wanglab/gogpt-training-data huggingface dataset:
Protein: Leucine rich repeat containing 8 VRAC subunit Aa (Leucine rich repeat containing 8 family, member A) (Q4V8W3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MIPITELRYFADTQPAYRILKPWWDVFTDYISIVMLMIAVFGGTLQVTQDKMICLPCKWVVNQTCKHHLNVSVPLHTEPKGIQYDLDRHQYNYVDAVCYENKLHWFAKYFPYLVLLHTLIFLACSNFWFKFPRTSSKLEHFVSILLKCFDSPWTTRALSETVVEESDPKPAGKMNGSMDKKASSVSDQDVEASVPMLQRTKSRIEQGIVDHSETGVLDKKEGEQAKALFEKVKKFRIHVEEGDIVHRLYIRQIIIKVIQFLIIICYTMYYVHYITFSVTCTVDIERLTGYRTYHCAHPLATLFKILACFYISLVVVYGLICMYTLYWIISRSLKRYSFESIREESSYSDIPDVKNDFAFMLHMIDQYDPLYSKRFAVFLSEVSGNKLRQLNLNNEWALEKLRQRITKNSQEKLELHLFMLSGIPDTVFDLVELEVLKLELIPDITIPPIIAQLSNLREMWLYHTPARIEAPALAFLRENLTSLHIKFTDIKEIPLWIYSLKNLSELHLTGNLSAENNRFIVIDGLRELKRLKVLRLKSNLTKLPQVVTDVGVHLQKLSINNEGTKLMVLNSLKKMVNLTELELLCCDLERIPHSIFSLHNLQEIDLKDNNLKTIEEIISFQHLHRLVCLKLWYNQIAYIPIQIGTLTNLERLYLNRNKIEKIPAQLFFCRKLRYLDLSHNNLTSIPADIGFLQNLQYFAVTANRIETLPPELFQCKKLRTLNLGNNCLTALPSRFGELSGLTQLELRGNRLEGLPVELSECRLLKRSGLIVEEDLFNTLPPELKEQLWRTDKEQA
Protein: H-2 class II histocompatibility antigen, A-K alpha chain (P01910)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPRSRALILGVLALTTMLSLCGGEDDIEADHVGSYGITVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFAQLRRFEPQGGLQNIATGKHNLEILTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVTDGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL
Protein: Decorin (Bone proteoglycan II) (PG-S2) (P21793)
Organism: Bos taurus (Bovine)
Function: May affect the rate of fibrils formation.
Subcellular location: Secreted, extracellular space, extracellular matrix. Secreted {ECO:0000250|UniProtKB:P07585}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Receptor protein-tyrosine kinase
- Y-box-binding protein 1
- Insulin-like growth factor 1
- Biglycan
- Toll-like receptor 4
- Lumican
- Toll-like receptor 2
- Aggrecan core protein
- Collagen type III alpha 1 chain
Sequence:
MKATIIFLLVAQVSWAGPFQQKGLFDFMLEDEASGIGPEEHFPEVPEIEPMGPVCPFRCQCHLRVVQCSDLGLEKVPKDLPPDTALLDLQNNKITEIKDGDFKNLKNLHTLILINNKISKISPGAFAPLVKLERLYLSKNQLKELPEKMPKTLQELRVHENEITKVRKSVFNGLNQMIVVELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITTIPQGLPPSLTELHLDGNKITKVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLNNNKLVKVPGGLADHKYIQVVYLHNNNISAIGSNDFCPPGYNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRAAVQLGNYK
Protein: Protein kinase (D4Q8H0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSLGASFVQIKFDDLQFFENCGGGSFGSVYRAKWISQDKEVAVKKLLKIEKEAEILSVLSHRNIIQFYGVILEPPNYGIVTEYASLGSLYDYINSNRSEEMDMDHIMTWATDVAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHNHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERLTIPSSCPRSFAELLHQCWEADAKKRPSFKQIISILESMSNDTSLPDKCNSFLHNKAEWRCEIEATLERLKKLERDLSFKEQELKERERRLKMWEQKLTEQSNTPLLLPLAARMSEESYFESKTEESNSAEMSCQITATSNGEGHGMNPSLQAMMLMGFGDIFSMNKAGAVMHSGMQINMQAKQNSSKTTSKRRGKKVNMALGFSDFDLSEGDDDDDDDGEEEDNDMDNSE
Protein: 5-hydroxymethyl-dUMP N-hydrolase (EC 3.2.2.-) (2'-deoxynucleoside 5'-phosphate N-hydrolase 1) (c-Myc-responsive protein RCL) (O43598)
Organism: Homo sapiens (Human)
Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18726892}. Nucleus {ECO:0000269|PubMed:9271375}.
