wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor Gibbin (AT-hook DNA-binding motif-containing protein 1) (Q5TGY3)
Organism: Homo sapiens (Human)
Function: Transcription factor required for the proper patterning of the epidermis, which plays a key role in early epithelial morphogenesis. Directly binds promoter and enhancer regions and acts by maintaining local enhancer-promoter chromatin architecture. Interacts with many sequence-specific zinc-finger transcription factors and methyl-CpG-binding proteins to regulate the expression of mesoderm genes that wire surface ectoderm stratification.
Subcellular location: Nucleus {ECO:0000269|PubMed:33644933}. Chromosome {ECO:0000269|PubMed:35585237}. Note=Associates with promoter and enhancer regions. {ECO:0000269|PubMed:35585237}.
Interaction partners:
Sequence:
MRVKPQGLVVTSSAVCSSPDYLREPKYYPGGPPTPRPLLPTRPPASPPDKAFSTHAFSENPRPPPRRDPSTRRPPVLAKGDDPLPPRAARPVSQARCPTPVGDGSSSRRCWDNGRVNLRPVVQLIDIMKDLTRLSQDLQHSGVHLDCGGLRLSRPPAPPPGDLQYSFFSSPSLANSIRSPEERATPHAKSERPSHPLYEPEPEPRDSPQPGQGHSPGATAAATGLPPEPEPDSTDYSELADADILSELASLTCPEAQLLEAQALEPPSPEPEPQLLDPQPRFLDPQALEPLGEALELPPLQPLADPLGLPGLALQALDTLPDSLESQLLDPQALDPLPKLLDVPGRRLEPQQPLGHCPLAEPLRLDLCSPHGPPGPEGHPKYALRRTDRPKILCRRRKAGRGRKADAGPEGRLLPLPMPTGLVAALAEPPPPPPPPPPALPGPGPVSVPELKPESSQTPVVSTRKGKCRGVRRMVVKMAKIPVSLGRRNKTTYKVSSLSSSLSVEGKELGLRVSAEPTPLLKMKNNGRNVVVVFPPGEMPIILKRKRGRPPKNLLLGPGKPKEPAVVAAEAATVAAATMAMPEVKKRRRRKQKLASPQPSYAADANDSKAEYSDVLAKLAFLNRQSQCAGRCSPPRCWTPSEPESVHQAPDTQSISHFLHRVQGFRRRGGKAGGFGGRGGGHAAKSARCSFSDFFEGIGKKKKVVAVAAAGVGGPGLTELGHPRKRGRGEVDAVTGKPKRKRRSRKNGTLFPEQVPSGPGFGEAGAEWAGDKGGGWAPHHGHPGGQAGRNCGFQGTEARAFASTGLESGASGRGSYYSTGAPSGQTELSQERQNLFTGYFRSLLDSDDSSDLLDFALSASRPESRKASGTYAGPPTSALPAQRGLATFPSRGAKASPVAVGSSGAGADPSFQPVLSARQTFPPGRAASYGLTPAASDCRAAETFPKLVPPPSAMARSPTTHPPANTYLPQYGGYGAGQSVFAPTKPFTGQDCANSKDCSFAYGSGNSLPASPSSAHSAGYAPPPTGGPCLPPSKASFFSSSEGAPFSGSAPTPLRCDSRASTVSPGGYMVPKGTTASATSAASAASSSSSSFQPSPENCRQFAGASQWPFRQGYGGLDWASEAFSQLYNPSFDCHVSEPNVILDISNYTPQKVKQQTAVSETFSESSSDSTQFNQPVGGGGFRRANSEASSSEGQSSLSSLEKLMMDWNEASSAPGYNWNQSVLFQSSSKPGRGRRKKVDLFEASHLGFPTSASAAASGYPSKRSTGPRQPRGGRGGGACSAKKERGGAAAKAKFIPKPQPVNPLFQDSPDLGLDYYSGDSSMSPLPSQSRAFGVGERDPCDFIGPYSMNPSTPSDGTFGQGFHCDSPSLGAPELDGKHFPPLAHPPTVFDAGLQKAYSPTCSPTLGFKEELRPPPTKLAACEPLKHGLQGASLGHAAAAQAHLSCRDLPLGQPHYDSPSCKGTAYWYPPGSAARSPPYEGKVGTGLLADFLGRTEAACLSAPHLASPPATPKADKEPLEMARPPGPPRGPAAAAAGYGCPLLSDLTLSPVPRDSLLPLQDTAYRYPGFMPQAHPGLGGGPKSGFLGPMAEPHPEDTFTVTSL
Protein: vesicle-fusing ATPase (EC 3.6.4.6) (A5WWM0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}.
