wanglab/gogpt-training-data huggingface dataset:
Protein: Heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) (AU-rich element RNA-binding protein 1) (Q60668)
Organism: Mus musculus (Mouse)
Function: Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q14103}. Cytoplasm {ECO:0000250|UniProtKB:Q14103}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasmic localization oscillates diurnally. {ECO:0000250|UniProtKB:Q14103}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein A3
- Heterogeneous nuclear ribonucleoprotein Q
- Far upstream element-binding protein 2
- Polyadenylate-binding protein-interacting protein 1
- DNA
- Heterogeneous nuclear ribonucleoprotein U
- Heterogeneous nuclear ribonucleoprotein K
- ELAV-like protein 1
- Transportin-1
- Cold shock domain-containing protein E1
Sequence:
MSEEQFGGDGAAAAATAAVGGSAGEQEGAMVAAAAQGPAAAAGSGSGGGGSAAGGTEGGSAEAEGAKIDASKNEEDEGHSNSSPRHTEAAAAQREEWKMFIGGLSWDTTKKDLKDYFSKFGEVVDCTLKLDPITGRSRGFGFVLFKESESVDKVMDQKEHKLNGKVIDPKRAKAMKTKEPVKKIFVGGLSPDTPEEKIREYFGGFGEVESIELPMDNKTNKRRGFCFITFKEEEPVKKIMEKKYHNVGLSKCEIKVAMSKEQYQQQQQWGSRGGFAGRARGRGGGPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSNQQSGYGKVSRRGGHQNSYKPY
Protein: Peptidyl-prolyl cis-trans isomerase CYP19-4 (PPIase CYP19-4) (EC 5.2.1.8) (Cyclophilin of 19 kDa 4) (Cyclophilin-5) (Rotamase CYP19-4) (Q8LDP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved during embryogenesis and organ development by regulating the folding of EMB30/GNOM, and thus, by modulating its activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10715321}. Membrane {ECO:0000269|PubMed:10715321}. Endoplasmic reticulum {ECO:0000269|PubMed:10189705}. Secreted {ECO:0000269|PubMed:10189705}. Note=Mostly cytoplasmic, also membrane-associated (PubMed:10715321). Present in endoplasmic reticulum and barely secreted (PubMed:10189705). {ECO:0000269|PubMed:10189705, ECO:0000269|PubMed:10715321}.
Interaction partners:
- UPF0235 protein At5g63440
- Ubiquitin-ribosomal protein eS31y fusion protein
- Probable cysteine protease RD21B
- ARF guanine-nucleotide exchange factor GNOM
- Cysteine proteinase RD21A
- Probable cysteine protease RD21C
- At1g09850
- Actin-12
- Tetratricopeptide repeat
- Pre-mRNA-splicing factor SYF2
Sequence:
MAKASFILLGTLFLFGAIASIQAKEDLKEVTHKVYFDVEIDGKSAGRVVIGLFGKAVPKTAENFRALCTGEKGVGKSGKPLHYKGSKFHRIIPSFMIQGGDFTHGNGMGGESIYGQKFADENFKLKHTGPGVLSMANSGEDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKVVIADSGELPL
Protein: G antigen 12B/C/D/E (GAGE-12B) (GAGE-12C) (GAGE-12D) (GAGE-12E) (A1L429)
Organism: Homo sapiens (Human)
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein eL15
Sequence:
MSWRGRSTYYWPRPRRYVQPPEMIGPMRPEQFSDEVEPATPEEGEPATQCQDPAAAQEGEDEGASAGQGPKPEAHSQEQGHPQTGCECEDGPDGQEMDPPNPEEVKTPEEGEKQSQC
Protein: Uncharacterized J domain-containing protein SPAC1071.09c (Q9UTQ5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDIDPYSVLGVEKDASDELIRRAYRKKALQHHPDRIHDEEKKVEARIEFDKVAIAYGVLSDKKRRKHYDKTGQLRETDADIDFDWKEWLDELYQGVVSGETLNEFKASYQYSEEEKCDVLKAYEKGKGSMDVILEEVMCCEISDEDRFRQVINNAIKDGKISKYKRFAPNEKKRKRRAKAAEREAQEAEELSMELGLDENLKKRRKAGASDEEALSALIRSRQKSRMYNLISNLESKYSKSSTKPKKSKKSRSKE
