wanglab/gogpt-training-data huggingface dataset:
Protein: Acetylornithine deacetylase (AO) (Acetylornithinase) (EC 3.5.1.16) (N-acetylornithinase) (NAO) (P23908)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of the amide bond of N(2)-acetylated L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to form L-ornithine, an intermediate in L-arginine biosynthesis pathway, and a branchpoint in the synthesis of polyamines.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01108, ECO:0000305}.
Interaction partners:
- Argininosuccinate synthase
- Ornithine carbamoyltransferase subunit F
- Ornithine carbamoyltransferase subunit I
- N-acetyl-gamma-glutamyl-phosphate reductase
- Acetylglutamate kinase
- Argininosuccinate lyase
- Acetylornithine/succinyldiaminopimelate aminotransferase
- Amino-acid acetyltransferase
- Diaminopropionate ammonia-lyase
- Phosphoenolpyruvate carboxylase
Sequence:
MKNKLPPFIEIYRALIATPSISATEEALDQSNADLITLLADWFKDLGFNVEVQPVPGTRNKFNMLASIGQGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMAGARYFAETTALRPDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVDELHPPIPGYECPPNHQLVEVVEKLLGAKTEVVNYCTEAPFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVIHHFCWH
Protein: Phosphorylated adapter RNA export protein (RNA U small nuclear RNA export adapter protein) (Q9H814)
Organism: Homo sapiens (Human)
Function: A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:11333016, ECO:0000269|PubMed:15574332}. Nucleus, Cajal body {ECO:0000269|PubMed:15574332}. Cytoplasm {ECO:0000269|PubMed:11333016}. Note=Located in the nucleoplasm and Cajal bodies. Shuttles between the nucleus and the cytoplasm. Shuttles between the nucleoplasm and Cajal bodies. {ECO:0000269|PubMed:11333016, ECO:0000269|PubMed:15574332}.
Interaction partners:
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein subunit 1
- Exportin-1
- Serrate RNA effector molecule homolog
- GTP-binding nuclear protein Ran
- Probable ATP-dependent RNA helicase DDX20
- Nucleolar and coiled-body phosphoprotein 1
- Gem-associated protein 5
- Gem-associated protein 2
- Gem-associated protein 6
Sequence:
MALEVGDMEDGQLSDSDSDMTVAPSDRPLQLPKVLGGDSAMRAFQNTATACAPVSHYRAVESVDSSEESFSDSDDDSCLWKRKRQKCFNPPPKPEPFQFGQSSQKPPVAGGKKINNIWGAVLQEQNQDAVATELGILGMEGTIDRSRQSETYNYLLAKKLRKESQEHTKDLDKELDEYMHGGKKMGSKEEENGQGHLKRKRPVKDRLGNRPEMNYKGRYEITAEDSQEKVADEISFRLQEPKKDLIARVVRIIGNKKAIELLMETAEVEQNGGLFIMNGSRRRTPGGVFLNLLKNTPSISEEQIKDIFYIENQKEYENKKAARKRRTQVLGKKMKQAIKSLNFQEDDDTSRETFASDTNEALASLDESQEGHAEAKLEAEEAIEVDHSHDLDIF
