wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclic AMP-responsive element-binding protein 3-like protein 3 (cAMP-responsive element-binding protein 3-like protein 3) (Transcription factor CREB-H) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 3] (Q91XE9)
Organism: Mus musculus (Mouse)
Function: Transcription factor that may act during endoplasmic reticulum (ER) stress by activating unfolded protein response target genes. Activated in response to cAMP stimulation. Binds to the cAMP response element (CRE). Activates transcription through box-B element (By similarity). Activates transcription through CRE. May function synergistically with ATF6. In acute inflammatory response, may activate expression of acute phase response (APR) genes. May be involved in growth suppression. Regulates FGF21 transcription. Plays a crucial role in the regulation of triglyceride metabolism and is required for the maintenance of normal plasma triglyceride concentrations.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q68CJ9}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q68CJ9}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 3]: Nucleus {ECO:0000250|UniProtKB:Q68CJ9}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. {ECO:0000250}.
Interaction partners:
- Cyclic AMP-responsive element-binding protein 3-like protein 1
- CREB-regulated transcription coactivator 2
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-responsive element-binding protein 3-like protein 2
- Cyclic AMP-dependent transcription factor ATF-6 beta
- Cyclic AMP-responsive element-binding protein 1
- Cyclic AMP-responsive element-binding protein 3
- Cyclic AMP-responsive element-binding protein 3-like protein 4
- Glycogen synthase kinase-3 beta
Sequence:
MDGDIAAGKMASPVCAMAPLDSMEVLDLLFDRQDGILRNVELAEGWILAREEQKVLLNSDSDEFLNCILGPGDSDPSSPLWSPADSDSGISEDLPSDPQDTPPRSGTEPANTVARCHTREQGKGPCPSYLPSTPCPEPPRTQVQESSVAIDLDMWSTDTLYPEEPAGSPSRFNLTVKELLLSGGSGDLQQHSLAASQLLGPGSGHCQELVLTEDEKKLLAKEGVTLPTQLPLTKYEERVLKKIRRKIRNKQSAQESRKKKKEYIDGLENRMSACTAQNQELQRKVLHLEKQNLSLLEQLKHLQALVVQSTSKPAHAGTCIAVLLLSFALIILPSISPFNSNKVDSPGDFVPVRVFSRTLHNHAASRVAPDVTPGSEVPGPWPDVGTPHKGPSSGGLSADWGNFLEIPMLDNLTEELDNSTLVLANSTEDLGRATLLDWVASEPLLSPGRVGLEIPGEMWLSWVPRWLRVRLVQDALGVL
Protein: ESSS subunit of NADH:ubiquinone oxidoreductase (Complex I) protein (Q9SLC8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transmembrane protein
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 10-B
- At1g67350
- NADH dehydrogenase 1 beta subcomplex subunit 9
- 2Fe-2S ferredoxin-like superfamily protein
- NADH dehydrogenase iron-sulfur protein 8-A, mitochondrial
- Excitatory amino acid transporter
- NADH dehydrogenase 1 beta subcomplex subunit 2
- NADH dehydrogenase 1 alpha subcomplex subunit 1
Sequence:
MPSTQSLTVAAKTLRNRIFSRSGSTSAGPSRWATPGHEERPKGYFMNRTPPAPGQSRKWEDWELPCYITSFLTIVILGVGLNAKPDLSIETWAHQKALERLEMEKLATAGDSSD
Protein: 5'-3' exoribonuclease 2 (EC 3.1.13.-) (DHM1-like protein) (DHP protein) (Q9H0D6)
Organism: Homo sapiens (Human)
Function: Possesses 5'->3' exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
Interaction partners:
- Decapping and exoribonuclease protein
- 5'-3' exoribonuclease 1
- ERI1 exoribonuclease 2
- CDKN2A-interacting protein
- m7GpppN-mRNA hydrolase
- Regulation of nuclear pre-mRNA domain-containing protein 1A
