDTFRSLLATCLNGTVKELRGELRILRESTQFLVQDFAGDLEQCRRIIMRRLQGEANRRGYDPPATRSFKKDYSMEGGLSKRESSWELQQQCGAGRGEQSVFPGWRELEVREDLLEAQQRCTALEKKLKQQREAHENHLSAMKDMYESKEYTLKRRVELLERLVERDSEKLRYILSDDSKDGHGKWGKRGHFKEEQDNYYSSGDDDCDEVRESSRLHTRSKQSLKAPAQKLLKKRRGGLVKEHESHQSQHPRQGPSDSWTPMLYDDVERRVRAQLLYGRQNSPNRPKGGGSGRDVGGPQKGGECRNRLEERRLENVARRLLNAVGEAKAKQKWPQADDEADHRRVGPWRTSNDVSTVARGLWAENVLQKRAARQL
Protein: Cathelicidin-2 (CATH-2) (Fowlicidin-2) (Myeloid antimicrobial peptide 27) (Q2IAL7)
Organism: Gallus gallus (Chicken)
Function: Binds bacterial lipopolysaccharide (LPS). Has potent antimicrobial activity against Gram-positive and Gram-negative bacteria (in vitro). Has hemolytic activity (in vitro). May play a role in the innate immune response.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Cathelicidin-1
- Cathelicidin-3
- Gallinacin-1
- Gallinacin-2
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor p65
- Transcription factor Jun
- Myeloid protein 1
- Gallinacin-6
- MHC_II_alpha domain-containing protein.
Sequence:
MLSCWVLLLALLGGVCALPAPLSYPQALIQAVDSYNQRPEVQNAFRLLSADPEPGPGVDLSTLRALNFTIMETECTPSARLPVDDCDFKENGVIRDCSGPVSVLQDTPEINLRCRDASSDPVLVQRGRFGRFLRKIRRFRPKVTITIQGSARFG
Protein: Guanine nucleotide-binding protein subunit alpha-12 (G alpha-12) (G-protein subunit alpha-12) (P27600)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF12/LARG) (By similarity). GNA12-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1). GNA12-dependent Rho signaling also regulates protein phosphatese 2A activation causing dephosphorylation of its target proteins (By similarity). Promotes tumor cell invasion and metastasis by activating RhoA/ROCK signaling pathway and up-regulating pro-inflammatory cytokine production (By similarity). Inhibits CDH1-mediated cell adhesion in process independent from Rho activation (By similarity). Together with NAPA promotes CDH5 localization to plasma membrane (By similarity). May play a role in the control of cell migration through the TOR signaling cascade.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q03113}; Lipid-anchor {ECO:0000250|UniProtKB:Q63210}. Lateral cell membrane {ECO:0000250|UniProtKB:Q03113}; Lipid-anchor {ECO:0000250|UniProtKB:Q63210}. Cytoplasm {ECO:0000250|UniProtKB:Q03113}. Note=CDH1 enhances cell membrane localization. {ECO:0000250|UniProtKB:Q03113}.
Interaction partners:
- Rho guanine nucleotide exchange factor 12
- Sphingosine 1-phosphate receptor 2
- Sphingosine 1-phosphate receptor 5
- Sphingosine 1-phosphate receptor 3
- Rho guanine nucleotide exchange factor 11
- Lysophosphatidic acid receptor 1
- Sphingosine 1-phosphate receptor 4
- Lysophosphatidic acid receptor 2
- Lysophosphatidic acid receptor 6
- Lysophosphatidic acid receptor 5
Sequence:
MSGVVRTLSRCLLPAEAGARERRAGAARDAEREARRRSRDIDALLARERRAVRRLVKILLLGAGESGKSTFLKQMRIIHGREFDQKALLEFRDTIFDNILKGSRVLVDARDKLGIPWQHSENEKHGMFLMAFENKAGLPVEPATFQLYVPALSALWRDSGIREAFSRRSEFQLGESVKYFLDNLDRIGQLNYFPSKQDILLARKATKGIVEHDFVIKKIPFKMVDVGGQRSQRQKWFQCFDGITSILFMVSSSEYDQVLMEDRRTNRLVESMNIFETIVNNKLFFNVSIILFLNKMDLLVEKVKSVSIKKHFPDFKGDPHRLEDVQRYLVQCFDRKRRNRSKPLFHHFTTAIDTENIRFVFHAVKDTILQENLKDIMLQ