Interaction partners:
- Vesicle
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 1b
- Charged multivesicular body protein 4c
- Charged multivesicular body protein 4c.
- Charged multivesicular body protein 5
- Charged multivesicular body protein 5
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 6
- Charged multivesicular body protein 3
Sequence:
MAANNNLQKAIDLANKASQEDKAENYEEALRLYQHAVQYFLHVVKYEAQGDKAKQSIRAKCAEYLDRAEKLKEYLKKKEKAPAKPVKESQSNDKGNESDGEEDPEKKKFQNQLSGAIVMEKPNIKWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKSLFTLAREHKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGNDNEGILVLGATNIPWTLDSAIRRRFEKRIYIPLPEEHARSFMFKLNLGTTPNSLTESDFMTLGKKTDGYSGADISIIVRDALMQPVRKVQSATHFKQVRGPSRSDPNVIVDDLLTPCSPGDPQAKEMTWMEVPGEKLLEPIVSMSDMLRSLSNTKPTVNEQDLEKLKKFTEDFGQEG
Protein: ATP synthase subunit 9, mitochondrial (Lipid-binding protein) (Q37315)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ATP synthase subunit alpha
- ATP synthase F
- ATP synthase F
- ATP synthase subunit a
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- V-type proton ATPase subunit d
- Vacuolar proton translocating ATPase 100 kDa subunit
- V-type proton ATPase subunit E
Sequence:
MKNIVKIEQLELASAVVELGKKVGAGLAAIGLTGAGAGVGIVFAAFILAVGMNPNLRGELFKLAMLGFALSEAVGLLALMMSFLILYS
Protein: Glycine cleavage system H protein 1, mitochondrial (P25855)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The glycine decarboxylase (GDC) or glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:25862457}.
Interaction partners:
- Aminomethyltransferase, mitochondrial
- Glycine dehydrogenase
- Glycine dehydrogenase
- Serine hydroxymethyltransferase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Glycine cleavage system H protein 3
- Serine--glyoxylate aminotransferase
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 2, mitochondrial
Sequence:
MALRMWASSTANALKLSSSVSKSHLSPFSFSRCFSTVLEGLKYANSHEWVKHEGSVATIGITAHAQDHLGEVVFVELPEDNTSVSKEKSFGAVESVKATSEILSPISGEIIEVNKKLTESPGLINSSPYEDGWMIKVKPSSPAELESLMGPKEYTKFCEEEDAAH
Protein: Probable ATP-citrate synthase (EC 2.3.3.8) (ATP-citrate (pro-S-)-lyase) (Citrate cleavage enzyme) (Q54YA0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: ATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- ATP citrate synthase
- Citrate synthase, mitochondrial
- Citrate synthase
- Citrate synthase, peroxisomal
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Probable cytoplasmic aconitate hydratase
- Succinate--CoA ligase subunit alpha, mitochondrial
- Probable malate dehydrogenase 3
- Probable malate dehydrogenase 1
- Probable malate dehydrogenase 2, mitochondrial
Sequence:
MTNSNFNHGNHGSNLPARLFTKQSQALIYNYKEAAVQRMLDFDNVSQRDTPSVGGLIHPGSDGGMYKAFFGFKELVIPVYNSVSEACQQCPNADVFLNFASHRSAYQSSLLALREPSIQTVVIIAEGVPENEARSLISIAKKLGKVIIGPATVGGIQAGCFKIGNTAGTIVYIMACKLYRSGSVGFVSKSGGLSNEMYNVLSRCTDGIYEGIAIGGDAFPGSTLTDHALRYEKLPEVQMIVILGELGGWDEYGIVEALKKGEITKPICAWVSGTVAKIFPTEVQFGHAGAKSGGETESADAKNKALREAGAVVPTSFEDFSNVIAATYAKLQSKGLVKPVEEPTPPELPLDFKTAVKAGKVRKPTSIISTICDDRGDELSYAGVPISEVCKEQYNMGDVIGLLWFKRKLPPYASKFFEMCLKLVADHGPCVSGAHNTIVAARAGKDLVSSLVSGLLTIGPRFGGAIDDSARVFQDAVDNNLQPSQFVEGMKSKGKRIPGIGHLIKSADEIDKRVVLLKDYAFTHFSSTKYLEYALEVEKYTLQKANNLILNVDGCIGVLFLDLLHSSGLFTQHEIKEIIDVGYLNGFFIVGRSVGLIGHALDQRRNKQGLYRHQADDVHYAL
