wanglab/gogpt-training-data huggingface dataset:
Protein: Calsyntenin-1 (Alcadein-alpha) (Alc-alpha) [Cleaved into: Soluble Alc-alpha (SAlc-alpha); CTF1-alpha (C-terminal fragment 1-alpha)] (Q9EPL2)
Organism: Mus musculus (Mouse)
Function: Induces KLC1 association with vesicles and functions as a cargo in axonal anterograde transport. Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation. In complex with APBA2 and C99, a C-terminal APP fragment, abolishes C99 interaction with PSEN1 and thus APP C99 cleavage by gamma-secretase, most probably through stabilization of the direct interaction between APBA2 and APP. As intracellular fragment AlcICD, suppresses APBB1-dependent transactivation stimulated by APP C-terminal intracellular fragment (AICD), most probably by competing with AICD for APBB1-binding. May modulate calcium-mediated postsynaptic signals.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:24613359}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12972431}; Single-pass type I membrane protein. Golgi apparatus membrane {ECO:0000250|UniProtKB:O94985}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, neuron projection {ECO:0000269|PubMed:12972431, ECO:0000269|PubMed:17332754}. Vesicle {ECO:0000269|PubMed:17332754}. Note=Localized in the postsynaptic membrane of both excitatory and inhibitory synapses. {ECO:0000269|PubMed:24613359}.; SUBCELLULAR LOCATION: [Soluble Alc-alpha]: Nucleus {ECO:0000250|UniProtKB:O94985}. Note=The AlcICD fragment is translocated to the nucleus upon interaction with APBB1. {ECO:0000250|UniProtKB:O94985}.
Interaction partners:
- Kinesin light chain 2
- Kinesin light chain 1
- Kinesin light chain 4
- Kinesin light chain 3
- Amyloid-beta A4 precursor protein-binding family A member 2
- Amyloid-beta precursor protein
- Major prion protein
Sequence:
MLRRPAPALAPAVRLLLAGLLCGGGVWAARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDSPLRFAESFEVTVTKEGEICGFKIHGQNVPFDAVVVDKSTGEGIIRSKEKLDCELQKDYTFTIQAYDCGKGPDGTGVKKSHKATVHIQVNDVNEYAPVFKEKSYKAAVVEGKQHSSILRVEAVDADCSPQFSQICSYEILTPDVPFTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISVKPTCSPGWQGWSSRIEYEPGTGALAVFPSIHLETCDEPVASVQATVELETSHIGKGCDRDTYSEKSLHRLCGAAAGTSELLPSPSSSFNWTVGLPTDNGHDSDQVFEFNGTQAVRIPDGVVTLDPKEPFTISVWMRHGPFGRKKETILCSSDKTDMNRHHYSLYVHGCRLVFLLRQDPSEEKKYRPAEFHWKLNQVCDEDWHHFVLNVEVPSVTLYVDGIPHEPFSVTEDYPLHPTKIETQLVVGACWQEYSGVESGNETEPATMASAGGDLHMTQFFRGNLAGLTVRSGKLADKKVIDCLYTCKEGLDLQVPEDANRGVQIQASSSQAVLTLEGDNVGELDKAMQHISYLNSRQFPTPGIRRLKITSTVKCFNEAACIEVPPVEGYVMVLQPEEPKISLSGVHHFARAASEFESAEGISLFPELRIISTITREVEPEADGSEDPTVQESLVSEEIVHDLDTCEVTVEGDELNAEQESLEVDVTRLQQKGIEASHSDLGVVFTGVETMASYEEVLHLLRYRNWHTRSLLDRKFKLICSELNGRYLSNEFKVEVNVIHTANPVEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSFLVFMIILGVFRIRAAHQRTMRDQDTGKENEMDWDDSALTITVNPMETYEDQHSSEEEEEEEEEEESEDGEEEEDITSAESESSEEEEGGPGDGQNATRQLEWDDSTLSY
Protein: LexA repressor 1 (EC 3.4.21.88) (Q8PN77)
Organism: Xanthomonas axonopodis pv. citri (strain 306)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
Sequence:
MPSLPPQRAAVLAFLQEQAQAGVSPSLAEIAQAFGFASRNAAQKHVQALADAGLIELLPNQKRGIRLPGGAGRDALLALPVLGRVAAGLPIGADIGLERQLWLDRALFSLRPDYLLQVQGDSMIDDGILDGDLVGVHRSNEARDGQIVVARVDGEITIKRLERGAERIRLLPRNRAHAPIVVAADADFAIEGLYCGLIRQG
Protein: Scopoletin 8-hydroxylase (EC 1.14.11.60) (2-oxoglutarate-dependent dioxygenase S8H) (Q9LE86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the pathway of sideretin biosynthesis from feruloyl CoA, a redox-active catecholic metabolite exuded by roots in response to iron deficiency in order to facilitate the uptake of iron; this pathway consists in the successive conversion from feruloyl CoA to scopoletin, from scopoletin to fraxetin and from fraxetin to sideretin. Catalyzes the biosynthesis of fraxetin via scopoletin hydroxylation.