Interaction partners:
Sequence:
MAAAMVPGRSESWERGEPGRPALYFCGSIRGGREDRTLYERIVSRLRRFGTVLTEHVAAAELGARGEEAAGGDRLIHEQDLEWLQQADVVVAEVTQPSLGVGYELGRAVAFNKRILCLFRPQSGRVLSAMIRGAADGSRFQVWDYEEGEVEALLDRYFEADPPGQVAASPDPTT
Protein: Cholesterol transporter ABCA5 (EC 7.6.2.-) (ATP-binding cassette sub-family A member 5) (Q8K448)
Organism: Mus musculus (Mouse)
Function: Cholesterol efflux transporter in macrophages that is responsible for APOAI/high-density lipoproteins (HDL) formation at the plasma membrane under high cholesterol levels and participates in reverse cholesterol transport. May play a role in the processing of autolysosomes.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8CF82}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8CF82}. Lysosome membrane {ECO:0000269|PubMed:15870284}; Multi-pass membrane protein {ECO:0000269|PubMed:15870284}. Late endosome membrane {ECO:0000269|PubMed:15870284}; Multi-pass membrane protein {ECO:0000269|PubMed:15870284}. Cell membrane {ECO:0000269|PubMed:32687853}. Note=Localized at cell membrane under high cholesterol levels. {ECO:0000269|PubMed:32687853}.
Interaction partners:
Sequence:
MATAIRDVGVWRQTRTLLLKNYLIKCRTKKSSVQEILFPLFFLFWLILVSMMHPNKKYEEVSDIELSPMDKFSLSNVILGYTPVTNITSSIMQRVSTDHLPKVIVTEEYANEKELVAASLSKSSNFVGVVFKDTMSYELRFFPEMIPVSSIYMNSREGCSKTCDAAQYWSLGFTVLQASIDAAIIQLKTNVSVWSELESTKAVIMGEAAVVEIDTFPRGVILIYLVIAFSPFGYFLAIHIVAEKEKKLKEFLKIMGLHDTAFWLSWVLLYASLIFLMSLLMAVIATASSLFPQSSSIVIFLLFFLYGLSSVFFALMLTPLFKKSKHVGVVEFFVTVVFGFVGLLIVLIESFPRSLVWLFSPLCQCAFLIGIAQVMHLEDFNEGALFSNLTEGPYPLIITIIMLALDSVFYVLLAVYLDQVIPGEFGLRRSSLYFLKPSYWSKNKRNYKELSEGNINGNISLNEIVEPVSSEFIGKEAIRISGIQKSYRKKTENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDINFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSVGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSSIFLKSKWGIGYRLSMYIDRYCATESLSSLVRQHIPAAALLQQNDQQLVYSLPFKDMDKFSGLFSALDIHSNLGVISYGVSMTTLEDVFLKLEVEAEIDQADYSVFTQQPREEETDSKSFDEMEQSLLILSETKASSVSTMSLWKQQVSTIAKFHFLSLKRESKSVRAVLLLLLIFFAVQIFMFFLHHSFKNAVVPIKLVPDLYFLKPGDKPHKYKTSLLLQNSTDSDINGLIEFFAHQNIMVAMFNDSDYVSAAPHSAALNVVRSEKDYVFSAVFNSTMVYCLPVMMNIISNYYLYHLNVTEAIQTWSTPFIQEITDIVFKIELYFQAALLGIIVTAMPPYFAMENAENHKIKAYTQLKLSGLLPSAYWVGQAVVDIPLFFVVLILMLGSLFAFHHGLYFYPAKFLAVVFCLIAYVPSVILFTYIASFTFKKILNTKEFWSFIYSVTALACVAITETTFFLQYAVTAVFHYTFCIAIPIYPLLGCLISFIKGSWKNMPKNENTYNPWDRLLVAVIMPYLQCILWIFLLQHYEKIHGGRSIRKDPFFRALSQKAKNKKFPEPPINEDEDEDVKAERLKVKELMGCQCCEEKPAIMVCNLHKEYDDKKDFLHSRKTTKVATKYISFCVKKGEILGLLGPNGAGKSTVINTLVGDVEPTSGKIFLGDYGSHSSEDDESIKCMGYCPQTNPLWPDLTLQEHFEIYGAVKGMSPGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGYFLEIKLKDWIENLEIDRLQREIQYIFPNASRQESFSSILAFKIPKEDVQSLSQSFAKLEEAKRTFAIEEYSFSQATLEQVFVELTKEQEEEDNSCGTLASTLWWERTQEDRVVF
Protein: Insulin-like growth factor 2 (Insulin-like growth factor II) (Q8UWF9)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
RGIVEECCFRSCDLNLLEQYCAKPAKSERDVSATSLQIIPMVPTLKQDVPRKHVTVKYSKYEVWQRKAAQRLRRGVPAILRARKFRRQAVKT
Protein: GPI mannosyltransferase 1 (EC 2.4.1.-) (GPI mannosyltransferase I) (GPI-MT-I) (Phosphatidylinositol-glycan biosynthesis class M protein) (PIG-M) (Q9EQY6)
Organism: Rattus norvegicus (Rat)
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI alpha-1,4-mannosyltransferase I, stabilizing subunit
- GPI alpha-1,6-mannosyltransferase 2
- Mannosyltransferase
- Glucosaminyl-phosphatidylinositol-acyltransferase PIGW
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dol-P-Man:Man
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Dolichol-phosphate mannosyltransferase subunit 1
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Dolichol-phosphate mannosyltransferase subunit 3
Sequence:
MSYTKHWGEWFLNLRVPPAGVFGVAFLARVALVFYGVFQDRTLLVRYTDIDYHVFTDAARFVTEGRSPYLRATYRYTPLLSWLLTPNVYLSELFGKFLFISCDLLTAFLLYRLLLLKGLGRRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLTTLYLIEKRLIACAAVFYGFAVHMKMYPVTYILPIALHLRPERDSDEGLRLARYSFQARLYDFLKRLCSWAVLLFVAIAGLTFLALSFGFYYKYGWEFLEHTYLYHLTRRDIRHNFSPYFYMLYLTAESKWSFTLGIAAFLPQFILLSAASFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVLLMLWFIGQALWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEDRLTERIKYD
Protein: F-box domain-containing protein (Q9XXI8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAPKCWSNLPSDVKREVLEHGDCQQWFNVRLCSRADMNLVDSLKLRIPFLKIQISNTTFSIIIVESPSAILRIDLHQKSGGNAEFSVEIFKNSDLELGNLIKTIENTTLDAEISNLLEKSIFHRKIDIATCQIQADGLQAENPVLAMIHAKFTENAPKKLIFSGKSMEENRFLAKFFENLNIDFVFRSWRKDLSREWGEGMNHLRIKIFEVSKWTTLLGDFEHFTAYDEIEPVMYMARILSRPMKRSHWFPGFHVPVAERLFRQIFRQEMFEKFENHSIRKSPINLKLWIFVKFTKCGISIFVGDPKDFNERDGTCDLEWMCPNCAPKTMENWFFRETIGKLHF