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (Q9VGK8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSESIAIGFLQYIITINYDDEEAQARKTSHEKSQKPKPKPEENHKEKEAISRKASGEGDLITVEIKQGLLRKQTATTTTGQAMNSHATATQNGQTTVVGHHRGFSQPSVTVAAAAATGSTAGDPWFLQTTGHQMPPTAPLRHNKRPAPQPNAVLGAGSSGTAPGSAVGAVLLHQQQLSQSQPHIVPPSIPPHHHHHRENNVHPIQAGAAAALHLSSHALNSHNLISSASNHSPKSPSQTQQQQQTTNQQQQQQQQQASHSILSTFAPAPTVAAVQPAGSQSVAGTAAAVAAVAQQQQQQHLQLLANCPPGGAGLMSSSLNAAQMGMHGAERALPPKSLALSGSQHGSNMLLHTAPQPPQASQPAAVVGVSGSGSAGMSTSLHSFDINGVTAGSGVNASSAWSSGSTTAMNHASLSPTALAPQQGRSRCEVKLNAMPWFHGSITRDEAEHLLQPREDGLFLVRESTNFPGDYTLCVCFQSKVEHYRVKYLENKLTIDDEEYFENLGQLVAHYEADADGLCTQLIKCLPKLGKQEFCINSKDFVDKGWVIPEAELQLRESIGKGEFGDVMLGILRNEKVAVKMLKDEGAVQKFLAEASVMTTLEHDNLVKFIGLVFTSKHLYLVTEYMSKGSLVDYLRSRGRQHITKKDQIIFAYDTASGMEYLEAKKVVHRDLAARNVLISEDCVAKVSDFGLAREECYNLDVGKLPIKWTAPEALKNGRFSNKSDMWSFGILLWEIYSFGRVPYPRIPLADVVKHVEVGYKMEAPEGCPPEIYEMMRQAWDLNPAKRPTFAELKVKLQLLNNATA
Protein: WD repeat-containing and planar cell polarity effector protein fritz homolog (mFrtz) (Homolog-13) (WD repeat-containing and planar cell polarity effector protein) (Q8C456)
Organism: Mus musculus (Mouse)
Function: Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. Together with FUZ and WDPCP proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q32NR9}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q32NR9}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q32NR9}.
Interaction partners:
- Protein inturned
- Protein fuzzy homolog
- Ciliogenesis and planar polarity effector 2
- Protein broad-minded
- Chaperonin-containing T-complex member BBS12
- BBSome complex assembly protein BBS10
- Tetratricopeptide repeat protein 8
- BBSome complex member BBS7
Sequence:
MSFCLTELHLWSLKSTLHIADRDIGVYQYYDKKDPSVSATEHGNLEEKQRLAESRDYPWTLKNRRPEKLRDSLKELEELMQSSPCVLSKWKSKYICQLLFGSGVLVSLSLSGPQLEKVVIDRSLVGKLISDTISDALLTDSFIILSFLAQNKLCFIQFTKKMDSLDGNKRLEKLSALDLKISYYDIPGPANRTIDRHLAVNSTQDLVVCWWPLVSDDVWPWTPVSSEKDRANMLLLGFTQGGLEVLSFVRTEWSPLDVHFGTKQPYQVFTVECSVSVDKEPMADSCIYESVRNKLHCVSVTRIPLRSKAISCCRNSTEDKLIVGCEDSSVILYEAHRGVTLLAQAELRPSLISCHPSGAILLVGSNQGELQIFDIALSPINIQLLAEDYSPKETLQFKKFFDVSSSLVQMQWMAPPVVFQKPKRGEICDLLFLRFNKGPLGVLLFKLGILTRGQLGLVDLILQYIHYSEVYEAISILRSMDWDTLGQQCLIGMGTIVNHLLRQRLTPEREAQLEASLGTFYAPTRPLLDTTILEYREPVSKYARRLFHHLLRYKRFEKAFLLAVDIGARDLFMDIHYLALDMGELALAEVARRRAHDIDVESVSSGVELLGPLDRRDMLNEGFASSALMPEGENKFPGLLPSIGSTHMQTLQQKIPNGPSSRWAIERRTEEEEEEEEEEEEELCTDSSGATTWNAEGELKEDQRKQDIGDVGSLRMVHFGLV
