wanglab/gogpt-training-data huggingface dataset:
Protein: Adiponectin receptor 1 (A0A8I6AFR8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSSHKGSAVAQGNGAPSSNRAADTVELAELGPLLEEKGKRAATSPAKVSSSSVCFPYFQVWEGRWRVIPYDVLPDWLKDNDYLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGFVLFLFLGILTMLRPNMYFMAPLQEKVVFGMFFLGAVLCLSFSWLFHTVYCHSEKVSRTFSKLDYSGIALLIMGSFVPWLYYSFYCSPQPRLIYLSIVCVLGISAIIVAQWDRFATPKHRQTRAGVFLGLGLSGVVPTMHFTIAEGFVKATTVGQMGWFFLMAVMYITGAGLYAARIPERFFPGKFDIWFQSHQIFHVLVVAAAFVHFYGVSNLQEFRYGLEGGCTDDSLL
Protein: Nuclear receptor coactivator 6 (Nuclear receptor coactivator-6 delta) (F6M2K4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVLDDLPNLEDIYTSLCSSTMEDSEMDFDSGLEDDDTKSDSILEDSTIFVAFKGNIDDKDFKWKLDAILKNVPNLLHMESSKLKVQKVEPWNSVRVTFNIPREAAERLRILAQSNNQQLRDLGILSVQIEGEGAINLALAQNRSQDVRMNGPMGAGNSVRMEAGFPMASGPGIIRMNNPATVMIPPGGNVSSSMMAPGPNPELQPRTPRPASQSDAMDPLLSGLHIQQQSHPSGSLAPPHHPMQPVSVNRQMNPANFPQLQQQQQQQQQQQQQQQQQQQQQQQQQLQARPPQQHQQQQPQGIRPQFTAPTQVPVPPGWNQLPSGALQPPPAQGSLGTMTANQGWKKAPLPGPMQQQLQARPSLATVQTPSHPPPPYPFGSQQASQAHTNFPQMSNPGQFTAPQMKSLQGGPSRVPTPLQQPHLTNKSPASSPSSFQQGSPASSPTVNQTQQQMGPRPPQNNPLPQGFQQPVSSPGRNPMVQQGNVPPNFMVMQQQPPNQGPQSLHPGLGGMPKRLPPGFSAGQANPNFMQGQVPSTTATTPGNSGAPQLQANQNVQHAGGQGAGPPQNQMQVSHGPPNMMQPSLMGIHGNMNNQQAGTSGVPQVNLSNMQGQPQQGPPSQLMGMHQQIVPSQGQMVQQQGTLNPQNPMILSRAQLMPQGQMMVNPPSQNLGPSPQRMTPPKQMLSQQGPQMMAPHNQMMGPQGQVLLQQNPMIEQIMTNQMQGNKQQFNTQNQSNVMPGPAQIMRGPTPNMQGNMVQFTGQMSGQMLPQQGPVNNSPSQVMGIQGQVLRPPGPSPHMAQQHGDPATTANNDVSLSQMMPDVSIQQTNMVPPHVQAMQGNSASGNHFSGHGMSFNAPFSGAPNGNQMSCGQNPGFPVNKDVTLTSPLLVNLLQSDISAGHFGVNNKQNNTNANKPKKKKPPRKKKNSQQDLNTPDTRPAGLEEADQPPLPGEQGINLDNSGPKLPEFSNRPPAKMLRVPTTEW
Protein: CCAAT/enhancer-binding protein alpha (C/EBP alpha) (P05554)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta. Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes. During early embryogenesis, plays essential and redundant functions with CEBPB (By similarity). Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP). Critical for the proper development of the liver and the lung (By similarity). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage. To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Down-regulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters. Proliferation arrest also depends on a functional binding to SWI/SNF complex (By similarity). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC1. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:8367486}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleolus {ECO:0000269|PubMed:20075868}.