Interaction partners:
- Xanthotoxin 5-hydroxylase CYP82C4
- Transcription factor MYB72
- Amino acid transporter AVT6B
- Fe
- Metal tolerance protein A2
- Ferric reduction oxidase 2
- Fe
- ABC transporter G family member 37
- Transcription factor MYB10
- Solute carrier family 40 member 2
Sequence:
MGINFEDQTTLFNFVVREGNGVKGMIDSGLSSVPRPFVQPLSERIPTQKALTCEATQPIDLSNLDGPQHKEVAKQIVEAAETLGFFQVVNHGVSVELLELLKSSAHEFFAQAPEEKSMYLKEVSPSKLVKYGTSFVPDKEKAIEWKDYVSMLYTNDSEALQHWPQPCREVALEFLNSSMEMVKNVVNILMENVGVTLEEEKMNGLMGTKMVNMNYYPTCPSPELTVGVGRHSDMGMLTVLLQDGIGGLYVKLDNGEWAEIPPVHGALVINIGDTLQILSNGKYKSAEHRVRTTNIGSRVSVPIFTAPNPSQKVGPLPEVVKRDGVARYKEFLFQDYMNNFFGQPHDGKKSLDFARAE
Protein: Fibroblast growth factor receptor 3 (FGFR-3) (EC 2.7.10.1) (Q9I8X3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Putative fibroblast growth factor 1
- Fibroblast growth factor
- Fibroblast growth factor
- Fibroblast growth factor 8
- Fibroblast growth factor 18a
- Son of sevenless homolog 1
- Son of sevenless homolog 2
- Fibroblast growth factor 16
- Fibroblast growth factor
- Fibroblast growth factor 8b
Sequence:
MVPLCLLLYLATLVFPPVYSAHLLSPEPTDWVSSEVEVFLEDYVAGVGDTVVLSCTPQDFLLPIVWQKDGDAVSSSNRTRVGQKALRIINVSYEDSGVYSCRHAHKSMLLSNYTVKVIDSLSSGDDEDYDEDEDEAGNGNAEAPYWTRSDRMEKKLLAVPAANTVKFRCPAAGNPTPSIHWLKNGKEFKGEQRMGGIKLRHQQWSLVMESAVPSDRGNYTCVVQNKYGSIKHTYQLDVLERSPHRPILQAGLPANQTVVVGSDVEFHCKVYSDAQPHIQWLKHIEVNGSQYGPNGAPYVNVLKTAGINTTDKELEILYLTNVSFEDAGQYTCLAGNSIGYNHHSAWLTVLPAVEMEREDDYADILIYVTSCVLFILTMVIIILCRMWINTQKTLPAPPVQKLSKFPLKRQVSLESNSSMNSNTPLVRIARLSSSDGPMLPNVSELELPSDPKWEFTRTKLTLGKPLGEGCFGQVVMAEAIGIDKEKPNKPLTVAVKMLKDDGTDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLRARRPPGMDYSFDTCKIPNETLTFKDLVSCAYQVARGMEYLASKKCIHRDPAARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSYGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFRQLVEDHDRVLSMTSTDEYLDLSVPFEQYSPTCPDSNSTCSSGDDSVFAHDPLPEEPCLPKHHHSNGVIRT
Protein: Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase (EC 2.4.1.256) (Alpha-1,2-glucosyltransferase ALG10 homolog) (Protein HOMOLOG OF YEAST ALG10) (Q8L638)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol. Can complement an ALG10-deficient yeast mutant.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21707802}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dol-P-Man:Man
- Dol-P-Man:Man
- dolichyl-phosphate beta-glucosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1B
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichol-phosphate mannosyltransferase subunit 1
Sequence:
MGKLAVAAITSLWVIPMSIIVNHIVPEPYMDEIFHVPQAQQYCNGNFRSWDPMITTPPGLYYLSLAHVASLFPGMLLMENTSQSFSEACSTSVLRSTNAVSAVLCGVLVYEIIRFLGPNLSDRKATFMALVMSLYPLHWFFTFLYYTDVASLTAVLAMYLTCLKRRYVLSALFGTLAVFIRQTNVVWMLFVACSGILDFTLDSSKQKGKQEVNQELHQSSNKKGATLRSNLRKRKSDISSDTSDPFNHGQTVPSTEDTSDLVYDIYTVISTSWNLKWRILIKFSPFIFVVVAFGIFILWNGGIVLGAKEAHVVSLHFAQIMYFSLVSALFTAPLHFSVNQLRHQFHQLHRNWSLSLILTLVALVAGFVSVHFFSLAHPYLLADNRHYPFYLWRKIINAHWLMKYILVPVYVYSWFSILTLLAKTRRQTWILVYFLATCGVLVPTPLIEFRYYTIPFYLFMLHSCVRSSSFATWLLIGTIFVSINVFTMAMFLFRPFKWSHEDGVQRFIW
Protein: ATP-dependent zinc metalloprotease FTSH 7, chloroplastic (AtFTSH7) (EC 3.4.24.-) (Q9SD67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable ATP-dependent zinc metallopeptidase.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:14630971}; Multi-pass membrane protein {ECO:0000269|PubMed:14630971}; Stromal side {ECO:0000269|PubMed:14630971}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- Protein TIC 100
- Non-canonical heme oxygenase HOZ, chloroplastic
- Protein TIC 56, chloroplastic
Sequence:
MTTTFEFLQPRIHGFATCCSSNSLLYSKASRFFNDRCRVYRQNPNRFVSNSITLPLQKKQVTVLRNHERFNLWDGFSRKKSRLVVNCQEDDQNESSSEEEESSQSTPAKSERKREKKEDKVWWSKGKKWQWQPIIQAQGIGVLLLQLSVVMFVMRLLRPGIPLPGSEPRIQTTFVSVPYSEFLSKVNSNQVQKVEVDGVQVLFKLRDDGKWQESETSRLSQSSESLLRTVAPTKRVVYSTTRPGDIKTPYEKMLGNNVEFGSPEKRSGGFFNSALIALFYIAVLAGLIRFPVSFSTSSTGQLRTRKAGGPDGGKVSGGGETITFADVAGVDEAKEELEEIVEFLRNPEKYVRLGARPPRGVLLVGLPGTGKTLLAKAVAGEAEVPFISCSASEFVELYVGMGASRVRDLFARAKKEAPSIIFIDEIDAVAKSRDGKFRMGSNDEREQTLNQLLTEMDGFDSNSAVIVLGATNRADVLDPALRRPGRFDRVVTVETPDKIGRESILRVHVSKKELPLGDDVNLGSIASMTTGFTGADLANLVNEAALLAGRKNKTNVEKIDFIQAVERSIAGIEKKSARLKGNEKAVVARHEAGHAVVGTAVANLLTGQPRVEKLSILPRTGGALGFTYIPPTSEDRYLLFIDELLGRLVTLLGGRAAEEVVYSGRISTGAFDDIRRATDMAYKAVAEYGLNQKIGPVSVATLSGGGIDDSGGSPWGRDQGKLVDLVQKEVTILLQSALDVALSVVRANPDVLEGLGAQLEEKEKVEGEELQKWLSMVVAPEELAVFVEGKQELLLPAQASSS
Protein: Lymphocyte antigen 6 complex locus protein G6c (Q9Z1Q4)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
- Lymphocyte antigen 6G6e
- Lymphocyte antigen 6 complex locus protein G5c
- Lymphocyte antigen 6 complex locus protein G5b
Sequence:
MKHLLLLTLSALLYCWVSADTRCHSCYKVPVLGCVDRQSCRLEPGHKCLTTNVYLGKMWVFSNLRCGTPEEPCREVFNETNHKLGLNYNTTCCDKDNCNSPAPRPTPALALISLTSLAGLGLWLLH
Protein: Defective proboscis extension response 2, isoform F (Defective proboscis extension response 2, isoform G) (Q59DZ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dpr-interacting protein theta
- Dpr-interacting protein eta, isoform B
Sequence:
MAMEGKCFGCIATPILVIMISISRAWTMQQQHLSPAIQQHPAVKSLSHLVDGNDNLLPMVSAPSSIDNDYVYIASVNRKFPQFGNSIDDEREAEEQPPEETTYPPPVFDFGMPRNITTRTGHTAAINCRVDNLGDKSVSWIRKRDLHILTAGILTYTSDERFKVVRTADSKDWTLHVKYAQPRDSGIYECQVNTEPKISMAFRLNVIVTPPDAKAIIAGPTDLYVKVGSSVTLTCHVKQPATSAQDIGPIYWYRGPYILTPFVAHPNDAAIDLQRISMESTLAEKLQSRLRIANAQLLDTGNYTCMPTTAEAASVVVNVINDESPAAMQKSRAIRTSGSMRSSRLVLLLAMVASSVVRWLIGGQRIGSNSCHDSCSNLSTLHINYCNLRAKITSHLKEHRCLGPGSTVES