Protein: ALMS motif domain-containing protein (Q381U9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFADRENLIMEAVAALERQRELTARSEGTMSDYEDDSLLDTYLRIKAEGQYKEPTRSDSSWSEQSGFDEFNEHTWSYGNQGITETASEICSQGGSRFDTFHGTSAGHYIYPTEQSRQVQVRKLGKGSPVRKREEPSLDETSLHKGSARVNETKWSDSLHMDVEQLNIELERIGRTDPSFLRQFRNVYGEMEEEEGRDQNQEMERISRSHEDGSQIAFVMTPKREKNLPEAASLSGKNGALTRAATRWNEYLMRDETTIEVSDVFDSDEEHGGGSSSLQHRGDSLMERRQRTKEKWEAKELQECTFRPQLSRASVSMFQKSSQSRDSVFQRLYQRNFAGKRSEGGNNSSVRELLLAEKDQLREMYGGATSTKGGADSFELFMFNILGSKDEQKAAFVDTKYQSPLARKLMTVRHENTFNRTTSYNGGHHDSGSSRGASFDSFLLRQDKHLANRTRTVRQIEESQRPSFKPQITNTSVRIAKRLLARNESEVGNVKSAPTLAAAVKKHRSPYVDPCTFKPETAPGSSGAKPSGVEVLFLDSVRRRNSIKAAQEKARSAEMKHPFKPTLNDERNRNVESYLSSKHLVAYTENLKRQKERLAEMREQKEREKEREMAEQATFRPKISRTPAYIRRMASSFALVRQQCAN
Protein: Ubiquitin carboxyl-terminal hydrolase 29 (EC 3.4.19.12) (Deubiquitinating enzyme 29) (Ubiquitin thioesterase 29) (Ubiquitin-specific-processing protease 29) (Q9ES63)
Organism: Mus musculus (Mouse)
Function: Deubiquitinase involved in innate antiviral immunity by mediating 'Lys-48'-linked deubiquitination of CGAS, thereby promoting its stabilization.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:32457395}. Note=Localizes to perinuclear region in response to herpes simplex virus-1 (HSV-1) infection. {ECO:0000269|PubMed:32457395}.
Interaction partners:
- Zinc finger, imprinted 1
Sequence:
MAHLKINGLVQIRSTNRSKHTRASQWKEAVIEIVERKQKVNLVVSFKLEERRRVFQLGDNVTGVVVSGELGLYHLDLTLRDDTSLLIDKLSSADVEHLKSFLDSSTPCESQQPMEPMSSQDDLESSDPFCGEHQEAACGSLNTTPESGTPLSRKMPLSMSNTTGGQKRGEKQGRKRKTEPSSSSAEVNKDIPKENTPDQKKKSRRYYSRNRGGKAEKAVTLREQEKRSNWKLEPAFNSKSYGRANLDGTILPIATCSDDRDVSIFGLEIITHNGVQSLPDPYLNQLKREGFPNLGNTCYMNSILQSVFGIPTFAKDLLTQGIPWEKVSYDDLIMPLSQLLVLKDIRDVEIKGELLTSVKKSISTVADTFSGNEQNDAHEFLSLCLDQLKLNMEKVNAMWDTERRNTCAGSAGTKRFVCPVGANFEFELHSSIICEGCGEATIKTEVSNYLSIDLHHGTKTHPLSIQKSFDLFFTPEKIEHNCEKCKNKNSVLKYTLRRLPRVLIVHLKRYQVTTDLLPVKSEQPVEISKYLNISSHCHENRKLPFPLANTSPDVSQGMMPGIFNQSMLSKKVISESCDPMVLQVGSSVDAEIQSFQIMYEDEDASEEQQQRGLESGSMLEPELVKTENRILRQKTSLATDSMMGDGYSFLPMLCEPLSIQDPGLAEMGLQEVPENPEFKNYEKINIYGKSDGRTNTELSKLYQNHGSRIKGLFLPASLASVSSQEDPEKDLSRSPELQEDDPHSFAFGSDDSKDGEMGDDLQNYRLVSVVSHFGSSPNSGHYVSDVYDFQKQAWLLYSDVQVFESSDPSIQENRLNSGYIFFYMHNEIFEELLKKASECKVLSTSKEEKRDIDYFSTLLNGLTYILEEF
Protein: Ribonuclease P protein component 3 (RNase P component 3) (EC 3.1.26.5) (Rpp30) (P60781)
Organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00756, ECO:0000269|PubMed:20675586}.