- Regulation of nuclear pre-mRNA domain-containing protein 1B
- Probable helicase senataxin
- Superkiller complex protein 2
- CDKN2AIP N-terminal-like protein
Sequence:
MGVPAFFRWLSRKYPSIIVNCVEEKPKECNGVKIPVDASKPNPNDVEFDNLYLDMNGIIHPCTHPEDKPAPKNEDEMMVAIFEYIDRLFSIVRPRRLLYMAIDGVAPRAKMNQQRSRRFRASKEGMEAAVEKQRVREEILAKGGFLPPEEIKERFDSNCITPGTEFMDNLAKCLRYYIADRLNNDPGWKNLTVILSDASAPGEGEHKIMDYIRRQRAQPNHDPNTHHCLCGADADLIMLGLATHEPNFTIIREEFKPNKPKPCGLCNQFGHEVKDCEGLPREKKGKHDELADSLPCAEGEFIFLRLNVLREYLERELTMASLPFTFDVERSIDDWVFMCFFVGNDFLPHLPSLEIRENAIDRLVNIYKNVVHKTGGYLTESGYVNLQRVQMIMLAVGEVEDSIFKKRKDDEDSFRRRQKEKRKRMKRDQPAFTPSGILTPHALGSRNSPGSQVASNPRQAAYEMRMQNNSSPSISPNTSFTSDGSPSPLGGIKRKAEDSDSEPEPEDNVRLWEAGWKQRYYKNKFDVDAADEKFRRKVVQSYVEGLCWVLRYYYQGCASWKWYYPFHYAPFASDFEGIADMPSDFEKGTKPFKPLEQLMGVFPAASGNFLPPSWRKLMSDPDSSIIDFYPEDFAIDLNGKKYAWQGVALLPFVDERRLRAALEEVYPDLTPEETRRNSLGGDVLFVGKHHPLHDFILELYQTGSTEPVEVPPELCHGIQGKFSLDEEAILPDQIVCSPVPMLRDLTQNTVVSINFKDPQFAEDYIFKAVMLPGARKPAAVLKPSDWEKSSNGRQWKPQLGFNRDRRPVHLDQAAFRTLGHVMPRGSGTGIYSNAAPPPVTYQGNLYRPLLRGQAQIPKLMSNMRPQDSWRGPPPLFQQQRFDRGVGAEPLLPWNRMLQTQNAAFQPNQYQMLAGPGGYPPRRDDRGGRQGYPREGRKYPLPPPSGRYNWN
Protein: Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53) (P62143)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62140}. Nucleus {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62140}. Note=Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. {ECO:0000250|UniProtKB:P62140}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- WD repeat-containing protein 82
- Retinoblastoma-associated protein
- Serine/threonine-protein phosphatase
- Protein phosphatase 1 regulatory subunit 3A
- Myosin light chain 9
- Protein phosphatase 1 regulatory subunit 3E
- Protein phosphatase 1 regulatory subunit 3C
- Protein phosphatase 1 regulatory subunit
Sequence:
MADGELNVDSLITRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRTANPPKKR
Protein: Isocitrate lyase (ICL) (Isocitrase) (Isocitratase) (EC 4.1.3.1) (Methylisocitrate lyase) (MICA) (EC 4.1.3.30) (Threo-D(S)-isocitrate glyoxylate-lyase) (Q6T267)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2-methylisocitrate.
Subcellular location: Glyoxysome {ECO:0000250|UniProtKB:P28299}.
Interaction partners:
- Malate synthase
- Aconitate hydratase, mitochondrial
- alanine--glyoxylate transaminase
- FMN-dependent dehydrogenase family protein
- Hydroxyisocaproate dehydrogenase, putative
- Glyoxylate reductase
- D-isomer specific 2-hydroxyacid dehydrogenase family protein
- methylisocitrate lyase
- Dihydrodipicolinate synthetase family protein
- Dihydrodipicolinate synthetase family protein
Sequence:
MGFLEDEDQKYWDDVQAVKAWWKDSRWRYTKRPYTAEQIVAKRGNLKIHYPSNDQSKKLWKILESNFEKKVASFTYGCLEPTMLTQMAKYLDTVYVSGWQSSSTASSTDEPSPDLADYPMNTVPNKVNQLFMAQLFHDRKQREERITTPKDQRSKLPNIDYLRPIIADADTGHGGLTAVMKLTKLFIERGAAGIHIEDQAPGTKKCGHMAGKVLVPISEHINRLVAIRAQADIMGTDLLAIARTDSEAATLITSTIDHRDHAFIVGSTNPNLQPLNDLMLAGEQAGKTGEELQAIEDQWIAQAGLKLFDDAVVDTIKAGVHVNKDALIKEYLTAAKGKSNSEARAIAKGITGVDIYWDWDAPRTREGYYRYQGGTQCAINRAVAYAPFADLIWMESKLPDYAQAKEFADGVHAVWPEQKLAYNLSPSFNWKKAMPREEQETYIKRLGALGYAWQFITLAGLHTTALISDQFARAYAKQGMRAYGELVQEPEMEQGVDVVTHQKWSGANYVDNMLKMLTGGVSSTAAMGKGVTEDQFKH
Protein: Cytochrome b6-f complex subunit 4 (17 kDa polypeptide) (P27589)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01344}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01344}.
