wanglab/gogpt-training-data huggingface dataset:
Protein: Dicarboxylate carrier 2 (FI11326p) (Q9VDM3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- GH17939p
- GH20441p
- GH07855p
- GH06435p
- GTP-binding nuclear protein Ran-like
- AT18965p
- GH26094p
- GH27720p
- GH14622p
- Sex-regulated protein janus-B
Sequence:
MSLRRGGLMSYNQRRIARWYFGGLASSMAAMVTHPIDLIKVLIQTQAEKLSVFQTTRKIVKEQGPLAMYNGISASMLRQYTYTLARFGIYSVGSGAMDTSTMAGKTCLAAIAGGIGGFVGAPADLINVRLQNDVKLPPEKRRNYKHAIDGLVRITREEGWKNLFNGSSMIALRGAFMTVGQIAFYEQSKSQMIKLGMPDYMGTYILASMISSVVATTLTQPIDVVKTRRMNAAPGEYSGLGDVFVKTSKEGPLAFFKGYVPSLSRLLPHTVLLFLGLEYLRTHFGYLPEPKQTGAFYRYDDVDD
Protein: Dihydropteridine reductase (EC 1.5.1.34) (Qdprb1 protein) (Q66IB5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAATDAQKVIVYGGKGALGSACVQYFKAKHWWVASIDLSANEEANANVTVKMTESFTEQANQVTADVGDLLGEEKVDAIFCVAGGWAGGSAKAKTLFKNADLMWKQSVWTSTICSHLATKHLREGGLLTLAGAKAALGPTAGCIGYGMAKASVHQLCQSLSAPNSGLPPGSAAVAILPVTLDTPMNRKFMPDADVSCWTPLEYITELFYKWTTGESRPPSGTLMQLVTADGKTEATPML
Protein: UMP-CMP kinase (EC 2.7.4.14) (Deoxycytidylate kinase) (CK) (dCMP kinase) (Nucleoside-diphosphate kinase) (EC 2.7.4.6) (Uridine monophosphate/cytidine monophosphate kinase) (UMP/CMP kinase) (UMP/CMPK) (Q4KM73)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}. Note=Predominantly nuclear. {ECO:0000255|HAMAP-Rule:MF_03172}.
Interaction partners:
- UMP-CMP kinase 2, mitochondrial
- Uridine monophosphate synthetase, isoform CRA_a.
- Uridine-cytidine kinase
- Ribonucleoside-diphosphate reductase
- Deoxycytidine kinase
- Uracil phosphoribosyltransferase homolog.
- Uridine-cytidine kinase
- Nucleoside diphosphate kinase A
- Nucleoside diphosphate kinase B
- Nucleoside diphosphate kinase, mitochondrial
Sequence:
MKPLVVFVLGGPGAGKGTQCARIVEKYGYTHLSAGELLRDERKNPDSQYGELIEKYIKEGKIVPVEITISLLKREMDQTMAANAQKNKFLIDGFPRNQDNLQGWNKTMDGKADVSFVLFFDCNNEICIDRCLERGKSSGRSDDNRESLEKRIQTYLESTKPIIDLYEEMGKVKKIDASKSVDEVFGDVMKIFDKEG
Protein: Peregrinol diphosphate synthase TPS1, chloroplastic (EC 4.2.1.174) (Terpene synthase 1) (VacTPS1) (A0A2K9RFZ7)
Organism: Vitex agnus-castus (Chaste tree)
Function: Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle disorders (e.g. premenstrual syndrome and mastodynia) (Probable). Terpene synthase that produces peregrinol diphosphate from geranylgeranyl diphosphate (GGPP).