Protein: GATA transcription factor 20 (Protein HAN-LIKE 1) (Q9ZPX0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Rop guanine nucleotide exchange factor 5
- Protein IQ-DOMAIN 18
- Protein IQ-DOMAIN 6
Sequence:
MMGYQTNSNFSMFFSSENDDQNHHNYDPYNNFSSSTSVDCTLSLGTPSTRLDDHHRFSSANSNNISGDFYIHGGNAKTSSYKKGGVAHSLPRRCASCDTTSTPLWRNGPKGPKSLCNACGIRFKKEERRATARNLTISGGGSSAAEVPVENSYNGGGNYYSHHHHHYASSSPSWAHQNTQRVPYFSPVPEMEYPYVDNVTASSFMSWN
Protein: 5-hydroxytryptamine receptor 1D (5-HT-1D) (5-HT1D) (Serotonin receptor 1D) (Q61224)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P28221}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P28221}.
Interaction partners:
- Basigin
- 5-hydroxytryptamine receptor 1B
- Sodium-dependent serotonin transporter
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 3A
- Guanine nucleotide-binding protein G
Sequence:
MSPPNQSLEGLPQEASNRSLNVTGAWDPEVLQALRISLVVVLSVITLATVLSNAFVLTTILLTKKLHTPANYLIGSLATTDLLVSILVMPISIAYTTTRTWNFGQILCDIWVSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAAAMIAAVWIISICISIPPLFWRQATAHEEMSDCLVNTSQISYTIYSTCGAFYIPSILLIILYGRIYVAARSRILNPPSLYGKRFTTAQLITGSAGSSLCSLNPSLHESHTHTVGSPLFFNQVKIKLADSILERKRISAARERKATKTLGIILGAFIICWLPFFVVSLVLPICRDSCWIHPALFDFFTWLGYLNSLINPVIYTVFNEDFRQAFQKVVHFRKIS
Protein: Malate dehydrogenase (EC 1.1.1.37) (A0A024R4K3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLSALARPASAALRRSFSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGVAADLSHIETKAAVKGYLGPEQLPDCLKGCDVVVIPAGVPRKPGMTRDDLFNTNATIVATLTAACAQHCPEAMICVIANPVNSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANTFVAELKGLDPARVNVPVIGGHAGKTIIPLISQCTPKVDFPQDQLTALTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVDAMNGKEGVVECSFVKSQETECTYFSTPLLLGKKGIEKNLGIGKVSSFEEKMISDAIPELKASIKKGEDFVKTLK
Protein: Fused predicted transporter subunits of ABC superfamily: ATP-binding components (E0SKG8)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
Sequence:
MLVTNNITMQFGSKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLAPSAGNVAIDTNERVGKLRQDQFAFEQYSVLDTVIMGHAELWEVKEERDRIYALSEMSEEDGYRVADLEVKYGEMDGYSAESRAGELLLGVGIPMEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQVLNERSSTMIIISHDRHFLNMVCTHMADLDYGELRIYPGNYDEYMTAATQARERLLADNAKKKAQIADLQSFVSRFSANASKSRQATSRARQIEKIQLEEVKASSRQNPFIRFDQDKKLFRNALEIDGLTKGFDNGPLFSQLKMLVEVGEKVAILGTNGIGKSTLLKTLVGELAPESGTVKWSENVRIGYYAQDHEYEFDGDLTVFDWMSQWKQENDDEQAVRSVLGRLLFSQDDIRKKVKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMALELYQGTLLFVSHDREFVSSLANRIVEITPGKVIDFSGNYEDYLRSRGIQ
Protein: Sterol 3-beta-glucosyltransferase UGT80B1 (EC 2.4.1.173) (Protein TRANSPARENT TESTA 15) (UDP-glucose:sterol glucosyltransferase 80B1) (Q9XIG1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of sterol glucosides. Catalyzes the synthesis of steryl glycosides (SGs) and acyl steryl glycosides (ASGs) which are the most abundant sterol derivatives in higher plants. Can act on several sterols like sitosterol, campesterol and stigmasterol. Is required for embryonic development, seed suberin accumulation, cutin formation and flavanoid accumulation in the seed coat. Both UGT80A2 and UGT80B1 are required for the normal production of SGs and ASGs in seeds.