Protein: G antigen 12I (GAGE-12I) (P0CL82)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSWRGRSTYYWPRPRRYVQPPEMIGPMRPEQFSDEVEPATPEEGEPATQRQDPAAAQEGEDEGASAGQGPKPEAHSQEQGHPQTGCECEDGPDGQEMDPPNPEEVKTPEEGEKQSQC
Protein: Voltage-dependent P/Q-type calcium channel subunit alpha (Q9NS89)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU003808}.
Interaction partners:
Sequence:
MARFGDEMPARYGGGGSGAAAGVVVGSGGGRGAGGSRQGGQPGAQRMYKQSMAQRARTMALYNPIPVRQNCLTVNRSLFLFSEDNVVRKYAKKITEWPPFEYMILATIIANCIVLALEQHLPDDDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFAFHKGSYLRNGWNVMDFVVVLTGILATVGTEFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMIPLLQIGLLLFFAILIFAIIGLEFYMGKFHTTCFEEGTDDIQGESPAPCGTEEPARTCPNGTKCQPYWEGPNNGITQFDNILFAVLTVFQCITMEGWTDLLYNSNDASGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYMEWISKAEEVILAEDETDGEQRHPFDGALRRTTIKKSKTDLLNPEEAEDQLADIASVGSPFARASIKSTKLENSTFFHKKERRMRFYIRRMVKTQAFYWTVLSLVALNTLCVAIVHYNQPEWLSDFLYYAEFIFLGLFMSEMFIKMYGLGTRPYFHSSFNCFDCGVIIGSIFEVIWAVIKPGTSFGISVLRALRLLRIFKVTKYWASLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFDEGTPPTNFDTFPAARMTVFQSLTGEDWNEVMYDGIKSQGGVQGGMVFSIYFIVLTLFGNYTLLNVFLAIAVDNLANVLELTKDEQEEEEAANQKLALQKAKEVAEVSPLSAANMSIAVKEQQKNQKPAKSVWEQRTSEMRKQNLLASREALYNEMDPDERWKAAYTRHLRPDMKTHLDRPLVVDPQENRNNNTNKSRAAEPTVDQRLGQQRAEDFLRKQARYHDRARDPSGSAGLDARRPWAGSQEAELSREDPYGRESDHHAREGSLEQPGFWDGEAERGKAGDPHRRHVHRQGGSRESRSGSPRTGADGEHRRHRAHRRPGEEGPEDKAERRARHREGSRPARGGEGEGEGPDGGERRRRHRHGAPATYEGDARREDKERRHRRRKENQGSGVPVSGPNLSTTRPIQQDLGRQDPPLAEDIDNMKNNKLATAESAAPHGSLGHAGLPQSPAKMGNSTDPGPMLAIPAMATNPQNAASRRTPNNPGNPSNPGPPKTPENSLIVTNPSGTQTNSAKTARKPDHTTVDIPPACPPPLNHTVVQVNKNANPDPLPKKEEEKKEEEEDDRGEDGPKPMPPYSSMFILSTTNPLRRLCHYILNLRYFEMCILMVIAMSSIALAAEDPVQPNAPRNNVLRYFDYVFTGVFTFEMVIKMIDLGLVLHQGAYFRDLWNILDFIVVSGALVAFAFTGNSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVFNILIVYMLFMFIFAVVAVQLFKGKFFHCTDESKEFEKDCRGKYLLYEKNEVKARDREWKKYEFHYDNVLWALLTLFTVSTGEGWPQVLKHSVDATFENQGPSPGYRMEMSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKMMEEYSLEKNERACIDFAISAKPLTRHMPQNKQSFQYRMWQFVVSPPFEYTIMAMIALNTIVLMMKFYGASVAYENALRVFNIVFTSLFSLECVLKVMAFGILNYFRDAWNIFDFVTVLGSITDILVTEFGNNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIGIDVEDEDSDEDEFQITEHNNFRTFFQALMLLFRSATGEAWHNIMLSCLSGKPCDKNSGILTRECGNEFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEYVRVWAEYDPAACGRIHYKDMYSLLRVMSPPLGLGKKCPPGVAYKRLLRMDLPVADDNTVHFNSTLMALIRTALDIKIAKGGADKQQMDAELRKEMMAIWPNLSQKTLDLLVTPHKSTDLTVGKIYAAMMIMEYYRQSKAKKLQAMREEQDRTPLMFQRMEPPSPTQEGGPGQNALPSTQLDPGGALMAHESGLKESPSWVTQRAQEMFQKTGTWSPEQGPPTDMPNSQPNSQSVEMREMGRDGYSDSEHYLPMEGQGRAASMPRLPAENQRRRGRPRGNNLSTISDTSPMKRSASVLGPKARRLDDYSLERVPPEENQRHHQRRRDRSHRASERSLGRYTDVDTGLGTDLSMTTQSGDLPSKERDQERGRPKDRKHRQHHHHHHHHHHPPPPDKDRYAQERPDHGRARARDQRWSRSPSEGREHMAHRQGSSSVSGSPAPSTSGTSTSRRGRRQLPQTPSTPRPHVSYSPVIRKAGGSGPPQQQQQQQQQQQQQQQQQQQQQQQQAVARPGRAATSGPRRYPGPTAEPLAGDRPPTGGHSSGRSPRMERRVPGPARSESPRACRHGGARWPASGPHVSEGPPGPRHHGYYRGSDYDEADGPGSGGGEEAMAGAYDAPPPVRHASSGATGRSPRTPRASGP
Protein: Pentatricopeptide repeat-containing protein 1, mitochondrial (O75127)
Organism: Homo sapiens (Human)
Function: Mitochondrial protein implicated in negative regulation of leucine tRNA levels, as well as negative regulation of mitochondria-encoded proteins and COX activity. Affects also the 3'-processing of mitochondrial tRNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19651879, ECO:0000269|PubMed:21857155}. Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- FAST kinase domain-containing protein 2
- Neugrin
- FAST kinase domain-containing protein 3
- Pseudouridylate synthase RPUSD4, mitochondrial
- Probable ATP-dependent RNA helicase DDX28
- Transcription termination factor 3, mitochondrial
- Pseudouridylate synthase TRUB2, mitochondrial
- Mitochondrial mRNA pseudouridine synthase RPUSD3
- Pentatricopeptide repeat-containing protein 2
- RCC1-like G exchanging factor-like protein
Sequence:
MDFVRLARLFARARPMGLFILQHLDPCRARWAGGREGLMRPMWAPFSSSSSQLPLGQERQENTGSLGSDPSHSNSTATQEEDEEEEESFGTLSDKYSSRRLFRKSAAQFHNLRFGERRDEQMEPEPKLWRGRRNTPYWYFLQCKHLIKEGKLVEALDLFERQMLKEERLQPMESNYTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVCAESPWKDSALQSALKLRQQLQAKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHKGHVVTEETFSFLLMGCIQDKKTGFRYALQVWRLMLSLGLQPSRDSYNLLLVAARDCGLGDPQVASELLLKPREEATVLQPPVSRQRPRRTAQAKAGNLMSAMLHVEALERQLFLEPSQALGPPEPPEARVPGKAQPEVDTKAEPSHTAALTAVALKPPPVELEVNLLTPGAVPPTVVSFGTVTTPADRLALIGGLEGFLSKMAEHRQQPDIRTLTLLAEVVESGSPAESLLLALLDEHQVEADLTFFNTLVRKKSKLGDLEGAKALLPVLAKRGLVPNLQTFCNLAIGCHRPKDGLQLLTDMKKSQVTPNTHIYSALINAAIRKLNYTYLISILKDMKQNRVPVNEVVIRQLEFAAQYPPTFDRYQGKNTYLEKIDGFRAYYKQWLTVMPAEETPHPWQKFRTKPQGDQDTGKEADDGCALGGR
Protein: Phosphatidate cytidylyltransferase, mitochondrial (EC 2.7.7.41) (CDP-diacylglycerol synthase) (CDP-DAG synthase) (Mitochondrial translocator assembly and maintenance protein 41 homolog) (TAM41) (O74339)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. Required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the mitochondrial respiratory chain in the mitochondrial inner membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P53230}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53230}; Matrix side {ECO:0000250|UniProtKB:P53230}.
