wanglab/gogpt-training-data huggingface dataset:
Protein: N-acylethanolamine-hydrolyzing acid amidase (EC 3.5.1.60) (Acid ceramidase-like protein) (Acylsphingosine deacylase NAAA) (EC 3.5.1.23) (N-acylsphingosine amidohydrolase-like) (ASAH-like protein) [Cleaved into: N-acylethanolamine-hydrolyzing acid amidase subunit alpha; N-acylethanolamine-hydrolyzing acid amidase subunit beta] (Q02083)
Organism: Homo sapiens (Human)
Function: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-lauroylethanolamine = N-stearoylethanolamine > N-arachidonoylethanolamine > N-oleoylethanolamine. Also exhibits weak hydrolytic activity against the ceramides N-lauroylsphingosine and N-palmitoylsphingosine.
Subcellular location: Lysosome {ECO:0000305|PubMed:10610717, ECO:0000305|PubMed:15655246, ECO:0000305|PubMed:18793752}. Membrane {ECO:0000269|PubMed:30301806}; Peripheral membrane protein {ECO:0000269|PubMed:30301806}.
Interaction partners:
- Fatty-acid amide hydrolase 1
- Polyphosphoinositide phosphatase
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Monoglyceride lipase
- Lysosome-associated membrane glycoprotein 2
- Protein VAC14 homolog
- Fatty-acid amide hydrolase 2
- Peroxisome proliferator-activated receptor alpha
Sequence:
MRTADREARPGLPSLLLLLLAGAGLSAASPPAAPRFNVSLDSVPELRWLPVLRHYDLDLVRAAMAQVIGDRVPKWVHVLIGKVVLELERFLPQPFTGEIRGMCDFMNLSLADCLLVNLAYESSVFCTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDERDKGWWWENAIAALFRRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPREGVVITRNRDGPADIWPLDPLNGAWFRVETNYDHWKPAPKEDDRRTSAIKALNATGQANLSLEALFQILSVVPVYNNFTIYTTVMSAGSPDKYMTRIRNPSRK
Protein: Uncharacterized protein YigF (P27842)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Inner membrane protein YigG
- Protein RarD
Sequence:
MSKEYMNDGSLSEKWKYRFNFYDQHGFPGFWGATPEYKAAFKALKVRQRLTIQMNFIAFFCSWIYLFVLGLWKKAIIVLLLGILSLFVGALIGVNILGIAVAAYVAVNTNKWFYEKEVKGLNTWSL
Protein: Umbelliferone 6-dimethylallyltransferase, chloroplastic (EC 2.5.1.139) (W0SKS3)
Organism: Petroselinum crispum (Parsley) (Petroselinum hortense)
Function: Prenylates umbelliferone in the presence of dimethylallyl diphosphate (DMAPP) at the 6 position to yield demethylsuberosin (DMS) as the main product, together with a minor amount of osthenol corresponding to 8-prenylated umbelliferone. No activity with other coumarine derivatives such as psoralen, bergapten and xanthotoxin, or with geranyl diphosphate or farnesyl diphosphate as prenyl donors.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:24354545}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSQTLMHSRFSSGFLHHQPEKGFLTLQTQRRHAKTLKGEKEFPSRVVSCHKNVDSSKNFSSSCEKSKTQEKILAQTLGATSDGEAIVQPNNDFEVTWQNTLRRKWDAFSIFSRPYSAICTIIGISSVSLLPLTSVADFSPAYFVGLLQALIPFLCANIYTSAINQLVDVDIDKINKPYLPLVSGEFSMGEGRAIVSALTFTCFAMAIMSHSVPLFVGVLVYFLIGTAYSVEHPLLRWKTKPAMAAFSMAGLMGLTIQPTVFYHIQNVLGKPMVFSRSVAFATMFFSIFAACLGAIKDIPDVEGDREFGNLTFSVRYGQEKVFSFCLNVLLLAYGSAVVVGASSSSLLCKTVSVIGHTVLASLLVLRAKSTNPKDPESTQSFYMFLFKLLYAEYVLIHFMR
