wanglab/gogpt-training-data huggingface dataset:
Protein: Insulinoma-associated protein 1 (Zinc finger protein IA-1) (Q01101)
Organism: Homo sapiens (Human)
Function: Sequence-specific DNA-binding transcriptional regulator that plays a key role in neurogenesis and neuroendocrine cell differentiation during embryonic and/or fetal development. Binds to the consensus sequence 5'-[TG][TC][TC][TT][GA]GGG[CG]A-3' in target promoters. Acts as a transcriptional repressor of NEUROD1 and INS expression via its interaction with cyclin CCND1 in a cell cycle-independent manner. Negatively regulates skeletal muscle-specific gene expression in endocrine cells of the pituitary by inhibiting the Notch signaling pathway. Represses target gene transcription by recruiting chromatin-modifying factors, such as HDAC1, HDAC2, HDAC3, KDM1A and RCOR1 histone deacetylases. Binds to its own promoter, suggesting autoregulation as a self-control feedback mechanism. Competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4'. Promotes the generation and expansion of neuronal basal progenitor cells in the developing neocortex. Involved in the differentiation of endocrine cells of the developing anterior pituitary gland, of the pancreas and intestine, and of sympatho-adrenal cells in the peripheral nervous system. Promotes cell cycle signaling arrest and inhibition of cellular proliferation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q63ZV0}.
Interaction partners:
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- Neurogenic differentiation factor 1
- Neurogenin-3
- Receptor-type tyrosine-protein phosphatase-like N
- REST corepressor 1
- C-Jun-amino-terminal kinase-interacting protein 1
- Sorbin and SH3 domain-containing protein 1
- G1/S-specific cyclin-D1
- Achaete-scute homolog 1
Sequence:
MPRGFLVKRSKKSTPVSYRVRGGEDGDRALLLSPSCGGARAEPPAPSPVPGPLPPPPPAERAHAALAAALACAPGPQPPPQGPRAAHFGNPEAAHPAPLYSPTRPVSREHEKHKYFERSFNLGSPVSAESFPTPAALLGGGGGGGASGAGGGGTCGGDPLLFAPAELKMGTAFSAGAEAARGPGPGPPLPPAAALRPPGKRPPPPTAAEPPAKAVKAPGAKKPKAIRKLHFEDEVTTSPVLGLKIKEGPVEAPRGRAGGAARPLGEFICQLCKEEYADPFALAQHKCSRIVRVEYRCPECAKVFSCPANLASHRRWHKPRPAPAAARAPEPEAAARAEAREAPGGGSDRDTPSPGGVSESGSEDGLYECHHCAKKFRRQAYLRKHLLAHHQALQAKGAPLAPPAEDLLALYPGPDEKAPQEAAGDGEGAGVLGLSASAECHLCPVCGESFASKGAQERHLRLLHAAQVFPCKYCPATFYSSPGLTRHINKCHPSENRQVILLQVPVRPAC
