wanglab/gogpt-training-data huggingface dataset:
Protein: Rac-like GTP-binding protein ARAC11 (EC 3.6.5.-) (GTPase protein ROP1) (P92978)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in cell polarity control during the actin-dependent tip growth of pollen tubes. May regulate callose synthase 1 (CALS1) activity through the interaction with UGT1.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with the membrane when activated.
Interaction partners:
- CRIB domain-containing protein RIC4
- CRIB domain-containing protein RIC3
- Interactor of constitutive active ROPs 1
- Rho GDP-dissociation inhibitor 1
- Rop guanine nucleotide exchange factor 1
- Pollen receptor-like kinase 2
- CRIB domain-containing protein RIC10
- Immunoglobulin E-set superfamily protein
- At1g12070
- Rop guanine nucleotide exchange factor 12
Sequence:
MSASRFVKCVTVGDGAVGKTCLLISYTSNTFPTDYVPTVFDNFSANVVVNGSTVNLGLWDTAGQEDYNRLRPLSYRGADVFILAFSLISKASYENVSKKWIPELKHYAPGVPIVLVGTKLDLRDDKQFFIDHPGAVPITTAQGEELRKQIGAPTYIECSSKTQENVKAVFDAAIRVVLQPPKQKKKKSKAQKACSIL
Protein: Uncharacterized protein Rv1318c (P9WQ33)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- cAMP/cGMP dual specificity phosphodiesterase Rv0805
- Nucleoside diphosphate kinase
- Pyruvate kinase
- Bifunctional
- GTP 3',8-cyclase 2
- GTP 3',8-cyclase 1
- 3,4-dihydroxy-2-butanone-4-phosphate synthase
- Riboflavin biosynthesis protein RibBA
- GTP cyclohydrolase 1
- CRP-like cAMP-activated global transcriptional regulator
Sequence:
MSAKKSTAQRLGRVLETVTRQSGRLPETPAYGSWLLGRVSESQRRRRVRIQVMLTALVVTANLLGIGVALLLVTIAIPEPSIVRDTPRWLTFGVVPGYVLLALALGSYALTRQTVQALRWAIEGRKPTREEERRTFLAPWRVAVGHLMFWGVGTALLTTLYGLINNAFIPRFLFAVSFCGVLVATATYLHTEFALRPFAAQALEAGPPPRRLAPGILGRTMVVWLLGSGVPVVGIALMAMFEMVLLNLTRMQFATGVLIISMVTLVFGFILMWILAWLTATPVRVVRAALRRVERGELRTNLVVFDGTELGELQRGFNAMVAGLRERERVRDLFGRHVGREVAAAAERERSKLGGEERHVAVVFIDIVGSTQLVTSRPPADVVKLLNKFFAIVVDEVDRHHGLVNKFEGDASLTIFGAPNRLPCPEDKALAAARAIADRLVNEMPECQAGIGVAAGQVIAGNVGARERFEYTVIGEPVNEAARLCELAKSRPGKLLASAQAVDAASEEERARWSLGRHVKLRGHDQPVRLAKPVGLTKPRR
Protein: Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1) (Q57WW6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
Interaction partners:
- Proliferating cell nuclear antigen
- Protein artemis
- DNA polymerase
- Endo/exonuclease Mre11
- DNA polymerase delta subunit 2, putative
- DNA repair protein RAD50
- Replication factor C, subunit 5, putative
- Replication factor C, subunit 2, putative
- DNA polymerase
- Replication factor C, subunit 4, putative
Sequence:
MGVLGLSKLLYDRTPGAIKEQELKVYFGRRIAIDASMAVYQFVIAMKGFQEGQSVELTNEAGDVTSHLSGIFFRTLRMIDEGLRPIYVFDGKPPTLKASELESRRQRAEDAKHEFEKAKEEGDDEAMEKMSKRMVRVGRDQMEEVKTLLRLMGIPVVQAPSEAEAQCAELVKKNKAWAVGTEDMDALAFGSRVMLRHLTYGEAKKRPIAEYHLDEILEASGFSMQQFIDLCILLGCDYVPRISGIGPHKAWEGIKKYGSLEAFIESLDGTRYVVPEEFNYKDARNFFLEPEVTPGEEIDIQFREPDEEGLIKFLVDEKLFSKERVLKGIQRLRDALTKKTQGRLDQFFTITKPQKQVNSEASTAGTKRNRGAVALPGVLQRKSSSGHKKAVKK
