wanglab/gogpt-training-data huggingface dataset:
Protein: Ligand-gated ion channel pHCl-B (Q5D6W0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
FDESSSDKEILDLLLEKKRYDKRLLPPVNDEDFCCGLQSPDMATNQNARRPHNRGTLTVNVNVLLLSLASPDESSLKYEVEFLLNQQWNDPRLQYGNKSHYDFLNALHHHDSIWTPDTYFIMHGDFKDPIIPMHFALRIFRNGTITYAMRRHLILSCQGSLHIFPFDDPKCSFSMESISYEEAQIKYVWKNDEDTLRKSPSLTTLNAYLIKNQTTACDQNSWRGNYSCLRVDLIFTRDRAFYFTTVFIPGIILVTSSFITFWLEWNAVPARSMIGVTTMLNFFTTSNGFRSTLPVVSNLTAMNVWDGVCMCFIYASLLEFVCVNYVGRKRPLHNVVYRPGENPVTQPGEKRQNAGAPNEIVACTTCGGSNSPCTHSANNGCATETCFVQVRKKEPPHPIRVAKTIDVIARITFPTAYAIFLIFFFVHYKGFS
Protein: Matrin-type domain-containing protein (Q3TXU6)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFNPQLQQQQQLQQQQQQLQQQLQQQQLQQQQQQILQLQQLLQQSPPQASLSIPVSRGLPQQSSPQQLLSLQGLHSTSLLNGPMLQRALLLQQLQGLDQFAMPPATYDGASLTMPTATLGNLRAFNVTAPSLAAPSLTPPQMVTPNLQQFFPQATRQSLLGPPPVGVPINPSQLNHSGRNTQKQARTPSSTTPNRKDSSSQTVPLEDREDPTEGSEEATELQMDTCEDQDSLVGPDSMLSEPQVPEPEPFETLEPPAKRCRSSEESTEKGPTGQPQARVQPQTQMTAPKQTQTPDRLPEPPEVQMLPRIQPQALQIQTQPKLLRQAQTQTSPEHLAPQQDQVEPQVPTQAQSQEQTSEKTQDQPQTWPQGSVPPPEQASGPACATEPQLSSHAAEAGSDPDKALPEPVSAQSSEDRSREASAGGLDLGECEKRAGEMLGMWGAGSSLKVTILQSSNSRAFNTTPLTSGPRPGDSTSATPAIASTPSKQSLQFFCYICKASSSSQQEFQDHMSEAQHQQRLGEIQHSSQTCLLSLLPMPRDILEKEAEDPPPKRWCNTCQVYYVGDLIQHRRTQEHKVAKQSLRPFCTICNRYFKTPRKFVEHVKSQGHKDKAQELKTLEKETGSPDEDHFITVDAVGCFESGQEEDEDDDEEEEEEGEIEAEEEFCKQVKPRETSSEQGKGSETYNPNTAYGEDFLVPVMGYVCQICHKFYDSNSELRLSHCKSLAHFENLQKYKAKNPSPPPTRPVSRKCAINARNALTALFTSSHQPSPQDTVKMPSKVKPGSPGLPPPLRRSTRLKT
Protein: Uncharacterized protein (Q38CI5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNVYGKDQRIHNGSRTKAESWVMHSFTAITGLQASCIAVCLFRMRGRLDNVLQNSYFITSPLQLNPVYHSQSCALEVNEDIAMFRNVTYTITGENVEYFFSRGAFNTRILFFLVAMTTFIALVNHTLLWLDISKIRYHFVVIRKDPLAVFQVSAAVAGIFQNYIVSREHKYMNDYLNTCNAPDRPSLHSVTPFIELYLLFGGTLVTFLINFLIAVILRCQKNPKEELIRENELMQMEKSMTGELPFSGDQLMLSQRSRGDANVSNSSIPNQRLAHSRGPSEGKEFRHVDPLASPTSQLSFARRDSVPASRVSVAREGRLSRGESARRALPSQASAWPPVSGRRSFTGPVSAPAFDDIIGDSTHR
Protein: Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.356) (B5DFE2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein Jumonji
- Polycomb protein EED
- SUZ12 polycomb repressive complex 2 subunit
- DNA
- Zinc finger protein AEBP2
- RB-binding protein 4, chromatin-remodeling factor.