Interaction partners:
- Runt-related transcription factor 1
- Cyclin-dependent kinase 4
- Forkhead box protein O1
- CCAAT/enhancer-binding protein beta
- Receptor-type tyrosine-protein kinase FLT3
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase inhibitor 1
- Transcription factor E2F1
- RUNX1 partner transcriptional co-repressor 1
- Transcription factor PU.1
Sequence:
MESADFYEAEPRPPMSSHLQSPPHAPSNAAFGFPRGAGPAPPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAAGPAGGGGDFDYPGAPAGPGGAVMSAGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPPHPHASPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHPAPAMGAAGLPGPGGSLKGLAGPHPDLRTGGGGGGGAGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELDTLRGIFRQLPESSLVKAMGNCA
Protein: Inner membrane transporter YgjI (P42590)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Glucosidase YgjK
- Evolved beta-galactosidase subunit beta
- Evolved beta-galactosidase subunit alpha
- Uncharacterized protein YgjJ
- HTH-type transcriptional regulator EbgR
- tRNA-binding protein YgjH
Sequence:
MSDTKRNTIGKFGLLSLTFAAVYSFNNVINNNIELGLASAPMFFLATIFYFIPFCLIIAEFVSLNKNSEAGVYAWVKSSLGGRWAFITAYTYWFVNLFFFTSLLPRVIAYASYAFLGYEYIMTPVATTIISMVLFAFSTWVSTNGAKMLGPITSVTSTLMLLLTLSYILLAGTALVGGVQPADAITVDAMIPNFNWAFLGVTTWIFMAAGGAESVAVYVNDVKGGSKSFVKVIILAGIFIGVLYSVSSVLINVFVSSKELKFTGGSVQVFHGMAAYFGLPEALMNRFVGLVSFTAMFGSLLMWTATPVKIFFSEIPEGIFGKKTVELNENGVPARAAWIQFLIVIPLMIIPMLGSNTVQDLMNTIINMTAAASMLPPLFIMLAYLNLRAKLDHLPRDFRMGSRRTGIIVVSMLIAIFAVGFVASTFPTGANILTIIFYNVGGIVIFLGFAWWKYSKYIKGLTAEERHIEATPASNVD
Protein: Meiotic drive suppressor wtf35 (A0A482AU66)
Organism: Schizosaccharomyces kambucha (Fission yeast)
Function: Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons. Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus; the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole (By similarity). Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote (By similarity).
Subcellular location: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKNNYTSLKSPLDEEDELKTDHEIDLEKGLLPEYNSEEEGALPPYSDISKLAKTVPEDSSTGPTETANPNVERRQGFKDSHPNIYSLLRLLISVLAVSVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPILFIAIFCFFETWTQAVAQCIKVTAIFLAQCVKACGKGIKHFLKKWENMPMAFSEVFLFNILVGSPRMNLRYIFGDRWGLKCSLAEHITFVVLSILVFIAETVKPGSIRVNLIRKMGYEAKQQVNEYTAVPLREMNPESEA
Protein: Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2 (BPG-independent PGAM 2) (Phosphoglyceromutase 2) (EC 5.4.2.12) (PGAM-I 2) (Q9M9K1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA). Required for guard cell function (e.g. blue light-, abscisic acid- (ABA), and low CO(2)-regulated stomatal movements) and fertility (e.g. pollen grains production).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Enolase 1, chloroplastic
- Bifunctional enolase 2/transcriptional activator
- Cytosolic enolase 3
- Phosphoglycerate kinase 3, cytosolic
- Phosphoglycerate kinase 1, chloroplastic
- Phosphoglycerate kinase 2, chloroplastic
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
- Triosephosphate isomerase, chloroplastic
- Triosephosphate isomerase, cytosolic
- Cleavage stimulation factor subunit 50
Sequence:
MGSSGDVNWKLADHPKLPKGKTIGLIVLDGWGESDPDQYNCIHKAPTPAMDSLKDGKPDTWRLIKAHGTAVGLPSEDDMGNSEVGHNALGAGRIYAQGAKLVDLALASGKIYEDEGFKYISQSFEKGTVHLIGLLSDGGVHSRLDQVQLLLKGFAERGAKRIRVHILTDGRDVLDGSSVGFVETLEADLAALRAKGVDAQVASGGGRMYVTMDRYENDWSVVKRGWDAQVLGEAPHKFKSALEAVKTLRAEPGANDQYLPSFVIVDDNGKAVGPIVDGDAVVTFNFRADRMVMHAKALEYKDFDKFDRVRVPDIRYAGMLQYDGELKLPSRYLVSPPLIDRTSGEYLAHNGVRTFACSETVKFGHVTFFWNGNRSGYFNEKLEEYVEIPSDSGISFNVQPKMKALEIAEKARDAILSGKFDQVRVNLPNGDMVGHTGDIEATVVACEAADRAVRTILDAIEQVGGIYVVTADHGNAEDMVKRDKSGKPALDKEGNLQILTSHTLKPVPIAIGGPGLSAGVRFRQDIETPGLANVAATVMNLHGFVAPSDYETSLIEVVEK
Protein: Polyamine oxidase 3 (OsPAO3) (EC 1.5.3.-) (Q7X809)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Flavoenzyme involved in polyamine back-conversion. Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives. Substrate preference is spermidine > norspermine > thermospermine > N(1)-acetylspermine > spermine. No activity detected when putrescine is used as substrate. Plays an important role in the regulation of polyamine intracellular concentration (Probable).