Interaction partners:
- Large ribosomal subunit protein eL8
- Ribonuclease P protein component 1
- Ribonuclease P protein component 2
- Ribonuclease P protein component 4
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS5
- Endoribonuclease Nob1
- 2-phosphosulfolactate phosphatase
Sequence:
MLEGIFDINHVFDEEGIKTLKRFGWDGSVAVQNHNEYSEEKINTAVEYGENCEFKVYSGVKISTKNQNEMEKAVKKYRNKVDILLVEGGDVKINRRVLEMNDVDILSTPELNRMDNGLDHILARLGSTNRVAVELNFGNLLKSKNYDRSKILWAFQRNLKLSKKYDTPVVISSGANDIYGIKAPGDLRGFLNTVADPLYSKKIIETTSKIIDYRLYLKNKNVLMPGLEIVEE
Protein: Chitinase-3-like protein 1 (BRP39 protein) (Breast regression protein 39) (Cartilage glycoprotein 39) (CGP-39) (GP-39) (Q61362)
Organism: Mus musculus (Mouse)
Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung.
Subcellular location: Secreted, extracellular space. Cytoplasm. Endoplasmic reticulum. Note=Detected in bronchoalveolar lavage (BAL) fluids. Localizes mainly to endoplasmic reticulum when overexpressed in cells, with some protein also detected throughout the cytoplasm.
Interaction partners:
- Interleukin-13 receptor subunit alpha-2
- Neutrophil gelatinase-associated lipocalin
- Insulin-like growth factor-binding protein 3 receptor
Sequence:
MHTSTEARMGMRAALTGFAVLMLLQSCSAYKLVCYFTSWSQYREGVGSFLPDAIQPFLCTHIIYSFANISSDNMLSTWEWNDESNYDKLNKLKTRNTNLKTLLSVGGWKFGEKRFSEIASNTERRTAFVRSVAPFLRSYGFDGLDLAWLYPRLRDKQYFSTLIKELNAEFTKEVQPGREKLLLSAALSAGKVAIDTGYDIAQIAQHLDFINLMTYDFHGVWRQITGHHSPLFQGQKDTRFDRYSNVNYAVQYMIRLGAQASKLLMGIPTFGKSFTLASSENQLGAPISGEGLPGRFTKEAGTLAYYEICDFLKGAEVHRLSNEKVPFATKGNQWVGYEDKESVKNKVGFLKEKKLAGAMVWALDLDDFQGTCQPKEFFPLTNAIKDALA
Protein: Trypanothione reductase (EC 1.8.1.12) (N(1),N(8)-bis(glutathionyl)spermidine reductase) (Q4QJG7)
Organism: Leishmania major
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Trypanothione synthetase
- Thioredoxin
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
- 3-methyl-2-oxobutanoate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta
- 2-oxoisovalerate dehydrogenase subunit alpha
- thioredoxin-dependent peroxiredoxin
- Tryparedoxin
Sequence:
MSRAYDLVVLGAGSGGLEAGWNAAATYKKKVAVVDVQATHGPPFFAALGGTCVNVGCVPKKLMVTGAQYMDLIRESGGFGWEMNRESLCPNWKTLIAAKNKVVNGINESYKSMFADTEGLSFHMGFGALQDAHTVLVRKSEDPNSDVLETLDTEYILIATGSWPTRLGVPGDEFCITSNEAFYLEDAPKRMLCVGGGYIAVEFAGIFNGYKPRGGYVDLCYRGDLILRGFDTEVRKSLTKQLGANGIRVRTNLNPTKITKNEDGSNHVHFNDGTEEDYDQVMLAIGRVPRSQTLQLDKAGVQTAKNGAVQVDAYSKTSVDNIYAIGDVTNRVMLTPVAINEGAAFAETVFGGKPRATDHTKVACAVFSIPPIGTCGMTEEEAAKNHETVAVYESCFTPLMHNISGSKHKEFMIRIITDQPSGEVLGVHMLGDSAPEIIQSVGICMKMGAKISDFHNTIGVHPTSAEELCSMRTPAYFYENGKRVEKLSSNL
Protein: PC-esterase domain-containing protein 1A (Protein FAM113A) (Sarcoma antigen NY-SAR-23) (Q9H1Q7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVFCLSSEEPRRPLRSDMVHFQASEVQQLLHNKFVVILGDSIQRAVYKDLVLLLQKDSLLTAAQLKAKGELSFEQDQLVAGGQLGELHNGTQYREVRQFCSGSGHHLVRFYFLTRVYSEYLEDVLEELTYGPAPDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNMAMPLGERITGGFLLPELQPLAGSLRRDVVEGNFYSATLAGDHCFDVLDLHFHFRHAVQHRHRDGVHWDQHAHRHLSHLLLTHVADAWGVELPKRGYPPDPWIEDWAEMNHPFQGSHRQTPDFGEHLALLPPPPSSLPPPMPFPYPLPQPSPPPLFPPLPQDTPFFPGQPFPPHEFFNYNPVEDFSMPPHLGCGPGVNFVPGPLPPPIPGPNPHGQHWGPVVHRGMPRYVPNSPYHVRRMGGPCRQRLRHSERLIHTYKLDRRPPAHSGTWPG