Protein: Variant surface glycoprotein (VSG), putative (Q57U38)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
SLINLEATAAEEAIKLSGAEAKLNGPLPAGLPTKVPPITTVTCEVHNKSKTKCLEAQCKWGGKKDDDGPCQASDKQVSEQTKQGGRDTTTGGDVKKEDKCTGKDEKTCGGTQGCKWEGTECKDFSLLVNNKISIIVSVSVSLVAF
Protein: Prespore-specific protein E (Protein 1I) (Q9GP84)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Peptidase C1A papain C-terminal domain-containing protein
- SrfA-induced gene F protein
- Prespore vesicle protein
Sequence:
MRFISIFLIIVALCVSSSWAFNFTDQPNSFRISGTGCGSGTTTVYFSTDGRCNSACGGSIRIKGEGNNVPNQQFTLNDYSKNVTNCSGTSNVASFRCPALVNTTSPTFTVNVGNSAYHVTCQYAQVTETPAGNSADKVAVGIAIIFGALISLLAL
Protein: 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase (EC 1.14.14.139) (7-alpha-hydroxy-4-cholesten-3-one 12-alpha-hydroxylase) (CYPVIIIB1) (Cytochrome P450 8B1) (Sterol 12-alpha-hydroxylase) (O88962)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in primary bile acid biosynthesis. Catalyzes the 12alpha-hydroxylation of 7alpha-hydroxy-4-cholesten-3-one, an intermediate metabolite in cholic acid biosynthesis (By similarity). Controls biliary balance of cholic acid and chenodeoxycholic acid, ultimately regulating the intestinal absorption of dietary lipids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O02766}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:O02766}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase type 7
- Aldo-keto reductase family 1 member D1
- Sterol 26-hydroxylase, mitochondrial
- Nuclear receptor subfamily 0 group B member 2
- Bile acid receptor
- Bile salt export pump
- Hepatic sodium/bile acid cotransporter
- Fibroblast growth factor 15
- Cholesterol 25-hydroxylase
- Bile acid-CoA:amino acid N-acyltransferase
Sequence:
MTLWCTVLGALLTVVGCLCLSLLLRHRRPWEPPLDKGFVPWLGHSMAFRKNMFEFLKGMRAKHGDVFTVQLGGQYFTFVMDPLSFGPIIKNTEKALDFQSYAKELVLKVFGYQSVDGDHRMIHLASTKHLMGQGLEELNQAMLDSLSLVMLGPKGSSLGASSWCEDGLFHFCYRILFKAGFLSLFGYTKDKQQDLDEADELFRKFRRFDFLFPRFVYSLLGPREWVEVSQLQRLFHQRLSVEQNLEKDGISCWLGYMLQFLREQGIASSMQDKFNFMMLWASQGNTGPTCFWVLLFLLKHQDAMKAVREEATRVMGKARLEAKKSFTFTPSALKHTPVLDSVMEESLRLCATPTLLRVVQEDYVLKMASGQEYQIRRGDKVALFPYLSVHMDPDIHPEPTAFKYDRFLNPDGTRKVDFYKSGKKIHHYSMPWGSGVSKCPGRFFALSEMKTFVLLMIMYFDFKLVDPDIPVPPIDPRRWGFGTSQPSHEVRFLYRLKPVQ