Interaction partners:
- ceramide glucosyltransferase
- Delta
- Cycloartenol-C-24-methyltransferase
- Protein TRANSPARENT TESTA 9
- Uncharacterized protein At4g19900
- Glycosyltransferase-pyrophosphoryl-undecaprenol N-acetylglucosamine transferase)
- Protein TRANSPARENT TESTA 16
Sequence:
MASNVFDHPLQELEGEDNGVKSEKASLLETSGSVDTTPEDSGHRSSDGHRGLDHCETAPVGLYGDMLINDSEIQYSRSLTEKGSPAIHNLKLDRLSEQEKQKLIVELVRIQNDGTVEVIDNGTPVSELWEFEPTKGQSTITYEKSLTESFRSIPRLKIAILVVGTRGDVQPFLAMAKRLQEFGHRVRLATHANFRSFVRAAGVEFYPLGGDPRELAAYMARNKGLIPSGPSEISKQRKQLKAIIESLLPACIEPDLETATSFRAQAIIANPPAYGHVHVAEALGVPIHIFFTMPWTPTNEFPHPLARVPQSAAYWLSYIVVDLMVWWSIRTYINDFRKRKLNLAPIAYFSTYHGSISHLPTGYMWSPHVVPKPSDWGPLVDVVGYCFLNLGSKYQPREEFLHWIERGSPPVYIGFGSMPLDDPKQTMDIILETLKDTEQRGIVDRGWGGLGNLATEVPENVFLVEDCPHDWLFPQCSAVVHHGGAGTTATGLKAGCPTTIVPFFGDQFFWGDRIYEKGLGPAPIPIAQLSVENLSSSIRFMLQPEVKSQVMELAKVLENEDGVAAAVDAFHRHLPPELPLPESSSEKKDEDDRPDLLQWFFIQIGKKCCLPCGGV
Protein: Type II secretion system protein E (T2SS protein E) (EC 7.4.2.8) (General secretion pathway protein E) (Protein-secreting ATPase) (Type II traffic warden ATPase) (Q00512)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: ATPase component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Acts as a molecular motor to provide the energy that is required for assembly of the pseudopilus and the extrusion of substrates generated in the cytoplasm.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:9882649}. Note=Membrane association is not an intrinsic property but requires the XcpY/GspL gene product. {ECO:0000269|PubMed:9882649}.
