wanglab/gogpt-training-data huggingface dataset:
Protein: SET-binding protein (SEB) (Q9Z180)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Polycomb group protein ASXL1
- Protein SET
- U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
- Splicing factor U2AF 35 kDa subunit
Sequence:
MEPREMLSSCRQRGSESEFLQGSSSRSPPAPGCSGEPLKGISVGGERMEPEEEDELGSGRDVDCNSNADSEKWVAGDGLEEQEFSIKEANFTEGSLKLKIQTTKRAKKPPKNLENYICPPEIKITIKQSGDQKVSRTGKNSKATKEDERNHSKKKLLTAGDPTASDLKAFQTQAYERPQKHSTLQYDPGHSQGFTSDTLKPKHQQKSSSQSHMEWSSNSDSGPATQNCFISPEAGRDTASTSKVPALEPVASFAKAQSKKGSTGGAWSQLSSSSKDLLLGSVVPSPSSHNSPATPSSSAECNGLQPLGDQDGGSTKDLPEPPTLSSKKKSSKKDMISQTLPNSDLDWVKSAQKAFETTEGKREAYSADSAQEASPARQSISSVSNPENDSSHVRITIPIKTPSLDPSNHKRKKRQSIKAVVEKIVPEKALASGISMSSEVVNRILSNSEGSKKDPRVPKLGKMIENETPSVGLETGGNAEKIVPGGASKQRKPPMVMTSPTRTEHAPSGKLSEIQHPKFAAKRRCSKAKPPAMLREAVLATAEKLMVEPPSAYPITPSSPLYTNTDSLTVITPVKKKRGRPKKQPLLTVETIHEGTSTSPVSPISREFPGTKKRKRRRNLAKLAQLVPGEDKPMSEMKFHKKVGKLGVLDKKTIKTINKMKTLKRKNILNQILSCSSSVALKAKAPPETSPGAASIESKLGKQINVSKRGTIYIGKKRGRKPRTELPPPSEEPKTAIKHPRPVSSQPDVPAVPSSFQSPVASSPAAMHPLSTQLGGSNGNLSPASTETNFSELKTMPNLQPISALPTKTQKGIHGGTWKLSPPRLMANSPSHLCEIGSLKEITLSPVSESHSEETIPSDSGIGTDNNSTSDQAEKSSESRRRYSFDFCSLDNPEAIPSDTSTKNRHGHRQKHLIVDTFLAHESLKKPKHKRKRKSLQNRDDLQFLAELEELITKFQVFRISHRGYTFYHENPYPSIFRINFDQYYPVPYIQYDPLLYLRRTSDLKSKKKRGRPAKTNDTMTKVPFLQGFSYPIPSGSYYAPYGMPYTSMPMMNLGYYGQYPAPLYLSHTLGAASPFMRPTVPPPQFHASSHVKISGATKHKAKHGVHLQGTVGMGLGDIQPSLNPPKVGGATLSSSRLHKRKHKHKRKHKEDRILGTHDNLSGLFAGKATGFSSHLLSERLSGSDKELPLVSEKSKHKERQKHQHGEASHKVSKNNFEVDTLSTLSLSDAQHWTQAKDKGDLSSEPVESCAKRYSGSGGDSTRSEGLDVFSEMNPSSDKWDSDMGGSKRRSFEGFGTYREKDIQAFKMNRKERGSYESSMSPGMPSPHLKVDQTAAHSKSEGSISAMMARKKPTAVDSVAIPSAPVLSLLAASAATSDAASSSLKKRFKRREIEAIQCEVRKMCHYTKLLSTKKNLDHVNKILKAKRLQRQSKTGNNFVKKRRGRPRKQPSQFDEDSRDQMPVLEKCIDLPSKRGQKPSLSPLALEPASGQDAVMATIEAVIHMAREAPPLPPPPPPPLPPPPPPPPPPPPLPKTARGGKRKHRPQPPAQPAQPTPQPLPQEEEVKAKRPRKSRASESDVLP
Protein: Protein UmuC (DNA polymerase V) (Pol V) (P04152)
Organism: Escherichia coli (strain K12)
Function: Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair. Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB). RecA and to a lesser extent the beta clamp-complex may target Pol V to replication complexes stalled at DNA template lesions.