Protein: GlcNAc transferase (Q54EX6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Myosin-2 heavy chain
Sequence:
MVVSKKPFIYTVGAVLIIVLIFQMNYYFRIDSKLTERDVKNSVNGGISGGINRNVVGEEIDPTIFVSLAAYRDVFCSDTINYIFNHANRPEKIFIGIVDQGSEFLEEDPNQDPSFPNSYCYRGLKVAPELIQSNVRRIALTVAQSKGPTLARYYATTLYNNETYFMQVDSHLRFIKGWDSLIINDLWLTKSYAPIGENGIPRTVLTHYPMAYNVEDSGLPVIDQTGVPRLCKGEFNSRGIITFNSFILKATTKPAECPYIAAGFFFTSGEAIKLVPFDPHLSNLFEGEEILYSVRMYSAGFRFFAPTLNVCFHYYSRPKSPKFWEDNKQYYLDMQKSVERLKYILRWPLENTPDLSEPQFAEIDKYTIANTTILTEYYQRWKIDVENKKVHWHQFCDQQPPQE
Protein: Guanylate cyclase soluble subunit alpha-1 (GCS-alpha-1) (EC 4.6.1.2) (Guanylate cyclase soluble subunit alpha-3) (GCS-alpha-3) (Soluble guanylate cyclase large subunit) (Q02108)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Guanylate cyclase soluble subunit beta-1
- Guanylate cyclase soluble subunit alpha-2
- cGMP-dependent protein kinase 1
- cGMP-dependent protein kinase 2
- Nitric oxide synthase 1
- Inosine triphosphate pyrophosphatase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Pyruvate kinase PKLR
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Bis
Sequence:
MFCTKLKDLKITGECPFSLLAPGQVPNESSEEAAGSSESCKATVPICQDIPEKNIQESLPQRKTSRSRVYLHTLAESICKLIFPEFERLNVALQRTLAKHKIKESRKSLEREDFEKTIAEQAVAAGVPVEVIKESLGEEVFKICYEEDENILGVVGGTLKDFLNSFSTLLKQSSHCQEAGKRGRLEDASILCLDKEDDFLHVYYFFPKRTTSLILPGIIKAAAHVLYETEVEVSLMPPCFHNDCSEFVNQPYLLYSVHMKSTKPSLSPSKPQSSLVIPTSLFCKTFPFHFMFDKDMTILQFGNGIRRLMNRRDFQGKPNFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRRWDNSVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVLIGEQARAQDGLKKRLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQLWQGQVVQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDCPGFVFTPRSREELPPNFPSEIPGICHFLDAYQQGTNSKPCFQKKDVEDGNANFLGKASGID
Protein: Rifin (C6KSL1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYTNILLFALPLNILVNTHKKPHTTARHTQKIPTTRSLSECELYAPVNYYSDPQMKEVMDNFNKQTQQRFHEYDERMKTTRQKCKDKCDKEIQKIILKDKLEKELMDKFATLDTDIQSDAIPSCVCEKSIAEKAEKGCLRCGYGLGSVAPMIGLTGSVAVNVWKTAELAAAMELAKQAGAAAGIKAGHLAGTKVVIDQLHTLGIYFVGGKPLESIIHVTNYMNVSVIYDKVYSHYTTLCTPRFVIDRPVGDFIFSGPVCNLVQPNHQGIWVKSSAQAIIKKKVEEAVAEGTQAADVVAKNTADEVTKAAIKTSTEAIDAATTTYYTPIIASIVAIVLIVLIMVIIYKILRYRRKRKMKKKLQYIKLLEE
Protein: Protein MANBAL (Q9NQG1)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MASDLDFSPPEVPEPTFLENLLRYGLFLGAIFQLICVLAIIVPIPKSHEAEAEPSEPRSAEVTRKPKAAVPSVNKRPKKETKKKR
Protein: Alpha-actinin-4 (Non-muscle alpha-actinin 4) (O43707)
Organism: Homo sapiens (Human)
Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA.