Protein: DNA ligase 3 (K7ERZ5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSKFRGLRYMSLAFKIFFPQTLRALSRKELCLFRKHHWRDVRQFSQWSETDLLHGHPLFLRRKPVLSFQGSHLRSRATYLVFLPGLHVGLCSGPCEMAEQRFCVDYAKRGTAGCKKCKEKIVKGVCRIGKVVPNPFSESGGDMKEWYHIKCMFEKLERARATTKKIEDLTELEGWEELEDNEKEQITQHIADLSSKAAGTPKKKAVVQAKLTTTGQVTSPVKGASFVTSTNPRKFSGFSAKPNNSGEAPSSPTPKRSLSSSKCDPRHKDCLLREFRKLCAMVADNPSYNTKTQIIQDFLRKGSAGDGFHGDVYLTVKLLLPGVIKTVYNLNDKQIVKLFSRIFNCNPDDMARDLEQGDVSETIRVFFEQSKSFPPAAKSLLTIQEVDEFLLRLSKLTKEDEQQQALQDIASRCTANDLKCIIRLIKHDLKMNSGAKHVLDALDPNAYEAFKASRNLQDVVERVLHNAQEVEKEPGQRRALSVQASLMTPVQPMLAEACKSVEYAMKKCPNGMFSEIKYDGERVQVHKNGDHFSYFSRSLKPVLPH
Protein: RE26467p (Tara 1B isoform) (Taranis, isoform B) (Q9NHB9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCTEVNSAMGLQATAATKRKHELTFDSKDANTTYTGNCAPPPVKANKWAISNNNYLESLEEQQQQQQSPSEPAVESNNNHIVLEASMDALKPTEPSISNGHEVTTAVAAMKSQAEVPLPPTASAAIPEDSIARLEVVTSAVPCEPWTSNGPTTPSAVAGPAASAEPVDCISKLQAVAVPSDPWGSIATRSTLATTLLSADELDDDDDDFEDDYEEEESIIPTYCPMRYHPFVPHPHPHSHQLPSHPHQQQPQQLSQQQPHPQQQQLAQQQQQHPQQQRSYAPGYGSRQPNYYSEPFPQQNCSRTGGPQHMTQSPPTPQQARGFAPPQWATAGSSPANPSSGAQQFYEPTNGGAYAPPAAPQQTIRCAENGKSYLDLGCSSGASGNAGGSPISPPPSSAPVVPFAGLPLHGLPLKRCCDGRPGGWCSANRSCYKDTRLKIRNLSMFKLSRFRQVSEQSLYRSVLICNTLKRIDREIEAEAKELHQAAQQHHQQAAAAAAAAAAAAAQAAQYHPAYQQQQQQQQSPPAPLHPHTQQQMDYAPVLNCARLANMDHYQQLSFQPQHQQQQQPSQPHSYHERLDSQPAYRGAAAGAGSFATQPSNCDTSAGASSSNTSGNSNNSSATAASSNSSLHPYDHYPFRESQSGRATPFPACPTTTAAAAAASAAAAASSGGAATTLSSNISSSPASSSTSSNTTSSTVISSSSGNTVSSNGTTPVAPTASSSNCDTSDSGYADDDSTRSINWSSVLSLSSQSALDPLNNNDLFSILPSAATPTAVPVSVPASSSSSSSGSTLAFSGSFTTVQASGGSSSSCGSSSTTATFTTLSTISSATHSLTSSYVSSISSNVSAGANTWEYGFLDMEFGLGSEFTELVPSCKLSSEDLFKSGLGGQVVTASRLHDNELEHPAHIMVGS
Protein: Pyridoxine/pyridoxamine 5'-phosphate oxidase (EC 1.4.3.5) (PNP/PMP oxidase) (PNPOx) (Pyridoxal 5'-phosphate synthase) (P0AFI7)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Interaction partners:
- Pyridoxal kinase PdxY
- Pyridoxine 5'-phosphate synthase
- Pyridoxine/pyridoxal/pyridoxamine kinase
- Pyridoxine 4-dehydrogenase
- 4-hydroxythreonine-4-phosphate dehydrogenase
- Phosphoserine aminotransferase
- Carbamoyl phosphate synthase large chain
- Aspartate carbamoyltransferase catalytic subunit
Sequence:
MSDNDELQQIAHLRREYTKGGLRRRDLPADPLTLFERWLSQACEAKLADPTAMVVATVDEHGQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLERQVMVIGKAERLSTLEVMKYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLPSFWGGFRVSLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP
Protein: DNA polymerase (EC 2.7.7.7) (Q5JQP8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU366014}.