Interaction partners:
- Cytochrome b6-f complex iron-sulfur subunit 2
- Cytochrome b6
- Cytochrome f
- Cytochrome b6-f complex subunit 5
- Cytochrome b6-f complex subunit 7
- Cytochrome b6-f complex subunit 8
- Cytochrome b6-f complex iron-sulfur subunit 1
- Cytochrome b6/f complex iron-sulfur subunit
- Photosystem II D2 protein
- Photosystem I P700 chlorophyll a apoprotein A1
Sequence:
MSIIKKPDLSDPDLRAKLAKGMGHNYYGEPAWPNDILYMFPICILGALGLIAGLAILDPAMIGEPADPFATPLEILPEWYLYPTFQILRILPNKLLGIAGMAAIPLGLMLVPFIESVNKFQNPFRRPIAMTVFLFGTAAALWLGAGATFPIDKSLTLGLF
Protein: Augurin-A (Esophageal cancer-related gene 4-A protein homolog) (Q566V9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Probable hormone (By similarity). Required for the proper formation of the central nervous system by attenuating cell proliferation during development.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9H1Z8}. Cytoplasm {ECO:0000250|UniProtKB:Q9H1Z8}. Apical cell membrane {ECO:0000250|UniProtKB:Q9H1Z8}.
Interaction partners:
Sequence:
MLSEKFHLRLLTLLTLLTALSLTDVASESKLEKLLMKRVDRDVKPAAAVAVSPSKAKEFLTSLKRPKRNLWDRSRPDVQQWIQQFMYMGFDEARLETDLAYWMDQHRSSDQGRQHHYDENAALGPRGAASYRHGANVNYDYY
Protein: 26S proteasome regulatory subunit RPN12 (Nuclear integrity protein 1) (P32496)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase.
Interaction partners:
- 26S proteasome regulatory subunit RPN9
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit RPN7
- Proteasome subunit beta type-5
- 26S proteasome regulatory subunit RPN13
- 26S proteasome regulatory subunit 4 homolog
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-2
- Proteasome subunit beta type-1
- 26S proteasome regulatory subunit 8 homolog
Sequence:
MPSLAELTKSLSIAFENGDYAACEKLLPPIKIELIKNNLLIPDLSIQNDIYLNDLMITKRILEVGALASIQTFNFDSFENYFNQLKPYYFSNNHKLSESDKKSKLISLYLLNLLSQNNTTKFHSELQYLDKHIKNLEDDSLLSYPIKLDRWLMEGSYQKAWDLLQSGSQNISEFDSFTDILKSAIRDEIAKNTELSYDFLPLSNIKALLFFNNEKETEKFALERNWPIVNSKVYFNNQSKEKADYEDEMMHEEDQKTNIIEKAMDYAISIENIV
Protein: BTB/POZ and TAZ domain-containing protein 1 (BTB and TAZ domain protein 1) (Q9FMK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Also targeted for degradation by the 26S proteasome pathway. May be involved in gametophyte development.
Subcellular location: Nucleus. Cytoplasm.