Subcellular location: Nucleus {ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:9508771}. Cytoplasm {ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:9508771}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:9508771}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). Nuclear translocation can be induced by the PI3 kinase inhibitor wortmannin or by cytochalasin D. Exclusively localized in the nucleus in a limited number of cell lines (breast cancer cell line MCF-7, oral floor cancer IMC-2, and bladder cancer KU-7). {ECO:0000250|UniProtKB:P57780, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:9508771}.
Interaction partners:
- Vinculin
- Alpha-actinin-1
- Nephrin
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- Synaptopodin
- Zyxin
- Podocin
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- PDZ and LIM domain protein 1
Sequence:
MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL
Protein: Iron-dependent extradiol dioxygenase (EC 1.13.11.25) (P9WNW7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the meta-cleavage of 3,4-dihydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione (3,4-DHSA) to produce 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid (4,9-DSHA).
Interaction partners:
- 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1
- Flavin-dependent monooxygenase, reductase subunit HsaB-triene-9,17-dione 4-hydroxylase, reductase subunit)
- Flavin-dependent monooxygenase, oxygenase subunit HsaA-triene-9,17-dione 4-hydroxylase, oxygenase subunit)-triene-9,17-dione monooxygenase)
- 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component
- 3-ketosteroid-9-alpha-monooxygenase, oxygenase component
- 3-oxosteroid 1-dehydrogenase
- Possible flavoprotein
- HTH-type transcriptional repressor KstR
- Acyl-CoA dehydrogenase IpdE1
- Acyl-CoA dehydrogenase FadE29
Sequence:
MSIRSLGYLRIEATDMAAWREYGLKVLGMVEGKGAPEGALYLRMDDFPARLVVVPGEHDRLLEAGWECANAEGLQEIRNRLDLEGTPYKEATAAELADRRVDEMIRFADPSGNCLEVFHGTALEHRRVVSPYGHRFVTGEQGMGHVVLSTRDDAEALHFYRDVLGFRLRDSMRLPPQMVGRPADGPPAWLRFFGCNPRHHSLAFLPMPTSSGIVHLMVEVEQADDVGLCLDRALRRKVPMSATLGRHVNDLMLSFYMKTPGGFDIEFGCEGRQVDDRDWIARESTAVSLWGHDFTVGARG
Protein: BARP protein (Q38CV8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSITFNNLWLLLTVLCTAGIRAHHVWNDCFADGSYPPLEGIPALCGVAEQLRGLPDTISSALVNVATASSKAFEAKVQAEEAVELAESKGLNVTKAKEAAVRATLAAEAAATAASNVEINAANIAAVPWSQRRQDAGLQKVALCDNVDKDVREAAAKCTKKAENVTAESLRAALEALENLVTDVKFQENLRKEDVEFHTELKSLEDHVEEAVRAQRQAEEAAAEAIKIVAADEEVRGYKKEEINQVAGTKKGHEANQTTGTNTGPVVNSVASPEGSVLLLMAGLFLGSVL
Protein: GATOR2 complex protein WDR24 (A0A499FJD3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKKRTTSGEGRERQRLPARRFRTTSPAALRADSVDGGSLLAPLLGLTDRAFSDCPDLADGAMEKMSRVTTALGGSVLTGRTMHCHLDAPANAISVCRDAAQVVVAGRSIFKIYAIEEEQFVEKLNLRVGRKPSLNLSCADVVWHQMDENLLATAATNGVVVTWNLGRPSRNKQDQLFTEHKRTVNKVCFHPTEAHVLLSGSQDGFMKCFDLRRKDSVSTFSGEATEAGPREWAMAGCVPILPVLSCRILRLHHSFAHGPMQDAESTANDARESWGCPLYPLGLCSGPQAGQSESVRDVQFSIRDYFTFASTFENGNVQLWDIRRPDRCERMFTAHNGPVFCCDWHPEDRGWLATGGRDKMVKVWDMTTHRAKEMHCVQTIASVARVKWRPECRHHLATCSMMVDHNIYVWDVRRPFVPAAMFEEHRDVTTGIAWRHPHDPSFLLSGSKDSSLCQHLFRDASQPVERANPEGLCYGLFGDLAFAAKESLVAAESGRKPYTGDRRHPIFFKRKLDPAEPFAGLASSALSVFETEPGGGGMRWFVDTAERYALAGRPLAELCDHNAKVARELGRNQVAQTWTMLRIIYCSPGLVPTANLNHSVGKGGSCGLPLMNSFNLKDMAPGLGSETRLDRSKGDARSDTVLLDSSATLITNEDNEETEGSDVPADYLLGDVEGEEDELYLLDPEHAHPEDPECVLPQEAFPLRHEIVDTPPGPEHLQDKADSPHVSGSEADVASLAPVDSSFSLLSVSHALYDSRLPPDFFGVLVRDMLHFYAEQGDVQMAVSVLIVLGERVRKDIDEQTQEHWYTSYIDLLQRFRLWNVSNEVVKLSTSRAVSCLNQASTTLHVNCSHCKRPMSSRGWVCDRCHRCASMCAVCHHVVKGLFVWCQGCSHGGHLQHIMKWLEGSSHCPAGCGHLCEYS