Protein: Regulatory factor X5 (F8W689)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEDEPDAKSPKTGGRAPPGGAEAGEPTTLLQRLRGTISKAVQNKVEGILQDVQKFSDNDKLYLYLQLPSGPTTGDKSSEPSTLSNEEYMYAYRWIRNHLEEHTDTCLPKQSVYDAYRKYCESLACCRPLSTANFGKIIREIFPDIKARRLGGRGQSKYCYSGIRRKTLVSMPPLPGLDLKGSESPEMGPEVTPAPRDELVEAACALTCDWAERILKRSFSSIVEVARFLLQQHLISARSAHAHVLKAMGLAEEDEHAPRERSSKPKNGLENPEGGAHKKPERLAQPPKDLEARTGAGPLARGERKKSVVESSAPGANNLQVNALVARLPLLLPRAPRSLIPPIPVSPPILAPRLSSGALKVATLPLSSRAGAPPAAVPIINMILPTVPALPGPGPGPGRAPPGGLTQPRGTENREVGIGGDQGPHDKGVKRTAEVPVSEASGQAPPAKAAKQDIEDTASDAKRKRGRPRKKSGGSGERNSTPLKSAAAMESAQSSRLPWETWGSGGEGNSAGGAERPGPMGEAEKGAVLAQGQGDGTVSKGGRGPGSQHTKEAEDKIPLVPSKVSVIKGSRSQKEAFPLAKGEVDTAPQGNKDLK
Protein: ATP synthase F(0) complex subunit e, mitochondrial (ATPase subunit e) (ATP synthase membrane subunit e) (Q06185)
Organism: Mus musculus (Mouse)
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. Minor subunit located with subunit a in the membrane.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MVPPVQVSPLIKFGRYSALIIGMAYGAKRYSYLKPRAEEERRIAAEEKKRLDELKRIERELAEAQDDSILK
Protein: Sm-like protein LSM4 (AtLSM4) (Protein EMBRYO DEFECTIVE 1644) (U6 snRNA-associated Sm-like protein LSM4) (F4K4E3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of LSM protein complexes, which are involved in RNA processing. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates developmental gene expression by the decapping of specific development-related transcripts. Component of the nuclear LSM2-LSM8 complex which is involved splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6 small nuclear RNAs (snRNAs) and is essential for accurate splicing of selected development-related mRNAs through the stabilization of the spliceosomal U6 snRNA. Plays a critical role in the regulation of development-related gene expression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23221597}. Nucleus {ECO:0000269|PubMed:23221597}.
Interaction partners:
- Sm-like protein LSM6A
- Sm-like protein LSM3A
- Sm-like protein LSM7
- Sm-like protein LSM36B
- Sm-like protein LSM2
- Sm-like protein LSM5
- Sm-like protein LSM3B
- Sm-like protein LSM8
- Small nuclear ribonucleoprotein Sm D2
- Sm-like protein LSM1B
Sequence:
MLPLSLLKTAQGHPMLVELKNGETYNGHLVNCDTWMNIHLREVICTSKDGDRFWRMPECYIRGNTIKYLRVPDEVIDKVQEEKTRTDRKPPGVGRGRGRGVDDGGARGRGRGTSMGKMGGNRGAGRGRG
Protein: Nickel-binding periplasmic protein (P33590)
Organism: Escherichia coli (strain K12)
Function: Involved in a nickel transport system, probably represents the nickel binder.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Nickel transport system permease protein NikC
- Nickel import ATP-binding protein NikE
- Nickel transport system permease protein NikB
- Nickel import ATP-binding protein NikD
- Nickel-responsive regulator