Interaction partners:
- Type II secretion system protein F
- Type II secretion system core protein G
- Type II secretion system protein L
- Secretin XcpQ
- Type II secretion system protein M
- Type II secretion system protein H
- Type II secretion system protein K
- Prepilin leader peptidase/N-methyltransferase
- Type II secretion system protein N
- Type II secretion system protein I
Sequence:
MMTAPLPDIAAPAAPPRRLPFSFAKRQGLLFLCLEEQYWLACRPQVELAAIAEAQRFAGRRLPLKALGEDAFNQALAASYQHDSSAAMQLAEDLGGSLDLAALADQVPETEDLMEQEDDAPIIRLINAILGEAIRENASDIHLETFEKRLVVRFRVDGVLREVLEPKRELAALLVSRIKVMARLDIAEKRIPQDGRISLRVGGREVDIRVSTLPSANGERVVLRLLDKQAGRLNLQHLGMSERDRKLMDETVRKPHGILLVTGPTGSGKTTTLYASLTTLNDRTRNILTVEDPIEYHLEGIGQTQVNAKVDMTFARGLRAILRQDPDVVMVGEIRDRETAEIAVQASLTGHLVLSTLHTNSAIGAITRLVDMGIEPFLLSSSMLGVLAQRLVRVLCPACKEPYRADEAECALLGVDPAAPPTLHRARGCGECHQHGYRGRTGIYELVVFDDHMRSLIHNESSEQEMTRHARTSGPSIRDDGRRKVLEGVTTVEEVLRVTREE
Protein: Kappa-conotoxin Mo1659 (P84713)
Organism: Conus monile (Necklace cone)
Function: Inhibits non-inactivating voltage-gated potassium channels in rat dorsal root ganglion neurons.
Subcellular location: Secreted {ECO:0000269|PubMed:15081394}.
Interaction partners:
Sequence:
FHGGSWYRFPWGY
Protein: ATP synthase subunit O, mitochondrial (Oligomycin sensitivity conferral protein) (OSCP) (Q96251)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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 and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:25862457}. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit delta', mitochondrial
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit beta-3, mitochondrial
- ATP synthase subunit 9
- ATP synthase subunit a-2
- ATP synthase subunit alpha
- ATP synthase subunit 9, mitochondrial
Sequence:
MANRFRSGISFFKTIAVTDSVSSVRSKSLFPALRTYATASAQTTANVKVPIALVGENGNFASWLYIAAVKMNSLEKIETDLSEMIEAMKTAPIFAQFTKDPSVPRGTRLAAIRDACDQAKFAEPTKNFLSLLAENGKLKNLDAIVKKFMQLTNAHRGDVKVLVTTVIPLPPAEEKELTETLQEIIGAGKKITVEQKIDPSIYGGLIVEFQQKVLDMSIRTRAQQMERLLREPVDFNNL
Protein: RNA polymerase II assembly factor RTP1 (Required for nuclear transport of RNA pol II protein 1) (Transport and Golgi organization protein 6 homolog) (Q12751)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the cytoplasmic assembly and the nuclear import of RNA polymerase II. May facilitate the starting interaction between RNA polymerase II subunits RPB2 and RPB3 and the subsequent interaction of the resulting complex with subunit RPB1. May also participate in the transport of RNA polymerase II through the nuclear pore complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23438601}.