Subcellular location: Peroxisome {ECO:0000269|PubMed:21796433}.
Interaction partners:
- Aminopropyl transferase
- Spermidine synthase 1
- Amine oxidase
- Amine oxidase
- Amine oxidase
- Polyamine oxidase 5
- N-carbamoylputrescine amidase
- Polyamine oxidase 4
- Os02g0254700 protein
- Polyamine oxidase 1
Sequence:
MANNSSYGENVRRKSHTPSAIVIGSGFAGIAAANALRNASFEVVLLESRDRIGGRIHTDYSFGFPVDLGASWLHGVCEENPLAPIIGRLGLPLYRTSGDDSVLFDHDLESYALYDTKGHQVPQELVEKIGKVFETILEETGKLREETKEDISIAKAIAIVMERNPHLRQEGIAHDVLQWYLCRMEGWFATDADAISLQGWDQEVLLPGGHGLMVRGYRPVINTLAKGLDIRLGHRVVEIVRHRNRVEVTVSSGKTFVADAAVIAVPLGVLKANTIKFEPRLPEWKEEAIRELSVGVENKIILHFSEVFWPNVEFLGVVSSTTYGCSYFLNLHKATGHPVLVYMPAGRLACDIEKLSDEAAAQFAFSQLKKILPNAAEPIHYLVSHWGSDENTLGSYTFDGVGKPRDLYEKLRIPVDNLFFAGEATSVQYTGTVHGAFSTGLMAAEECRMRVLERFRELDMLEMCHPAMGEQTATVSVPLLISRL
Protein: DUF1308 domain-containing protein (Q387L1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNIYEWQSIDEDAFGADGDHTSLNLSGHFSSSGSTSISRTHCGSSDVSDGVSSHEKLLRELTKLRDRLEGNSERYASVNNLSRLRHRIEKGLLMVEEFLKETPQHHAENALNNPATHQVDMRYLETLVTALENEPNVTKVCASFRVAVSSGGWETVPVDLVSCGGLRWVKVRAASTYSLQNEANKSGWENPITRLLLAAKESKLPFMQVPEVVVLFSCIPPATMADAVRSMGARPVSIAELKVRAAGGPLQALWRRDDFLPPRVSLPKYVCFDTTALVALCSEACFAESVESNVAALRGFRVLAEQQRRDKSDPCVRSHIEPILNQYSRWLDVHVMEKELRGHIQKNGRCSVDNPSVVSVEVSWLQKLVDLTADGESPREPLSESVVVRRMREDQAKRREIGDQNNCLNWIVADVTLAEFRWILETIAGPRELRRALSLLQCCSVVHASSQYVELCDSPITHVSLLASTSKVSQRNLLVFGLGDALRAIVISSNRQILNVALNQGVELMVATHPARALIEQKVRGMSRREGLLAPPPISTGVNV
Protein: Expressed protein (Q9SIY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEVVAVGSMKTQRQETWACSVTESFLLLVGKNLACLLLVAESLLIGLVAVDQRLSVKEGYKRGSRIEENKDASDSDDDDDDEDADEDDDDEDDANDEDFSGGEGDEGEEEADPEDDPVTNGGGGSDDEDDDDEEGDNDDEDEDNEDEEEDDDEEDDDDVRQPPSKKRK
Protein: LanC-like protein 2 (Testis-specific adriamycin sensitivity protein) (Q9NS86)
Organism: Homo sapiens (Human)
Function: Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes.