- Dipeptide transport system permease protein DppB
- Putrescine export system permease protein SapB
- Probable pyruvate-flavodoxin oxidoreductase
- Probable D,D-dipeptide transport system permease protein DdpB
- Dipeptide transport system permease protein DppC
Sequence:
MLSTLRRTLFALLACASFIVHAAAPDEITTAWPVNVGPLNPHLYTPNQMFAQSMVYEPLVKYQADGSVIPWLAKSWTHSEDGKTWTFTLRDDVKFSNGEPFDAEAAAENFRAVLDNRQRHAWLELANQIVDVKALSKTELQITLKSAYYPFLQELALPRPFRFIAPSQFKNHETMNGIKAPIGTGPWILQESKLNQYDVFVRNENYWGEKPAIKKITFNVIPDPTTRAVAFETGDIDLLYGNEGLLPLDTFARFSQNPAYHTQLSQPIETVMLALNTAKAPTNELAVREALNYAVNKKSLIDNALYGTQQVADTLFAPSVPYANLGLKPSQYDPQKAKALLEKAGWTLPAGKDIREKNGQPLRIELSFIGTDALSKSMAEIIQADMRQIGADVSLIGEEESSIYARQRDGRFGMIFHRTWGAPYDPHAFLSSMRVPSHADFQAQQGLADKPLIDKEIGEVLATHDETQRQALYRDILTRLHDEAVYLPISYISMMVVSKPELGNIPYAPIATEIPFEQIKPVKP
Protein: Soluble calcium-activated nucleotidase 1 (SCAN-1) (EC 3.6.1.6) (Apyrase homolog) (Q8K4Y7)
Organism: Rattus norvegicus (Rat)
Function: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > IDP >> UTP > CDP = GTP = ITP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12167635}; Single-pass type II membrane protein {ECO:0000269|PubMed:12167635}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12167635}; Single-pass type II membrane protein {ECO:0000269|PubMed:12167635}. Note=Processed form: Secreted.
Interaction partners:
- Bifunctional purine biosynthesis protein ATIC
- 5'-nucleotidase
- UMP-CMP kinase
- 5'-nucleotidase, cytosolic IA
- 5'-nucleotidase
- Adenine phosphoribosyltransferase
- Ectonucleoside triphosphate diphosphohydrolase 5
- Ribonucleoside-diphosphate reductase
- AMP deaminase 3
- 5',3'-nucleotidase, mitochondrial
Sequence:
MPIQPFDQREWNEPMHSLRISVGGLPVLASMTKATDPRFRPRWRVILTSFVGAALLWLLYSHHQTPVSGRPPIHNAHNWRLRQERISQYNDTYPLSPPQRTPGGIRYRIAVIADLDTGSKAQEENTWFSYLKKGYLTLSDSGDRVSVEWDKDRGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVIYQIEGTKAVPWVILSDGDGAVEKGFKAEWLAVKDEHLYVGGLGKEWTTTTGEVVNENPEWVKVVGHRGSVEHENWVSSYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPRRASHERYSEREDERKGSNLLLSAAQDFRDISVRQVGALVPTHGFSSFKFIPNTDDQIIVALKSEEDNGRIATYVMAFTLDGRFLLPETKIGSVKYEGIEFI
Protein: Polycomb group RING finger protein 3 (RING finger protein 3A) (Q8BTQ0)
Organism: Mus musculus (Mouse)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity (By similarity). Plays a redundant role with PCGF5 as part of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females.
Subcellular location: Nucleus {ECO:0000269|PubMed:28596365}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28596365}. Note=Recruited by the non-coding RNA Xist to specific nuclear foci that probably correspond to the inactivated X chromosome. {ECO:0000269|PubMed:28596365}.