Protein: Sodium/potassium-transporting ATPase subunit alpha-1 (Na(+)/K(+) ATPase alpha-1 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-1) (Q8VDN2)
Organism: Mus musculus (Mouse)
Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17408578}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P06685}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P06685}. Melanosome {ECO:0000250|UniProtKB:P05023}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit beta-3
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit alpha-2
- Protein ATP1B4
- Phospholemman
- Sodium/potassium-transporting ATPase subunit alpha-3
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MGKGVGRDKYEPAAVSEHGDKKGKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRSATEEEPPNDDLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAEEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWFALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIEVCCGSVMEMREKYSKIVEIPFNSTNKYQLSIHKNPNASEPKHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLLLPDEQFPEGFQFDTDDVNFPVDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNQVNPRDAKACVVHGSDLKDMTSEELDDILRYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIVGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPFHLLGIRETWDDRWVNDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGAALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
Protein: Receptor protein-tyrosine kinase (EC 2.7.10.1) (A0A8I5ZQB9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MLLETLYLFLFILVCQGTSNRLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYTIQEVAGYVLIALNTVERIPLENLQIIRGNALYENTYALAVLSNYGTNKTGLRELPMRNLQEILIGAVRFSNNPILCNMETIQWRDIVQDVFLSNMSMDVQRHLTGCPKCDPSCPNGSCWGRGEENCQKLTKIICAQQCSRRCRGRSPSDCCHNQCAAGCTGPRESDCLVCHRFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGPDYYEVEEDGVSKCKKCDGPCRKVCNGIGIGEFKDTLSINATNIKHFKYCTAISGDLHILPVAFKGDSFTRTPPLDPRELEILKTVKEITGFLLIQAWPENWTDLHAFENLEIIRGRTKQHGQFSLAVVGLNITSLGLRSLKEISDGDVIISGNRNLCYANTINWKKLFGTPNQKTKIMNNRAEKDCKATNHVCNPLCSSEGCWGPEPTDCVSCQNVSRGRECVDKCNILEGEPREFVENSECIQCHPECLPQTMNITCTGRGPDNCIKCAHYVDGPHCVKTCPSGIMGENNTLVWKFADANNVCHLCHANCTYGCAGPGLKGCQQPEGPKIPSIATGIVGGLLFIVVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQAHLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPYGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKYLVDSSSSIEPFLILLKSLRQGDERMHLPSPTDSNFYRALMEEEDMEDVVDADEYLIPQQGFFNSPSTSRTPLLSSLSANSNSSAVACINRNGSCRVKEDAFLQRYSSDPTSVLTEDNIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLHPAPGRDLHYQNPHSNAVSNPEYLNTAQPTCLSSGFDSSALWIQKGSHQMSLDNPDYQQDFFPKEAKPNGIFKGPTAENAEYLRVAPPSSEFIGA
Protein: 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 (EC 2.5.1.108) (Diphthamide biosynthesis protein 1) (Diphtheria toxin resistance protein 1) (Ovarian cancer-associated gene 1 protein) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1) (Q9BZG8)
Organism: Homo sapiens (Human)
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity). Acts as a tumor suppressor.
Subcellular location: Nucleus {ECO:0000269|PubMed:10519411}. Cytoplasm {ECO:0000269|PubMed:10519411}. Note=Punctate, primarily perinuclear localization. {ECO:0000269|PubMed:10519411}.