Protein: Defensin-1 (A4L7R7)
Organism: Pinus sylvestris (Scotch pine)
Function: Plant defense peptide. Has antifungal activity against B.cinera, F.oxysporum, F.solani and H.annosum with IC(50) values of 0.4 ug/ml, 2.9 ug/ml, 0.9 ug/ml and 1.4 ug/ml, respectively. Has modest antifungal activity against C.albicans and T.reesei. Causes thickening of F.oxysporum hyphae and an increase in their branching. Lacks antibacterial activity against the Gram-negative bacteria E.coli and E.carotovora.
Subcellular location: Secreted {ECO:0000250|UniProtKB:O65740}.
Interaction partners:
Sequence:
MAGKGVGSRLSTLFLLVLLVITIGMMQVQVAEGRMCKTPSGKFKGYCVNNTNCKNVCRTEGFPTGSCDFHVAGRKCYCYKPCP
Protein: Secretoglobin family 1D member 2 (Lipophilin-B) (O95969)
Organism: Homo sapiens (Human)
Function: May bind androgens and other steroids, may also bind estramustine, a chemotherapeutic agent used for prostate cancer. May be under transcriptional regulation of steroid hormones.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Mammaglobin-A
- Lysosomal acid lipase/cholesteryl ester hydrolase
- Mammaglobin-B
- Secretoglobin family 1D member 1
- Hepatic triacylglycerol lipase
Sequence:
MKLSVCLLLVTLALCCYQANAEFCPALVSELLDFFFISEPLFKLSLAKFDAPPEAVAAKLGVKRCTDQMSLQKRSLIAEVLVKILKKCSV
Protein: Threonine--tRNA ligase (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Q58597)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine, but does not detectably transfer it to tRNA(Thr). Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain. Has no activity on correctly acylated L-seryl-tRNA(Ser) or L-threonyl-tRNA(Thr). Deacylates correctly charged glycyl-tRNA(Gly), but not glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA adenine 76 has been dehydroxylated) nor the 2'-fluoro tRNA derivative, strongly suggesting the editing function is tRNA catalyzed.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
Interaction partners:
- Leucine--tRNA ligase
- Probable translation initiation factor IF-2
- Valine--tRNA ligase
- Histidine--tRNA ligase
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL11
- Isoleucine--tRNA ligase
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL3
Sequence:
MKMLLIHSDYLEFEAKEKTKIAEETENLKGKLDECLACFIAVEREDENNPEGTAIGAVEEIEKVANQLKVNNIVVYPYAHLSSDLSSPETAVKVLKDIESILKERGYNVLRAPFGWYKAFKISCKGHPLSELSRKIVAKEEKKEEGEESKFYLLNPETEEIIELNENNINIIKDEELLALAKHELGIREHKEHDEPPHVKFIKEKDICSYEEASDPGHFRWYPKGKLMRDLLADYVYNLVVNMGAMPVETPIMYDLGNPAIREHADKFGERQYRFRQGNKELMLRFAACFGQFMMKKDMYLLPRYLPLKLYELSTYSFRYEQRGELVGLKRLRCFTMPDMHTVCLNLEQAMEEFEKQFWECLKTGDDLNLSYSVIFRFTKDFFDEHRDWFFKIAKEYKNKYGKDVILEILPKRKHYWVGKVDIAVIDSLGRPIENPTVQIDVESAKRFDIKVHTNEGEIYPIILHCSPTGSIERVLCGLLEKAAIEAEKGNAPMLPVWLSPIQVRVIPVAERHYDYALKVAEKLRENNIRADFDDREESVSKKIRNAGKEWVPYVVVIGDEEMESDKLTVTIREKSTLKKPYKEKMTLDELIERIKKETANYPYRPLPLPIRCSLQPKFH
Protein: Pentatricopeptide repeat-containing protein At5g67570, chloroplastic (Protein DELAYED GREENING 1) (Protein EMBRYO DEFECTIVE 1408) (Q9FJW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of early chloroplast development and chloroplast gene expression in a SIGF-dependent manner.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18400937}.