Interaction partners:
- GDSL esterase/lipase At5g45920
- Early nodulin-like protein 16
Sequence:
MAITATQNDGVSLNANKISYDLVETDVEIITSGRRSIPAHSGILASVSPVLTNIIEKPRKIHGGSSKKVIKILGVPCDAVSVFVRFLYSPSVTENEMEKYGIHLLALSHVYMVTQLKQRCTKGVGERVTAENVVDILQLARLCDAPDLCLKCMRFIHYKFKTVEQTEGWKFLQEHDPFLELDILQFIDDAESRKKRRRRHRREQNLYLQLSEAMECIEHICTEGCTLVGPSSNLDNKSTCQAKPGPCSAFSTCYGLQLLIRHFAVCKKRVDGKGCVRCKRMIQLLRLHSSICDQSESCRVPLCRQYKNRGEKDKKMVEDTKWKVLVRRVASAKAMSSLSQSKKKKSEVLFKEEAEDLIRIRNKLM
Protein: Probable ATP-dependent helicase Lhr (Large helicase-related protein) (P96901)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Endonuclease 8 2 lyase Nei 2)
- Endonuclease 8 1 lyase Nei 1)
- Probable transcriptional regulatory protein
- Conserved protein
- DNA repair protein RadA
- Putative bifunctional exonuclease/endonuclease protein Rv2191
- Conserved ala-, pro-rich protein
- Putative cytochrome P450 139
Sequence:
MRFAQPSALSRFSALTRDWFTSTFAAPTAAQASAWAAIADGDNTLVIAPTGSGKTLAAFLWALDSLAGSEPMSERPAATRVLYVSPLKALAVDVERNLRTPLAGLTRLAERQGLPAPQIRVGVRSGDTPPALRRQLVSQPPDVLITTPESLFLMLTSAARQTLTGVQTVIIDEIHAIAATKRGAHLALSLERLDDLSSRRRAQRIGLSATVRPPEELARFLSGQSPTTIVAPPAAKTVELSVQVPVPDMANLTDNTIWPDVEARLVDLIESHNSTIVFANSRRLAERLTARLNEIHAARCGIELAPDTNQQVAGGAPAHIMGSGQTFGAPPVLARAHHGSISKEQRAVVEEDLKRGQLKAVVATSSLELGIDMGAVDLVIQVQAPPSVASGLQRIGRAGHQVGEISRGVLFPKHRTDLLGCAVSVQRMLAGEIETMRVPANPLDILAQHTVAAAALEPLDADAWFDTVRRAAPFATLPRSLFEATLDLLSGKYPSTEFAELRPRLVYDRDTGTLTARPGAQRLAVTSGGAIPDRGLFAVYLATERPSRVGELDEEMVYESRPGDVISLGATSWRITEITHDRVLVIPAPGQPARLPFWRGDDAGRPAELGAALGALTGELAALDRTAFGTRCAGLGFDDYATDNLWRLLDDQRTATAVVPTDSTLLVERFRDELGDWRVILHSPYGLRVHGPLALAVGRRLRDRYGIDEKPTASDNGIVVRLPDTVSAGEDSPPGAELFVFDADEIDPIVTTEVAGSALFASRFRESAARALLLPRRHPGRRSPLWQQRQRAARLLEVARKYPDFPIVLETVRECLQDVYDVPILVELMARIAQRRVRVAEAETAKPSPFAASLLFGYVGAFMYEGDTPLAERRAAALALDGTLLAELLGRVELRELLDPDVIAATSRQLQHLAADRVARDAEGVADLLRLLGPLTEDEIAARAGAPEVSGWLDGLRAAKRALVVSFAGRSWWVAVEDMGRLRDGVGAAVPVGLPASFTEAVADPLGELLGRYARTHTPFTTAAAAARFGLGLRVTADVLGRLASDGRLVRGEFVAAAKGSAGGEQWCDAEVLRILRRRSLAALRAQAEPVSTAAYGRFLPAWQHVSAGNSGIDGLAAVIDQLAGVRIPASAIEPLVLAPRIRDYSPAMLDELLASGDVTWSGAGSISGSDGWIALHPADSAPMTLAEPAEIDFTDAHRAILASLGTGGAYFFRQLTHDGLTEAELKAALWELIWAGRVTGDTFAPVRAVLGGAGTRKRAAPAHGGHRPPRLSRYRLTHAQARNADPTVAGRWSALPLPEPDSTLRAHYQAELLLNRHGVLTKDAVAAEGVAGGFATLYKVLSAFEDAGRCQRGYFIESLGGAQFAVASTVDRLRSYLDGVDPEQPDYHAVVLAAADPANPYGAALPWPASSADGTARPGRKAGALVVLVDGELAWFLERGGRSLLTFTDDPEANHAAAIGLADLVTAGRVASILVERADGMPVLQPGGRASAALTALLAAGFVRTPRGLRRR
Protein: Transporter 1 ATP-binding cassette sub-family B isoform 2 (A0A0S2Z4R8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAELLASAGSACSWDFPRAPPSFPPPAASRGGLGGTRSFRPHRGAESPRPGRDRDGVRVPMASSRCPAPRGCRCLPGASLAWLGTVLLLLADWVLLRTALPRIFSLLVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQAPADAPE
Protein: Bifunctional malic/malolactic enzyme (EC 1.1.1.40) (EC 4.1.1.101) (Malolactic enzyme) (MLE) (NADP-dependent malic enzyme) (NADP-ME) (O34962)
Organism: Bacillus subtilis (strain 168)
Function: Bifunctional enzyme with both malic and malolactic enzyme activities. In the absence of NADPH, catalyzes the reversible decarboxylation of malate to pyruvate. Can use NAD and NADP, but with a very strong preference for NADP. In the presence of excess NADPH, catalyzes the non-oxidative decarboxylation of malate to lactate. During growth on glucose, contributes to NADPH balancing via oxidation of the NADPH produced in excess by other enzymatic reactions. Can also catalyze the decarboxylation of oxaloacetate.