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MASLSTPNINNTTFVNSKTQLPAVKVHLQKCYVGPWLNRGSKHMFTNYQFGHRQISKVAKYQASPDVVQVCDKVEHSTAQSFELVDKKIEDNIRYVKELLNSIDDGHISVSAYDTAWFALIRDLDGRDCPQFPSTIEWIADNQLADGSWGDEDFYSAYDRLINTLACVLALRTWNVHPEKSEKGISYIKENLHELEDAEAENMTCAFELLFPVLLKRAENLGINEIPYDAPIIKEIYNIRDTKLTRIPLEVLHERSTSILYGMEGLENLDLDWQKLMKLQTPEGSFLTSPAATAFAFMYTKDENCLKYIKYILDKFNGAAVDVYPVDLFARLWAVDRLQRLGISRFFESEIKDCLSYVHRFWTEKGIFSGRHALFHDLDDTSMGFRLLRQHGYDMDPNVFKHFQKDGRFHCLGGDMSDSLTVTYNLYRASQTQFPGEEILEEARNFCYNFLQDRAARNQLVDKWVISKHLADEMRTGLQLPWYASLPRVEARYYLQHYAGSGDVWLGKNFFRMEDISNDKYKEIAKLDFSRCQAQHQFEWTYMQGWYESSNVQEFGISRKDLLVAYFLAAATIFERERTKERIVWAKSHIVSRMIKSFFTNETTSLEEKVALLTGFEDNINGLHKITSAKREHEHVDILLATLHQLLGEFDEYASHQLKNAWRVWLTKLEQGEAGAEAELLVTTLNICAGHDIAFKEDILSQNEYKTLSNLTNKICQQLTQIQNKKVMETNDSNSIQDKEIEHDMQALVKSVLEEAVGIDRNIKQTFLSVAKTYYYGAYIAAETIDVHIFKVLFEPVI
Protein: tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (Pombe glycoprotease 2) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein kae1) (tRNA threonylcarbamoyladenosine biosynthesis protein kae1) (O94637)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Pgp2 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000269|PubMed:16823372}.
Interaction partners:
- EKC/KEOPS complex subunit SPAP27G11.07c
- EKC/KEOPS complex subunit SPAC4H3.13
- EKC/KEOPS complex subunit cgi121
- Threonylcarbamoyl-AMP synthase
- EKC/KEOPS complex subunit gon7
Sequence:
MGKPLIALGLEGSANKLGVGIILHDTNGSAKILANVRHTYITPPGQGFLPSDTAKHHRAWIIPLIKQAFAEAKISFKDIDCICFTKGPGIGAPLNSVALCARMLSLIHKKPLVAVNHCIGHIEMGREITGAQNPVVLYVSGGNTQVIAYSEKKYRIFGETLDIAIGNCLDRFARIIGLSNAPSPGYNIMQEAKKGKRFIELPYTVKGMDCSFSGLLSGVEAAATELLDPKNPSSVTKQDLCYSLQETGFAMLVEITERAMAHIRADSVLIVGGVGCNERLQQMMAEMSSDRGADVFSTDERFCIDNGIMIAQAGLLAYKTGDRCAVAESTITQRYRTDDVYISWRD
Protein: 26S proteasome non-ATPase regulatory subunit 2 (Q54BC6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 7
Sequence:
MPQKEVTIPVPAKGGSNKEEDKKDNKDTEEKNTTTNTTTKDNKKDKKKDKKEETLSPEDEKLKNDLELLVERSRDEKEEIALAALEALKTEIRSSTSSMTSVPKPLKFLRNHYSTLVDIYKNSKEGKAKTSLADILSVLAMANGNDERDTLKYKLLGSGEAIASWGHEYVKHLATEIGVEYDIKKEENQSVEDLLKLVDEIVPFQMTHNAEPEACDLLLEVEQLSKIFQYIDENNYSRVCLYLFKCSYYVPGPDDINILKVCVEIYIKMKQYPDALRVAMKISDPELITEIFKLVENNKSILQQLGFLVARQKIVPDNFNYDSISDIINNSKLSEYFMNLATDLDIREPKLPEEIFQSHLDSTSAIADSARMNLASSFVNAFVNAGFGKDKLMTAEEDTKWWFKNRELGILSTVASTGMVVLWDIDGGLTKIDKFLYSQEKHCSNGALMAIGMLTSGIRSEMDPALSLLAEHINSSNTGTRISAIFGLGLAYAGTQRQDLMSLLSPCLDDDKEKMEFIGIVGLALGLIFIGSCDPELSTLFVQTLIQRGTAASESHARFLHLGLGLLYLGKQDAAELALETLKAIEGKGGEYARLTVEACAYAGTGNVLKVQNMLHFCSDGQENPHHGLAVLSIALIAMGEELGSDMCLRMFDHLLQKGNVHIKRAIPLALGLLSPSNPRIAIMDILSKLSHDNDPEVAQGAILSLGLIGAGTNNARIGGMLRALAVFYGKDVHLFFVRIAQGLLHLGKGTMTINPYHSDRTLMSPVAVGGLLALLHAGLDIKNILSTQSHYLFFSIVCSMYPRMLMTLDEDLKPLPVSVRVGQSVDIVGLAGKPKTITGFQTHTTPVLLGYNERAELATDDYIPLTNILEGIVILKPNPNASVTSPLASKKN