Subcellular location: Nucleus {ECO:0000269|PubMed:12566319}. Cytoplasm {ECO:0000269|PubMed:12566319}. Cell membrane {ECO:0000269|PubMed:12566319, ECO:0000269|PubMed:16979580}. Note=Localizes to the juxta-nuclear vesicles (PubMed:16979580). Associates with the cortical actin cytoskeleton (PubMed:16979580). Cholesterol depletion by methyl-beta-cyclodextrin causes partial dissociation from the cell membrane in vitro and an enhanced cell detachment from the matrix in vivo (PubMed:16979580). Membrane-association is important for the increased cellular sensitivity to an anticancer drug (adriamycin) (PubMed:16979580). {ECO:0000269|PubMed:16979580}.
Interaction partners:
- Epidermal growth factor receptor kinase substrate 8
Sequence:
MGETMSKRLKLHLGGEAEMEERAFVNPFPDYEAAAGALLASGAAEETGCVRPPATTDEPGLPFHQDGKIIHNFIRRIQTKIKDLLQQMEEGLKTADPHDCSAYTGWTGIALLYLQLYRVTCDQTYLLRSLDYVKRTLRNLNGRRVTFLCGDAGPLAVGAVIYHKLRSDCESQECVTKLLQLQRSVVCQESDLPDELLYGRAGYLYALLYLNTEIGPGTVCESAIKEVVNAIIESGKTLSREERKTERCPLLYQWHRKQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNETDRLVHWCHGAPGVIHMLMQAYKVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAHGCRIPDRPYSLFEGMAGAIHFLSDVLGPETSRFPAFELDSSKRD
Protein: CLAVATA3/ESR (CLE)-related protein 42 [Cleaved into: CLE42p] (Q6IWB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signal peptide that regulates cell fate. Represses tracheary element differentiation but promotes the formation of procambial cells.
Subcellular location: [CLE42p]: Secreted, extracellular space {ECO:0000250|UniProtKB:O49519}.
Interaction partners:
- CLAVATA3/ESR
- CLAVATA3/ESR
- Leucine-rich repeat receptor-like protein kinase TDR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- Protein CLAVATA 3
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
Sequence:
MRSPHITISLVFLFFLFLIIQTHQRTIDQTHQIGSNVQHVSDMAVTSPEGKRRERFRVRRPMTTWLKGKMIGANEHGVPSGPNPISNR
Protein: BAG cochaperone 4 (A0A8I6AP78)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSALRRSGYGPSDGPSYGRYYGPGGGDVPVHVPPPLYHPLRPEPPQPPVSWRGRGGAPAETTWPGEGAGGDGYYPSGGAWAEPSRAGGGHQVSLQVFSGAPVGKSWAEGILALQPIIFSSLITFFQSLNSYANGAYGPPYPPGPATASAASYSGAYYVPGYAQGTYSTDIPSTYRSPGNSPTPVSRWMYPQQDCPTEAPPLRGQVPGYPASQNPAMTLPHYPYGDGNRTVPQSGATGRPQDDAWASSAYGMGARYPWPSAAPSAPSGNLYMTESASPWPGNSSPQPPPSPPPQQPKDSSYSYSQSGQGMNRHSFPCSVRQYESPGAVNNDESDLLDSQVQYSAEPQLYGNTSSEHPSNQVPSNNLPEECFSSDEGTPPSIKKIIHVLEKVQYLEQEVEEFVGKKTDKAYWLLEEMLTKELLELDSVETGGQDSVRQARKEAVCKIQAILEKLEKKGL
Protein: P2Y purinoceptor 13 (P2Y13) (G-protein coupled receptor 86) (G-protein coupled receptor 94) (Q9BPV8)
Organism: Homo sapiens (Human)
Function: Receptor for ADP. Coupled to G(i)-proteins. May play a role in hematopoiesis and the immune system.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- P2Y purinoceptor 12
- P2Y purinoceptor 11
- HCG2039996
- P2X purinoceptor 1
- P2X purinoceptor 6
- Myeloid cell nuclear differentiation antigen
- P2Y purinoceptor 14
- P2Y purinoceptor 4
- P2X purinoceptor 5
- P2X purinoceptor 2
Sequence:
MTAAIRRQRELSILPKVTLEAMNTTVMQGFNRSERCPRDTRIVQLVFPALYTVVFLTGILLNTLALWVFVHIPSSSTFIIYLKNTLVADLIMTLMLPFKILSDSHLAPWQLRAFVCRFSSVIFYETMYVGIVLLGLIAFDRFLKIIRPLRNIFLKKPVFAKTVSIFIWFFLFFISLPNTILSNKEATPSSVKKCASLKGPLGLKWHQMVNNICQFIFWTVFILMLVFYVVIAKKVYDSYRKSKSKDRKNNKKLEGKVFVVVAVFFVCFAPFHFARVPYTHSQTNNKTDCRLQNQLFIAKETTLFLAATNICMDPLIYIFLCKKFTEKLPCMQGRKTTASSQENHSSQTDNITLG