Interaction partners:
Sequence:
MNEDKEQKINIHDILNTRPKLTKKTALDVFFEDLDDNVITPINEYVLDSGSSSSSSIYQALKCSNNNEFVAVLLQKFQNLHIHVLEQQRRLIESKSDLLPISLHDMKYVDELINLLIIHGIDANLSPTMKIPFDSKRINTFKKGQKSAEYETPRWHTINNDTLSQVITVFYNVLTSERSSDYLREIISKGSAYANILLGLIVLHLQLPNRYSSQMITNLEDTQETYTLFGVYTLLVETIQDEKVREPILSKLTTLTLRRPENGLISLIDFVLGVRDAEDIDIEKFNRIYQILMSKPKTMTNLQYLTELFKQIYDGLTFVNRPILVTCLNGLILKFYLRNKRIVNDFLFKKVRSIIFNSPLTDHTAKELNDVINVLISLSKNSSSDLLNDLVTSCPDEDGTTPGQFFLYVWIYALFLKKNQKLDPLEINKLSISDNKSTDSIHFPEQSSSKYYEVVLSLLKSLIVITENFQYLNVLSLNLLNFEHEKWKYLIDLDTQLPYISVKNTDMAELFFEKGSKNSQISEFLQDMDLSIELFMEFLVLLNDEEQSKTLFLDILKRWVHHTKKSEKRSSDNHSGMPSVTDNALILMDLKLLECMNNRFKTKIVNKPKDVLIVIDQLIDVVQEKDETIQEVEADSDDEVEEGEETEELDPNENSSYKIILQLLSTVLSESSSSILLQNSYILKSISRKLQSFNTNASEIDALLASIDNILINGHTTERNDNIEIEMDEERLDKAITSLHDPLVPIKSYGLTELRHLAEKKSPVISLEKVLQIHLDYLKNMDPFIYLNVIKGLTTLCELEPETILPLLAEFYANKKKKNRLDDVLKVGEVFINYIQRQNELFQGKLAYLIIDTCLSIVRPNDSKPLDNRWRMSSMSILGMCLQINARGVSDRIRDMLDCVFGILQLEQPQNHLKDKDDSFLMRRSAVHLIHDLLYSTGFDLLPFEYNYDKLKTLLSYVRDQDEDYMVCEQIDKLLTVLDSL
Protein: DNA damage tolerance protein rad31 (P79064)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Could be involved in a ubiquitin-related process important for DNA damage tolerance. Acts in a process which is defective in the checkpoint rad mutants and which involves hus5.
Interaction partners:
- Ubiquitin-activating enzyme E1-like
- Ubiquitin-like protein pmt3/smt3
- SUMO-conjugating enzyme ubc9
- E3 SUMO-protein ligase pli1
- Elongation factor 3
- Ubiquitin-like-specific protease 1
- E3 SUMO-protein ligase nse2
- E3 ubiquitin-protein ligase complex slx8-rfp subunit slx8
Sequence:
MGNHNINAEEIALYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFKKKLHELNPLVEIDTDTSLISEIDEGKISKFSMVIATQLDYEEFCRINELTRICNASFYATSCFGLYGFAFCDLINHNFAIDRVVDNTKVEEDMFIVQKPMKEAFQSILGETLKPRLAKKIPTLYPAMLSLLKSKKSDPDSIRQVCIEQKLNEKTVLNGEFLSKFSSNISFQWTPVMSVVGGVVSQDALNSISKKQFPIDNFWIFDAESGLAPIYRL
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 3 (PP4R3) (P40164)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Core regulatory subunit of the histone H2A phosphatase complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Protein STD1
- Serine/threonine-protein phosphatase 2A activator 1
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase PP1-1
- Serine/threonine-protein phosphatase 2A activator 2
- Serine/threonine-protein phosphatase 2B catalytic subunit A2
- Serine/threonine-protein kinase RAD53
- Serine/threonine-protein phosphatase 2B catalytic subunit A1
Sequence:
MSLPGTPTTSPTPMDEDTEQAVSVNTEPKRVKVYILENNEWKDTGTGFCIGEVDEGKFAYLVVSDEDSPTETLLKSKLEGNIEYQRQEETLIVWKDLGGKDIALSFEESMGCDTLCEFIVHVQRNIESNISLVTVKSSDNGLGSVHDIITGPVTLPSNDQQQNSQTLLEALKILNENTSFDFLKNETIEFILQSNYIDTLISHFHKAEEEKIPKDLFLLSNIIKTLILYNKRDILESMVEDDRIMGIVGILEYDTEYPTSKANHRKYLGSKGPNFKEVIPLENEDLKIIMKKCFRLQFLKDVVLVRFLDDHNFNLISEIVMDLETCIIDFLQVGTFLDRLIELYDTKTLPESSSEKEKFVQKRKDGIRLLQQCVQMSINLDAVDRSKFYKTLVRKGLFKVLDYAFHMETDSNVRILATDTIITIIEHDILLIHNVQNEDSFKRQHKSAPDDKSSHRKYPQDYSSSTDSKLLLILSTILLSDRSPGLREQVVQALNTLLHPEGCVGNGEGSYDLMGRSNYEAKNTSEDFPSFSYGLNSDSINLNNYHYSSDEMNNLEPESESEFQVMEYFANFYNKIAPILFGPLIKKDITTEMAEIDGQIEKVTKDDLLLIHLVKLVSFVCTEHDRVLSRRFILENGILDSVSKLIGGNHMMQLRLTAVRCIKNLMCLDDKYYHRYMISKNLYAPVFKLFQENIDKNNLANSCIQDFFRIIITECRAYQSDGHNRKEKTNGSYDGNGNDVKTNVNNNRTNFTILNKYLVQTYGDVLRKATDIPFIQDMLETGEENQPDHSSFENSIEGGNDISVNMSTDGFASNHLEDIDIKNVKRLHSEIEHFENDPHYSGDQLAFKKSVDQMNAST
Protein: Uncharacterized protein (Q4GYF3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Transcription initiation protein, putative
Sequence:
MVGGYLRMPRDNTRSSHLTDVEEESSAGSATKRCKLEGGSCDGDSNMAITSDGVDVNVADGLTLIQSYILSPTSSRSFWHTGVAAVSSSRAGENDTPPNNRGNMLGPLSAVGANNNLLPMVPSEEENSDAPPDCARSACSGSLCEGDGNEGVASVSGGAVPSSVNLSSSSSLKECTSVCVVDHAVMCNIVPLLPKKHPEYGLVLQIVPLTLWPPPKAEVSGIGSEGGDLGKSLQTTVSFASQLHNDYLLRSDVTVLHPPTDAAQGVIVEWVSGDIGYTADSKGLWAEQRLFSQRYYTMSPVERLDIRHNGCSDNNYGKDDAEVRYTAPHLPPTTLRGAVLEQLRRFRVNPRYAPTSLTNGTRNKEWVLLFARVIEVGQDCIALTSRLMRAWTTAPSRETIAMCDVLLDEVIHIGIAPQQEPHRLSLVCPSVAHRILVSQHRWMNVDKRTELSVAGSMQVVARELLEVILQAMRGTLRHRIALQYELIRLLRAKPLMFANNELVVQYSRWYTTIAPPNVILHVLAGSTIFSGVMSQLHIVSGRVMARSQVERVCGNGGDAALQHHCGGSLLDDDMEDNDVSEDPPASDNEPSRKRGRPRDEVKNRYAPANGANHDGSDDNHDDNDNDSDSDDNDDNDDDSDSDDGEEGDECSGEEEEGTGDTESTNIISDNQNYQRHDVSAWLRAISDSADNIPLVDLVSVPYEMDLLDEGFVTRFCAILRGQDPTNNKGGGSSHGVGGSGSGSGAAGSSPSGHTGCDEVALSCVASWLKRTRCTMTTADLESYVRKLSR
Protein: Cadherin-related family member 1 (Photoreceptor cadherin) (prCAD) (Protocadherin-21) (Q96JP9)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be required for the structural integrity of the outer segment (OS) of photoreceptor cells (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Localized at the junction between the inner and outer segments of rod and cone photoreceptors cells. Confined to the base of the OS. Localized on the edges of nascent evaginating disks on the side of the OS opposite the connecting cilium. Expressed at postnatal day 2 at the apical tip of the rod photoreceptor cells, the site of the developing OS. Colocalized with rhodopsin between postnatal days 2 and 9 at the base of the growing OS region (By similarity). {ECO:0000250}.