Interaction partners:
- 2-
- Diphthine methyl ester synthase
- Diphthamide biosynthesis protein 3
- Elongation factor 2
- Esterase OVCA2
- Diphthine methyltransferase
- RNA-binding protein 8A
- DnaJ homolog subfamily C member 24
- Diphthine--ammonia ligase
- Elongator complex protein 3
Sequence:
MAALVVSGAAEQGGRDGPGRGRAPRGRVANQIPPEILKNPQLQAAIRVLPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTEAEVMVMGDVTYGACCVDDFTARALGADFLVHYGHSCLIPMDTSAQDFRVLYVFVDIRIDTTHLLDSLRLTFPPATALALVSTIQFVSTLQAAAQELKAEYRVSVPQCKPLSPGEILGCTSPRLSKEVEAVVYLGDGRFHLESVMIANPNVPAYRYDPYSKVLSREHYDHQRMQAARQEAIATARSAKSWGLILGTLGRQGSPKILEHLESRLRALGLSFVRLLLSEIFPSKLSLLPEVDVWVQVACPRLSIDWGTAFPKPLLTPYEAAVALRDISWQQPYPMDFYAGSSLGPWTVNHGQDRRPHAPGRPARGKVQEGSARPPSAVACEDCSCRDEKVAPLAP
Protein: Large ribosomal subunit protein bL9m (39S ribosomal protein L9, mitochondrial) (L9mt) (MRP-L9) (Q9BYD2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL23
Sequence:
MAAPVVTAPGRALLRAGAGRLLRGGVQELLRPRHEGNAPDLACNFSLSQNRGTVIVERWWKVPLAGEGRKPRLHRRHRVYKLVEDTKHRPKENLELILTQSVENVGVRGDLVSVKKSLGRNRLLPQGLAVYASPENKKLFEEEKLLRQEGKLEKIQTKAGEATVKFLKSCRLEVGMKNNVKWELNPEIVARHFFKNLGVVVAPHTLKLPEEPITRWGEYWCEVTVNGLDTVRVPMSVVNFEKPKTKRYKYWLAQQAAKAMAPTSPQI
Protein: Transport protein particle subunit trs85-1 (TRAPP subunit trs85-1) (O94731)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the TRAPP I and TRAPP II complexes. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II seems to play a role in intra-Golgi transport. Has a role late in meiosis following DNA replication (By similarity).
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250}.
Interaction partners:
- Uncharacterized protein C13G6.05c
- Transport protein particle 20 kDa subunit
- Transport protein particle subunit trs31
- Transport protein particle subunit bet5
- Transport protein particle subunit bet3
- Transport protein particle subunit trs23
- Uncharacterized protein C15A10.12c
- Uncharacterized protein CC285.14
- Transport protein particle subunit trs120
- GTP-binding protein ypt1
Sequence:
MDIATNFITRSLSEIAPNASQSSLHVTPSSVSNNAFGLKLRQLISDTYCPHIFIMASDDTENFMKRKGFDDFASFIRPFGDRIFQSSTNNSAISKETLDSRIFDNDHDSIRFVPMEAVQVPRQWKRNKAWNTENGLENCANSRFAPGGDIDSFRVLSQKLIEEWVQSGSNNYPENGFLNPILDYLKLLLSGNPVAEHETFSHPVGCLIVITSHNTNPMATVMRLFKEINNAPFPNFISKEILHYYLFIHDEDNNDLSNSKQIFQQMRRSLGANSHFIRLRSNYISAKPLDTDRYDTSSIQSLKNAPRDSMESESFCSSSDDAKPITFVTKNLRKFPIPEWRSSLEVQAESEQSCLPLYPLLPVEEVEGMKKFVQTMLYDSIYPFMQRCVRAWEEDLTPQYGNLTTRLLFASKKYWSRNHSSHSQGNYDPLSLIYSSEKQESIKRKMADFSFMLRDYKRAYEIYDEIRNTFSQDKAWNYLASCEEIQIICLLMQNRNISLKSQISYLNKWFDEMVYIYAVRLHSFYYTFRSVLVTSLLLSLKPAFSIDFAASWLAKILEPGPISLNPFETSFLNTTIAGMYSNKEHVGVTDGNRRRKAAFWFAYSAGFWRDCGHCKMAEICWNLANRVYSKSGWESLSEHMLDLKPTLSENFRVKNTFH
Protein: POC1 centriolar protein homolog A (WD repeat-containing protein 51A) (Q8JZX3)
Organism: Mus musculus (Mouse)
Function: Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control. Acts in concert with POC1B to ensure centriole integrity and proper mitotic spindle formation (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Component of both mother and daughter centrioles. {ECO:0000250}.