Protein: Sphingosine kinase 1 (EC 2.7.1.91) (Q8L7L1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the production of sphingolipid metabolites. Phosphorylates sphingosine and various sphingoid long-chain base (LCB) products, such as phytosphingosine (PHS, 4-hydroxysphinganine), 4-hydroxy-8-sphingenine, 4,8-sphingadienine, D-erythro-dihydrosphingosine and D,L-threo-dihydrosphingosine. Is required for abscisic acid (ABA) signaling that mediates stomatal closure, inhibition of seed germination and root elongation. May function upstream of PLDALPHA1 and phosphatidic acid (PA) in an amplification response to ABA that mediates stomatal closure.
Subcellular location: Vacuole membrane {ECO:0000305|PubMed:18643979, ECO:0000305|PubMed:21330371}; Peripheral membrane protein {ECO:0000305|PubMed:18643979, ECO:0000305|PubMed:21330371}. Note=Associated with the tonoplast.
Interaction partners:
- Sphingosine-1-phosphate lyase
- Alkaline ceramidase
- Neutral ceramidase 1
- Sphinganine C4-monooxygenase 2
- Sphinganine C4-monooxygenase 1
- 3-dehydrosphinganine reductase TSC10B
- 3-dehydrosphinganine reductase TSC10A
- Neutral ceramidase 3
- Neutral ceramidase 2
- Sphingolipid delta
Sequence:
MDRQPERENDELPSPAIISDRVLVNGVVTPLTLTAEGELRSTESGRRKSTLAKEILSFVVEGNKVRVKTLVEKGGGICCRGSAGDYARNDFVFEPLSDESRKLWSDKFHQHLVSLGRPKKLLVFVNPFGGKKTARKIFQEEVKPLFEDANIQLEIQETKYQLHAKEIVRSMDVSKYDGIVCVSGDGILVEVVNGLLEREDWKTAIKLPIGMVPAGSGNGMIKSLLEPVGLPCSATSATISIIRGRTRSLDVATISQGTTKFFSVLMLAWGLVADIDIESEKFRWMGSARFDIYGLQRIICLRQYHGRILFVPAPGFESYGQRASCSIDKEPSGSDKTLVYQGPDSKLENLDWREMKGPFVSVWLHNVPWGAENTLAAPDAKFSDGFLDLIVMKDCPKLALLSLMTKLSDGTHVQSPYASYLKVKAFVLEPGARIDEPDKEGIIDSDGEVLARGRKSYKCDQKALMSYDKLQISVDQGLATLFSPE
Protein: Peroxisomal targeting signal receptor (PTS1 receptor) (PTS1R) (Peroxin-5) (O94325)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35056}. Peroxisome matrix {ECO:0000250|UniProtKB:P35056}. Note=Cycles between the cytosol and the peroxisome matrix. Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins. Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol. Cys-7 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (By similarity). The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzyme UBP15, resetting PEX5 for a subsequent import cycle (By similarity). {ECO:0000250|UniProtKB:P35056, ECO:0000250|UniProtKB:P50542}.