Protein: Topoisomerase I damage affected protein 7 (P53882)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Single-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MNSNSTIGRTTLGESDTISLSFSEPSSSLNSRSTDVVFASTSTLVPQQGSLTSLPPVSSTATPTYYSTSLTYDETLHTSIDVSSTSTLVSSTDSSSSSEQDTYSSQYDPATSSYSIITPSMSIFSSTSPMSSSSSITSEWSSLTSTTPTLSSSATSLSSSWSSLSSPSSLLVSSSLSLSLSSSYSDTKLFSFDSRSSIFSPSTPTVISPSYTYLSSISATSFQISTTSELSSSWFSTISSPSTISNKDTTFPSSSRNTSTSFYSSSLSSTNDFSTISKSSKLSPSASSSTVSISTISVPTSSSVSSSSSKVPSNRPSSSSSSDDTTSAYSSTYTFQSLQSTTSSSIPPTTQTPSTSTISTSPIPTSSQVFNTVAISSSEDSKTIYYFYTQTYDITDSSTTFVTGLPTTIAVAKSEVTSFSAPSSTITADMSFYQHWLDGSLDNNKNQGTSKTNTGTIVGSVVGSVGGILICVLVVWFMLVRKRKAKRHFKENDSFCHEIGRRTGFPTTAQAKEASLQAQDSGSQQRNTETASANNPFSNEFNFKARGNPPPVPPPRNVTAMNGSFQNMRSNFMDQENRFSYGSSFTYSSLGSSTQGGFSTLSSNSIRLGRGLDNDISHDERNTVQNNSQGFLREII
Protein: Mitochondrial inner membrane m-AAA protease component AFG3L2 (EC 3.4.24.-) (EC 3.6.-.-) (AFG3-like protein 2) (Paraplegin-like protein) (Q9Y4W6)
Organism: Homo sapiens (Human)
Function: ATP-dependent protease which is essential for axonal and neuron development. In neurons, mediates degradation of SMDT1/EMRE before its assembly with the uniporter complex, limiting the availability of SMDT1/EMRE for MCU assembly and promoting efficient assembly of gatekeeper subunits with MCU. Required for paraplegin (SPG7) maturation. After its cleavage by mitochondrial-processing peptidase (MPP), it converts paraplegin into a proteolytically active mature form (By similarity). Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP). Involved in the regulation of OMA1-dependent processing of OPA1.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:10395799, ECO:0000305|PubMed:22354088, ECO:0000305|PubMed:31327635}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Complex I assembly factor TIMMDC1, mitochondrial
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Prohibitin 1
- Prohibitin-2
- Stress-70 protein, mitochondrial
- ATP-dependent clpX-like chaperone, mitochondrial
- Small ribosomal subunit protein uS12m
- Lon protease homolog, mitochondrial
- Small ribosomal subunit protein bS16m
Sequence:
MAHRCLRLWGRGGCWPRGLQQLLVPGGVGPGEQPCLRTLYRFVTTQARASRNSLLTDIIAAYQRFCSRPPKGFEKYFPNGKNGKKASEPKEVMGEKKESKPAATTRSSGGGGGGGGKRGGKKDDSHWWSRFQKGDIPWDDKDFRMFFLWTALFWGGVMFYLLLKRSGREITWKDFVNNYLSKGVVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGSVDTFERNLETLQQELGIEGENRVPVVYIAESDGSFLLSMLPTVLIIAFLLYTIRRGPAGIGRTGRGMGGLFSVGETTAKVLKDEIDVKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSTLEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDSINQKHFEQAIERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQGDMVLEKPYSEATARLIDDEVRILINDAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMVELLGPRPFAEKSTYEEFVEGTGSLDEDTSLPEGLKDWNKEREKEKEEPPGEKVAN