Interaction partners:
- Centromere protein W
Sequence:
MAAPSQEDPSLERHFKGHRDAVTCVDFSLNTKHLASGSMDSTLMIWHMKPQSRAYRFTGHKDAVTCVNFSPSGHLLASGSRDKTVRIWVPNVKGESTVFRAHTATVRSVHFCSDGQSLVTASDDKTVKVWSTHRQRFLFSLTQHINWVRCAKFSPDGRLIVSASDDKTVKLWDKTSRECIHSYCEHGGFVTYVDFHPSGTCIAAAGMDNTVKVWDARTHRLLQHYQLHSAAVNALSFHPSGNYLITASSDSTLKILDLMEGRLLYTLHGHQGPATTVAFSRTGEYFASGGSDEQVMVWKSNFDIVDYGDMKARRPPPLTSSSGTLPKMDLPVPPGRDRSLESVQGEPQESISMPQTLTSTLEHIVGQLDILTQTVSILEQRLTLTEDRLKQCLENQQLIMQRTPP
Protein: Evasin P1128 (A0A0K8R6B3)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5 and CXCL8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MFIALGIQLFVAVTYAAGKDDEHFSVDYCGMNCTQQEDGSWTACSGRNEECRCYHESGKKNGLCLSTTYIDFSQYGNPSDSDIAAASPRP
Protein: Trafficking protein particle complex subunit 5 (Q8IUR0)
Organism: Homo sapiens (Human)
Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Trafficking protein particle complex subunit 3
- Trafficking protein particle complex subunit 9
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit 8
- Trafficking protein particle complex subunit 6A
- Trafficking protein particle complex subunit 10
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 4
- Trafficking protein particle complex subunit 6B
Sequence:
MEARFTRGKSALLERALARPRTEVSLSAFALLFSELVQHCQSRVFSVAELQSRLAALGRQVGARVLDALVAREKGARRETKVLGALLFVKGAVWKALFGKEADKLEQANDDARTFYIIEREPLINTYISVPKENSTLNCASFTAGIVEAVLTHSGFPAKVTAHWHKGTTLMIKFEEAVIARDRALEGR
Protein: Bestrophin-2a (Vitelliform macular dystrophy 2-like protein 1) (Q8NFU1)
Organism: Homo sapiens (Human)
Function: Forms calcium-sensitive chloride channels. Permeable to bicarbonate.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:E1BF86}; Multi-pass membrane protein {ECO:0000269|PubMed:35789156}. Basolateral cell membrane {ECO:0000269|PubMed:20407206}; Multi-pass membrane protein.
Interaction partners:
- Glutamine synthetase
- Cyclic nucleotide-gated channel alpha-2
Sequence:
MTVTYTARVANARFGGFSQLLLLWRGSIYKLLWRELLCFLGFYMALSAAYRFVLTEGQKRYFEKLVIYCDQYASLIPVSFVLGFYVTLVVNRWWSQYLCMPLPDALMCVVAGTVHGRDDRGRLYRRTLMRYAGLSAVLILRSVSTAVFKRFPTIDHVVEAGFMTREERKKFENLNSSYNKYWVPCVWFSNLAAQARREGRIRDNSALKLLLEELNVFRGKCGMLFHYDWISVPLVYTQVVTIALYSYFLACLIGRQFLDPAQGYKDHDLDLCVPIFTLLQFFFYAGWLKVAEQLINPFGEDDDDFETNFLIDRNFQVSMLAVDEMYDDLAVLEKDLYWDAAEARAPYTAATVFQLRQPSFQGSTFDITLAKEDMQFQRLDGLDGPMGEAPGDFLQRLLPAGAGMVAGGPLGRRLSFLLRKNSCVSEASTGASCSCAVVPEGAAPECSCGDPLLDPGLPEPEAPPPAGPEPLTLIPGPVEPFSIVTMPGPRGPAPPWLPSPIGEEEENLA
Protein: Tricyclene synthase Oc15, chloroplastic (AmOc15) (EC 4.2.3.105) (Myrcene synthase Oc15) (EC 4.2.3.15) (Terpenoid synthase Oc15) (Q84ND0)
Organism: Antirrhinum majus (Garden snapdragon)
Function: Contributes to floral scent emission.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250}.