Protein: Replicative DNA helicase DnaB (EC 5.6.2.3) (DNA 5'-3' helicase DnaB) [Cleaved into: Endonuclease PI-MtuHIP (EC 3.1.-.-) (Mtu DnaB intein)] (P9WMR3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
Interaction partners:
- DNA primase
- Chromosomal replication initiator protein DnaA
- Uncharacterized protein Rv0057
- DNA polymerase I
- Single-stranded DNA-binding protein
- DNA ADP-ribosyl transferase
- DNA 3'-5' helicase
- Protein RecA
- Large ribosomal subunit protein bL9
- DNA polymerase III subunit alpha
Sequence:
MAVVDDLAPGMDSSPPSEDYGRQPPQDLAAEQSVLGGMLLSKDAIADVLERLRPGDFYRPAHQNVYDAILDLYGRGEPADAVTVAAELDRRGLLRRIGGAPYLHTLISTVPTAANAGYYASIVAEKALLRRLVEAGTRVVQYGYAGAEGADVAEVVDRAQAEIYDVADRRLSEDFVALEDLLQPTMDEIDAIASSGGLARGVATGFTELDEVTNGLHPGQMVIVAARPGVGKSTLGLDFMRSCSIRHRMASVIFSLEMSKSEIVMRLLSAEAKIKLSDMRSGRMSDDDWTRLARRMSEISEAPLFIDDSPNLTMMEIRAKARRLRQKANLKLIVVDYLQLMTSGKKYESRQVEVSEFSRHLKLLAKELEVPVVAISQLNRGPEQRTDKKPMLADLRESGCLTASTRILRADTGAEVAFGELMRSGERPMVWSLDERLRMVARPMINVFPSGRKEVFRLRLASGREVEATGSHPFMKFEGWTPLAQLKVGDRIAAPRRVPEPIDTQRMPESELISLARMIGDGSCLKNQPIRYEPVDEANLAAVTVSAAHSDRAAIRDDYLAARVPSLRPARQRLPRGRCTPIAAWLAGLGLFTKRSHEKCVPEAVFRAPNDQVALFLRHLWSAGGSVRWDPTNGQGRVYYGSTSRRLIDDVAQLLLRVGIFSWITHAPKLGGHDSWRLHIHGAKDQVRFLRHVGVHGAEAVAAQEMLRQLKGPVRNPNLDSAPKKVWAQVRNRLSAKQMMDIQLHEPTMWKHSPSRSRPHRAEARIEDRAIHELARGDAYWDTVVEITSIGDQHVFDGTVSGTHNFVANGISLHNSLEQDADVVILLHRPDAFDRDDPRGGEADFILAKHRNGPTKTVTVAHQLHLSRFANMAR
Protein: Myelin-associated glycoprotein (Myelin-associated glycoprotein isoform X1) (F1QSA4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Oligodendrocyte myelin glycoprotein b
- 2',3'-cyclic nucleotide 3' phosphodiesterase.
- Reticulon
- Reticulon 4 receptor.
- Oligodendrocyte transcription factor 1
- Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1-B
Sequence:
MKGLELLLLPLLLLLKDASAQWNVWMPRDISAMTNSCVVIPCSFTYPSGIRPYRGVHGIWYFGHPYPQLFPPVVLKSRTDIVHESYKGRTKLLGDLTQKNCTLLISNIGVEHSGKYYFRADLGGANIYTFPDFTKLQVLDQPNIDVPEEIVSDQSLDLTCYVPDNCPDMSPEIHWMYTDYLPDPVFTPDQVEEGNTAVLSSTLTFTPKPMHNGQLLGCRVNFPNTTYVYERLITLDIRYAPRTVWVNVSQEVMEGSSVVLHCDVDSNPAPMITWYFGDKELMSETASNSSLSLENLTPEQEGVYTCVGDNGYGNMNTSMYLAVNYPPREPWINESLTVLEGSSVSLQCTSKGNPMPTLTWLKDGELVGTITAEEGSVLELHEIMPQADGVYRCLAENEHGRASSSLNITVEFAPVLLDDSKCTIVREGVQCVCIASGNPEPAIEFYLPDLNVTINNSNNRFNYYTHSDGYTSTGVIKLQDKGERGNNGDTAVHVHCSITNIYGSETIRLELQQEKKYMMAVIVGTIGGVAVIAFIIAAVRYVGQNNKKENGNPGQDVGSKVENPSMFYSAVKKDKQSLRKKVLKTELLGSKFNSILEEGTGDDSDYQSVGPMAGMERQELNYAALEFLHGRHREGVFRRADGDGSDYTEIKAK
Protein: Olfactory receptor (Q8VG01)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363047}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Receptor-transporting protein 1
- Receptor-transporting protein 2
Sequence:
MGYTNLSYLNPGTVILIGIPGLEHVQFWIGFPFFVVCLVALLGNLFLLIIIPTERSLHQPMYIFLAVLAATDLGLCLAIAPKMLAIFWFGSCSMAFDACLTQLFFIHALQGMESGVLLAMAFDRYVAICDPLRHTAVLTPLFLLRVVLVVAIRATVLVGVLPILLKRLQWFHSVVIVHSYCEHMAVVKLAAEDVRINKSYGLFVAFAILGFDMIFVFISYILIFRAVFRLPQKEARSKAFNTCTAHIVVFLEFYILAFFSFFSHRFGHVSPYVHILLSTIYLLLPPALNPIVYGVKTKEIRKWVVQIFVLKSNTQ
Protein: No mechanoreceptor potential C, isoform H (Q9VMR4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Inactive
- Transient receptor potential cation channel trpm
- SD02261p
- MIP30126p
- Piezo-type mechanosensitive ion channel component
Sequence:
MSQPRGGRGGGRGGGVGRKTPSSLTGPPDESATPSERATPASKADSDPKDDSSSNGDKKDMDLFPAPKPPSAGASIRDTANKVLGLAMKSEWTPIEAELKKLEKYVANVGEDGNHIPLAGVHDMNTGMTPLMYATKDNKTAIMDRMIELGADVGARNNDNYNVLHIAAMYSREDVVKLLLTKRGVDPFSTGGSRSQTAVHLVSSRQTGTATNILRALLAAAGKDIRLKADGRGKIPLLLAVESGNQSMCRELLAAQTAEQLKATTANGDTALHLAARRRDVDMVRILVDYGTNVDTQNGEGQTPLHIAAAEGDEALLKYFYGVRASASIADNQDRTPMHLAAENGHAHVIEILADKFKASIFERTKDGSTLMHIASLNGHAECATMLFKKGVYLHMPNKDGARSIHTAAAYGHTGIINTLLQKGEKVDVTTNDNYTALHIAVESAKPAVVETLLGFGADVHVRGGKLRETPLHIAARVKDGDRCALMLLKSGASPNLTTDDCLTPVHVAARHGNLATLMQLLEDEGDPLYKSNTGETPLHMACRACHPDIVRHLIETVKEKHGPDKATTYINSVNEDGATALHYTCQITKEEVKIPESDKQIVRMLLENGADVTLQTKTALETAFHYCAVAGNNDVLMEMISHMNPTDIQKAMNRQSSVGWTPLLIACHRGHMELVNNLLANHARVDVFDTEGRSALHLAAERGYLHVCDALLTNKAFINSKSRVGRTALHLAAMNGFTHLVKFLIKDHNAVIDILTLRKQTPLHLAAASGQMEVCQLLLELGANIDATDDLGQKPIHVAAQNNYSEVAKLFLQQHPSLVNATSKDGNTCAHIAAMQGSVKVIEELMKFDRSGVISARNKLTDATPLQLAAEGGHADVVKALVRAGASCTEENKAGFTAVHLAAQNGHGQVLDVLKSTNSLRINSKKLGLTPLHVAAYYGQADTVRELLTSVPATVKSETPTGQSLFGDLGTESGMTPLHLAAFSGNENVVRLLLNSAGVQVDAATIENGYNPLHLACFGGHMSVVGLLLSRSAELLQSQDRNGRTGLHIAAMHGHIQMVEILLGQGAEINATDRNGWTPLHCAAKAGHLEVVKLLCEAGASPKSETNYGCAAIWFAASEGHNEVLRYLMNKEHDTYGLMEDKRFVYNLMVVSKNHNNKPIQEFVLVSPAPVDTAAKLSNIYIVLSTKEKERAKDLVAAGKQCEAMATELLALAAGSDSAGKILQATDKRNVEFLDVLIENEQKEVIAHTVVQRYLQELWHGSLTWASWKILLLLVAFIVCPPVWIGFTFPMGHKFNKVPIIKFMSYLTSHIYLMIHLSIVGITPIYPVLRLSLVPYWYEVGLLIWLSGLLLFELTNPSDKSGLGSIKVLVLLLGMAGVGVHVSAFLFVSKEYWPTLVYCRNQCFALAFLLACVQILDFLSFHHLFGPWAIIIGDLLKDLARFLAVLAIFVFGFSMHIVALNQSFANFSPEDLRSFEKKNRNRGYFSDDDMPTPRPPPVENYVDSRFSEFRRKHKDDLRMHPINSFELLFFAVFGQTTTEQTQVDKIKNVATPTQPYWVEYLFKIVFGIYMLVSVVVLINLLIAMMSDTYQRIQAQSDIEWKFGLSKLIRNMHRTTTAPSPLNLVTTWFMWIVEKVKARMKKKKRPSLVQMMGIRQASPRTKAGAKWLSKIKKDSVALSQVHLSPLGSQASFSQANQNRIENVADWEAIAKKYRALVGDEEGGSLKDSDAESGSQEGSGGQQPPAQVGRRAIKATLADTTK
Protein: Thialysine N-epsilon-acetyltransferase (EC 2.3.1.-) (Diamine acetyltransferase 2) (EC 2.3.1.57) (Spermidine/spermine N(1)-acetyltransferase 2) (SSAT-2) (Q96F10)
Organism: Homo sapiens (Human)
Function: Catalyzes the N-acetylation of the amino acid thialysine (S-(2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene group substituted with a sulfur. May also catalyze acetylation of polyamines, such as norspermidine, spermidine or spermine. However, ability to acetylate polyamines is weak, suggesting that it does not act as a diamine acetyltransferase in vivo.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:12803540}. Note=Intracellular organelles. {ECO:0000305|PubMed:12803540}.
Interaction partners:
- Diamine acetyltransferase 1