Protein: Non-muscle alpha-actinin 4 (Q3ULT2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVDYHAANQAYQYGPNSGGGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKQRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANMVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPSLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAAPGALDYKSFSTALYGESDL
Protein: RE12363p (Q8IGW4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKFQKAGASRRDSREVDGTVIIGRRDNSEDRTWQGQKYEKHVLKEKLPSNDLKADYLDNGWGGDPGSEDDYRDIKDSYDPVVVIDNGLEQVGVHRRYCRMTENTVLDGSGDTLINNNNNELKIMRKSTDQPMPRLPMTPKRAKGGTVSTKKPMPTVHRVLLYSTQSPRLGRKQQFSTQRLSVKQQSSKVLGAGDERQTVLLLEPEHKQEDHRSAIDFDRNDDFDEDDDLDNLSNFDESDTASVLSDTEDGYRAHAFKLTHSVDRFSSPQSTPSFLSSQSSEDDLKNPDSLLVPSLFPYVPPYLSFSSNTKRGPRVPPDLHRVLKWRITNIMPKVVRLILANSGMRMLKKTNDWMGVWGKHLKSPCFKAIRSYQKINHLPGSFRIGRKDSCWKNLQRQMGKHSNKEFGFMPRTYIIPNDLGALRRHWPKYAQRNTKWIIKPPASARGAGIRVINRWGQIPKRRPLIVQKYIERPLLINGSKFDLRLYVLVTSVNPLRVFMYHNGLARFASVKYSAKTDTLNDRCMHLTNYSINKFSSNYSKNEDVNACHGHKWTIKSLWTYLANRGVRTDCLWEALRSLVLRTILAGENGINSMIRANVESKYSCFELFGFDVILDSDLVPWLLEVNISPSLHSELPLDAHVKAPLVQGVLNTALYNVPPKLSLDKQKELAAEFSFPPGTQMCYDKRLYVNYLSREEKIKHNTFTRKSMEDRNEYVDAILNNLTPDDVRCLIIAEDELARCAPLERIFPTDQTHKYLKYNDTPRYYNRLLDAWESRYANNRTEGIALLRDYCQNKYHLQVPTPPAKKDSNDEETTPATPNTVKEEIES
Protein: E3 ubiquitin-protein ligase MARCHF4 (EC 2.3.2.27) (Membrane-associated RING finger protein 4) (Membrane-associated RING-CH protein IV) (MARCH-IV) (RING finger protein 174) (RING-type E3 ubiquitin transferase MARCHF4) (Q9P2E8)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that may mediate ubiquitination of MHC-I and CD4, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein {ECO:0000269|PubMed:14722266}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 H
Sequence:
MLMPLCGLLWWWWCCCSGWYCYGLCAPAPQMLRHQGLLKCRCRMLFNDLKVFLLRRPPQAPLPMHGDPQPPGLAANNTLPALGAGGWAGWRGPREVVGREPPPVPPPPPLPPSSVEDDWGGPATEPPASLLSSASSDDFCKEKTEDRYSLGSSLDSGMRTPLCRICFQGPEQGELLSPCRCDGSVKCTHQPCLIKWISERGCWSCELCYYKYHVIAISTKNPLQWQAISLTVIEKVQVAAAILGSLFLIASISWLIWSTFSPSARWQRQDLLFQICYGMYGFMDVVCIGLIIHEGPSVYRIFKRWQAVNQQWKVLNYDKTKDLEDQKAGGRTNPRTSSSTQANIPSSEEETAGTPAPEQGPAQAAGHPSGPLSHHHCAYTILHILSHLRPHEQRSPPGSSRELVMRVTTV
Protein: Profilin (D3U1G2)
Organism: Gossypium raimondii (Peruvian cotton) (Gossypium klotzschianum subsp. raimondii)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSWQTYVDEHLMCDIDGTGHHLSAAAIVGHDGSIWAQSSNFPKCQPKEITDIMKDFDEPGHLAPTGLHLGGAKFMVIQGEPGAVIRGKKGSGGVTIKKTAQALVFGIYEEPVTPGQCNMVVERLGDYLAEQGL
Protein: Type VI collagen alpha-1 chain (Q1T7A8)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
FSSPADITILLDGSASVGSHNFDTTKRFAKRLAERFLTAGRTDPAHDVRVAVLQYSGTGQQQPERAALQFLQNYTVLASTVDAMGFFNDATDVTDALGYVTRFYREASSGAAKKKLL