Interaction partners:
Sequence:
MAFCISYVGALLPCSLSTRTKFAICHNTSKLHRAAYKTSRWNIPGDVGSTPPPSKLHQALCLNEHSLSCMAELPMDYEGKIKETRHLLHLKGENDPIESLIFVDATLRLGVNHHFQKEIEEILRKSYATMKSPIICEYHTLHEVSLFFRLMRQHGRYVSADVFNNFKGESGRFKEELKRDTRGLVELYEAAQLSFEGERILDEAENFSRQILHGNLAGMEDNLRRSVGNKLRYPFHTSIARFTGRNYDDDLGGMYEWGKTLRELALMDLQVERSVYQEELLQVSKWWNELGLYKKLNLARNRPFEFYTWSMVILADYINLSEQRVELTKSVAFIYLIDDIFDVYGTLDELIIFTEAVNKWDYSATDTLPENMKMCCMTLLDTINGTSQKIYEKHGYNPIDSLKTTWKSLCSAFLVEAKWSASGSLPSANEYLENEKVSSGVYVVLVHLFCLMGLGGTSRGSIELNDTQELMSSIAIIFRLWNDLGSAKNEHQNGKDGSYLNCYKKEHINLTAAQAHEHALELVAIEWKRLNKESFNLNHDSVSSFKQAALNLARMVPLMYSYDHNQRGPVLEEYVKFMLSD
Protein: 5-aminolevulinate synthase (EC 2.3.1.37) (5-aminolevulinic acid synthase) (Delta-ALA synthase) (Delta-aminolevulinate synthase) (Q8I4X1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Serine hydroxymethyltransferase
- Delta-aminolevulinic acid dehydratase
- GDP-L-fucose synthase
- NAD
- indole-3-glycerol-phosphate synthase
Sequence:
MRKKRTLKVSINEIKKYCPFVKNIQFLYNTNEKKNNLVLSVMSDLCPVGKAINEKHFIIIDNKSKINIIKILKQANMQSKVLVQCIKNKNIEKENMSNDDLLKSGKRNNNVLFYDILEKNKNDHSFQINDNTIQKNNIIYKYINSLDEYKLFKNNCNNNLKDLLNKLYTDKRYRIFTILNKYRINYPNVYIENNKLMLPSFYEFYQKYGYKPCIGNIRYQLSASFEDNNKNICSFSHKNKENYLFNFWNLHIDNVSNEKTVVWCSNDYLCLSNNEKIIEVGIETLKKIGNSSGGTRNISGSLLNHTHLEYIIAKWYNKESSLLFTSGYIANVGALETLGKLLNLIYISDEMNHASIINGIRESRCEKFIFKHNDMNDLERILYNLRINKQYENRKIMIVFESIYSMSGHISNIEYIVQLAKKYNALTYVDEVHAVGLYGNKGSGYLEELHLCNHIDIINGTLSKAIGSLGGFICANKYYIDVIRSYSSHFIFTTSLTPVNINTSAEAIHIIQNDMSLRKKLTQVVNKTKQKLQERGIQVLHNNSHIVVLMINSAEKCKQICDDLLKEYNIYIQPINYPTVPMGMERIRITPSPFHTDEQIFKLVNSLYTLFKKYQVNMFDKKNKHTLMKL
Protein: DRBM domain-containing protein (U4PRH5)
Organism: Caenorhabditis elegans
Interaction partners:
- Ribonuclease 3
- Endoribonuclease dcr-1
- DRBM domain-containing protein
- Importin N-terminal domain-containing protein
- Large ribosomal subunit protein mL44
Sequence:
MEQESGGKKSNEQLLSEREAIMRQLAMLGSGPEDLDVDDEEEDEEEEVEKMEEGVEETMENASVVKETTPVKDENIVEDSNSSEELFPYLDSPPEDKIQEISANDTEIDQIDSPIRFEGVKNPAQKMDVDGEEGTSTDARPVSGSSGSSVGEQIRAPVPVLKTIMDRIDLDKSNPLPEGWTVISHQSGMPVYYHKFTRVVTHSKPYLVEGIVRDHEIPVSSIPCLYKKIMDELHENVEKQSSKCPMTYEESQSMLEIPVKELRMSPDRYQKYCEKRFKFKQITVHRYINPAEKEGVVLKKRMNTILKKRGFDADYDQLKKNNKPGDVLLSSSTGAILIDLTPCPTNINKRSGSKKPYLLNPMGKTTVAVLNEFVQRLAKGTLLYEIEDTRNIHCPYKATALLTMKMCTLREMAGQCKESLVVLSEIAANDENSTTYSQGLLPDLRRFPVGSGVGANKKTARLVAARDALLKLIPKLRVSEDNVCDGMVEEDGTQQGFEELFKKVKIDSPNLVQMCTQCAIPKPYNLLRDAVSRSLRWNGMELVMKKEMIGNGSQLSKVILILGDIQEEAEAVGVKQATQMASQRLFKKMHPELLTYGSFLEIYGRLDDKSKIDNAKKQHDEVVRLPDTGNLLAPNFIVLSKLSEEMKNISLVYPPRKFLYGLATNSTGIKHDIRNVLTQTLMATLPPPPPQFFPMIGGPPLMHPTFSTSAPPPPPPPQPMEYGYNPMKQMPSRKRGRHDDSSSPSHQKPHK
Protein: ENL/AF9-related, isoform B (A0A0B4KG69)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00376}.