Interaction partners:
- Prominin-1
- Transmembrane 4 L6 family member 5
- Retinal-specific phospholipid-transporting ATPase ABCA4
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- Retinal guanylyl cyclase 1
- Aryl-hydrocarbon-interacting protein-like 1
- Multiple inositol polyphosphate phosphatase 1
- Retina and anterior neural fold homeobox protein 2
- Membrane-associated phosphatidylinositol transfer protein 3
Sequence:
MRRCRWAALALGLLRLCLAQANFAPHFFDNGVGSTNGNMALFSLPEDTPVGSHVYTLNGTDPEGDPISYHISFDPSTRSVFSVDPTFGNITLVEELDREREDEIEAIISISDGLNLVAEKVVILVTDANDEAPRFIQEPYVALVPEDIPAGSIIFKVHAVDRDTGSGGSVTYFLQNLHSPFAVDRHSGVLRLQAGATLDYERSRTHYITVVAKDGGGRLHGADVVFSATTTVTVNVEDVQDMAPVFVGTPYYGYVYEDTLPGSEVLKVVAMDGDRGKPNRILYSLVNGNDGAFEINETSGAISITQSPAQLQREVYELHVQVTEMSPAGSPAAQATVPVTIRIVDLNNHPPTFYGESGPQNRFELSMNEHPPQGEILRGLKITVNDSDQGANAKFNLQLVGPRGIFRVVPQTVLNEAQVTIIVENSAAIDFEKSKVLTFKLLAVEVNTPEKFSSTADVVIQLLDTNDNVPKFDSLYYVARIPENAPGGSSVVAVTAVDPDTGPWGEVKYSTYGTGADLFLIHPSTGLIYTQPWASLDAEATARYNFYVKAEDMEGKYSVAEVFITLLDVNDHPPQFGKSVQKKTMVLGTPVKIEAIDEDAEEPNNLVDYSITHAEPANVFDINSHTGEIWLKNSIRSLDALHNITPGRDCLWSLEVQAKDRGSPSFSTTALLKIDITDAETLSRSPMAAFLIQTKDNPMKAVGVLAGTMATVVAITVLISTATFWRNKKSNKVLPMRRVLRKRPSPAPRTIRIEWLKSKSTKAATKFMLKEKPPNENCNNNSPESSLLPRAPALPPPPSVAPSTGAAQWTVPTVSGSLTPQPTQPPPKPKTMGSPVQSTLISELKQKFEKKSVHNKAYF
Protein: Coiled-coil domain-containing protein 40 homolog (Flagellar-associated protein 172) (A8IQT2)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm complexes, which are responsible for ciliary beat regulation, by acting as a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella. Together with CCDC39/FAP59 forms a 96-nm-long complex in flagella. This complex does not act as a physical ruler, but rather act as a negative regulator for radial spokes: the complex lays along specific protofilaments, masking radial spoke binding sites and allowing recruitment of inner dynein arm (IDA) and nexin-dynein regulatory complexes (N-DRC).
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:25395538}.
Interaction partners:
Sequence:
MADPMDQPSTSDPVDNQIFGEQGGLRPDHPLLRRAQEALKVQFEANRTRLQEELREKANALKQAKARREALGVELYGFQQNLAKLQLNLETTHQNYQCEDQLNQLKQQLSLEEGDTKGERSRRVCVCVCRVCCRIDTLQDNLKGTQQQLALVSAQLEAQKRETRAALETLAEAEVGGCVRDEALSAIQDGMREQQQQELSLVLEIEGYKKDVVREQLKHESLTAVVRKVEGDAVFVQKQIEGAQERQARLQEILAKLAKSLEHTEAEGEADAVDRAITKVAAEGRAIEEEMLSALSDQTTAEKATSKTAADTQELRKRIRAEELAVVETENELAKLQVDILNTEAHNSRLGETLGLLDEELRDKGRTIEKYELEIKRRNDEIEKKTREIDILNRRRDCRGSAALDTRPLQAPPPPQVKSDLALTTPMYTPPPVPQPSVGMTVTTEKLVSDMEKALTKREIISVKGRATAAKSKSSTPAGSATASSRASPSASVASSTLTRNQLDRATTDLAKSIKDLEAGRYRPVVEDAAAVGEELGRAQDKLGRVVALLEGLRQAAPHLAGELDKVLCHVADVRA