Interaction partners:
- Peroxisomal targeting signal 2 receptor
- Peroxisomal membrane protein pex14
- Peroxisomal membrane protein pex13
- Peroxisome assembly protein 12
- Peroxisomal ATPase pex6
- Probable proteasome subunit beta type-5
- Serine/threonine-protein kinase tel1
- Peroxisomal biogenesis factor 11
- Peroxisome biogenesis factor 10
- 2-hydroxyacyl-CoA lyase
Sequence:
MSVEAGCSTLSNPLKKLTSTAVVNNSTPSAQYRKHLTKSQSRTYAPLQTLSEDQFTSFKNLQGNNSPLGNVVKNPVSLKTGNHTGTTTRGGSKENWVHSFSSLQQQNSKSAWTSEFSEVFLNSSENDRFRNLNQPLKQSFFGSAGLNLSSNTEIPLQSSLAIDETELAKKFEEASQISNKLEKEKDATGSKSIEELWEEHQKQLKNAGLEPASLEEYQKQWEDFLKSNNISDDPYTSSVNSFANDNLAHNKNIDPQIFQHSDTDNVVENSLQTEDVYSQNQDESSEVVKELNGIDPFVEAMNLIKNGGSISKAAVLLEQSVKENPQHFEAWKWLGRIHTLLGNESRVVEALLEAVKLDSTNLDLMMDLAVSYVNQSLNVQALVCLEDWIVNSFPQYRNRFAKINERFEEKDSANDLLKMQMYFLDVAYELSLAKKRSSKVQAGLGIIMYMLKEYERSADCFRQALQDEPSNEILWNKLGAALTNAEKNTEAVSSYNRAVSLQPQYVRVRSNMAVSNINLGYFEDAAKHLLAAIDIIQNSSTSMESCESNEELWEMLRKVFLIGFQSTDLASQSYPGANTSYIRAQLSDLQGWPGVELE
Protein: Septin (C8VAK9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Septin
- Septin-type G domain-containing protein
- Septin B
- Septin
Sequence:
MAATATRPRTPGRGQAPIDPPPVPSENGHSQTKDSSRRTSSSLGFLRRSKSTEPIGSKPRGKKMSKAQMEEELRRQREARPKQPPRLPDFSPPPVIETFGGDETRNGVADVTSPLSPSQSRPSRSAMSTPVPPDYSDPYARTESMTHRGRYSYASSYVSTVNNPRRLRRRKDPTPYNILVIGARNSGKTSFLNFLRKSLALPPHKHPSRAPDEVEYDSHNPASEGYTSHYLETEIDGERVGLTLWDSQGLEKNVVDIQLRGVTGFLESKFEETLNEEMKVVRSPGARDTHIHCTFLILDPSRLDENIAAAERAAQGTPRASDSKVLGVLDENFDLQVLRTVIGKTTVVPVISKADTITTAHMAYLRKAVWDSLKKANIDPLEILTLEDQEEYTSSEGEDEEDGETSEAEDAAGETEGGHTKEETEPKAPESPTQRSEGSQQDVGSQAVPLLPFSILSPDKYSLQGDGPIGRKFPWGFADPYNPEHCDFLKLKDSVFSEWRSELREASRVIWYERWRTSRLNRHDAIASPKPRSFGGRTGPDFARRPSGLKHAQNGCHCHIPVSLARPVSFGVPRCQSNWKLSELTVG
Protein: DNA polymerase epsilon catalytic subunit A (EC 2.7.7.7) (DNA polymerase II subunit A) (Q6FNY7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: DNA polymerase II participates in chromosomal DNA replication.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA polymerase epsilon subunit D
- DNA polymerase epsilon subunit B
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM5
- DNA polymerase epsilon subunit C
- DNA polymerase
- DNA replication licensing factor MCM4
- Candida glabrata strain CBS138 chromosome M complete sequence
- DNA replication licensing factor MCM3
- DNA polymerase alpha subunit B
Sequence:
MSTARFKRGNGQAGSLSNGYAVTAQQLLQAAKVDDIDAMMGFERYVPPQYNGRVDPDRLDQVPGRTGWLVNMHPTLISEEIASGGGSDYNPSAAGIAGVDFYFLDEEGGSFKSSITYDPYFFVTVTDDARLNDVEEFLKKYLETCLKDISTLKKEDLKLDNHLLGLQKSLIKLSFVNSNQLFEARKLLRPILAENESNKQQRNVFKHSNISNGNGMLSSNVNRFASSSVQDKKDAKQYIEDIREYDVPYHVRVSIDKDIRVGKWYKVTHEGFFVWPDKVAFADPVVLAFDIETTKAPLKFPEASVDQVMMISYMIDGDGFLITNREIISEDIEDFEYTPKPELQGHVTIFNEVDELAVLQRFFEHIRDVRPTVISTFNGDFFDWPFIEKRASVRGLDMFEEIGFAPDSEGEYKSSYCVHMDCFRWVKRDSYLPQGSQGLKAVTQAKLGYNPIELDPELMTPYAYERPQQLSEYSVSDAVATYYLYMKYVHPFIFSLCTIIPLNPDEVLRKGTGTLCEMLLMVQAYQGNILLPNKHTDPLERFYDGHLLESETYVGGHVESLEAGVFRSDLATEFKIDTSAIDELIEDLPHALKFAVEVENKAKMEDVTNFEEIKEQIKEQLLELKENNKRHEKPLIYHVDVASMYPNIMTTNRLQPDSIKTEKDCASCDFNRPGKSCARRLKWAWRGEFYPAKSDEYNMIKRALQNETFPNKNKFSKKPYLTFDELSYSEQVAHIKKRLTEYSKKVYHRIKVSEIVEREAIVCQRENPFYVNTVKSFRDRRYEFKGLAKKWKGKMSSIDRNDKHGKDEANKMVVLYDSLQLAHKVILNSFYGYVMRKGSRWYSMEMAGITCLTGATIIQMARALVERVGRPLELDTDGIWCILPKSFPENFFLKLENGKKLFVSYPCSMLNYRVHQKFTNHQYQELVDPVKHKYETHSENTIFFEVDGPYKAMILPTSKEEGKGIKKRYAVFNEDGSLAELKGFELKRRGELQLIKNFQSDIFKVFLDGKTLEECYASVAAVSNRWLDILDNKGSMLEDEDLVSLICENRSMSKSLKEYEGQKSTSITTAKRLGEFLGEDMVKDKGLQCKYIISSKPHGAPVTERAIPVAIFSSDINVKRSFLRRWTMDHSLDNFDIRTILDWGYYRERLASVIQKIITIPAALQNVPNPVPRVEHPDWLKRRIAVKEDKFKQSKLERFLSKSSQEPQNRRIKDIEELFHEDDDIKRIKLAKVTSRNKNKRNRDVQKNDEESLVLPATMPSMEEDYVSWLSYQKIKWKIQRRDRIRRTQLFGKSGETNSRSVLGSMIRKQAEMFANGSWEVLQYRDNYEAGAVDAYVIINGKVQVLKIYVPRTLYINFKTDSVPLKKIKNCEVERSNAILPNDARINNDSASPLFKLTLSEQVYLDELEDSGSVLNDESVLGIYESHISPAQKALMDLGTTISFKSKKVGSLGKSLQDGFHLKDLTSVGNDRYLSHFDLNVCYLLHIDTNIDYEFFVIFRSWENKLSIFVKKPSNNAQELLESTIIGIFKEQYHKRKDRITKFNKYINLSDNVDMNSNHYTDKKKLFKAINQEFAMIKEQKGQQVLLLMQSPFPSLIKKNIRYSTQIPIIELSMNILALPQLNWQNVMINKLCSYIISTSYWVSHLVSLSQHSNVPICNINLEKMDFVIDVIYARRLKLDNIILWWNEQSPLPDHGGMENDFDQNTSWIMNDLDFPNINVPDVYDNVVLEVSIENLVVNTILCSTLINEAEGSDLVDMNTVDVSDKPVGNNQGIVQDSFSHDALAVLKSLLKEWWDRALEKNITADLLVNSLVSWVYSTDSKLFDGSLRYHIHNLTKKSLFQLMNEFNELGSFIVSADRNRLLIKTNKISPETCYAYSHYMIKSIRSNPMFTYLDLNIERYWDLLIWMDKYNFSGLSCSQIEEREKQDYTAYSNWQIKYYLPRIYQSEFEDWAMIILDSMVKTKRAFLESSYGTQRATQIVTGLTPQSDTEDISPLSSFSKEIGKPLLQRVNKLFRNQREFILDPGFSEDYAFPILPGSHIKMDDPLLEFIKSLFQILLLSKSTTLEVRQLRKEVLKFLEIREFAKEAEFQNPSDSLVINGILCEYCSYVSDLDLCRDGLDGKFQCPRCDKSINDSLLQEHMIQNLAIEYQTYITQDLRCEKCHTVKRDLMSTNCNCSGNWVCTTKPEKLSNIVKIYKQVAEFYNYSLVKNALESLY