Protein: Type IV pilus assembly protein PilF (Q9HXJ2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Essential component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. Plays an essential role in the outer membrane localization and assembly of PilQ into secretins which are dodecamers of PilQ.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:18776008}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
Interaction partners:
- Fimbrial assembly protein PilQ
- Type IV pilus inner membrane component PilN
- Type IV pilus inner membrane component PilM
- Type IV pilus inner membrane component PilO
- Type IV pilus non-core minor pilin PilE
- Type IV pilus inner membrane component PilP
- Type IV pilus retractation ATPase PilT
- Type IV pilus ATPase PilU
- Prepilin leader peptidase/N-methyltransferase
- HTH cro/C1-type domain-containing protein
Sequence:
MTVRAALVFLLAVGLTGCVTSGDQNPLKTDKGRDEARDAYIQLGLGYLQRGNTEQAKVPLRKALEIDPSSADAHAALAVVFQTEMEPKLADEEYRKALASDSRNARVLNNYGGFLYEQKRYEEAYQRLLEASQDTLYPERSRVFENLGLVSLQMKKPAQAKEYFEKSLRLNRNQPSVALEMADLLYKEREYVPARQYYDLFAQGGGQNARSLLLGIRLAKVFEDRDTAASYGLQLKRLYPGSLEYQEFQAEK
Protein: Cytosolic sulfotransferase 5 (AtSOT5) (EC 2.8.2.-) (Flavonoid 7-sulfotransferase 3a) (AtST3a) (Q9M1V2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to specifically catalyze the sulfate conjugation of flavones and flavonols. Strictly specific for the position 7. Substrate preference is kaempferol 3-sulfate > isorhamnetin > kaempferol.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At1g30610, chloroplastic
- Pentatricopeptide repeat-containing protein At2g41720
- Pentatricopeptide repeat-containing protein At5g27270
- Putative pentatricopeptide repeat-containing protein At2g02150
- Pentatricopeptide repeat-containing protein At5g04810, chloroplastic
- Protein THYLAKOID ASSEMBLY 8, chloroplastic
- CRM-domain containing factor CFM2, chloroplastic
- Pentatricopeptide repeat-containing protein At3g49170, chloroplastic
- Protein REGULATOR OF FATTY ACID COMPOSITION 3
- Endoribonuclease YBEY, chloroplastic
Sequence:
MEMNLRIEDLNEETKTLISSLPSDKDFTGKTICKYQGCWYTHNVLQAVLNFQKSFKPQDTDIIVASFPKCGTTWLKALTFALLHRSKQPSHDDDHPLLSNNPHVLVPYFEIDLYLRSENPDLTKFSSSPRLFSTHVPSHTLQEGLKGSTCKIVYISRNVKDTLVSYWHFFTKKQTDEKIISSFEDTFEMFCRGVSIFGPFWDHVLSYWRGSLEDPNHVLFMKFEEMKAEPRDQIKKFAEFLGCPFTKEEEESGSVDEIIDLCSLRNLSSLEINKTGKLNSGRENKMFFRKGEVGDWKNYLTPEMENKIDMIIQEKLQNSGLKF
Protein: Nucleotide/sugar transporter family protein (F4JU87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MRNNPVLPVSDPPLAGENDSDGKGVDDRLFKGSAMTKRGAYAALSYMACAVLVFSRIRFSGFRSSFMLVLFNKAALSSYDFPCVNVITLFQMVSSSLFLYALRRRKIISFTAADSFSIDSASTFVPVKTLFHTLPLAIAYLLYMLASMASVRGVNVPMYTTLRRTTVAFTMVIEYMLTGQRYTRSIIGSVGIILLGAFFAGARDLSFDFYGYGVVFLANISTAVYLATIARTGKSSGLNSFGLMWSNGIICGPILMIWTFICGDLEKTINFPHLLTPGFMVVLLCSCVLAFVLNYCIFLNTTLNSALTQTICGNMKDLFTVGLGWMLFGGLPFDLMNVIGQLFGFFGSGLYAYYKIIGR
Protein: Brevinin-2SN3 (E7EKH6)
Organism: Sylvirana spinulosa (Fine-spined frog) (Hylarana spinulosa)
Function: Antimicrobial peptide. Active against a variety of Gram-negative and Gram-positive bacterial strains. Active against fungus C.glabrata 090902 but not against C.albicans ATCC 10231. Shows hemolytic activity against human erythrocytes.