Protein: Transcription factor Sox-18B (xSox18beta) (SRY (sex determining region Y)-box 18B) (Q90ZH7)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor. Binds to the consensus DNA sequence 5'-AACAAT-3'. Also binds 5'-CACAAT-3' and 5'-AATAAT-3' but with a lower affinity. Acts partially redundantly with sox7 during cardiogenesis, acting indirectly through nodal-signaling to induce mesodermal, organizer and endodermal tissues, which then interact to initiate cardiogenesis. Also acts as an antagonist of beta-catenin signaling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
Sequence:
MHRSSYCREETTLCQGVNSTWVPPADTVPEASLTPHSPPAPDSPAPSPKPGYGYSACEEKPGDPRIRRPMNAFMVWAKDERKRLAQQNPDLHNAVLSKMLGQSWKNLTSAEKRPFVEEAERLRVQHLQDHPNYKYRPRRKKQAKKLKRMDPSHHLRNEGYTGGQPMVNLSHFRELHPLGGSGELESYGLPTPEMSPLDVLEPSEPAFFPPHMREDPDPGLFRTYQHEMDFSQEKTLREISLPYSTSPSHMGSFLRTPTPSAFYYKPHGGSSARTPLGQLSPPPEAPALDAMDHLNHAELWGDFDLNEFDQYLNMSRTQGPGYSFPMSKLGGPRTIPCEENSLISALSDASTAMYYTPCITG
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q5QPD2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGN
Protein: Copper binding protein 2 (F4YAW1)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MAIVKMVMAVVIMAASLGGKLGAAQVHHVVGGDRGWDVSSDVASWSSGRSFRVGDKIWFAYAAAQESIAEVNSPEEYESCDVSNPIRMYTDGIDGIPLDGEGIRYFVSGKEESCKNGLKLHVEVMPFGNPEPERPRVAVAAAAPTTPSGSARLYGSSVLLLAGLWLCYMAI
Protein: Decarboxylase orsB (EC 4.1.1.-) (Orsellinic acid/F9775 biosynthesis cluster protein B) (Q5AUW9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Decarboxylase; part of the gene cluster that mediates the biosynthesis of orsellinic acid, as well as of the cathepsin K inhibitors F9775 A and F9775 B. The non-reducing polyketide synthase orsA produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units. Further modifications by the decarboxylase orsB and the tyrosinase-like protein orsC lead to the production of F9775 A and F9775 B. The functions of orsD and orsE remain unclear since only orsB and orsC are required to convert orsellinic acid into F9775 A and F9775 B.
Interaction partners:
- Tyrosinase-like protein orsC
Sequence:
MTPPLLALEEHYYSTAIFNSIGETFQRTLQGVPGLADQLRSLGDGRLEAMNRGNISLQVVSHAFTPGGPSAEACRAGNDELAAEIAQISDPQRFAAFAVLPVADPTASAAELDRSVSELGFVGALIDNHADGKHFDGHDYDVLWAKACELDVPIYLHPTWPSARMAENFMGSYPVPVGISLGGPGWGWHPDVGLHVLKLFAAGVFDRFPRLKIIVGHMGEMLPYMLERASDMSTRWGGWGPRDRPLRQVWDENIWITTSGSWSLAPLKCILHNTKVERIMYSVDYPFESNERGLEWFKELEGSGLLTEEQLEMVAYRNAEDLLKVHMKKEQ
Protein: UDP-glucose 4-epimerase 5 (AtUGE5) (EC 5.1.3.2) (UDP-galactose 4-epimerase 5) (Q9SN58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the interconversion between UDP-glucose and UDP-galactose.
Interaction partners:
- ADP-glucose phosphorylase
- UTP--glucose-1-phosphate uridylyltransferase 2