Protein: Tubulin polyglutamylase TTLL6 (EC 6.3.2.-) (Protein polyglutamylase TTLL6) (Tubulin--tyrosine ligase-like protein 6) (Q8N841)
Organism: Homo sapiens (Human)
Function: Polyglutamylase which modifies both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins. Preferentially mediates ATP-dependent long polyglutamate chain elongation over the initiation step of the polyglutamylation reaction. Preferentially modifies the alpha-tubulin tail over a beta-tail. Promotes tubulin polyglutamylation which stimulates spastin/SPAST-mediated microtubule severing, thereby regulating microtubule functions. Mediates microtubule polyglutamylation in primary cilia axoneme, which is important for ciliary structural formation and motility. Mediates microtubule polyglutamylation in motile cilia, necessary for the regulation of ciliary coordinated beating. Polyglutamylates non-tubulin protein nucleotidyltransferase CGAS, leading to CGAS DNA-binding inhibition, thereby preventing antiviral defense response.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A4Q9E8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A4Q9E8}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:22246503}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:22246503}. Note=CEP41 is required for its transport between the basal body and the cilium axoneme. {ECO:0000269|PubMed:22246503}.
Interaction partners:
- Centrosomal protein of 41 kDa
- Cytosolic carboxypeptidase 6
- Cytosolic carboxypeptidase-like protein 5
Sequence:
MGALLLHPSRRGPAGVVASWTSSPAGRDGGVGIAGAWYFPRASSQAREMPQCPTLESQEGENSEEKGDSSKEDPKETVALAFVRENPGAQNGLQNAQQQGKKKRKKKRLVINLSSCRYESVRRAAQQYGFREGGEDDDWTLYWTDYSVSLERVMEMKSYQKINHFPGMSEICRKDLLARNMSRMLKMFPKDFRFFPRTWCLPADWGDLQTYSRSRKNKTYICKPDSGCQGKGIFITRTVKEIKPGEDMICQLYISKPFIIDGFKFDLRIYVLVTSCDPLRIFVYNEGLARFATTSYSRPCTDNLDDICMHLTNYSINKHSSNFSRDAHSGSKRKLSTFSAYLEDHSYNVEQIWRDIEDVIIKTLISAHPIIRHNYHTCFPNHTLNSACFEILGFDILLDHKLKPWLLEVNHSPSFSTDSRLDKEVKDGLLYDTLVLINLESCDKKKVLEEERQRGQFLQQCCSREMRIEEAKGFRAVQLKKTETYEKENCGGFRLIYPSLNSEKYEKFFQDNNSLFQNTVASRAREEYARQLIQELRLKREKKPFQMKKKVEMQGESAGEQVRKKGMRGWQQKQQQKDKAATQASKQYIQPLTLVSYTPDLLLSVRGERKNETDSSLNQEAPTEEASSVFPKLTSAKPFSSLPDLRNINLSSSKLEPSKPNFSIKEAKSASAVNVFTGTVHLTSVETTPESTTQLSISPKSPPTLAVTASSEYSGPETDRVVSFKCKKQQTPPHLTQKKMLKSFLPTKSKSFWESPNTNWTLLKSDMNKPHLISELLTKLQLSGKLSFFPAHYNPKLGMNNLSQNPSLPGECHSRSDSSGEKRQLDVSSLLLQSPQSYNVTLRDLLVIATPAQLDPRPCRSHASAMRDPCMQDQEAYSHCLISGQKGCERS
Protein: Sodium- and chloride-dependent transporter XTRP3B (IMINO-K) (Solute carrier family 6 member 20B) (O88575)
Organism: Mus musculus (Mouse)
Function: Does not show transporter activity with a range of tested amino acids including proline, glutamine, glutamic acid, leucine, alanine, histidine, glycine and arginine.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:16174864}; Multi-pass membrane protein {ECO:0000269|PubMed:16174864}. Note=Located in the apical brush border membrane of kidney proximal tubule cells.