Interaction partners:
- RNA polymerase sigma factor sigF, chloroplastic
- GTP-binding protein At2g22870
- At1g76620/F14G6_22
- Methionyl-tRNA formyltransferase, mitochondrial
- Expressed protein
- Titan9
- Gb|AAF56406.1
- DNA replication ATP-dependent helicase/nuclease JHS1
- At1g56200/F14G9_26
- Alpha-N-acetylglucosaminidase
Sequence:
MDASVVRFSQSPARVPPEFEPDMEKIKRRLLKYGVDPTPKILNNLRKKEIQKHNRRTKRETESEAEVYTEAQKQSMEEEARFQTLRREYKQFTRSISGKRGGDVGLMVGNPWEGIERVKLKELVSGVRREEVSAGELKKENLKELKKILEKDLRWVLDDDVDVEEFDLDKEFDPAKRWRNEGEAVRVLVDRLSGREINEKHWKFVRMMNQSGLQFTEDQMLKIVDRLGRKQSWKQASAVVHWVYSDKKRKHLRSRFVYTKLLSVLGFARRPQEALQIFNQMLGDRQLYPDMAAYHCIAVTLGQAGLLKELLKVIERMRQKPTKLTKNLRQKNWDPVLEPDLVVYNAILNACVPTLQWKAVSWVFVELRKNGLRPNGATYGLAMEVMLESGKFDRVHDFFRKMKSSGEAPKAITYKVLVRALWREGKIEEAVEAVRDMEQKGVIGTGSVYYELACCLCNNGRWCDAMLEVGRMKRLENCRPLEITFTGLIAASLNGGHVDDCMAIFQYMKDKCDPNIGTANMMLKVYGRNDMFSEAKELFEEIVSRKETHLVPNEYTYSFMLEASARSLQWEYFEHVYQTMVLSGYQMDQTKHASMLIEASRAGKWSLLEHAFDAVLEDGEIPHPLFFTELLCHATAKGDFQRAITLINTVALASFQISEEEWTDLFEEHQDWLTQDNLHKLSDHLIECDYVSEPTVSNLSKSLKSRCGSSSSSAQPLLAVDVTTQSQGEKPEEDLLLQDTTMEDDNSANGEAWEFTETELETLGLEELEIDDDEESSDSDSLSVYDILKEWEESSKKE
Protein: Synaptotagmin-14 (Synaptotagmin XIV) (SytXIV) (Q7TN84)
Organism: Mus musculus (Mouse)
Function: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent.