- DNA
- Histone deacetylase 1
- Metal-response element-binding transcription factor 2
- Histone deacetylase 2
Sequence:
MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKTMFSSNRQKILERTETLNQEWKQRRIQPVHIMTSVSSLRGTRECSVTSDLDFPAQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPDEREEKQKDLDDSRDDKETCPPRKFPADKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTISVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPVPTEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP
Protein: Ribosomal lysine N-methyltransferase set11 (EC 2.1.1.-) (Meiotically up-regulated gene 76 protein) (SET domain-containing protein 11) (O74405)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that trimethylates 60S ribosomal protein L12 (rpl1201 and rpl1202) at 'Lys-4' and may dimethylate L12 also at 'Lys-40' and 'Lys-41'. Overexpression causes a severe growth defect. Has a role in meiosis.
Subcellular location: Cytoplasm. Nucleus, nucleolus.
Interaction partners:
- Cytochrome c
Sequence:
MSNKQNIESEVSWVKSKGAFVHPSLEFSVIPDAGSCVLANNDINENTVLLKLPPNILINKRTCSRYSFRDKLTSFQFLSWLISEDVHSNLEISPYYTKALPQGFSFHPVTLTSDHPLWSILPDEVRNSLLERKNVMAFDYEQVKKFVSVDQPTFQWGWLCVNTRCLYYDTGSKNTEDHLTLAPIFEYFNHSPEAQTALINTRGTITIKSTRRIDKGEQIFLCYGPHGNDKLFTEYGFCLSNNPNISIQLDRFIEFDKWQQSFLQDHGYWNDYTCSLHGASFRTLVGVRTLLVSPSEKLNDASYDQTRRVLQYINGFSDGSRDRQDVEDYLKKVLQELLCEAEECKEKVKGISDGSYVFICAEQLWKDRIMCCQYLMEHSFE
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (B4E2Q0)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
Sequence:
MDSLLPPSRFSYFKKYPLHAIRRYLSTLRNQRAEEQVARFQKIPNGENETMIPVLTSKKASELPVSEVASILQADLQNGLNKCEVSHRRAFHGWNEFDISEDEPLWKKYISQFKNPLIMLLLASAVISVLMHQFDDAVSITVAILIVVTVAFVQEYRSEKSLEELSKLVPPECHCVREGKLEHTLARDLVPGDTVCLSVGDRVPADLRLFEAVDLSIDESSLTGETTPCSKVTAPQPAATNGDLASRSNIAFMGTLVRCGKAKGVVIGTGENSEFGEVFKMMQAEEAPKTPLQKSMDLLGKQLSFYSFGIIGIIMLVGWLLGKDILEMFTISVSLAVAAIPEGLPIVVTVTLALGVMRMVKKRAIVKKLPIVETLGCCNVICSDKTGTLTKNEMTVTHIFTSDGLHAEVTGVGYNQFGEVIVDGDVVHGFYNPAVSRIVEAGCVCNDAVIRNNTLMGKPTEGALIALAMKMGLDGLQQDYIRKAEYPFSSEQKWMAVKCVHRTQQDRPEICFMKGAYEQVIKYCTTYQSKGQTLTLTQQQRDVYQQEKARMGSAGLRVLALASGPELGQLTFLGLVGIIDPPRTGVKEAVTTLIASGVSIKMITGDSQETAVAIASRLGLYSKTSQSVSGEEIDAMDVQQLSQIVPKVAVFYRASPRHKMKIIKSLQKNGSVVAMTGDGVNDAVALKAADIGVAMGQTGTDVCKEAADMILVDDDFQTIMSAIEEGKGIYNNIKNFVRFQLSTSIAALTLISLATLMNFPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRKPPRNWKDSILTKNLILKILVSSIIIVCGTLFVFWRELRDNVITPRDTTMTFTCFVFFDMFNALSSRSQTKSVFEIGLCSNRMFCYAVLGSIMGQLLVIYFPPLQKVFQTESLSILDLLFLLGLTSSVCIVAEIIKKVERSREKIQKHVSSTSSSFLEV
Protein: AT3G19900 protein (Q8LDI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein NAP1
- Protein ABIL1
- Dirigent protein 16
- Dirigent protein 18
- Protein PIR
- Actin-related protein 2/3 complex subunit 3
- At4g14145
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2
Sequence:
MMSIVSSHHHCQQSVIHERSGIGTISKVSCSRYCGPCFSGRLAFSHSLCLKTTYGKTDRRKFSRICSIVDDEGNLDNSDDEEKESLDDKTKRQANDMNRANLERMVGSDDSAFNGLDLATLIRQKYGKSYDVQLIKKEFMGKNLLAMNVMWKYREQRSFPLTEEEYILRLDDVANMLKCWGAVSHIRSSLAKSKERPRIGKAVSIFIDMDSTGGRANEWIYK
Protein: E3 ubiquitin-protein ligase HECTD3 (EC 2.3.2.26) (HECT domain-containing protein 3) (HECT-type E3 ubiquitin transferase HECTD3) (Q5T447)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus facilitating cell cycle progression by regulating the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}.