Interaction partners:
- Angiotensin-converting enzyme 2
- Leucine zipper transcription factor-like protein 1
- Collectrin
- FYVE and coiled-coil domain-containing protein 1
Sequence:
MESPSAHAVSLPEDEELQPWGGAGGPGQHPGRPRSTECAHPGVVEKVRPKWDNPLQFLLVCISYAVGLGNVWRFPYLCQMYGGGNFLVPYIIMLIVEGMPLLYLELAVGQRMRQGSIGAWRTISPYLSGVGIASLVVSFLASVYFNVINTWALWYLFHSFQDPLPWSVCPLNSNHTGYDEECEKASSTQYFWYRKTLNISPSIQENGGVQWEPALCLTLAWLMVYLCILRGTESTGKVVYFTTSLPYFVLIIYLVRGLTLHGATNGLAYMFTPKIEQLANPKAWINAATQIFFSLGLGCGGLIAFASYNEPSNDCQKHALIVSVINSTTAIFSSIVTFSIYGFKATFNYENCLNKVILLLTNSFDLEDGFLTVSNLEEVKNYLASTYPNKYSEVFPHIRNCSLESELDTAVQGTGLAFIVYTEAIKNMEVSQLWSVLYFFMLLTLGMGSMVGTGTAILTPLTDSKIISSYLPKEAISGLVCLLNCAIGMVFTMEAGNYWFDLFNDYTATLSLLLIVLVETIAVCYVYGLKRFESDLRAMTGRTLSWYWKVMWAFVSPLLIVGLFIFYLSDYILTGTLQYQAWDATQGHVVTKDYPTYALAVIGLLVASSTMCIPLVALGTFVTRHFKIREQFSAA
Protein: Cytochrome f (Q6H8M0)
Organism: Nostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.)