Interaction partners:
- Protein UmuD
- Beta sliding clamp
- Protein RecA
- DNA polymerase II
- DNA polymerase III subunit alpha
- DNA polymerase III subunit delta'
- LexA repressor
- DNA polymerase III subunit epsilon
- UvrABC system protein A
- DNA polymerase I
Sequence:
MFALCDVNAFYASCETVFRPDLWGKPVVVLSNNDGCVIARNAEAKALGVKMGDPWFKQKDLFRRCGVVCFSSNYELYADMSNRVMSTLEELSPRVEIYSIDEAFCDLTGVRNCRDLTDFGREIRATVLQRTHLTVGVGIAQTKTLAKLANHAAKKWQRQTGGVVDLSNLERQRKLMSALPVDDVWGIGRRISKKLDAMGIKTVLDLADTDIRFIRKHFNVVLERTVRELRGEPCLQLEEFAPTKQEIICSRSFGERITDYPSMRQAICSYAARAAEKLRSEHQYCRFISTFIKTSPFALNEPYYGNSASVKLLTPTQDSRDIINAATRSLDAIWQAGHRYQKAGVMLGDFFSQGVAQLNLFDDNAPRPGSEQLMTVMDTLNAKEGRGTLYFAGQGIQQQWQMKRAMLSPRYTTRSSDLLRVK
Protein: Prolactin-inducible protein (Gross cystic disease fluid protein 15) (GCDFP-15) (Prolactin-induced protein) (Secretory actin-binding protein) (SABP) (gp17) (P12273)
Organism: Homo sapiens (Human)
Subcellular location: Secreted.
Interaction partners:
- Zinc-alpha-2-glycoprotein
- T-cell surface glycoprotein CD4
- Keratin, type II cytoskeletal 7
- Keratin, type I cytoskeletal 20
- Protein LIAT1
- Kell blood group glycoprotein
- Lactotransferrin
- Apolipoprotein D
- Mammaglobin-A
- Progesterone receptor
Sequence:
MRLLQLLFRASPATLLLVLCLQLGANKAQDNTRKIIIKNFDIPKSVRPNDEVTAVLAVQTELKECMVVKTYLISSIPLQGAFNYKYTACLCDDNPKTFYWDFYTNRTVQIAAVVDVIRELGICPDDAAVIPIKNNRFYTIEILKVE
Protein: Cell death regulator Aven (Q9NQS1)
Organism: Homo sapiens (Human)
Function: Protects against apoptosis mediated by Apaf-1.
Subcellular location: Endomembrane system; Peripheral membrane protein. Note=Associated with intracellular membranes.