- UTP--glucose-1-phosphate uridylyltransferase 1
- UDP-sugar pyrophosphorylase
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM3
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- UDP-sulfoquinovose synthase, chloroplastic
- Galactinol synthase 6
- Galactinol synthase 10
Sequence:
MMARNVLVSGGAGYIGSHTVLQLLLGGYSVVVVDNLDNSSAVSLQRVKKLAAEHGERLSFHQVDLRDRSALEKIFSETKFDAVIHFAGLKAVGESVEKPLLYYNNNLVGTITLLEVMAQHGCKNLVFSSSATVYGSPKEVPCTEEFPISALNPYGRTKLFIEEICRDVYGSDPEWKIILLRYFNPVGAHPSGDIGEDPRGIPNNLMPFVQQVAVGRRPHLTVFGNDYNTKDGTGVRDYIHVIDLADGHIAALRKLEDCKIGCEVYNLGTGNGTSVLEMVDAFEKASGKKIPLVIAGRRPGDAEVVYASTERAESELNWKAKYGIEEMCRDLWNWASNNPYGYDSSSEDNSH
Protein: GH14389p (Q95U13)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEYPPQCPCPMPQSCPKNVHTGPHIGSNIISNIDQSSSCSSSMLLSATSNSNIGGGSSSSSSSSSSTTLPACSSATTTTTASALTTSRGPVKNVTPNNSNSSGHTSTNSCRSSNNSNNSSNSSCQTIEMTSWATAATNTTSTTATTATTGTQCQMLVKTELKGENPQVTKMQYEAHVMPPPTPPESYCASDEKLLDDQEQEAELELRLRLGLGLEKSHGGQQHIEAYDLTCSTPPPVTVPQAAAVPRKARIGKSMAREMVYAAQQQLLPEKQLKQPKEAAAKLEAEPEMPFVLKAEIKAETKIKIEHDGEAQASTHISQLPDLKPTIKTEPEQELEQEAASVPSVAKTEPQPEVEVEREQQEPPVDEEQQPTPGGSKQRFNLLALSSGNKKTKTNNSYKSLIKQAEPKSYLCPGRRFIRRHGRAPAKYVKRRQMILTQRQQQRMRLQRREQQQQRRQQREAAAEVVAGAVVTPSLAGNPIEQAGSEVSIVKDQAPNSSATPSASPKRARPRKQEIAALHLLEGLDTTLSRGYFSDPELNHSSRKQAPTAVGGLYAASSPLTTATDHRGKQTTAEKRSKSETKKPPSGESSESGLPCKKPRKEPAGKVKGKGKKTTAGAAATTIASTAETQTEAVNAITASNQETNNNEYQTADLQAQKFRECPAVTDAKVAGTATSTSTASQQQNQQHSDEQHQFLVPSQPATASATAALAATPPPSRQGQATHTKRTRSRCKFGNRKRQRHRPGGVSYELDVTQPPATKANVVPKWNNGWMWAGKAFQGAVFLNSDDPLVLRTCYPAMRHVEGDIIRIRDCVLLKANEDNELPYVAKVAHLWQNPEDGEMMMSLLWYYRPEHTDQGRQRNDCPDEVYASRHRDHNSVACVEDKCYVLTFSEYCRYRRRLRAAEEDVEDVSIVPRRPSIATAPGFPVRTVPEHTNPELVMFCRRAYEFRTRRLLKLPHKNGLVCSSS
Protein: Iron regulatory protein 1B (EC 4.2.1.3) (Q9VGZ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361275}.
Interaction partners:
- Isocitrate dehydrogenase
- Citrate synthase
- Probable citrate synthase, mitochondrial
- ATP-citrate synthase
- non-specific serine/threonine protein kinase
- Frataxin homolog, mitochondrial
- Probable isocitrate dehydrogenase subunit alpha, mitochondrial
- Mitoferrin
- Isocitrate dehydrogenase
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
Sequence:
MSGANPFAQFEKTFSQAGTTYKYFDLASIDSKYDQLPYSIRVLLESAVRNCDNFHILEKDVQSILGWSPALKQGSNDVEVSFKPARVILQDFTGVPAVVDFAAMRDAVLDLGGDPEKINPICPADLVIDHSVQVDFARAPDALAKNQSLEFERNKERFTFLKWGAKAFNNMLIVPPGSGIVHQVNLEYLARVVFENDATDGSKILYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQSISMLLPEVIGYKLEGKLSPLVTSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFPIDENTLGYMKQTNRSEKKIDIIRQYLKATQQLRNYADAAQDPKFTQSITLDLSTVVTSVSGPKRPHDRVSVSDMPEDFKSCLSSPVGFKGFAIAPEAQSAFGEFQWDDGKTYKLHHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEKGLSILPYIKTSLSPGSGVVTYYLKESGVIPYLEKLGFDIVGYGCMTCIGNSGPLEENVVNTIEKNGLVCAGVLSGNRNFEGRIHPNTRANYLASPLLVIAYAIAGRVDIDFEKEPLGVDANGKNVFLQDIWPTRSEIQEVENKHVIPAMFQEVYSKIELGSQDWQTLQVSEGKLFSWSADSTYIKRPPFFEGMTRDLPKLQSIQKARCLLFLGDSVTTDHISPAGSIARTSPAARFLSERNITPRDFNSYGSRRGNDAIMSRGTFANIRLVNKLVEKTGPRTVHIPSQEELDIFDAAERYREEGTPLVLVVGKDYGSGSSRDWAAKGPFLLGVKAVIAESYERIHRSNLVGMGIIPLQFLPGQSAETLNLTGREVYNIALPESGLKPGQKIQVEADGTVFETILRFDTEVDITYYKNGGILNYMIRKMLS
Protein: Glutamate receptor interacting protein 2 (E0CXE0)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MVELIKREGSTLGLTISGGTDKDGKPRVSNLRPGGLAARSDLLNVGDYIRSVNGIHLTRLRHDEIITLLKNVGERVVLEVEYELPPPAPENNPRIISKTVDVSLYKEGNSFGFVLRGGAHEDLHKSRPLVLTYVRPGGPADREGSLKVGDRLLSIDGIPLHGASHATAIATLQQCSHEALFQVEYDVATPDTVANASGPLVVEIAKTPGSALGISLTTGSHRNKPAITIDRIKPASVVDRSGALHAGDHILAIDGTSTEHCSLVEATKLLASVTEKVRLEILPSPQSRRPLKPPEAVRIQRSEQLHRWDPSAPSCHSPRPSHCRAPTWAAGGPDQSRSVSSTPFSSPTMNPAFPCANASTLPRGPMSPRTTAGRRRQRRKEHRSSLSLASSTVGPGGQIVHTETTEVVLCGDPLSGFGLQLQGGIFATETLSSPPLVRFIEPDSPAERCGLLQVGDRVLAINGIATEDGTMEEANQLLRDAALARKVVLEIEFDVAESVIPSSGTFHVKLPKRRGVELGITISSASRKRGEPLIISDIKKGSVAHRTGTLEPGDKLLAIDNIRLDHCPMEDAVQILRQCEDLVKLKIRKDEDNSDEQESSGAVSYTVELKRYGGPLGITISGTEEPFDPIIISGLTKRGLAERTGAIHVGDRILAINSVSLKGRPLSEAIHLLQVAGETVTLKIKKQLDRPLLPRQSGSLSEASDVDEDPPEALKGGLLATRFSPAVPSVDSAVESWGSSATDGGFGGTGSYTPQVAVRSVTPQEWRPSRLKSSPPPLEPRRTSYTPGPSDESFPEEEGDWEPPMRRPVSPLSTPSHLPLF
Protein: Protein RFS1 (RAD55 suppressor protein 1) (P38234)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Membrane raft {ECO:0000269|PubMed:19064668}.
Interaction partners:
- Protoplast secreted protein 2
- Flavoprotein-like protein YCP4
- Uncharacterized protein YBR053C
- Suppressor of hydroxyurea sensitivity protein 2
- Platinum sensitivity protein 3
- Uncharacterized glycosyl hydrolase YBR056W
- Putative uncharacterized protein YBR051W
Sequence:
MPKVAILIYSVDDIIATLAENEKKGIEIAGGEAEIFQVPDVSYKTEYATEEGKEAAKVAKTNADFSYKILTRETLVEYDYYLFGIPTKFGNFPAEWKSFWDSNTGGLWAKGSLHGKIAGLFVSGAISGKGDTEMCIMNAMSTLVHHGVIYVPLGYKNAYKELTDVEDVNGSCAWGAGCVSGIDGGRPPSLSELRVHQLQGKAFYDRIKDL
Protein: Calcium permeable stress-gated cation channel 1 (Transmembrane protein 63C) (D3ZNF5)
Organism: Rattus norvegicus (Rat)
Function: Acts as an osmosensitive calcium-permeable cation channel (By similarity). Required for the functional integrity of the kidney glomerular filtration barrier.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9P1W3}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8CBX0}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at mitochondria-ER contact sites. {ECO:0000250|UniProtKB:Q9P1W3}.