Interaction partners:
- Histidinol-phosphate aminotransferase
- Protein kes1
Sequence:
MIFGKTHFLSYNILRYSTKRWMNRHSYSHHAKCTVAQLLKQNLLTFENQRIQPEEELKENLTKVVNYFQAPIDVAVGYGSGVFRQAGYSQKENPMIDFIFQVEDPVKWHKINLQQNPSHYSFVKNFGPGFVSTLQESFGTGVYYNTHVEVEGNIIKYGVTSKKDVYEDLKNWNTMYLAGRFQKPVVILKGEDEFYKENSYNLSSALHVGLLMLADRFTEFDLYKTIVSLSYLGDIRMSFFAENPRKVENIVSKQIAFFRKLYLPLLYAEPGVHFIESSEVLKSMDPSDNSRYLSFHQNITKDSISRLLNGLPLNLVKILGLKPDTSSFEKCAELMLTNQISTRSLLISKSIKKLTSFSILTQSIKGIFTAGVIRSFVYVYAKLKKGLLSKWGR
Protein: Galactose-responsive transcription factor (Q5A5R1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- RFX-like DNA-binding protein RFX2
- Transcriptional regulator of filamentous growth FLO8
Sequence:
MSETNEIKLETEPKQPPYPIEQACDSCRKRKLKCSKEFPRCSKCIQHEWCCSYSPRTIRSPLTRAHLTEVENRVSQLEGILHYLLPDHDIDEIINDHDKAILAPIRQKLQPSPKPCAPTEMHSPIDSITYPLRQSKSNPIPEEYPKSRIKQEIIDDFLLNNITTTTKNNDYITPTVFNSSVNSTAQSSSLTSPSSLLSLNSYDGTIEEVLELDQPQLKKVKLEPSVSTSNSSSSSPTQFSLFNDYNLDMIFEGVVDETVNV
Protein: Translation machinery-associated protein 46 (DRG family-regulatory protein 1) (Q12000)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosome-interacting GTPase 1
- Protein GIR2
- Ribosome-interacting GTPase 2
- Small ribosomal subunit protein eS19A
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein eS7A
- Small ribosomal subunit protein uS13A
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein uS2A
Sequence:
MPPKKGKQAQAAGKKKDNVDKTFGMKNKNRSTKVQKYIKQVQSQSDPKKEEMRLKKLEEKKRREAEEAERRALFNPVADQRVRAGVDPKSMVCALFKLGNCNKGAKCKFSHDLNVGRRMEKKDLYQDTRSEKENDTMDNWDEEKLRKVILSKHGNPKTTTDKVCKYFIEAVENGKYGWFWICPNGGDKCMYRHSLPEGFVLKTNEQKRLERESLEKQPKITLEEFIETERGKLDKSKLTPITIANFAQWKKDHVIAKINAEKKLSSKRKPTGREIILKMSAENKSFETDNADMPDDVTQGSAWDLTEFTDALKKADHQDDGGIKDYGDGSNPTFDIKKANSATLA
Protein: Energy-coupling factor transporter transmembrane protein EcfT (ECF transporter T component EcfT) (A2RI03)
Organism: Lactococcus lactis subsp. cremoris (strain MG1363)
Function: Part of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. In this organism these probably include biotin, thiamine precursor, niacin, pantothenic acid, queuosine precursor, riboflavin and thiamine. Uptake of niacin or riboflavin into proteosomes containing EcfA1A2T and Niax or RibU has been demonstrated. Uptake requires hydrolyzable Mg-ATP and is substrate-specific; NiaX-containing proteosomes did not transport riboflavin.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21135102}; Multi-pass membrane protein {ECO:0000305|PubMed:21135102}.