Interaction partners:
- Apoptotic protease-activating factor 1
- Bcl-2-like protein 1
- Caspase-9
Sequence:
MQAERGARGGRGRRPGRGRPGGDRHSERPGAAAAVARGGGGGGGGDGGGRRGRGRGRGFRGARGGRGGGGAPRGSRREPGGWGAGASAPVEDDSDAETYGEENDEQGNYSKRKIVSNWDRYQDIEKEVNNESGESQRGTDFSVLLSSAGDSFSQFRFAEEKEWDSEASCPKQNSAFYVDSELLVRALQELPLCLRLNVAAELVQGTVPLEVPQVKPKRTDDGKGLGMQLKGPLGPGGRGPIFELKSVAAGCPVLLGKDNPSPGPSRDSQKPTSPLQSAGDHLEEELDLLLNLDAPIKEGDNILPDQTSQDLKSKEDGEVVQEEEVCAKPSVTEEKNMEPEQPSTSKNVTEEELEDWLDSMIS
Protein: Bent (Q8ST85)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKVTVIDKPAPPNGPLKVDEINSESCTLHWNPPDDDGGQPIDNYVVEKLDETTGRWIPAGETDGPVTALKVGGLTPGHKYKFRVRAKNRQGTSEPLTTAQAIIAKNPFDVPTKPGTPTIKDFDKEFVDLEWTRPEADGGSPITGYVVEKRDKFSPDWEKCAEISDDITNAHVPDLIEGLKYEFRVRAVNKAGPGSPSDATETHVARPKNTPPKIDRNFMSDIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNINGTDRHNVKVTILDAPSVPEGPLRNGD
Protein: Anon1A3 (Q9U4R2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
GVENLPSVAEAKQNHVDEVKPISEEPGNSSEEVPKAEEPLKSSGETSENGAATETAAAPKEPASVMDVDEDETLVENTPSANKEKALDDEKEPEQKSEEHAAAVLESKEQNEPAKEPTPEPMEVDGSSKGSSDTAQVDTPAIENVSAAPETEAAAKTTESSNDVVEVATEGKATVLEVPAAEPKEAESTVESAEELTETSTVVVTEPKEAASCEEEPSKVVDSAEPKEAESNTDESATPVPIDVSTAPASNDVSKPLEIDTTLVKTADSPAKEPQEICEVKKAEINVNGEPKIVNSSAEVGENAAPKVCN
Protein: Meiotically up-regulated gene 114 protein (O14183)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDNKKGGLFKIAKKLRNGTKVWARAGYFKCKLLKITTTGAPCLFAGRLKRRYDATFQSMVEIFRQEIANDVTCGRVETALLYFVNKFFRSVGCFGKGKEREVKTDRQRDTGSGEQRIRLERDTETLYQSQLRINQVNGWMSGWMQISLILQ
Protein: Putrescine export system ATP-binding protein SapD (P0AAH4)
Organism: Escherichia coli (strain K12)
Function: Part of a putrescine export transport system, does not play a role in resistance to antimicrobial peptides. Stimulates K(+)-uptake proteins TrkG and TrkH to import K(+), may act via ATP-binding rather than ATP hydrolysis.
Subcellular location: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Putrescine export system permease protein SapB
- Putrescine export system permease protein SapC
- Probable ABC transporter periplasmic-binding protein SapA
- Putrescine export system ATP-binding protein SapF
- Dipeptide transport system permease protein DppC
- Probable D,D-dipeptide transport system permease protein DdpC
- Glutathione transport system permease protein GsiD
- Nickel transport system permease protein NikC
- Oligopeptide transport system permease protein OppC
- Arginine transport ATP-binding protein ArtP
Sequence:
MPLLDIRNLTIEFKTGDEWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVNKDNWRVTADRMRFDDIDLLRLSARERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIVTPRLTGAKNHLYACHFPLNMEKE
Protein: Dihydroorotate dehydrogenase (DHOD) (DHODase) (DHOdehase) (EC 1.3.-.-) (Dihydroorotate oxidase) (P07670)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the conversion of dihydroorotate to orotate. Participates in the pyrimidine biosynthetic pathway.