Interaction partners:
Sequence:
MDYERALRLLRLPQLPPGAQLVKSAWLSLCLQERRLVDVAGFSIFIPSRYLDHPQPSKAEQDASIPPGTHEALLQTALSPPPPPTRPVSPPQKAKEAPNTQAQPISDDEASDGEETQVSAADLEALISGHYPTSLEGDCEPSPAPAVLDKWVCAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRRGKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLPGPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNTHGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
Protein: Leucine-rich repeat transmembrane neuronal protein 3 (Q86VH5)
Organism: Homo sapiens (Human)
Function: Exhibits a limited synaptogenic activity in vitro, restricted to excitatory presynaptic differentiation (By similarity). May play a role in the development and maintenance of the vertebrate nervous system.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Catenin alpha-3
- Neurexin-2
- Neurexin-1
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- Neurexin-3
- Glypican-1
Sequence:
MGFNVIRLLSGSAVALVIAPTVLLTMLSSAERGCPKGCRCEGKMVYCESQKLQEIPSSISAGCLGLSLRYNSLQKLKYNQFKGLNQLTWLYLDHNHISNIDENAFNGIRRLKELILSSNRISYFLNNTFRPVTNLRNLDLSYNQLHSLGSEQFRGLRKLLSLHLRSNSLRTIPVRIFQDCRNLELLDLGYNRIRSLARNVFAGMIRLKELHLEHNQFSKLNLALFPRLVSLQNLYLQWNKISVIGQTMSWTWSSLQRLDLSGNEIEAFSGPSVFQCVPNLQRLNLDSNKLTFIGQEILDSWISLNDISLAGNIWECSRNICSLVNWLKSFKGLRENTIICASPKELQGVNVIDAVKNYSICGKSTTERFDLARALPKPTFKPKLPRPKHESKPPLPPTVGATEPGPETDADAEHISFHKIIAGSVALFLSVLVILLVIYVSWKRYPASMKQLQQRSLMRRHRKKKRQSLKQMTPSTQEFYVDYKPTNTETSEMLLNGTGPCTYNKSGSRECEIPLSMNVSTFLAYDQPTISYCGVHHELLSHKSFETNAQEDTMETHLETELDLSTITTAGRISDHKQQLA
Protein: DNA topoisomerase 1 (EC 5.6.2.1) (DNA topoisomerase I) (Maintenance of killer protein 1) (P04786)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).
Subcellular location: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli (By similarity). {ECO:0000250}.
Interaction partners:
- DNA topoisomerase 2
- DNA topoisomerase 3
- Tyrosyl-DNA phosphodiesterase 1
- Topoisomerase 1-associated factor 1
- Protein TRI1
- ATP-dependent helicase SGS1
- Ribonuclease H2 subunit A
- Chromosome segregation in meiosis protein 3
- DNA polymerase alpha-binding protein
- Cell division control protein 45
Sequence:
MTIADASKVNHELSSDDDDDVPLSQTLKKRKVASMNSASLQDEAEPYDSDEAISKISKKKTKKIKTEPVQSSSLPSPPAKKSATSKPKKIKKEDGDVKVKTTKKEEQENEKKKREEEEEEDKKAKEEEEEYKWWEKENEDDTIKWVTLKHNGVIFPPPYQPLPSHIKLYYDGKPVDLPPQAEEVAGFFAALLESDHAKNPVFQKNFFNDFLQVLKESGGPLNGIEIKEFSRCDFTKMFDYFQLQKEQKKQLTSQEKKQIRLEREKFEEDYKFCELDGRREQVGNFKVEPPDLFRGRGAHPKTGKLKRRVNPEDIVLNLSKDAPVPPAPEGHKWGEIRHDNTVQWLAMWRENIFNSFKYVRLAANSSLKGQSDYKKFEKARQLKSYIDAIRRDYTRNLKSKVMLERQKAVAIYLIDVFALRAGGEKSEDEADTVGCCSLRYEHVTLKPPNTVIFDFLGKDSIRFYQEVEVDKQVFKNLTIFKRPPKQPGHQLFDRLDPSILNKYLQNYMPGLTAKVFRTYNASKTMQDQLDLIPNKGSVAEKILKYNAANRTVAILCNHQRTVTKGHAQTVEKANNRIQELEWQKIRCKRAILQLDKDLLKKEPKYFEEIDDLTKEDEATIHKRIIDREIEKYQRKFVRENDKRKFEKEELLPESQLKEWLEKVDEKKQEFEKELKTGEVELKSSWNSVEKIKAQVEKLEQRIQTSSIQLKDKEENSQVSLGTSKINYIDPRLSVVFCKKYDVPIEKIFTKTLREKFKWAIESVDENWRF
Protein: Plakophilin-1 (P97350)
Organism: Mus musculus (Mouse)