Subcellular location: Cellular thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_00610}; Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00610}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MRNACTRARLTRTARAMVKTLFIAIASVTFFFTSDLALPQSAAAYPFWAQQTYPETPREPTGRIVCANCHLAAKPTEVEVPQSVLPDTVFKAVVKIPYDTSVQQVGADGSKVGLNVGAVLMLPEGFKIAPEDRIPEELKEEIGDVYFQPYGEDKDNIVIVGPLPGEQYQEIVFPVLSPNPANDKNIHFGKYSVHVGGNRGRGQVYPTGEKSNNNLYSAAATGTISKIAKQEGEDGSVKYLVDIKTESGEVVSDTIPAGPELIVSEGQAVTAGDALTNNPNVGGFGQLDAEIVLQDANRVGWLIAFVALVMLAQVMLVLKKKQVEKVQAAEMNF
Protein: Homeobox protein Nkx-3.1 (Homeobox protein NK-3 homolog A) (P97436)
Organism: Mus musculus (Mouse)
Function: Transcription factor, which binds preferentially the consensus sequence 5'-TAAGT[AG]-3' and can behave as a transcriptional repressor (By similarity). Plays an important role in normal prostate development, regulating proliferation of glandular epithelium and in the formation of ducts in prostate. Acts as a tumor suppressor controlling prostate carcinogenesis, as shown by the ability to suppress growth and tumorigenicity of prostate carcinoma cells. Plays a role in the formation of minor salivary glands (particularly palatine and lingual glands).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- RAC-alpha serine/threonine-protein kinase
- RAC-gamma serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- Androgen receptor
- Probasin
- Transmembrane protease serine 2
- Hepatocyte nuclear factor 3-alpha
Sequence:
MLRVAEPREPRVEAGGRSPWAAPPTQSKRLTSFLIQDILRDRAERHGGHSGNPQHSPDPRRDSAPEPDKAGGRGVAPEDPPSIRHSPAETPTEPESDAHFETYLLDCEHNPGDLASAPQVTKQPQKRSRAAFSHTQVIELERKFSHQKYLSAPERAHLAKNLKLTETQVKIWFQNRRYKTKRKQLSEDLGVLEKNSPLSLPALKDDSLPSTSLVSVYTSYPYYPYLYCLGSWHPSFW
Protein: Probable mitochondrial pyruvate carrier 1 (MPC1) (O74847)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P53157}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable mitochondrial pyruvate carrier 2
- Large ribosomal subunit protein eL8
- Small nuclear ribonucleoprotein-associated protein B
Sequence:
MNASEKLSQKAAQSVTRRFITWLKSPDFRKYLCSTHFWGPLSNFGIPIAAILDLKKDPRLISGRMTGALILYSSVFMRYAWMVSPRNYLLLGCHAFNTTVQTAQGIRFVNFWYGKEGASKQSVFENIMQAAKHPESGTRQK
Protein: HL05804p (Straw, isoform A (EC 1.10.3.-, EC 1.16.3.1)) (Q7JQF6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKAMDLNGFYQTFISFLIWGAFSNFPEVFAVRVANSQQNQPKKENQPDLTPMGSFWQQHVATPSSSTPFDSPFFSATHGLVQTHPSIGGSHSGPAPLNGNSLGSGAPSSILAGTKPALTAGSGYLNSRGSLPTSARYPANKITGTVVEPNPKSPFRHLDFSTSATAELRRNPALSAPDECARACREGEPPRICYYHFTLEYYTVLGAACQVCTPNATNTVWSHCQCVLADGVERGILTANRMIPGPSIQVCENDKVVIDVENHMEGMEVTIHWHGIWQRGSQYYDGVPFVTQCPIQQGNTFRYQWTGNAGTHFWHAHTGLQKLDGLYGSVVVRQPPSRDPNSHLYDFDLTTHIMLISDWLHEDAAERYPGRLAVNTGQDPESMLINGKGQFRDPNTGFMTNTPLEIFTITPGRRYRFRMINAFASVCPAQVTIEGHGMTVIATDGEPVHPVDVNTIISFSGERYDFVISADQPVGAYWIQLRGLGECGIRRAQQLAILRYARGPYQPASSPPTYDVGIPQGVVMNPLDAQCNRQRNDAICVSQLKNALEIDRGILAEKPDVKIFLPFRFFVYRAEDLFQPNTYNRFLVAPTGDHVISLIDEISYLSAPAPLTSQYNDINPDQFCNGDNRPADCGPNCMCTHKIDIPLNAIVEVVLVDEVQQPNLSHPFHLHGYGFSVIGIGRSPDSSVKKINLKHALDLDRRGLLHRQYNLPPTKDTIAVPNNGYVVLRFRADNPGFWLFHCHFLFHIVIGMNLILQVGTNADLPPVPPGFPTCGDHTPSIPIN
Protein: Arabinogalactan peptide 3 (OsAGPEP3) (A9UGV7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
Subcellular location: Vacuole, aleurone grain membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MASRILYAAAVVAAVAVSSLAGVAYAADAPAPSPTSGAAAVSSSLVAAVLCPAVALLLGNLRQ