Subcellular location: Secreted {ECO:0000305|PubMed:24055160}.
Interaction partners:
Sequence:
MFTLKKPLLLLVFLGMISLSLCQDERGADEDDGGEMTEEEKRGAFGNLLKGVAKKAGLKILSIAQCKLSGTC
Protein: Syntaxin-binding protein 6 (Amisyn) (Q8NFX7)
Organism: Homo sapiens (Human)
Function: Forms non-fusogenic complexes with SNAP25 and STX1A and may thereby modulate the formation of functional SNARE complexes and exocytosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12145319}. Membrane {ECO:0000269|PubMed:12145319}; Peripheral membrane protein {ECO:0000269|PubMed:12145319}.
Interaction partners:
- Syntaxin-4
- Syntaxin-binding protein 5
- Solute carrier family 22 member 17
- Cochlin
- Synaptosomal-associated protein 23
- Syntaxin-3
- Alpha-soluble NSF attachment protein
- Vesicle-associated membrane protein 8
- Synaptosomal-associated protein 25
- Exocyst complex component 4
Sequence:
MSAKSAISKEIFAPLDERMLGAVQVKRRTKKKIPFLATGGQGEYLTYICLSVTNKKPTQASITKVKQFEGSTSFVRRSQWMLEQLRQVNGIDPNGDSAEFDLLFENAFDQWVASTASEKCTFFQILHHTCQRYLTDRKPEFINCQSKIMGGNSILHSAADSVTSAVQKASQALNERGERLGRAEEKTEDLKNSAQQFAETAHKLAMKHKC
Protein: Zinc finger protein 281 (GC-box-binding zinc finger protein 1) (Transcription factor ZBP-99) (Zinc finger DNA-binding protein 99) (Q9Y2X9)
Organism: Homo sapiens (Human)
Function: Transcription repressor that plays a role in regulation of embryonic stem cells (ESCs) differentiation. Required for ESCs differentiation and acts by mediating autorepression of NANOG in ESCs: binds to the NANOG promoter and promotes association of NANOG protein to its own promoter and recruits the NuRD complex, which deacetylates histones. Not required for establishement and maintenance of ESCs (By similarity). Represses the transcription of a number of genes including GAST, ODC1 and VIM. Binds to the G-rich box in the enhancer region of these genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:10448078}.