Interaction partners:
Sequence:
MAGPGPGAVLESPRQLLGRVRFLAEAARSLRAGRPLPAALAFVPREVLYKLYKDPAGPSRVLLPVWEAEGLGLRVGAAGPAPGTGSGPLRAARDSIELRRGACVRTTGEELCNGHGLWVKLTKEQLAEHLGDCGLQEGWLLVCRPAEGGARLVPIDTPNHLQRQQQLFGVDYRPVLRWEQVVDLTYSHRLGSRPQPAEAYAEAVQRLLYVPPTWTYECDEDLIHFLYDHLGKEDENLGSVKQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEGDNLKKLSDVSIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPTSLVRYPRLEGTDPEVLYRRAVLLQRFIKILDSVLHHLVPAWDHTLGTFSEIKQVKQFLLLSRQRPGLVAQCLRDSESSKPSFMPRLYINRRLAMEHRACPSRDPACKNAVFTQVYEGLKPSDKYEKPLDYRWPMRYDQWWECKFIAEGIIDQGGGFRDSLADMSEELCPSSADTPVPLPFFVRTANQGNGTGEARDMYVPNPSCRDFAKYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSKDFPAVDSVLVKLLEVMEGMDKETFEFKFGKELTFTTVLSDQQVVELIPGGAGIVVGYGDRSRFIQLVQKARLEESKEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLTRFEDFEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPARIYIYPDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYAAYNCVAIDTDMSPWEE
Protein: Enhancer of polycomb homolog (A0A8I6G2P8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU361124}.
Interaction partners:
Sequence:
MSKLSFRARALDASKPLPVFRCEDLPDLHEYASINRAVPQMPTGMEKEEESEHHLQRAISAQQVYGEKRDNMVIPVPEAESNIAYYESIYPGEFKMPKQLIHIQPFSLDAEQPDYDLDSEDEVFVNKLKKKMDICPVQFEEMIDRLEKGSGQQPVSLQEAKLLLKEDDELIREVYEYWIKKRKTCRGPSLIPSVKQEKRDGSSTNDPYVAFRRRTEKMQTRKNRKNDEASYEKMLKLRRDLSRAVTILEMIKRREKSKRELLHLTLEIMEKRYNLGDYSGEIMSEVMAQRQPVKPTYAIPIIPITNSSQFKHQDVTDAKEFKVNKQDKADLIRPKRKYEKKPKVLPSSAAAPQQPSPAALPGFSAKDLNQYDFPSSDEEPLSQVLSGSSEAEEENDPDGPFAFRRKAGCQYYAPHLDQTGNWPWTSPKDGGLGDVRYRYCLTTLTVPQRCLGFARRRVGRGGRVLLDRAHSDYDSMFHHLDLDMLSSPQPSPVNQFANTSETNTSDRPSSKDLSQILVDIKSCRWRHFRPRTPSLPDSDSGELSSRKLHRSISRAGPAQPGAHTCSASTQSRSSSGSTHCAFTAEQYQQHQQQLALMQQQQLAQTQQQQANSSSSTAAPQGFVSKTLDSASAQFAASALMTSEQLMGFKMKDDVVLGIGVNGVLPASGVYKGLHLSSTTPTALVHTSPSTAGSTLLQPSNITQTSGSHSALSHQVTAANSATTQVLFGNNIRLTVPSSVPTVNSIAPINARHIPRTLSAVPPSALKLAAAANCQVSKVPSSSSVDSVPRENHESEKPALNNIADNTVAMEVT
Protein: Interleukin 12 receptor subunit beta 2 (F1LRH7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Interleukin-12 receptor subunit beta-1
- Tyrosine-protein kinase JAK2
- Interleukin-12 subunit alpha
- Tyrosine-protein kinase
- Paralemmin 3
- Interleukin-12 subunit beta
- Signal transducer and activator of transcription 1
- Interleukin-6
- Interleukin-4
- Interferon gamma
Sequence:
MAHTVRGCSLALIFLFMWLLIKANIDVCKLGTVTVQPAPVIPLGSTANISCSLNPKQGCSHYPSYNELILLKFVNDVLVEKLHGKKVHGHPSHSSIFQVTNLSLGMTLFVCKLNCSNSQKTQPVPVCGVEISVGVAPESPQSISCVQKGEHGTVACSWNSGKVTYLKTYYTLQLTGPNNVTYQNQCYSDNRQNCSRLDLGINLTPDLAESRFIVHVTATNDLGNSSSLLHTFTFLDIVRPLPPWDIRINFLNASGSRCTLQWEDEGQVVLNRLRYQPLNSTSWNMVNATNAKGRYDLQDLRPFTEYEFQISSKLHLSQGSWSNWSESLRTRTPEEEPVGTLDIWYMKQDIDCDRQQISLFWKSLNPSEARGKILHYQVTLQEVTKKTTLQNTTRHTFWTGVIPRTGAWTASVSAANSKGTSAPTHINIVDLCGTGFLAPHQVSAKSGNMDNIMVTWQPPGKADSVIREYIVEWRALQQGSVMNLTPHWLRIPPYNMSALISEKIKPYICYEIRVHALSEDQGGCSSIRGDSSHKVPLSGPHITAITEKKESLFISWTHIPFLEQRGCILHYRIYWKERHSTAQPELCEIQYRHSQNSHPISSLQPKVTYVLWMTAVTAAGESPQGNEREFCPQGKANWKTFVISSICIAIIVVGTFSIRYFRQKAFTLLSTLKPQWYCRTIPDPANSTWVKKYPIMEEKIQPPMDNLLMAWSAPEEPEPLIINEVLYQMIPVGRQPYCFKRGQGFQGYSTSKEDTIYLATNPQTTGTLTAESRQLVNLYKVLGSRDPDSKLGNLTSPLTVTPVNYLPTHEGYLPSNIEDLSSHEVDPSDSLDLDHQHISLSIFASSSLRPLTFCGERLTLDRLKMGYEK
Protein: Selenoprotein P (SeP) [Cleaved into: Selenoprotein Se-P10; Selenoprotein Se-P6; Selenoprotein Se-P2; Selenoprotein Se-P1] (P25236)
Organism: Rattus norvegicus (Rat)
Function: Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis.
Subcellular location: Secreted {ECO:0000269|PubMed:2037562}. Note=Passes from plasma into the glomerular filtrate where it is removed by endocytosis mediated by LRP2 in the proximal tubule epithelium. {ECO:0000250|UniProtKB:P70274}.
Interaction partners:
- Selenoprotein W
- Type I iodothyronine deiodinase
- Methionine-R-sulfoxide reductase B1
- Glutathione peroxidase 1
- Selenoprotein S
- Selenoprotein K
Sequence:
MWRSLGLALALCLLPYGGAESQGQSPACKQAPPWNIGDQNPMLNSEGTVTVVALLQASUYLCLLQASRLEDLRIKLENQGYFNISYIVVNHQGSPSQLKHAHLKKQVSDHIAVYRQDEHQTDVWTLLNGNKDDFLIYDRCGRLVYHLGLPYSFLTFPYVEEAIKIAYCEKRCGNCSFTSLEDEAFCKNVSSATASKTTEPSEEHNHHKHHDKHGHEHLGSSKPSENQQPGALDVETSLPPSGLHHHHHHHKHKGQHRQGHLESUDMGASEGLQLSLAQRKLURRGCINQLLCKLSEESGAATSSCCCHCRHLIFEKSGSAITUQCAENLPSLCSUQGLFAEEKVIESCQCRSPPAAUHSQHVSPTEASPNUSUNNKTKKUKUNLN
Protein: Flotillin-2 (Epidermal surface antigen) (ESA) (Membrane component chromosome 17 surface marker 1 homolog) (Q60634)
Organism: Mus musculus (Mouse)
Function: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. May be involved in epidermal cell adhesion and epidermal structure and function.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250}; Peripheral membrane protein {ECO:0000269|PubMed:9153235}. Endosome {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q14254}; Lipid-anchor {ECO:0000250|UniProtKB:Q14254}. Note=Membrane-associated protein of caveolae. {ECO:0000250}.