Interaction partners:
- Inner centromere protein
- Inactive ubiquitin thioesterase OTULINL
Sequence:
MTASPESMGQKFRNMTANECFQSRSTVLQGQPFGGIPTVLLLNIILWVCVVLVYSFLRKAAWDYGRLALLIHNDSLTSLIYGEQSEKSSPSEVYLEAERRDKGFSTWFFNSLTMRDRDLINKCGEDARIYIMFQYHLIIFVLILCIPSLGIILPVNYIGSALDWSSHFGRTTIVNVSTESQFLWLHSIFAFMYFLTNFAFMGHHCLGFVPKKNLHFTRTLMITYVPTEIQDPETISKHFHEAYPGCVVTRVHFCYDVRNLIDLDDQRRHAMRGRLYYTAKAKKTGKVMIKVHPCSHLCFCKCWTCFKEVDAEQYYSELEEQLTDEFNAELNRVQLKRLDLIFVTFQDARTVKRIHNDYKYINCGRHPMQSSVTTIVKNNHWRVARAPHPKDIIWKHLSIRRFSWWARFIAINTSLFFLFFFLTTPAIIINTIDMYNVTRPIEKLQSPVVTQFFPSVLLWAFTVIMPLLVYFSAFLEAHWTRSNQNLIIMYKCYIFLVFMVVILPSMGLTSLDVFLRWLFDIYYLEHATIRFQCVFLPDNGAFFINYVITSALFGTGMELMRLGSLCTYCTRLFLSRSEPERVHIRKNLAMDFQFGREYAWMLNVFSVVMAYSITCPIIVPFGLLYLCMKHITDRYNMYYSYAPTKLNAQIHMAAVYQAIFAPLLGLFWMLFFSILRVGSLHSITLFSLSSIIISVIIAFSGVFLGKFRIAQQYEQPEEETETVFDVEPSSTTSTPTSLLYVATVLQEPELNLTPASSPARHTYGTMNSQPEEGEEESGLRGFARELDPAQFQEGLELEGQSH
Protein: A disintegrin and metalloprotease (A3QZA9)
Organism: Pneumocystis carinii
Interaction partners:
Sequence:
MQYLFKYMTLFPLLKGIHASLITQQTNIHEIFTLEDVVLYPHEISKKSIDSYSSFDLTFALPYHYQQTEYPNWMKKYVKLTMTPNLDLINENSHLQIHNEDGEVISSEKIDRNNHRVYRGDAFVTYTENSIGLLEKRWHKIGWARISLHQDGDLPIFEGTFSLSNDLYTVKTAKNYMLLKEAHEPQISASEKSMVLWIESNKPPKTLRKRSNLYLDNKCMLNSIYDEPTPLDQATFSYGSGEISAGEKLALSSSRIRLTNYIGDNSGCPKYKQVAYVGAALDCNYISMFESSSNATNHIISLYNRVSAIYEETFNISLGLLNVTIMGRTCPNENPKVSWNVACSSHYNISTRLKHFSLWRSGIKDSIALWSLFTTCRNTMEVGIAWYGVLCQDIIPKGPHSNWVSGTNVIASPANIEHIVLAHEIGHGFGASHDCTSESCKNESASCCPLSSTVCDTNEMYIMNPKSSISARKFSPCSIGQVCNNLKKKLVNSNCLKNNKNVSLISRRKCGNGIVEEGEDCDCGGEKGCKGNPCCNPKTCKFTKGSVCE
Protein: Histone deacetylase 4 (HD4) (EC 3.5.1.98) (P83038)
Organism: Gallus gallus (Chicken)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6NZM9}.
Interaction partners:
- Protein kinase domain-containing protein.
- Calcium/calmodulin-dependent protein kinase type IV
- Deacetylase sirtuin-type domain-containing protein.