Interaction partners:
- Energy-coupling factor transporter ATP-binding protein EcfA1
- Energy-coupling factor transporter ATP-binding protein EcfA2
- Biotin transporter BioY
- Pantothenic acid transporter PanT
- Thiamine transporter ThiT
- Biotin transporter BioY2
- Thiamine precursor transporter HmpT
- Putative cobalt ABC transporter permease protein
- Putative cobalt ABC transporter ATP-binding protein
- Riboflavin transporter RibU
Sequence:
MQNMLMGRYIPGDSIIHRMDPRSKLLVMIAFVVIIFLAHDWLGYLLLVLYTLAGVLLSKISVSYFLRGLRPMIGLILFTVIFQMLFTNGQHVIFSLWFIKISTESLINAVYIFFRFVLIIFMSTILTLTTPPLTLADGIEKGLGPLKKIKVPVHELGLMLSISLRFIPTLMDDTTMIMNAQKARGMDFGEGNLLKKIKSVIPILIPLFVSSFRRADDLAVAMESRGYQGGDGRTKYRQLKWQSRDSLLVVSIIIMTILLILWSKVS
Protein: Serine rich endogenous peptide 4 (AtSCOOP4) (Phytocytokine SCOOP4) (Precursor of serine rich endogenous peptide phytocytokine 4) (Secreted transmembrane peptide 10) (Q570K8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation. Inhibits root growth. Prevents general growth and development. Exhibits antibacterial effects against Pseudomonas syringae pv. tomato DC3000, Ralstonia solanacearum, Bacillus subtilis and Agrobacterium tumefaciens, thus being an antimicrobial peptide (AMP).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:B3H7I1}. Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:B3H7I1}. Note=The precursor of SCOOP4, PROSCOOP4, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP4 in the apoplasm. {ECO:0000250|UniProtKB:B3H7I1}.
Interaction partners:
- Transmembrane protein
- Serine rich endogenous peptide 12
Sequence:
MATKTSNLGHLLLSLFILLLFILSQVGVAQAKRLQQRNKLRLDCVPLPPPPPPLRGIVKPPIASFHSASPKDKGP
Protein: Proteasome subunit alpha type-1-A (20S proteasome alpha subunit F-1) (Proteasome 30 kDa subunit) (Proteasome component 2A) (AtPSM30) (Proteasome subunit alpha type-6) (Protein ARSENIC TOLERANCE 5) (P34066)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Negatively regulates thiol biosynthesis and arsenic tolerance.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-1
- Proteasome subunit beta type-2-B
- Proteasome subunit beta type-3-A
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-4
- Proteasome subunit beta type-6
- Proteasome subunit beta type-2-A
- Proteasome subunit alpha type-2-B
- Proteasome subunit alpha type-6-A
- Proteasome subunit alpha type-5-A
Sequence:
MFRNQYDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSELSSHQRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGSRSQAAKTYLERRFESFGDSSREDLIKDAILAVRETLQGETLKSSLCTVAILGVDEPFHFLDQEAIQKVIDTFEKVPEEEEGEGEAGEGEAEAAEAAPAERGGGVAGDQDVAPMEM