Function: Seems to play a role in junctional plaques (By similarity). May facilitate the formation of intermediate filaments (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:27015268, ECO:0000269|PubMed:27375112}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13835}. Cytoplasm {ECO:0000269|PubMed:27015268, ECO:0000269|PubMed:27033150, ECO:0000269|PubMed:27375112, ECO:0000269|PubMed:29678907}. Cell junction, desmosome {ECO:0000269|PubMed:27033150, ECO:0000269|PubMed:27375112, ECO:0000269|PubMed:29678907}. Cell membrane {ECO:0000269|PubMed:27015268}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q13835}. Note=Colocalizes with EIF4A1 in stress granules following arsenate or hydrogen peroxide treatment (By similarity). Localizes to nucleoli following DNA damage (By similarity). Located in the cytoplasm during early tooth development, however localizes to the cell membrane in ameloblasts during molar growth (PubMed:27015268). Ca(2+)-mediated localization to the cell membrane in dental epithelial cells is inhibited via WNT3A (PubMed:27015268). Initially localized to the cytoplasm however as keratinocyte differentiation proceeds becomes localized to cell junctions as early cell-cell contacts become linear as part of membrane sealing (PubMed:27375112). Localized to lateral cell contacts in colocalization with DSP as epithelial sheet formation completes (PubMed:27375112). Localizes to the cytoplasm when the phosphorylated form interacts with YWHAG (PubMed:29678907). Protein stability is increased and localizes to the cytoplasm when phosphorylated at the N-terminus by AKT2 (By similarity). The unphosphorylated form is preferentially localized to desmosomes (By similarity). {ECO:0000250|UniProtKB:Q13835, ECO:0000269|PubMed:27015268, ECO:0000269|PubMed:27375112, ECO:0000269|PubMed:29678907}.
Interaction partners:
- Desmoplakin
- Desmoglein-1-alpha
- Desmoglein-3
- Junction plakoglobin
- Desmoglein-2
- Plakophilin-3
- Desmocollin-2
- Envoplakin
- Desmocollin-1
- Desmocollin-3
Sequence:
MNHSPLKTALAYECFQDQDNSTLALPSDQKMKTGTSGRQRVQEQVMMTVKRQKSKSSQSSTLSHSNRGSMYDGLADNYNNYGTTSRSSYFSKFQAGNGSWGYPIYNGTLKREPDNRRFSSYSQMENWSRHYPRGSCATPGAGSDICFMQKIKASRSEPDLYCDPRGTLRKGTLGSKGHKTTQNRCSFYSTCSGQKAVKKCPVRPPSCTSKQDPVYVPPISCNKDLSFGHSRASSKICSEDIECSGLTIPKAVQYLCSQDEKYQAIGAYYIQHTCFQDESAKQQVYQLGGICKLVDLLRSPNQNVQQAAAGALRNLVFRSTPNKLETRRQNGIREAVSLLRRSGSTEIQKQLTGLLWNLSSTDELKEELVADALPVLTDRVIIPFSGWCDGNSNMSREVVDPEVFFNATGCLRNLSSADAGRQTMRNYSGLIDSLMAYVQNCVAASRCDDKSVENCMCILHNLSYRLDAEVPTRYRQLEYNTRNAYTEKSSTGCFSNRGDKMMNNNYDCPLPEEETNPKGSSWLYHSDAIRTYLNLMGKSKKDATLEACAGALQNLTASKGLMSNGMSQLIGIKEKGLPQIARLLQSGNSDVVRSGASLLSNMSRHPVLHRVMGNQVFPEVTRLLTSHTGNTSNSEDILSSACYTVRNLMTSQPQMAKQYFSNSMLNNVFNLCRNTASSPKAAEAARLLLSDMWASKELQSVLRQQGFDRNMMGNIAGANNLRNFTSRF
Protein: Follicle-stimulating hormone receptor (Follitropin receptor) (Q98T84)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361222}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361222}.