Protein: Iron stress-induced chlorophyll-binding protein (CP43') (Q55274)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Functions as an antenna for photosystem I (PSI) under iron-limiting conditions, when phycobilisomes disappear. In the (PSI)3(Isi3)18 complex most of the harvested energy is probably used by PSI; in other PSI-containing supercomplexes a large part of the energy will probably not be used for light harvesting, but rather is dissipated to protect the organism from light damage.
Subcellular location: Cellular thylakoid membrane {ECO:0000269|PubMed:14556907, ECO:0000269|PubMed:16086587}; Multi-pass membrane protein {ECO:0000269|PubMed:14556907, ECO:0000269|PubMed:16086587}.
Interaction partners:
- Photosystem I iron-sulfur center
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I reaction center subunit III
- Photosystem I reaction center subunit XI
- Photosystem I reaction center subunit II
- Photosystem I reaction center subunit IX
- Photosystem I reaction center subunit VIII
- Photosystem I reaction center subunit IV
- Photosystem I reaction center subunit PsaK 1
Sequence:
MQTYGNDTVQYEWWAGNARFADQSGLFIAAHVAQAALTAFWAGAFTLFEISRFDPTQAMGDQGLILLPHLATLGWGVGDGGQIVDTYPYFVIGSIHLIASAVLGAGALFHTLRAPADLSTLKGQGKKFHFTWENPQQLGIILGHHLLFLGAGALLLAGKAMYWGGLYDATTQTVRLVSQPTLDPLVIYGYQTHFASISSLEDLVGGHIFVGFLLIGGGIWHILVPPLGWAKKVLLFSGEAILSYSLGGIALAGFVAAYFCAVNTLAYPPEFYGPPLAIKLGIFPYFADTVELPMHAHTSRAWLANAHFFLAFFFLQGHLWHALRALGFDFKRVEQAFDSLQT
Protein: Nucleoprotein (Nucleocapsid protein) (NC) (Protein N) (P59595)
Organism: Severe acute respiratory syndrome coronavirus (SARS-CoV)
Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. May modulate transforming growth factor-beta signaling by binding host SMAD3.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170, ECO:0000269|PubMed:19106108}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:17210170}. Host nucleus {ECO:0000269|PubMed:18155731}. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. {ECO:0000255|HAMAP-Rule:MF_04096}.
Interaction partners:
Sequence:
MSDNGPQSNQRSAPRITFGGPTDSTDNNQNGGRNGARPKQRRPQGLPNNTASWFTALTQHGKEELRFPRGQGVPINTNSGPDDQIGYYRRATRRVRGGDGKMKELSPRWYFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLNQLESKVSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPKKDKKKKTDEAQPLPQRQKKQPTVTLLPAADMDDFSRQLQNSMSGASADSTQA
Protein: Regulatory protein E2 (P03122)
Organism: Bovine papillomavirus type 1
Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:17189189}. Note=Colocalizes with DDX11 at early stages of mitosis.