Subcellular location: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAIEGGERTCGVHELICIRKVSPEAVGFLSAVGVFIVLMLLLFLYINKKFCFENVGGFPDLGSGYNTRTNSQDKMYNSYMDRDEPGSSSESEDEALGKYHEALSRTHNSRWPLVDSRQKSYAWETRQKYSPLSAEYDGYSTEASMEDGNCIQRMRRTPPLDELQPPPYQDDSGSPHLSCTPSEIGDAKCEISHCSNSPRCSFNKCPSEGSTGHEAESYHNKGYEDDVPSDSTAVLSPEDMSAQGSSSQLPKPFDPEPEAKYGTLDVTFDYDSERQKLLVTVTAVTDIPTYNRTGGNSWQVHLVLLPIKKQRAKTSIQRGPCPVFTETFKFNHVESEMIGNYAVRFRLYGVHRMKKEKIVGEKIFYLTKLNLQGKMSLPVILEPSYNPSGCDSQVSLSEASCGDSTSSCQSLQHGSVPEILIGLLYNATTGRLSAEVIKGSHFKNLAANRPPNTYVKLTLLNSMGQEMSKCKTSTRRGQPNPVYKETFVFQVALFQLSDVTLILSVYNRRSMKRKEMIGWISLGLNSSGEEELRHWTAMKESKGQQVCRWHALLES
Protein: Hexosyltransferase (EC 2.4.1.-) (Q584I2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}.
Interaction partners:
Sequence:
MSPLKMRPTQARRRPRTADIAVILLLVMSLLIICCNLHRIHVVSTFLDENQAGVSQPIDEDEYLMFVPSNVAAVWKAQRFLAVLGIPSVDNSERSRRRDLQRQTCWKYSGVATRSNNFSGSLLPLYLLAPHQSNSYLISHSLKEEAARTHDIITLPTNDVSPSTRKKIGENGNWGIEAEVAMSRKTYLWLRFALHMFPNVSYIVKGDDDIFIRVPKYLADLRVMPRHGLYMGRYNYYNRIWRRNQLTYVNGYCITLSRDTAQAIISYKPLERLVNMPFSMWDYFDFLDLGMFYEDVMVGMILREKVVYRNLISVDTKACRFHNAGPGSVRKYISNKSVVIHHVSEEHYNELFDIFPVGEGGDKPSAVRWLYPGSGTLPCFQH
Protein: Killer cell lectin-like receptor, subfamily A, member 17 (Lectin-like transmembrane protein) (NK receptor Ly-49Q) (Q9JMA4)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MSEQEVTYSTVRFHKSSGLQNQVRPEDNQGSREAGHKECSIPWHLIVIAFGILCVLLLVIVAVLVTNILQYKQEKHELQETLNCHHNCSTMQNDINAKEEMLRNMPLECSTGDDLLKSLNREQKRWYSETKSVLNSSKHPGGSLEIHWFCYGIKCYYFIMNKKGWRKCKQICEHYSLSLLKIDAEDELKFLQLQVTPDSYWIGFSFDKKSEKWTWIENGTSKYALNMSTYNVKSGECVFLSKTRLENNKCEHVYPCICEKRLDKFPDSLPNNS
Protein: Putative secreted frizzled related protein (Q80W55)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
KTIYKLNGVSDRDLKKSVLWLKDSLQCTCEEMNDINAPYLVMGQKQGGELVITSVKRWQKGQREFKRISRSIRKLQC
Protein: 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) (P41572)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- Glucose-6-phosphate 1-dehydrogenase
- Probable 6-phosphogluconolactonase
- ribose-5-phosphate isomerase
- Probable transaldolase
- Ribulose-phosphate 3-epimerase
- transketolase
- transketolase
- mannose-6-phosphate isomerase
- Isocitrate dehydrogenase
Sequence:
MSGQADIALIGLAVMGQNLILNMDEKGFVVCAYNRTVAKVKEFLANEAKDTKVIGADSLEDMVSKLKSPRKVMLLVKAGSAVDDFIQQLVPLLSAGDVIIDGGNSEYQDTSRRCDELAKLGLLFVGSGVSGGEEGARHGPSLMPGGHEAAWPLIQPIFQAICAKADGEPCCEWVGDGGAGHFVKMVHNGIEYGDMQLICEAYHIMKSLGLSADQMADEFGKWNSAELDSFLIEITRDILKYKDGKGYLLERIRDTAGQKGTGKWTAIAALQYGVPVTLIGEAVFSRCLSALKDERVQASSVLKGPSTKAQVANLTKFLDDIKHALYCAKIVSYAQGFMLMREAARENKWRLNYGGIALMWRGGCIIRSVFLGNIKDAYTSQPELSNLLLDDFFKKAIERGQDSWREVVANAFRWGIPVPALSTALSFYDGYRTAKLPANLLQAQRDYFGAHTYELLGQEGQFHHTNWTGTGGNVSASTYQA
Protein: Diaminohydroxyphosphoribosylamino-pyrimidine deaminase (DRAP deaminase) (EC 3.5.4.26) (Riboflavin-specific deaminase) (P87241)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in riboflavin biosynthesis. Converts 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1H,3H)-pyrimidinedione 5'-phosphate (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 2,5-diamino-6-ribosylamino-4
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- 6,7-dimethyl-8-ribityllumazine synthase
- Probable GTP cyclohydrolase-2
- Riboflavin synthase
- Pseudouridylate synthase C18B11.02c
- Guanylate kinase
- Elongation factor 2
- WW domain-containing protein C2F3.14c
- Large ribosomal subunit protein uL5m
Sequence:
MQIPEKYLSSVDNVEEETQILFALSKQKDADLGMLDSKQEQIALTIGNKPIKVKQSLQSLHQSRGSTGSVLWKTSVKVVPWLLQQSWFMNSLTPKTSILELGSGISGLAGILLSPFVGNYVASDKQLYLKKIRENLDQNNASDVEVHELDWKSTPYPKDWTFDFLDYVLFFDCIYNPHLNAHLVSCLASLAERYPGMQCLFAQELRDQETLVDFLERVRPYFEVDLIKMEEINKTSVASSTNLPPANMSLFIMKPYNHEEYMLKALNEAKKCEPTDSAFCVGAVIVQNGKIVSTGYSRERPGNTHAEECAIEKFMLKNPTDSLEGAIMYSTMEPCSKRLSKKVSCTDLIVKQKFSTVVLGSLEPDIFVKCEGVDLLKKAGIVVIEKLTFQDDCLREAVRGHPPKH
Protein: Sulfotransferase (EC 2.8.2.-) (D3YVV6)
Organism: Mus musculus (Mouse)
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
Sequence:
MARWPAPPPPPPPPPPLAAPPLLPGASTKGPPARKLLFMCTLSLSVTYLCYSLLGGSGSLQFPLALQEPPGSAAEPPPSLLSPSLPPPRVRPGASSPPPDNASRGPPPEPPERFTTPAADGWGLASGGGARDAWPRSPPAPGDAVTEQDALLGRGAQEPGAAEELEGRRAANGSAERGPASTPDYGEKKLPQALIIGVKKGGTRALLEAIRVHPDVRAVGVEPHFFDRNYEKGLEWYRNVMPKTLDGQITMEKTPSYFVTNEAPKRIHSMAKDIKLIVVVRNPVTRAISDYTQTLSKKPEIPTFEVLAFKNRTLGLIDASWSAIRIGIYALHLENWLQYFPLSQILFVSGERLIVDPAGEMAKVQDFLGLKRVVTEKHFYFNKTKGFPCLKKPEDSSAPRCLGKSKGRTHPRIDPDVIHRLRKFYKPFNMMFYQMTGQDFQWEQEEGDK
Protein: Acyl-CoA-binding domain 3 (B3H4G6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEVFLEMLLTAVVALLFSFLLAKLVSVATVENDLSSDQPLKPEIGVGVTEDVRFGMKMDARVLESQRNFQVVDENVELVDRFLSEEADRVYEVDEAVTGNAKICGDREAESSAAASSENYVIAEEVILVRGQDEQSDSAEAESISSVSPENVVAEEIKSQGQEEVTELGRSGCVENEESGGDVLVAESEEVRVEKSSNMVEESDAEAENEEKTELTIEEDDDWEGIERSELEKAFAAAVNLLEESGKAEEIGAEAKMELFGLHKIATEGSCREAQPMAVMISARAKWNAWQKLGNMSQEEAMEQYLALVSKEIPGLTKAGHTVGKMSEMETSVGLPPNSGSLEDPTNLVTTGVDESSKNEIVSGER