Interaction partners:
- Flotillin-1
- Cadherin-1
- Catenin beta-1
- Coronin-1C
- Catenin delta-1
- Catenin alpha-1
- E3 ubiquitin-protein ligase CBL
- Caveolin-1
- Stomatin
- CD81 antigen
Sequence:
MGNCHTVGPNEALVVSGGCCGSDYKQYVFGGWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEIVVLSGDNSKVTSEVNRLLAELPASVHALTGVDLSKIPLIKNATGAQV
Protein: SCL-interrupting locus protein homolog (Q8JGS1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays an essential role in early embryonic development. Plays an important role in the regulation of centriole duplication (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q60988}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q15468}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q15468}.
Interaction partners:
- Centrosomal P4.1-associated protein
- Serine/threonine-protein kinase PLK4
- Spindle assembly abnormal protein 6 homolog
- Abnormal spindle-like microcephaly-associated protein
- WD repeat domain 62
- Centrosomal protein of 135 kDa
- Centrosomal protein 192.
- Microcephalin 1
- Centrosomal protein of 63 kDa
- Kinesin family member 11
Sequence:
MNRVQVDFKGLPAHILENSIAAESLQNTRSSDNVLTPLTFPKSKVALWDPSANGEVVSLHFSYYRNPRLFLVEKALRLAHRHARQTNKPRFFCFLLGTLAVDSDEEGVTITLDRFDPGREQTGCLGKAPTALLPGDILVPCVFEAQHAASSTVHSSEDLNISFKMLQHFCCSKELLELSKLLTLRAQLSCSENMDRLTFNLSWAAVTLACTLDAVPIRAVPIIPTALARNLSSPAGVTQNSKRGFLTMDQTRKLLLILESDPKAYTLPLVGIWLSGVTHIHNPLVWAWCLRYLHSSSLQDKVLSEGGTFLVVLYSLTHRDPEFYQCKPSTGQQQLSFQLLTSRDSLTLYKNVEPSEGRPLQFELSSENQNQETVLFEEVLSQSVLTGTTLGAASAAPQNKLSISDHDSGVEDEDLSPRPSPNPHPVSQQTKRVHPLVPELSMVLDGSFLDGSVVNTQGSTPLSHSQSNVHRRNSSPALQGLSVLRPLVQGSVTKPPPIRRPLTPILSQPKNKLHPNPSQQTPQHSVSRKSLPSMRRSREGSSASSVSSSSSSSSTKNASPNGSFHQQRQRLSQGFPNKPQLIYSGPPTSGHSSAKKSSSVPSQTPVPHPSQHRIFHSTPAVNPCNCCTNHPSVAPLYQNNTWQGTPGYPTAVHSPCVFHCSPETVPPGDHCLSPSRQSLGCRVSPTKSPVCYHSTPPHYSPSSGPCVPTIISNKGLVEQTPSCQAQCCQVKGSKEPCLDTPMGLLPADAYRMLIDQERQLKLLQLQIQKLLESQSKVPEVSSEQNAQQQRPNQVPASPPKRTSVSIAVGTGASLFWSTPQETSTHEASSLEWQTETEPKSGCQNDSTVTSRDRSESACHYSEEHCPGSPQHPTSPQHNTSSGFGVQMFQSPVLGESASMYYQSQSQSKDLSENREIDDPRFYHELLGQVQSRLQDSVIVEDKVEQDQQSLLKTQSLSPVVHQSRKPLTTSSIPQTQKTKQPSSPPNQDRVLSATLKQLQQFGVNIDLDSSQEKTTRATVESASTLACINPEAVIPRLALSEPVGASIWGPSGSVDLSLEANAIALKYLSDSQLSRLSLGSQSSSPHSDPSTILLRRPAVEKSNVALSILSPSNMSLATCKYMKKYGLIEGEISSEEEQEDPIQVDSALGCSVQHETSKTISLGQEREEQNTAVLKNITNKPVVNLHTSPIDSQEQILQDLRPKMQLLLRGGTNSEKENATKRNLIERRSSLTENQRTQEVVDPQGSVGNFLDLSRLRQLPKLF
Protein: Lanosterol 14-alpha demethylase (LDM) (EC 1.14.14.154) (CYPLI) (Cytochrome P450 51A1) (CYP51) (Cytochrome P450-14DM) (Cytochrome P45014DM) (Cytochrome P450LI) (Sterol 14-alpha demethylase) (Q8K0C4)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in sterol biosynthesis. Catalyzes 14-alpha demethylation of lanosterol and 24,25-dihydrolanosterol likely through sequential oxidative conversion of 14-alpha methyl group to hydroxymethyl, then to carboxylaldehyde, followed by the formation of the delta 14,15 double bond in the sterol core and concomitant release of formic acid. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q64654}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:Q64654}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lanosterol synthase