Interaction partners:
- E3 ubiquitin-protein ligase RING1
- RING1 and YY1-binding protein
- E3 ubiquitin-protein ligase RING2
- Polycomb group RING finger protein 5
- Chromobox protein homolog 7
- Chromobox protein homolog 2
- Chromobox protein homolog 8
- YY1-associated factor 2
- Polycomb group RING finger protein 2
- Polycomb group RING finger protein 1
Sequence:
MLTRKIKLWDINAHITCRLCSGYLIDATTVTECLHTFCRSCLVKYLEENNTCPTCRIVIHQSHPLQYIGHDRTMQDIVYKLVPGLQEAEMRKQREFYHKLGMEVPGDIKGEACSAKQHLDPRNGETKADDNSNKETAEEKQEEDNDYHRSDEQVSICLECNSSKLRGLKRKWIRCSAQATVLHLKKFIAKKLNLSSFNELDILCNEEILGKDHTLKFVVVTRWRFKKAPLLLHYRPKMDLL
Protein: CROL GAMMA (Crooked legs, isoform C) (O61362)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQHVSAASSVPSVVTPVVTTGGTTITLGGPPPLPKSEHKEDGKPPHGIEMYKVNIEDISQLFTYHEVFGKIHGDVVNHQLAAAHGGQLPPPPPLPPQVTSHAASAAAAAAAASTNNAAVAAVMASANAAAAAAAAASAGGGLPPATSGNGGQQVTVTTTSSSTSSGGSTTSGGTTTTAGQTPHQCDVCGKKYTRKEHLANHMRSHTNETPFRCEICGKSFSRKEHFTNHILWHTGETPHRCDFCSKTFTRKEHLLNHVRQHTGESPHRCSYCMKTFTRKEHLVNHIRQHTGETPFKCTYCTKAFTRKDHMVNHVRQHTGESPHKCTYCTKTFTRKEHLTNHVRQHTGDSPHRCSYCKKTFTRKEHLTNHVRLHTGDSPHKCEYCQKTFTRKEHLNNHMRQHSSDNPHCCNVCNKPFTRKEHLINHMSRCHTGDRPFTCETCGKSFPLKGNLLFHQRSHTKGQEMERPFACEKCPKNFICKGHLVSHMRSHSGEKPHACTLCSKAFVERGNLKRHMKMNHPDAMMPPPPVHPHPQIPAGVLTQVKQEVKPIIIPHHSATTTMHTIQQITAGAAGGAGAVQLTPGLVPLVTSTLISHNAAAQQQSQKQQAAAAAAAQQQAAAAAAAQQQAAQQQAAAAHQQHQQQVAAQHQQQAAVAAHQQQQQQLQQQQQLLQLSIQQAAHHHQQEQHRQQQQQQHQQQQQQQHHQQQQQGHPQAPPPQQQQQPPPIALISDPSALARAAIQLQHLPANVEQHPVVY
Protein: Transcription factor (Q90979)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEEHGVTQTEHMATIEAHAVAQQVQQVHVATYTEHSMLSADEDSPSSPEDTSYDDSDILNSTAADEVTAHLAAAGPVGMAAAAAVATGKKRKRPHVFESNPSIRKRQQTRLLRKLRATLDEYTTRVGQQAIVLCISPSKPNPVFKVFGAAPLENVVRKYKSMILEDLESALAEHAPAPQEVNSELPPLTIDGIPVSVDKMTQAQLRAFIPEMLKYSTGRGKPGWGKESCKPIWWPEDIPWANVRSDVRTEEQKQRVSWTQALRTIVKNCYKQHGREDLLYAFEDQQTQQQTTTTHSIAHLVPSQTVVQTFSNPDGTVSLIQVGTGATVATLADASELPTTVTVAQVNYSAVADGEVEQNWATLQGGEMTIQTTQASEATQAVASLAEAAVAASQEMQQGATVTMALNSEAAAHAVATLAEATLQGGGQIVLSGETAAAVGALTGVQDANGLVQIPVSMYQTVVTSLAQGNGPVQVAMAPVTTRIADSAVTVDGQAVEVVTLEQ
Protein: Guanine nucleotide-binding protein G(t) subunit alpha-2 (Transducin alpha-2 chain) (P50149)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:31696965}. Photoreceptor inner segment {ECO:0000269|PubMed:31696965}. Note=Localizes mainly in the outer segment in the dark-adapted state, whereas is translocated to the inner part of the photoreceptors in the light-adapted state. During dark-adapted conditions, in the presence of UNC119 mislocalizes from the outer segment to the inner part of rod photoreceptors which leads to decreased photoreceptor damage caused by light. {ECO:0000269|PubMed:31696965}.