Interaction partners:
Sequence:
MMCFILSWLMMHAGNMCLGSYACLANGTTRSFLCLGSKVHQMPYHIPKNTTYVEIKLTRIIMLPSRAMSSLHDLKRILVSENGVLQRIEAYAFANLTKLEEITITKSKNLVCMDRHTFWGLPKLRYLTISNTGLTVLPDFSKVQSAAFEFLFDLEDNMHIEVIPSNAFAGLTSGTITELRLTKNGITEVDRNAFNGTKIEKLFLMGNQQLKRIHNYAFLGAEGPLVLDISRTAISSLPENMLRRLKLLIATSVYSLRWLPNLEIFTELTQANLTYPSHCCAFKNFKKNKSEKNRLCNDSTIRNQEPYFFEEHCKDVIEVRCYPEPDAFNPCEDIMGFTFLRVLIWFISVLAVLGNFTVLLVLLSSRTKLTVPKFLMCHLAFADFCMGLYLLIIGSVDLQTRSHYYNYGIEWQTGVGCGTAGFLTVFASELSVYTLTAITLERWHTITYAMRLERQLRLHHACSVMAFGWLFSVLAALTPVIGVSSYMKTSICLPMDVETASSQAYIMLLLILNVLAFVTVCACYVRIYLTVRHPASVPDSADARVAKRMAVLVFTDFLCMAPISFFAISAALKQPLITVSHAKVLLVLFYPINSCANPFLYAFFTKSFKQDFFVLTSRFGCFESRARVYRTETSSLHNGPRMRSPKNSDGTLYSLGHVAHPH
Protein: Dynein light chain, cytoplasmic (8 kDa cytoplasmic dynein light chain) (O94111)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}.
Interaction partners:
- Cytoplasmic dynein intermediate chain
- Dynein heavy chain, cytoplasmic
- Nucleoporin NSP1
- Nuclear distribution protein nudF
- Actin-related protein
- Nuclear movement protein nudC
- Dynein light chain
- Nuclear pore complex protein An-Nup159
- Dynein light intermediate chain
- P150 dynactin NUDM
Sequence:
MASEKKDKLEPQIKSVDMSEDMQQEAVEVAIEAMEKYHIEKDIAQYIKREFDSRKGATWHCVVGRNFGSFVTHETKHFIYFYLGHCAILLFKTQ
Protein: CD22 protein (O60926)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MESKTEKWMERIHLNVSERPFPPHIQLPPEIQESQEVTLTCLLNFSCYGYPIQLQWLLEGVPMRQAAVTSTSLTIKSVFTRSELKFSPQWSHHGKIVTCQLQDADGKFLSNDTVQLNVKHTPKLEIKVTPSDAIVREGDSVTMTCEVSSTNPEYTTVSWLKDGTSLKKQNTFTLNLREVTKDQSGKYCCQVSNDVGPGRSEEVFLQVQYAPEPSTVQILHSPAVEGSQVEFLCMSLANPLPTNYTWYHNGKEMQGRTEEKVHIPKILPWHAGTYSCVAENILGTGQRGPGAELDVQYPPKKVTTVIQNPMPIREGDTVTLSCNYNSSNPSVTRYEWKPHGAWEEPSLGVLKIQKVGWDNTTIACARCNSWCSWASPVALNVQYAPRDVRVRKIKPLSEIHSGNSVSLQCDFSSSHPKEVQFFWEKNGRLLGKESQLNFDSISPEDAGSYSCWVNNSIGQTASKAWTLEVLYAPRRLRVSMSPGDQVMEGKSATLRCESDANPPVSHYTWFDWNNQSLPYHSQKLRLEPVKVQHSGAYWCQGTNSVGKGRSPLSTLTVYYSPETIGRRVAVGLGSCLAILILAICGLKLQRRDAESSEMQRPPRTCDDTVTYSALHKRQVGDYENVIPDFPEDEGIHYSELIQFGVGERPQAQENVDYVILKH
Protein: Ferrochelatase (EC 4.98.1.1) (A0A8I5ZR41)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000607}.