Interaction partners:
Sequence:
METACERLHVAQETQMQLIEKSSDKLQDHILYWTAVRTENTLLYAARKKGVTVLGHCRVPHSVVCQERAKQAIEMQLSLQELSKTEFGDEPWSLLDTSWDRYMSEPKRCFKKGARVVEVEFDGNASNTNWYTVYSNLYMRTEDGWQLAKAGADGTGLYYCTMAGAGRIYYSRFGDEAARFSTTGHYSVRDQDRVYAGVSSTSSDFRDRPDGVWVASEGPEGDPAGKEAEPAQPVSSLLGSPACGPIRAGLGWVRDGPRSHPYNFPAGSGGSILRSSSTPVQGTVPVDLASRQEEEEQSPDSTEEEPVTLPRRTTNDGFHLLKAGGSCFALISGTANQVKCYRFRVKKNHRHRYENCTTTWFTVADNGAERQGQAQILITFGSPSQRQDFLKHVPLPPGMNISGFTASLDF
Protein: Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.3) (EC 2.7.4.4) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) (P05081)
Organism: Gallus gallus (Chicken)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Exhibits nucleoside diphosphate kinase catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor (By similarity). Also catalyzes at a very low rate the synthesis of thiamine triphosphate (ThTP) from thiamine diphosphate (ThDP) and ADP.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:2229026}.
Interaction partners:
- Uncharacterized protein.
- Adenylate kinase 7.
- Pribosyltran domain-containing protein.
- Adenylosuccinate lyase
- Adenylate kinase 4
- Thiamine pyrophosphokinase
- Pyruvate kinase PKM
- Adenosine kinase
- Uncharacterized protein
- Adenylate kinase isoenzyme 6
Sequence:
MSTEKLKHHKIIFVVGGPGSGKGTQCEKIVHKYGYTHLSTGDLLRAEVSSGSERGKKLQAIMEKGELVPLDTVLDMLRDAMLAKADTSKGFLIDGYPREVKQGEEFEKKIAPPTLLLYVDAGKETMVKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYKGRGIVRQLNAEGTVDEVFQQVCSYLDKL
Protein: Transcription factor FAMA (Basic helix-loop-helix protein 97) (AtbHLH97) (bHLH 97) (Transcription factor EN 14) (bHLH transcription factor bHLH097) (Q56YJ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator. Together with MYB88 and MYB124, ensures that stomata contain just two guard cells (GCs) by enforcing a single symmetric precursor cell division before stomatal maturity. Together with SPCH and MUTE, regulates the stomata formation. Required to promote differentiation and morphogenesis of stomatal guard cells and to halt proliferative divisions in their immediate precursors. Mediates the formation of stomata. Prevents histone H3K27me3 marks and derepresses stem cell gene expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17088607}.
Interaction partners:
- Transcription factor ICE1
- Transcription factor SCREAM2
- Protein EPIDERMAL PATTERNING FACTOR 1
- Protein EPIDERMAL PATTERNING FACTOR 2
- EPIDERMAL PATTERNING FACTOR-like protein 9
- Retinoblastoma-related protein 1
- LRR receptor-like serine/threonine-protein kinase ERL1
- Transcription factor MYB88
- Probable small nuclear ribonucleoprotein F
- Subtilisin-like protease SBT1.2
Sequence:
MDKDYSAPNFLGESSGGNDDNSSGMIDYMFNRNLQQQQKQSMPQQQQHQLSPSGFGATPFDKMNFSDVMQFADFGSKLALNQTRNQDDQETGIDPVYFLKFPVLNDKIEDHNQTQHLMPSHQTSQEGGECGGNIGNVFLEEKEDQDDDNDNNSVQLRFIGGEEEDRENKNVTKKEVKSKRKRARTSKTSEEVESQRMTHIAVERNRRKQMNEHLRVLRSLMPGSYVQRGDQASIIGGAIEFVRELEQLLQCLESQKRRRILGETGRDMTTTTTSSSSPITTVANQAQPLIITGNVTELEGGGGLREETAENKSCLADVEVKLLGFDAMIKILSRRRPGQLIKTIAALEDLHLSILHTNITTMEQTVLYSFNVKITSETRFTAEDIASSIQQIFSFIHANTNISGSSNLGNIVFT