Interaction partners:
- Rhodopsin
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 9
- Guanine nucleotide-binding protein G
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
- Guanine nucleotide-binding protein G
Sequence:
MGSGISAEDKELARRSKELEKKLQEDADKEAKTVKLLLLGAGESGKSTIVKQMKIIHQDGYSPEECLEFKSVIYGNVLQSILAIIRAMSTLGIDYAEPSCADAGRQLNNLADSTEEGTMPPELVDVIRKLWKDGGVQACFDRAAEFQLNDSASYYLNQLDRITDPNYLPNEQDVLRSRVKTTGIIETKFSVKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDDEVNRMHESLHLFNSICNHKFFAATSIVLFLNKKDLFEEKIKKVHLSICFPEYDGNNSYEDAGNYIKSQFLDLNMRKDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Protein: Kinetoplast-associated protein 4 (Histone H1-like protein p16) (Q07053)
Organism: Crithidia fasciculata
Function: Histone H1-like DNA-binding protein involved in the organization and segregation of kinetoplast DNA (kDNA). The mitochondrial DNA of kinetoplastid protozoa consists of about 5,000 minicircles and 20 to 30 maxicircles. These circular DNAs are held together by catenation into a highly organized compact disk structure referred to as a kinetoplast DNA (kDNA) network. Binds preferentially to a specific fragment of minicircle DNA and is able to compact kDNA networks through DNA charge neutralization and condensation.
Subcellular location: Mitochondrion matrix, kinetoplast {ECO:0000269|PubMed:8446592, ECO:0000269|PubMed:8552084}. Mitochondrion matrix {ECO:0000269|PubMed:8446592, ECO:0000269|PubMed:8552084}. Note=Present both within the kDNA disk and in the mitochondrial matrix at opposite edges of the kDNA disk. {ECO:0000269|PubMed:8552084}.
Interaction partners:
Sequence:
MLRFVPRRLAIGAYTLFMMEQKNNPKLKGLKIADRGKMTSKLYKALNPNDKAALEKRAAAHPGFKRKEKEPKELKAAKAAKTSTPRAPSEYAKFVQANIGRFEKLPHLDRMKAVAKLWKQQQMRTGKP
Protein: Uracil nucleotide/cysteinyl leukotriene receptor (UDP/CysLT receptor) (G-protein coupled receptor 17) (Q6NS65)
Organism: Mus musculus (Mouse)
Function: Dual specificity receptor for uracil nucleotides and cysteinyl leukotrienes (CysLTs). Signals through G(i) and inhibition of adenylyl cyclase. May mediate brain damage by nucleotides and CysLTs following ischemia (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cysteinyl leukotriene receptor 1
- P2Y purinoceptor 12
Sequence:
MNGLEAALPSLTDNSSLAYSEQCGQETPLENMLFACFYLLDFILAFVGNALALWLFIWDHKSGTPANVFLMHLAVADLSCVLVLPTRLVYHFSGNHWPFGEIPCRLTGFLFYLNMYASIYFLTCISADRFLAIVHPVKSLKLRRPLYAHLACAFLWIVVAVAMAPLLVSPQTVQTNHTVVCLQLYREKASHHALASLAVAFTFPFITTVTCYLLIIRSLRQGPRIEKHLKNKAVRMIAMVLAIFLICFVPYHIHRSVYVLHYRGGGTSCAAQRALALGNRITSCLTSLNGALDPVMYFFVAEKFRHALCNLLCSKRLTGPPPSFEGKTNESSLSARSEL
Protein: Acetylxylan esterase (Q1HFU0)
Organism: Emericella nidulans (Aspergillus nidulans)
Interaction partners:
Sequence:
MMWFRFLLVALLWSLGSATIMENGQPRADPYPGQCSTIDLDSSWRSYDADAPEISYKGRWDSKHISWWSAPGLKLQFSGKKLALSFGEHTSEGTLVAYRIGTLDWLFTNVTADATYQFVGEGTHYEELPGDGDHIFEMRVQIAGVSVDVDDHLTKPPTFKKKVEIIGGSASLTGGQYATYETLSAWSFVYAQGLGNVEFGITAYPGACLVDMQCYGGGVHGMIWYWHRASDPGSRARNMYGGEPEEWDVTAEQPADLVIIQMGGNDHRHPNEIPGENFYQGYVDLIENIHQHWPDASIVIMTQWGIWNQEGSEYTQSVIYEEEIQRVYEHFKDRKWRFVYLFHTDGILGHNDINPKNHPTDVGHIKIASHLLQWTNLMLGWELNPRGEMQHGTLYWNDMEGY