- Squalene monooxygenase
- Squalene synthase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Delta
- Methylsterol monooxygenase 1
- Delta
- Ergosterol biosynthetic protein 28 homolog
- Delta
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
Sequence:
MVLLGLLQSGGWVLGQAMEQVTGGNLLSTLLIACAFTLSLVYLFRLAVGHMVQLPAGAKSPPHIYSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNSKNEDLNAEEVYGRLTTPVFGKGVAYDVPNAIFLEQKKIIKSGLNIAHFKQYVPIIEKEAKEYFQSWGESGERNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFTHAAWLLPAWLPLPSFRRRDRAHREIKNIFYKAIQKRRLSKEPAEDILQTLLDSTYKDGRPLTDEEISGMLIGLLLAGQHTSSTTSAWMGFFLAKDKPLQEKCYLEQKAVCGEDLPPLTYDQLKDLNLLDRCIKETLRLRPPIMTMMRMAKTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWAERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCVGENFAYVQIKTIWSTMLRLYEFDLINGYFPTVNYTTMIHTPENPVIRYKRRSK
Protein: Ankyrin repeat domain-containing protein, chloroplastic (AKRP) (Protein EMBRYO DEFECTIVE 2036) (Q05753)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the initial differentiation of the proplastid during the embryo development and in plastid differentiation linked to cell differentiation, morphogenesis and organogenesis during the plant life cycle.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:17092312}.
Interaction partners:
- Ankyrin repeat domain-containing protein EMB506, chloroplastic
- Phytochrome-interacting ankyrin-repeat protein 2
- Ankyrin repeat-containing protein BDA1
- La-related protein 6C
- AT3G13950 protein
- Probable ubiquitin-conjugating enzyme E2 31
- Vesicle-associated protein 2-2
- Probable 3-deoxy-D-manno-octulosonic acid transferase, mitochondrial
- Pentatricopeptide repeat-containing protein At5g67570, chloroplastic
- E3 ubiquitin-protein ligase XBAT32
Sequence:
MQSLSTPHTISLLLPRTSPSRLSPSLHSLAFPTRLRSLSYSSQTSILPDAGDDFIVGDCLVYEDGVFEDPYLDKEVTQVAKQERKKNRRGGAKRLDESEIEPENLVPEEWRDIQAEVNLTKKDKRKIAQEMEFGVRVEKKRQGLIPLRKVDLNDFLTYKEAKLAQLRPVILDKPGNFSDDSGASSDGETAVSSPSERVAPKNPRWAVYGKGFDHVAKFFNSDKYDPSDKKSDGPRKLLSKEEKFMLNSRNPDLAVATSKKWLPLHTLAACGEFYLVDSLLKHNLDINATDVGGLTVLHRAIIGKKQAITNYLLRESANPFVLDDEGATLMHYAVQTASAPTIKLLLLYNADINAQDRDGWTPLHVAVQARRSDIVKLLLIKGADIEVKNKDGLTPLGLCLYLGREIRTYEVMKLLKEFPLSRHKKRLVTTDEDIE
Protein: Mannosidase alpha class 2C member 1 (H3BQH9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAAPALKHWRTTLERVEKFVSPLYFTDCNLRGSFLTPERLPYQEAVQRDFRPAQVGDSFGPTWWTCWFRVELTIPEAWVGQEVHLCWESDGEGLVWRDGEPVQGLTKEGEKTSYVLTDRLGERDPRSLTLYVEVACNGLLGAGKGSMIAAPDPEKMFQLSRAELAVFHRDVHMLLVDLELLL
Protein: Ubiquitin-conjugating enzyme E2 variant 1 (O45495)
Organism: Caenorhabditis elegans