Interaction partners:
Sequence:
MLTLWLVGLPLRAPKGPVVYGSSRACQPWRCQSGPAVVATTEKAHHAKTTKPQAQPERRKPKTGILMLNMGGPETLGEVQDFLQRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQEQYRRIGGGSPIKMWTSKQGEGMVKLLDELSPDTAPHKYYIGFRYVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNEVGRKPTMKWSTIDRWPTHPLLIQCFADHILKELDHFPEEKRSEVVILFSAHSLPMSVVNRGDPYPQEVGATVHRVMEQLGYPNPYRLVWQSKVGPVPWLGPQTDEAIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAQKCGAENIRRAESLNGNPLFSKALADLVHSHIQSNKLCSTQLSLSCPLCVNPVCRKTKSFFTSQQL
Protein: AMP deaminase (EC 3.5.4.6) (Myoadenylate deaminase) (P15274)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: AMP deaminase plays a critical role in energy metabolism.
Interaction partners:
- Adenine phosphoribosyltransferase 1
- IMP-specific 5'-nucleotidase 1
- Adenosine kinase
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase 2
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine-5'-monophosphate dehydrogenase 4
- Inosine-5'-monophosphate dehydrogenase 3
- Inosine-5'-monophosphate dehydrogenase 2
- Adenylosuccinate synthetase
Sequence:
MDNQATQRLNDLSLEPAPSHDEQDGSGLVIDIDQRKIGDEQAGVVVDDETPPLEQQDSHESLAADSRNANFSYHENQQLLENGTKQLALDEHDSHSAILEQPSHSTNCSSSNIAAMNKGHDSADHASQNSGGKPRTLSASAQHILPETLKSFAGAPVVNKQVRTSASYKMGMLADDASQQFLDDPSSELIDLYSKVAECRNLRAKYQTISVQNDDQNPKNKPGWVVYPPPPKPSYNSDTKTVVPVTNKPDAEVFDFTKCEIPGEDPDWEFTLNDDDSYVVHRSGKTDELIAQIPTLRDYYLDLEKMISISSDGPAKSFAYRRLQYLEARWNLYYLLNEYQETSVSKRNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKHKLRHSKDEKVIFRDGKLLTLDEVFRSLHLTGYDLSIDTLDMHAHKDTFHRFDKFNLKYNPIGESRLREIFLKTNNYIKGTYLADITKQVIFDLENSKYQNCEYRISVYGRSLDEWDKLASWVIDNKVISHNVRWLVQIPRLYDIYKKTGIVQSFQDICKNLFQPLFEVTKNPQSHPKLHVFLQRVIGFDSVDDESKVDRRFHRKYPKPSLWEAPQNPPYSYYLYYLYSNVASLNQWRAKRGFNTLVLRPHCGEAGDPEHLVSAYLLAHGISHGILLRKVPFVQYLYYLDQVGIAMSPLSNNALFLTYDKNPFPRYFKRGLNVSLSTDDPLQFSYTREPLIEEYSVAAQIYKLSNVDMCELARNSVLQSGWEAQIKKHWIGKDFDKSGVEGNDVVRTNVPDIRINYRYDTLSTELELVNHFANFKRTIEEK
Protein: Intraflagellar transport protein 139 (A9XPA6)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Interaction partners:
Sequence:
MADRVLALVHYYAREGYFRHVQTVCNEVLKKRPGDGVLTFWRAYGLLMEGNTADAMRDLSSIQGNSDLELAVAAAQLLGHESAKVPDHDAIIDLQAKLEIEERTASDQPCLHLASFYLYTKSKERARGLVERVLRNQPDMVPAQVLLGWIIISQQQDDEYDMLFDESELDDALSHFEQAVEHDHNDLEALLGKAKIMELKKQLGPCLDVLTEINVRFGWFVPALVEKTRMLMMLGDWEQVTETLQRVLAADQQNIMAQAWNCMISLTREGNNKQAAKQLQDLFSSMNRQEPKNAELFFRVARPFGRLACSDPTLLGITYLMADRAAQLRPEMAAYVVEAAAQKLMMDETTNATERFTQALQLDELNLEANAGALEAQIMAGELEEAAGQIMFLEDMFTNAAAAGGGKRKGRGTGDMDDDPDMADPSLGTSSDNPTLLYLKGLLAWKQGMPSEGLGLLERSIAALFSAAADFHGPSLELYAALNPARITAVVRLLLQSIGGEPRAPTEAPSPLISKVTRALDLLNKQAPALQESALLHARALYLNGNLDGALRKAGEILRMNPEESSAHLLICSVYVAQDKPELAVSALDQAVSSNFAIRETPLYHVVQAKVLVANNKLDDAKRVLESAMNLPGVRTALTVQQRARLGRKVVEPTLHERATVYLLLADVLARQSKIPDAPEAKKYIQDAIREFEGTSEEVRVTVADCELAIARGDVEGALKKLRRIPKESPHYVKARMAMADIYLRHRKDKAAYIKCYMDLVDHTPDYDSYCMLGEAFMQIQEPEKAVRAFESALEFSPKDVDLITRCARALVTSHDYQRAIDYYTKAIANARGGAQHALQLELGNLLVRLRQYPAATAAINKALERNRDGLPATENLQLDVEAWSMLAKVHKGKLEMEGYSQAQSRALELQKQLLLKLRGELPEAVALQRERTAAICFDLAEQSKRARQFDRAMELYMEALRHHDTHVPSMLAVAKLHLANGDTDACQAQCVTLLKHDPDNEEASIMLAELMFHKEHYDTAIYHFQQLLERSPNHYGALAQLILLLRRAGRLEDVPRYFALAEAGSPKAVMDPGYHYCKGIYNRYINNPREALKELNLARKDTRWGSQAILHMVEIYLNPDNDAVWEEKENADTPESRQAVATARSLLKQVRGADTTTQRYRVLESYAIMAGKDKNEIEASLNVLLDLANQDPNNVPVLLAMATGFMMLKQTPKARNQLKRVQKIQYKPDEAEEFERSWLLLADIHIQGGKYDLAQDLCQKCLKYNKSCAKAWEIMGQIMEREQAYKDAADHYENAWKHENQASAQVGFKLAFNYLKARRYVEAVDVCHKVIKAFPDYPKIRKEILEKARMGLKP
Protein: Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (EC 2.5.1.58) (EC 2.5.1.59) (CAAX farnesyltransferase subunit alpha) (FTase-alpha) (Ras proteins prenyltransferase subunit alpha) (Type I protein geranyl-geranyltransferase subunit alpha) (Q580J3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein farnesyltransferase subunit beta
- intramembrane prenyl-peptidase Rce1
- CAAX prenyl protease
- Farnesyl pyrophosphate synthase
- squalene synthase
Sequence:
MNKSAVRSEESRQSSSLPSTYSSSSLNSEDERLALLSDINALQALFPGVTPKEETPLIKHPNMTPAVFSKKFDYVMGIYRAVGVTFKGTRVGPSTPQWLLLTSFVIQQNASHYSAWKDRRDVFLQPSRLLTSTRDAFMAENGQQCCGDKSDSLAKVIQEWLPAQCDVQGPTGEYSVWRAIRWELKAMERFALMNPKNFQAWHHRGEMLREALMHANSAVTGSRSAFDGYLLTCHNMQFSDIDERVFCDAALDDDSKNYHAWLYRSWFVHSFPFLLHPPSWDSLLGGDQGTEDKHSELHAAPFRSFTVEEDWLHKCLQPIIPECPLSDELTSTAKRILHDCMNNSAWCHRFYVFEHDLIVPLIRVIPPQQTEEAKLILKRLCECEMFYALQWCAYEPCNESSFVHARCVAVLHQAVAIHLCLSSHEDAPHVFLRDDEIIQVAGSSSLRHMNLRDKLRWGAFLETFRLLLCQVNVLSDVITPRAEEFRSGGEGRDDATISVIRKRRSQFLLDNTHQVYTARYRCLFTILEYMWRCYFTVSDRENVAAALPPEVYAGGDAEAAALAQQQSDDCVKFFLEAELQALRLARRLFVEDDIRRKYWKHEMNIVMNRDYV