- Spermidine synthase
- Ornithine decarboxylase
- Guanidino acid hydrolase, mitochondrial
- Elongin-C
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Diamine oxidase [copper-containing]
- Peroxisomal N
- Hypoxia-inducible factor 1-alpha
Sequence:
MASVRIREAKEGDCGDILRLIRELAEFEKLSDQVKISEEALRADGFGDNPFYHCLVAEILPAPGKLLGPCVVGYGIYYFIYSTWKGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRLAVLDWNQRAMDLYKALGAQDLTEAEGWHFFCFQGEATRKLAGK
Protein: E3 ubiquitin-protein ligase IPI1 (EC 2.3.2.27) (IPA1-interacting protein 1) (Q5Z8R1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functions as an E3 ligase that promotes polyubiquitination of SPL14/IPA1 for subsequent proteasomal degradation. Regulates plant architecture by modulating SPL14/IPA1 abundance. Promotes the degradation of SPL14/IPA1 in panicles, while it stabilizes SPL14/IPA1 in shoot apices. Ubiquitinates the SPL14/IPA1-mediated complex with 'Lys-48'-linked polyubiquitin in panicles and 'Lys-63'-linked polyubiquitin chains in the shoot apex.
Subcellular location: Nucleus {ECO:0000269|PubMed:28298520}.
Interaction partners:
Sequence:
MGAEEEEEPASAVGREGGGGGGGARAAGAGAGGDTADDDDSGESAAAVVPCSICLDAVVAGGGDRSTARLQCGHEFHLDCIGSAFNAKGVMQCPNCRQIERGNWLYANGSRPSQDVSNDDWGHDEDFYDANQPETSRSVFLPFRFQWCPIGRLAQLPSVFDEGESAPPVTFHDFMGQNFTSEHLPVSAPGATPPGPYIAYFQPLQSSASSSSSHVTERTMDGTTYHDHWNPLPGPSDGRPLATVHPIDFHHNHWTHLPNSYSQPNSNNGVAEQMAIPVVPMRVGGLDSDSQQRGSLPSVYGNGSGSRSRIPSVPPMAPQFMRPHGNINEQYQQNSSSLYAAPQRRTAVQAVQDSMNFTLFPQAPTGPNSMETEDAGGNQFYAWERDRFAPYPLMPVDSEANWWGSTPQSHGVTDHSAAPGRRLFGQWIGAGRSPPPPPPPPADNSSYRQMHIPRM
Protein: Elongation of very long chain fatty acids protein (EC 2.3.1.199) (Very-long-chain 3-oxoacyl-CoA synthase) (Q9VCY6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAAVNATQVDYWNFLFTDLADPRTNDWFLIKSPLPLLGILAFYLFFVLSWGPKFMKDRKPFKLERTLLVYNFFQVALSVWMVYEGVVIWQYYSWRCQPVDWSRTPKAYREARVVYVYYLAKITELLDTIFFVLRKNDRQVTFLHVYHHTVMPMISWGTSKYYPGGHGTFIGWINSFVHIIMYSYYFLSAFGPQMQKYLWWKKYITNLQMIQFCCAFIHQTQLLYTDCGYPRWSVCFTLPNAVFFYFLFNDFYQKSYKKKQAAAKEKALSADNNNDGCAKDLNKAIQLQQEKQKAL
Protein: Prolyl 4-hydroxylase subunit alpha 2 (E7EPI9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKRQLVTNSFLHHLLIGQKRPRNAPRTLPSVTMKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEGDYYHTVLWMEQVLKQLDAGEEATT
Protein: DNA-binding protein REPIN1 (60 kDa origin-specific DNA-binding protein) (60 kDa replication initiation region protein) (ATT-binding protein) (DHFR oribeta-binding protein RIP60) (Zinc finger protein 464) (Q9BWE0)
Organism: Homo sapiens (Human)
Function: Sequence-specific double-stranded DNA-binding protein required for initiation of chromosomal DNA replication. Binds on 5'-ATT-3' reiterated sequences downstream of the origin of bidirectional replication (OBR) and a second, homologous ATT sequence of opposite orientation situated within the OBR zone. Facilitates DNA bending.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5U4E2}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5U4E2}.