Function: Involved in protein ubiquitination, but has no ubiquitin ligase activity on its own. The uev-1-ubc-13 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63. Involved in sorting Lys-63-linked polyubiquitinated maternal membrane proteins for degradation by targeting to multivesicular bodies. Required for glr-1-containing glutamate receptor trafficking in neurons. May have a role in synaptic transmission at motorneurons. May be involved in the ubiquitination and growth of intracellular polyglutamine protein aggregates.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21179194}. Nucleus {ECO:0000269|PubMed:21179194}. Cell projection, dendrite {ECO:0000269|PubMed:21179194}. Perikaryon {ECO:0000269|PubMed:21179194}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 13
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-conjugating enzyme E2 W
- Ubiquitin-conjugating enzyme E2 2
- Lipid desaturase domain-containing protein
- UBiquitin Conjugating enzyme
- Ubiquitin-conjugating enzyme E2 variant 3
- Polyubiquitin-A
- Ubiquitin-like domain-containing protein
- E2 ubiquitin-conjugating enzyme
Sequence:
MVDVPRNFRLLEELEEGQKGKGDGNISWGLEDDSDMTLTRWTASIIGPPRTPYESRIYNLQIQCGGNYPREPPTVRFTTKVHMVGVNQSNGVIDKRNLTTLRNWSNSYMIKTVLEDIRKNMMMAKENLKLQQPAEGAMF
Protein: Uncharacterized protein (G8BHG7)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Uncharacterized protein
Sequence:
MSKDETISYCNDQLGPLPTTAPKVSDNVTDLFSFKGKVVSVTGSSGGIGWAVAEGFAQAGADVAIWYHSHNADEKAKYLQEKYGVKSIAYGCNIGVAEEVQKTVDQIESDFGKIDVFVANAGIPWTDGPEIDVQDLSKWTKIIDTDLNSVYYCAHAIGPIFRKQGKGSLVITASMSATIVNVPQLQAAYNVAKAGVKHLSKSLAVEWAPFARVNSVSPGYISTNLTTFANPDLQKKWVQLTPLGREGHPKELVGAYLYLASDAATFTTGCDLAVDGGYTVP
Protein: PHD finger protein 21A (F1M6K4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related
- Lysine-specific histone demethylase
- Histone deacetylase 1
- REST corepressor 1
- Histone deacetylase 2
- Zinc finger protein 217
- REST corepressor 2
- Histone deacetylase 1
- TP53-binding protein 1
- p125
Sequence:
QLRQNLIVKQEQPDKFQIQPLSQSENKLQTAQQQPLQPLQQQQQQQQQQQQQQQQQQQQQQQQHAQQSAAPPSLTASQKTTTASMITTKTLPLVLKAATATMPASVVGQRPTIAMVTAINSQKAVLSTDVQNTPVNLQTSSKVTGPGAEAQIVAKNTVTLQVQATPPQPIKVPQFIPPPRLTPRPNFLPQVRPKPVAQNNIPIAPAPPPMLAAPQLIQRPVMLTKFTPTTLPTSQNSIHPVRVVNGQTATIAKTFPMAQLTSIVIATPGTRLAGPQTVQLSKPSLEKQTVKSHTEAEEKQAESRTVTPPAAPKPKREENPQKLAFMVSLGLVTHDHLEEIQSKRQERKRRTTANPVYSGAVFEPERKKSAVTYLNSTMHPGTRKRGRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQPVSLPSPTSTDGDIHEDFCSVCRKSGQLLMCDTCSRVYHLDCLEPPLKTIPKGMWICPRCQDQMLKKEEAIPWPGTLAIVHSYIAYKAAKEEEKQKLLKWSSDLKQEREELEQKVKELSSSISKCMEMKNTILARQKEMRSSLDKVKQLIRLIHGIDLSKPVDSEATVGALSNGPDCTPPANAASTPAPSPSSQSCTANCNQGEETK
Protein: LD11278p (Peroxiredoxin 2540-1 (EC 1.11.1.15, EC 1.11.1.7)) (A1Z892)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Peroxiredoxin-5
Sequence:
MRLGQTVPNFEADTTKGPIKFHEWQGNSWVVLFSHPADFTPVCTTELGRIAVHQPEFAKRNTKCLAHSVDALNSHVDWVNDIKSYCLDIPGDFPYPIIADPTRDLAVTLGMLDEEQKKDPEVGKTIRALFIISPDHKVRLSMFYPMSTGRNVDEILRTIDSLQLTDRLKVVATPANWTPGTKVMILPTVTDEEAHKLFPKGFDKVSMPSGVNYVRTTENY