Interaction partners:
- Pyruvate kinase
- Malate dehydrogenase
- Pyruvate carboxylase
- Pyruvate dehydrogenase E1 component subunit beta
- Fumarate hydratase class II
- L-lactate dehydrogenase
- Phosphate acetyltransferase
- Putative thiamine pyrophosphate-containing protein YdaP
- Uncharacterized phosphotransferase YvkC
- Pyruvate dehydrogenase E1 component subunit alpha
Sequence:
MSLREEALHLHKVNQGKLESKSKVEVRNAKDLSLAYSPGVAEPCKDIHEDINKVYDYTMKGNMVAVVTDGTAVLGLGNIGPEAALPVMEGKAVLFKSFAGVDAFPIALNTNDVDKIVETVKLLEPTFGGVNLEDIAAPNCFIIEERLKKETNIPVFHDDQHGTAIVTVAGLVNALKLSGKSMSSIKVVANGAGAAGIAIIKLLHHYGVRDIVMCDSKGAIYEGRPNGMNDVKNEVAKFTNQDRKDGSLKDVIVDADVFIGVSVAGALTKEMVQSMAKDPIIFAMANPNPEIMPEDAREAGASVVGTGRSDFPNQVNNVLAFPGIFRGALDVRATHINEEMKIAAVEAIASLVSEDELSADYVIPAPFDKRVAPAVAKAVAKAAMETGVARITVDPEEVAEKTRKLTIIGE
Protein: Photoactivated adenylate cyclase subunit alpha (EC 4.6.1.1) (Photoactivated adenylyl cyclase subunit alpha) (Q76L34)
Organism: Euglena longa (Euglenophycean alga) (Astasia longa)
Function: Acts as a photoreceptor for the step-up photophobic response.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:16121285}.
Interaction partners:
Sequence:
MYILVWKEGQQIKTFQDLEECGQFQIASNITDGQIFSVSVTPTMSKGGETGETQLRRLMYLSASTEPEKCNAEYLADMAHVATLRNKQIGVSGFLLYSSPFFFQVIEGTDEDLDFLFAKISSDPRHERCIVLANGPCTGRMYGEWHMKDSHIDNITKHPAIKTILFQIARSFSSMWSYLPKNAANMLLLGKNPNKQAPEPMSVVVTFIYLVEFSSILAHPGLTEQCADILAAFVDACVRNVEGTGGQVAKFITGICMAYWPINRAEDALVGLQQLSEDLAELRSQQPPGSALSLIYSRCGVHYGRALLCNAGFRKADFTLLGDCINTASRITSLSVKLKVPLLLSFEVRCLLGDEMREELESAGLHKVKGRDKPVQVYQFNAPELDSAVVRTKIEQFNPGRYRALCPVKPYDSLHPAQRPPIFDDTPRDSQPKVNQMQRRDSLVDRLSMIAKLAFPSSMMVGGESQLITLTYISQAAHPMSRLDLSSIQRVSFSRNESSNITGSLLYVNGLFVQTLEGPKSAVVSLYLKIRQDKRHKDVVAVFMAPIEERVYGSPLDMTAATEEMLATFPPLQDVLSQLAKSFISLETYVPSTVVRYLTAGNNPRNLQPVSVEVVMLATDICSFTPLSERCSLTEVWTICNTFIDACTSAICNEGGEVIKLIGDCVTAYFPPTAADNAVHACQEIVSFCAQLRDAFRDVLDCRSVVACGVGLDFGQVIMAQCGSLGMTEFVVAGEVSARVMEVEALTREAGRAIVITEPVADRLSPKLRDTGIVPCQEGVDGVPCYGILGVEWELDVAIIKKNIYGFHEARAQAALKKVDDGTNAPGRGAPAAGVPSSPKARALGRTSSVSSYTPDLNETLDPRMAESVFNDLCNQRGDAPNNSIAAKLRQAANDDRLDLGRMLQGPHELMPVLQAIKQLTNLRMLNMSDNFVDDNNVGELAESCIPMRSLQVLDLSNNPGLTKVIALKRLIKHNTQIREILLNGTRIAPMEQRKLQSSMNVNRMCASTDSKSSHKYDH