Interaction partners:
- Homeobox protein NANOG
- POU domain, class 5, transcription factor 1
Sequence:
MKIGSGFLSGGGGTGSSGGSGSGGGGSGGGGGGGSSGRRAEMEPTFPQGMVMFNHRLPPVTSFTRPAGSAAPPPQCVLSSSTSAAPAAEPPPPPAPDMTFKKEPAASAAAFPSQRTSWGFLQSLVSIKQEKPADPEEQQSHHHHHHHHYGGLFAGAEERSPGLGGGEGGSHGVIQDLSILHQHVQQQPAQHHRDVLLSSSSRTDDHHGTEEPKQDTNVKKAKRPKPESQGIKAKRKPSASSKPSLVGDGEGAILSPSQKPHICDHCSAAFRSSYHLRRHVLIHTGERPFQCSQCSMGFIQKYLLQRHEKIHSREKPFGCDQCSMKFIQKYHMERHKRTHSGEKPYKCDTCQQYFSRTDRLLKHRRTCGEVIVKGATSAEPGSSNHTNMGNLAVLSQGNTSSSRRKTKSKSIAIENKEQKTGKTNESQISNNINMQSYSVEMPTVSSSGGIIGTGIDELQKRVPKLIFKKGSRKNTDKNYLNFVSPLPDIVGQKSLSGKPSGSLGIVSNNSVETIGLLQSTSGKQGQISSNYDDAMQFSKKRRYLPTASSNSAFSINVGHMVSQQSVIQSAGVSVLDNEAPLSLIDSSALNAEIKSCHDKSGIPDEVLQSILDQYSNKSESQKEDPFNIAEPRVDLHTSGEHSELVQEENLSPGTQTPSNDKASMLQEYSKYLQQAFEKSTNASFTLGHGFQFVSLSSPLHNHTLFPEKQIYTTSPLECGFGQSVTSVLPSSLPKPPFGMLFGSQPGLYLSALDATHQQLTPSQELDDLIDSQKNLETSSAFQSSSQKLTSQKEQKNLESSTGFQIPSQELASQIDPQKDIEPRTTYQIENFAQAFGSQFKSGSRVPMTFITNSNGEVDHRVRTSVSDFSGYTNMMSDVSEPCSTRVKTPTSQSYR
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 (Oligosaccharyl transferase subunit DAD1) (Defender against cell death 1) (DAD-1) (P61805)
Organism: Rattus norvegicus (Rat)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Serine/threonine-protein kinase Chk1.
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Tumor suppressor candidate 3
- Dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit TMEM258
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2
- Oligosaccharyltransferase complex subunit OSTC
Sequence:
MSASVVSVISRFLEEYLSSTPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGFISCVGSFILAVCLRIQINPQNKADFQGISPERAFADFLFASTILHLVVMNFVG
Protein: 65 kDa invariant surface glycoprotein (Q587F1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMKYLLVFAIIATRIPVLLATNGGDKHVKANKKLTKEGAAALCKMKHLADKVAEERSQELKDRTQIFAGYIEFELYRIDYWLEKLNGPKGRKDGYAKLSDSDIEKVKEIFNKAKDGIAKQLPEAKKAGEEAEKLHTEVKKAAANARGVRLSEGTNSSGLYRILDWYCFKEGENAGKSDNCDGVKFSVHYETHRRRNVIDCSSTGYEENYDWSANALQVALNSWENVKPKKLESAGSDMNCNIGQSSESHPCTMTEEWQTPYKETVEKLRELEDAYQRGKKAHDAMLGYANTAYAVNTKVEQEKPLTEVIAAAKEAGKKGAKIIIPAAAPATPTNSTKNEDSASTEHVDRGIATNETQVEVGIDADFDSLLDATEAAEVTRRHQRTAMIILAVLVPAIILVVTAVAFFIMVKRRRNSSQDVDTGKAEGGVSSVKVVM
Protein: Chorismate mutase 2 (AtCM2) (EC 5.4.99.5) (CM-2) (Q9S7H4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:B4FUP5}.
Interaction partners:
- Chorismate synthase, chloroplastic
- Arogenate dehydratase/prephenate dehydratase 1, chloroplastic
- Arogenate dehydratase/prephenate dehydratase 2, chloroplastic
- Arogenate dehydratase 3, chloroplastic
- Arogenate dehydratase 5, chloroplastic
- Arogenate dehydratase 4, chloroplastic
- Arogenate dehydratase/prephenate dehydratase 6, chloroplastic
- Arogenate dehydrogenase 1, chloroplastic
- Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
- Shikimate kinase 2, chloroplastic
Sequence:
MARVFESDSGSGCSNVLSLDLIRESLIRQEDTIVFSLIERAKFPLNSPAFEESRCLDSGSFSSLTEFFVRETEIIQAKVGRYEYPEENPFFLENIPHSVFPTHKYPSALHPKALSVNINKQIWDIYFKELLPLFVKPGDDGNYPSTAASDLACLQALSRRIHYGKFVAEVKFRDAPQDYEPAIRAQDREALMKLLTFEKVEEMVKKRVQKKAETFGQEVKFNSGYGDESKKKYKVDPLLASRIYGEWLIPLTKLVEVEYLLRRLD