Protein: SAGA-associated factor 29 (Q9USW9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Chromatin reader component of the transcription regulatory histone acetylation (HAT) complex SAGA. Sgf29 specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3). In the SAGA complex, sgf29 is required to facilitate crosstalk between gcn5 acetyltransferase activity and H3K4me3 recognition. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SAGA complex subunit Ada2
- Histone acetyltransferase gcn5
- SAGA complex subunit Spt7
- SAGA complex/transcription factor TFIID complex subunit Taf12
- Probable ubiquitin carboxyl-terminal hydrolase 8
- SAGA complex subunit Sgf73
- SAGA complex subunit Ngg1
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex subunit Sus1
- SAGA complex/transcription factor TFIID complex subunit Taf10
Sequence:
MVRPINAEEDVTSMWVKFHESLNPIRSSLIKQEECYKTVDGDDNPIEERIKACDAGIQTSEEQKKELEHTMQSLEMIINVLEKANEKPVITNSPLTRSRRNRGTSFTANTVTFTPGMSVAFKLPYTRHNEGGDWIQCIIIKVTGEGAKQRFEVQDPEPDDDGNAGQIYKTTANHLIQIPAKGTPLPPISPKTNVLARYPETTTFYRAEVIRTLPDGSCKLRFEGEEEVGKETVVERHLVLEYNG
Protein: Glycine receptor subunit alpha-3 (Q91XP5)
Organism: Mus musculus (Mouse)
Function: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Channel characteristics depend on the subunit composition; heteropentameric channels display faster channel closure (By similarity). Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents. Contributes to increased pain perception in response to increased prostaglandin E2 levels. Plays a role in the regulation of breathing rhythm, especially of the duration of the postinspiratory phase. Plays a role in cellular responses to ethanol (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000305|PubMed:12975813, ECO:0000305|PubMed:15131310, ECO:0000305|PubMed:19723286}; Multi-pass membrane protein {ECO:0000305}. Synapse {ECO:0000269|PubMed:12975813, ECO:0000269|PubMed:15131310, ECO:0000269|PubMed:19723286}. Perikaryon {ECO:0000269|PubMed:19723286}. Cell projection, dendrite {ECO:0000250|UniProtKB:P24524}. Cell membrane {ECO:0000269|PubMed:20978350}; Multi-pass membrane protein {ECO:0000305}. Note=Partially colocalizes with GPHN that is known to mediate receptor clustering at postsynaptic membranes. {ECO:0000269|PubMed:15131310}.
Interaction partners:
- Glycine receptor subunit beta
- Glycine--tRNA ligase
Sequence:
MAHVRHFRTLVSGFYFWEAALLLSLVATKETNSARSRSAPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVTCNIFINSFGSIAETTMDYRVNIFLRQKWNDPRLAYSEYPDDSLDLDPSMLDSIWKPDLFFANEKGANFHEVTTDNKLLRIFKNGNVLYSIRLTLTLSCPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQDEAPVQVAEGLTLPQFLLKEEKDLRYCTKHYNTGKFTCIEVRFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDAAPARVALGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRKNKTEAFALEKFYRFSDTDDEVRESRFSFTAYGMGPCLQAKDGVVPKGPNHAVQVMPKSPDEMRKVFIDRAKKIDTISRACFPLAFLIFNIFYWVIYKILRHEDIHQQQD