Interaction partners:
- Nuclear transcription factor Y subunit beta
- Huntingtin-associated protein 1
- Nuclear transcription factor Y subunit gamma
- Leucine-rich repeat and WD repeat-containing protein 1
- Origin recognition complex subunit 4
- Origin recognition complex subunit 3
- Origin recognition complex subunit 2
- Origin recognition complex subunit 5
- Origin recognition complex subunit 1
- Origin recognition complex subunit 6
Sequence:
MLERRCRGPLAMGLAQPRLLSGPSQESPQTLGKESRGLRQQGTSVAQSGAQAPGRAHRCAHCRRHFPGWVALWLHTRRCQARLPLPCPECGRRFRHAPFLALHRQVHAAATPDLGFACHLCGQSFRGWVALVLHLRAHSAAKRPIACPKCERRFWRRKQLRAHLRRCHPPAPEARPFICGNCGRSFAQWDQLVAHKRVHVAEALEEAAAKALGPRPRGRPAVTAPRPGGDAVDRPFQCACCGKRFRHKPNLIAHRRVHTGERPHQCPECGKRFTNKPYLTSHRRIHTGEKPYPCKECGRRFRHKPNLLSHSKIHKRSEGSAQAAPGPGSPQLPAGPQESAAEPTPAVPLKPAQEPPPGAPPEHPQDPIEAPPSLYSCDDCGRSFRLERFLRAHQRQHTGERPFTCAECGKNFGKKTHLVAHSRVHSGERPFACEECGRRFSQGSHLAAHRRDHAPDRPFVCPDCGKAFRHKPYLAAHRRIHTGEKPYVCPDCGKAFSQKSNLVSHRRIHTGERPYACPDCDRSFSQKSNLITHRKSHIRDGAFCCAICGQTFDDEERLLAHQKKHDV
Protein: HEAT repeat-containing protein (Q9M033)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage stimulating factor 64
- Cleavage stimulation factor subunit 77
- 30-kDa cleavage and polyadenylation specificity factor 30
- Cleavage and polyadenylation specificity factor subunit 1
- Nuclear poly
- FIP1[V]-like protein
- Cleavage and polyadenylation specificity factor subunit 3-I
- Nuclear poly
- Flowering time control protein FY
Sequence:
MASYSRARLKDLANSAKSATELPPKLQRLRYMRRDLQKDDSVFPTELLPHLFDLLSDQFGAVRKFVAEILGEIGLKYVELIPEIVPLLIKSLEDETPAVARQVIACGADLFRSTLERVAVQGLHSSELNDLLESSWTWLIKFKDEICSVAFKQGNSGVKLCAMKFVEALILLYTPHEGIEADFNISILRGGHPVLKIGDLSIEASQKLGLLLDQLRHPAAKSLNSSTIIVLINSLSSVAKKRPAYCGRILPVLLSLDPLSFLKGVYAAATNLALKTVFLSCLKCTHPAAAPDRLTSALKEIEGGGQAAKAKDLFYKTNGSIQDKDSVEDTKVSVEENPLCASSDVAESNLSRKRSGSEYNIDLNGDASDGKRARITPSVSEESTDGLNGNDGVSLPRVASTSTGPSDSRGVSDSGPAQQLVGLFGTLVSQGEKAIGSLEILISSISADLLTDVVMANMHNIPPNCSSYADGTDELVMNMCIVGSDAQIKYPPSFVAGVLSLSTAFPPIAALINPHNEDEEVYSVHVDQQMFPAEDARTPPGLLATCDTSFPENEESNTVSPQNVHYIGNRESGIPGLESSAQHDGSGALVTNVLSSTNVEAASKNQNASFSGKLLVDVIPSMSVDKLEEFSPKAVGTVASASQFVLPKISAPVVDLSDEEKDSLQKLVFLRIVEAYKQISMSGGSQLRFSLLAHLGVEFPSELDPWKILQEHVLSDYLNHEGHELTVRVLYRLYGEAEAEQDFFSSTTAASAYESFLLTVAEALRDSFPPSDKSLSKLLGDSPHLPKSVLMLLESFCCPGSGEVEKDLQHGDRVTQGLSAVWSLILMRPGIRNDCLNIALQSAVHHLEEIRMKAIRLVANKLYSLSFITEQIEEFAKDRLFSVVSDDCDKMDLDLKSPPNKPQHSISGMSMETPSEATSSSTSVTEAQRCLSLYFALCTKVLRIFTILRLMTNLVFNIYKNASDPVKQAIHLQIPILVRTMGSSSELLKIIADPPSGSDNLLIQVLQTLTEGPTPSSELILTIRKLFDTRIKDVEILFPILPFLPRDDVLRIFPHMVNLPMEKFQVALSRVLQGSSQSGPVLSPSEALIAIHSIDPARDGIPLKQVTDACNTCFAQRQTFTQQVLAGVLNQLVQQIPLPMLFMRTVLQAIGAFPALSDFILEILSRLVSKQIWKYPKLWVGFLKCTQTTQPQSYKVLLQLPPLQLGNALTKIPALRAPLTAHASQPEIQSSLPRSTLAVLGLVPDSQGTQTSQVQANETQTSQEQQQQQASEPQQTSQSQQVSVPLSHSQVDHQEPSQVVASQSQSSPIGTVQSAMSQSQNSPIDTGRSEMSQSQNSPIDTGRSEMSQSQNSPIDTGRSEMSQSQNSPIDTGRSEMSESQSSPIGQSQSSPIGTGQSDMSQTPQVSDSSAPEPTSHTRTSDPQASSQTLRDDDEKIDDTATSENEVTEIEKSKESSEEEEEEEEEEE
Protein: 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1 (At3BETAHSD/D1) (EC 1.1.1.418) (4alpha-carboxysterol-C3-dehydrogenase/C4-decarboxylase isoform 1-1) (Reticulon-like protein B24) (AtRTNLB24) (Sterol-4-alpha-carboxylate 3-dehydrogenase 1, decarboxylating) (Q9FX01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 3beta-hydroxysteroid-dehydrogenase/decarboxylase involved in sterol synthesis. Catalyzes the formation of 3-oxosteroids from 3beta-hydroxysteroids-4alpha-carboxylate. Involved in the regulation of inflorescence internodes and leaves growth, probably by affecting auxin transporter activity possibly by altering sterol composition in the membranes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43050}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Methylsterol monooxygenase 1-2
- Methylsterol monooxygenase 1-3
- Methylsterol monooxygenase 1-1
- Methylsterol monooxygenase 2-1
- Methylsterol monooxygenase 2-2
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3
- Squalene synthase 1
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2
- Ergosterol biosynthetic protein 28
- Reticulon-like protein B18
Sequence:
MVMEVTETERWCVVTGGRGFAARHLVEMLVRYQMFHVRIADLAPAIVLNPHEETGILGEAIRSGRVQYVSADLRNKTQVVKGFQGAEVVFHMAAPDSSINNHQLQYSVNVQGTTNVIDACIEVGVKRLIYTSSPSVVFDGVHGTLNADESLPYPPKHNDSYSATKAEGEALILKANGRSGLLTCCIRPSSIFGPGDKLMVPSLVTAARAGKSKFIIGDGSNFYDFTYVENVVHAHVCAERALASGGEVCAKAAGQAYFITNMEPIKFWEFMSQLLEGLGYERPSIKIPASLMMPIAYLVELAYKLLGPYGMKVPVLTPSRVRLLSCNRTFDSSKAKDRLGYSPVVPLQEGIKRTIDSFSHLKAQNQPKTEVTETIQWKKQTLIAIVILITLYHNFVATTGSSSVIITAVSKVLLVSSIFMFINGILPEKMKVFGSKKID