- Nuclear pore complex protein Nup155
- Mothers against decapentaplegic homolog 3
- Paired amphipathic helix protein Sin3a
- G1/S-specific cyclin-D1
- SUMO-conjugating enzyme UBC9
Sequence:
MSSQSHPDGLSGRDQPVELLNPPRVNHMPSSVDVSTALPLQVAPTSVPMDLRLDHQFPMPVTEPTLREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQEMLAMKHQQELLEHQRKLEQHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRFWYGKTQHSSLDQSSPPQSGVSGTYNHPVLGMYDSKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACNSAPGSGPSSPNNSSNNISAENGITGSVTSIQAETSLAHRLVNREGSVTQLPLYTSPSLPNITLGLPATGPSSGGSAQQDAERLAIPALQQRISLFPGTHLTPYLSTTTLERDGGTAHNPLLQHMVLLEQPTAQTPLVTGLPLHAQSLVGGERVSPSIHKLRQHRPLGRTQSAPLPQNAQALQQLVIQQQHQQFLEKHKQQFQQQQLHINKIISKPNEPARQHESHPEETEEELREHQALLEEPYSDRVSSQKEVPGLANMVQVKQEPIESDEEEAEPQQELESGQRQAEQELLFRQQALLLEQQRIHQLRNYQASLEAAGMPVSFGGHRPLSRAQSSPASATFPMSVQEPPTKPRFTTGLVYDTLMLKHQCTCGNTNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLTSMFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVIELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGTGAGVGFNVNMAFTGGLDPPMGDTEYLTAFRTVVMPIANEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGRVVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRANANAVHSMEKVIEIHSKYWHSLQRYASTVGYSLVEAQKCENEEAETVTAMASLSVGVKPAEKRPDDEPMEEEPPL
Protein: Rab proteins geranylgeranyltransferase component A 1 (Choroideremia protein homolog) (Rab escort protein 1) (REP-1) (Q9QXG2)
Organism: Mus musculus (Mouse)
Function: Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
- Ras-related protein Rab-7a
- Geranylgeranyl transferase type-2 subunit beta
- Ras-related protein Rab-3A
- Ras-related protein Rab-27A
- Rab proteins geranylgeranyltransferase component A 2
- Ras-related protein Rab-38
- Ras-related protein Rab-1B
- Ras-related protein Rab-6A
- Ras-related protein Rab-27B
Sequence:
MADNLPSDFDVIVIGTGLPESIIAAACSRSGQRVLHVDSRSYYGGNWASFSFSGLLSWLKEYQENSDVVTENSMWQEQILENEEAILLSSKDKTIQHVEVFCYASQDLHKDVEEAGALQKNPASVMSAQATEAAEAAEAAEATEAAEAAEAAEAACLPTAEESLSTRSCELPAEQSQCMGPESSPQVNDAEVGEKETQSDAKSSTEQSSEILPKVQDNTETPKRNVITYSQIIKEGRRFNIDLVSKLLYSRGLLIDLLIKSNVSRYAEFKNITRILAFREGTVEQVPCSRADVFNSKQLTMVEKRMLMKFLTFCVEYEDHPDEYKAYEETTFSEYLKTQKLTPNLQYFVLHSIAMTSETTSSTVDGLKATKKFLQCLGRYGNTPFLFPLYGQGELPQCFCRMCAVFGGIYCLRHSVQCLVVDKESRKCKAIVDQFGQRIISKHFVIEDSYLSENTCSGVQYRQISRAVLITDGSVLKPDSDQQVSILTVPAEESGSFAVRVIELCSSTMTCMKGTYLVHLTCMSSKTAREDLERVVQKLFTPYTEIEAENEQVEKPRILWALYFNMRDSSDISRDCYNDLPSNVYVCSGPDCNLGNDNAVQQAEIVFQKICPNEDFCPAPPNPEDIILDGDSSQQEVSESSVIPETNSETPKESTVLGDSEEPSE
Protein: EP300-interacting inhibitor of differentiation 2B (EID-2B) (EID-2-like inhibitor of differentiation 3) (EID-3) (Q96D98)
Organism: Homo sapiens (Human)
Function: Acts as a repressor of MYOD-dependent transcription, glucocorticoid receptor-dependent transcription, and muscle differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:15970276}.
Interaction partners:
- Melanoma-associated antigen E1
Sequence:
MAEPTGLLEMSELPGDSSVPQVGTASGVSDVLRGAVGGGVRVQEAREGPVAEAARSMARMPGPVPGPIPSSVPGLASAPDPHQQLAFLEINRQLLFREYLDGSSMIPVRLLRDFEERRRLFVEGCKAREAAFDADPPQMDFAAVAFTVALTASEALSPLAD