Protein: SKP1 component dimerisation domain-containing protein (Q388H1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVIFDDVENSNRVGGNEGGIRPIFVQLTPNAPLPSEEYLRLVALSKAPPPPDSEGSTLHSARNCRERSARVNGRRSPTKTNVRPRPPVTATQKWGDNAMSLINSKEEAVQRHEFALHVRGARYCRLLETMLDSSDLQLEPLHYDPKDPNMGRRPNGTEGNPANSLPPVILPQATQKGCVALFTYLDLITKRVPSMLSKPLRAPLEELVQPWELEFLLYSCMGDDVRNAITHIDEDGTADKRGRAPTNDTRPSYYSTILEKAPRSVDLLLEVALLSDFLLVEPLRQLTCAFIASLALNASSEEELLQLSGLQRPMTEDELEPLYYQFPFLRPDNHAKN
Protein: IQ motif and Sec7 domain ArfGEF 1 (A0A2R8Y7T6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MKGYGSAVWSLMWKYCISVRTLSVEGEAPSSETGTSLDSPSAYPQGPLVPGSSLSPDHYEHTSVGAYGLYSGPPGQQQRTRRPKLQHSTSILRKQAEEEAIKRSRSLSESYELSSDLQDKQVEMLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSVTNDGSQLGALVSPECGDLSEPTTLKSPAPSSDFADAITELEDAFSRQVKSLAESIDDALNCRSLHTEEAPALDAARARDTEPQTALHGMDHRKLDEMTASYSDVTLYIDEEELSPPLPLSQAGDRPSSTESDLRLRAGGAAPDYWALAHKEDKADTDTSCRSTPSLERQEQRLRVEHLPLLTIEPPSDSSVDLSDRSERGSLKRQSAYERSLGGQQGSPKHGPHSGAPKSLPREEPELRPRPPRPLDSHLAINGSANRQSKSESDYSDGDNDSINSTSNSNDTINCSSESSSRDSLREQTLSKQTYHKEARNSWDSPAFSNDVIRKRHYRIGLNLFNKKPEKGVQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSTMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCICNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKMKLEDFIKNLRGVDDGEDIPREMLMGIYERIRKRELKTNEDHVSQVQKVEKLIVGKKPIGSLHPGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFSLYGMQVLLFENQYYPNGIRLTSSVPGADIKVLINFNAPNPQDRKKFTDDLRESIAEVQEMEKHRIESELEKQKGVVRPSMSQCSSLKKESGNGTLSRACLDDSYASGEGLKRSALSSSLRDLSEAGKRGRRSSAGSLESNVEFQPFEPLQPSVLCS
Protein: Nuclear factor 1 (Q5VW27)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPSSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSASPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQLRICDWTMNQNGRHLYPSTSEDTLGITWQSPGTWASLVPFQVSNRTPILPANVQNYGLNIIGEPFLQAETSN
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase (EC 2.3.1.51) (Q7KTI0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform E
- Glycerol-3-phosphate acyltransferase 4, isoform D
- BcDNA.GH07066
- 1-Acylglycerol-3-phosphate O-acyltransferase 4, isoform A
- Seipin
- phosphatidate phosphatase
- O-acyltransferase
- Phospholipid/glycerol acyltransferase domain-containing protein
- Dihydroxyacetone phosphate acyltransferase
- Reticulon-like protein
Sequence:
MACTCEVIGLACVVALILSATAKAPYQMRMFFIFFGAGLIVFLCVPFMILRPRDYRNALFPSWCFRQLCRLVGITMEVRGLENVRKDHGAVVIMNHQSAVDLCVLAYLWPVIGRATVVSKKEVLYIPFFGIGAWLWGTLYIDRSRKTDSINSLQKEAKAIQERNCKLLLFPEGTRNSKDSLLPFKKGSFHIALQGKSPVQPVVISKYSFMDDEKKTFRPGHALIHILPEVSTEKYKREDVQLLIDECQSIMQTEYTKLSKEGQALSSKKQA
Protein: Keratin-associated protein 4-8 (Keratin-associated protein 4.8) (Ultrahigh sulfur keratin-associated protein 4.8) (Q9BYQ9)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 4-3
- Keratin-associated protein 4-1
- Keratin-associated protein 17-1
- Keratin-associated protein 4-5
- Keratin-associated protein 3-1
- Keratin-associated protein 9-3
- Keratin-associated protein 9-8
- Keratin-associated protein 9-4
- Keratin-associated protein 2-1
- Keratin-associated protein 1-5
Sequence:
MVNSCCGSVCSDQGCGQDLCQETCCCPSCCQTTCCRTTCYRPSYSVSCCCRPQCCQSVCCQPTCCRPSCCVSSCCKPQCCQSVCCQPTCCHPSCCISSCCRPSCCVSSCCKPQCCQSVCCQPNCCRPSCSISSCCRPSCCESSCCRPCCCLRPVCGRVSCHTTCYRPACVISTCPRPVCCASSCC
Protein: Zinc finger protein ZAT2 (Protein DUO1-ACTIVATED ZINC FINGER 1) (Q9SIJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the regulation of male germ cell division by DUO1.
Subcellular location: Nucleus {ECO:0000269|PubMed:24876252}.
Interaction partners:
- Transcription factor DUO1
- At4g35700
- Protein HAPLESS 2
- Homeodomain-like superfamily protein
- Protein GAMETE EXPRESSED 2
- Zinc finger
- Protein DMP9
Sequence:
MSNTSNSDPNSDIPFASSNVTLPSYNQNPRRKRTKLTNNEVGSSSSSPRPKPVTQPDPDASQIARPCTECGKQFGSLKALFGHMRCHPERQWRGINPPSNFKRRINSNAASSSSSWDPSEEEHNIASCLLMMANGDVPTRSSEVEERFECDGCKKVFGSHQALGGHRATHKDVKGCFANKNITEDPPPPPPQEIVDQDKGKSVKLVSGMNHRCNICSRVFSSGQALGGHMRCHWEKDQEENQVRGIDLNVPAATSSDTTLGCSLDLRLGL
Protein: RNA guanylyltransferase (O61120)
Organism: Trypanosoma brucei gambiense
Interaction partners:
Sequence:
MSATDVASELRSDAPEYVPTFPRCKQSENVTAFESPVVFLMFGCRGAGKSTQSTLLSKTYNLLYLSSGDIYKSGKQPFVELRKILNEHFGDGKERVYNGVVLDRFIANTEFEAFYVQSALRSVGLPVPFVFMLAIDQGLAAKRAEERGDNKGGNQRWRAVEQKAQAITANTVYAPIQCLKTIRVESDMTIDDVFNEIKTTIANQLPPDLFSLQLPREARREVEGTVLVEDYELYMELANDVHTVVGNLRGRRDSVPLSNVGAHLDKEYFSFANKRLRSQLTTMHVTLKADGLRFLVMKHKTRGYIGFPSAFTHCYELNDLFEGVEMAPKPYTELKKWMNDKSCELPADFLLDTEVVVHEKKPTLYIIDFIYFWGLDGRRMQFEQRLKVLREYFGDMKPQGQVIAMKDYVPINKIRTLVEEMKRRTELPVDGLIFQHNGSYRFGSDKFLIKWKPVHLCTVDFRLANGRVENGVWTFDLFVTDDFIEENGFREVAYPGATALIPASVVEENGLQNGMIIEMALSEKESVKKTSPNAPSEKTRWTFRNARNDKPSPNKYSIVTRICELMHVDLDELVSLCEKVPFYRNV