Interaction partners:
- Transcription initiation factor IIB
- TATA-box-binding protein
- RNA polymerase II elongation factor Ell
- Cyclin-dependent kinase 9
- DNA-directed RNA polymerase II subunit RPB3
- Alhambra, isoform P
- Ell-associated factor Eaf
- TBP-associated factor 3
- Transcription initiation factor TFIID subunit 1
- AF4/FMR2 family member lilli
Sequence:
MAVKVQFEIGHTSKLRSKKTPHPQAFTHDWEIYVQGVNKADISAFVEKVVFVLHESFPKPKRVVKEPPYAIQESGYAGFLLPVEIYFRNRDEPKRIVYQYDLVLQSTGPPQHHVEVKTHIFEAPSEEFRTKLMRGGGVPVFGANIGAGSLARTLSPSVGSGETAHSNEMSGVKAKGVPGTISMNSDLNTGKKHKSRSEDPGKSNAFSALFGPPITKTSVTANNMAQVPVSKHSPEAKSAAVGGKGVFHEGREKASKDRDKSSGGDKPREKDKKDRHGRDKDRKSSKSGDGKHERDKEKSKKDKSRDKEREREQGSGNTTSANALTVATSVGTAGGLVKHTASPKPGKPNEMGAPSPKKTANDSAAGAVAPTSRSKERDEHKSVKSESKDKERSSSKKSKKDKKDKDKQRDESKDKRMPKDERPGQSDSPASGNLQSAHLQQQSQVASTGKATPTSVGSNSSSSMVSNIGKQKEEATGKHSEKAAESKGDKSTSNGNATDTKKSHKHKKKEKSKDKEKERNDRDKDKDKERDKDKLKEREKDKQHVTGSEKSSTVDPSPKLEGASPATEGGAPDKTPVSASASSGSKKEKHKKSKEKSSGKDEKRQREAVDKQADTKHTGKSQQSQSGQSKTPSNLDLSDMDSAQSAPDLAATNALAAAAAATLQHSDSSNSSFPDLPARSSSQQKPTKGNTGSGKETKSTVKEHKGKSKQNDKTLEKNTDKTEKPDKTPDPKVDKSEKSEKEDKKRNRRSSQSSNSGSGAGVTGAFIEPPVKASKKEQGKAAGEKSKSPSLRPPRETNSTGTGGGTPNAGAGFLAPPSSSPSNNHSAAVAASLNNNNNNNNNNTNSNSSHSPGEMTTPGQLQLPTEYLSELQELHHKIMTLQDNEELQHVVEMIAATGCYEITHKTFDFDLCKLDRGTVQRLQEFLATSVSXHSLTSATGPALYS
Protein: Neuropeptide S (P0C0P7)
Organism: Rattus norvegicus (Rat)
Function: May play an important anorexigenic role. Modulates arousal and anxiety as well as increases locomotor activity. Binds to its receptor NPSR1 with nanomolar affinity to increase intracellular calcium concentrations.
Subcellular location: Secreted.
Interaction partners:
- Neuropeptide S receptor
- Corticotropin-releasing factor receptor 1
- Hypocretin neuropeptide precursor
- Relaxin-3
Sequence:
MIGSLKLNLILALSLSVVHVIWSYPVLSSKVPGKPDYFLILLSTCPARLEGSDGLAFLKPILEKTSMKRSFRNGVGSGVKKTSFRRAKQ