Interaction partners:
- Multifunctional protein pyr1-3
- Uridine 5'-monophosphate synthase
- Protein transport protein got1 homolog
- Cytochrome b5 heme-binding domain-containing protein
- Cytochrome b5 reductase
- Decaprenyl-diphosphate synthase
- Cytochrome b5 domain-containing protein
- Bifunctional purine biosynthetic protein purD
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
- GMP synthase
Sequence:
MEWPINKPIYDINKSWEDNLENGPFIEGYKKVDRNDNKDPSKYIDFLGQKLASPIGVPAGPLLNSQWVKFALEAGFDLPTYKTIRSHEHFGHPVPNVMYLDLESEDKQFTKSDSGSTLHATQTIPTTMDQLAITNSFGMPSMGKEYLYKDIALAHSYLGSGQSMIVSITGTASSAHDFLQDFVDTVRIACDAGAKMVEVNYSCPNVVTGEGQIYHNPDAVYEISSTLVKELSSKNIPLIIKVGVMDDLEKMERLFQQAERAGVAAIAGINTLSMKVTDKITGEPSLGASRLTSGVCGAPIRSAALDWVSTASSIIKKQNSKLKLLGCGGIVKPEHFDDFLNSGADIAMSATGLMWDPYIAMKWHNNNKNN
Protein: BOS complex subunit TMEM147 (Transmembrane protein 147) (Q9SX96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Nicalin
- Calcium load-activated calcium channel
- Calcium load-activated calcium channel
- At4g24330
- Uncharacterized protein At5g49945
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL18y
- Protein Asterix
- Large ribosomal subunit protein uL5y/uL5x/uL5w
- Large ribosomal subunit protein uL5z
Sequence:
MTLFHFFNCAILTFGPHAVYYSATPLSEYDTLGTSVKAAVVYLATALVKLVCLATFLQVSETEVFDPYQEALKAMIGFIDVAGLYYALAQLTHRNISQNHKFQAVGLGWAFADSVLHRLAPLWVGARGLEFTWDYVLQGLEANANLVFTISLAALGSLMWLRKNKPKSLIPIIYTCAVIIATMPSITSYLKRVNGWHFPKIVGFELATSLVMAFISCQLFILCQRPSL
Protein: Matrix protein 2 (Proton channel protein M2) (P0DOF5)
Organism: Influenza A virus (strain A/Udorn/307/1972 H3N2)
Function: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}.
Interaction partners:
Sequence:
MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRFFEHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVSIELE
Protein: Isopenicillin-N N-acyltransferase (IAT) (IPN acyltransferase) (EC 2.3.1.164) (Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 40 kDa form) (Penicillin biosynthetis cluster protein aatA) [Cleaved into: Acyl-coenzyme A:6-aminopenicillanic acid acyltransferase 11 kDa subunit; Acyl-coenzyme A:6-aminopenicillanic acid acyltransferase 29 kDa subunit] (B6HLT9)
Organism: Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum)
Function: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:18439860}. Note=The unprocessed preprotein is translocated inside peroxisomes and regulates its self-processing. {ECO:0000269|PubMed:18439860}.
Interaction partners:
- Pc21g10800 protein
- Pc22g23250 protein
- Isopenicillin N synthase
- Pc13g09140 protein
- Arginase
- argininosuccinate lyase
- Argininosuccinate synthase
- Arginine biosynthesis bifunctional protein ArgJ
Sequence:
MLHILCQGTPFEIGYEHGSAAKAVIARSIDFAVDLIRGKTKKTDEELKQVLSQLGRVIEERWPKYYEEIRGIAKGAERDVSEIVMLNTRTEFAYGLKAARDGCTTAYCQLPNGALQGQNWDFFSATKENLIRLTIRQAGLPTIKFITEAGIIGKVGFNSAGVAVNYNALHLQGLRPTGVPSHIALRIALESTSPSQAYDRIVEQGGMAASAFIMVGNGHEAFGLEFSPTSIRKQVLDANGRMVHTNHCLLQHGKNEKELDPLPDSWNRHQRMEFLLDGFDGTKQAFAQLWADEDNYPFSICRAYEEGKSRGATLFNIIYDHARREATVRLGRPTNPDEMFVMRFDEEDERSALNARL
Protein: Sin3A, isoform A (Sin3A, isoform F) (A1Z927)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
Sequence:
MMKRTRVDEVQFGTRPVPQTSGGVGVGVVGVTGGGPTSGGGGTATVGVNTTGVTIGTVVPSAHNATISGIGSIHHRILTPQHGGAQTIAYLPSTTPTATNLKTTTSIVDSTTAGGPVGAGAQVAVGVGSAAGGGGVVVSTGSTGTQTLQYTTSYSVASIQAGGTLKANTADGANTVQIHVTGGGAANNPASAQTVSSSSQTGTIRQRTISGTQTVATAVGNLATISQQQPVQQSPLGKAQTPPSSVVANSIPVGGTTPPQGQSGNATPRLKVEDALSYLDQVKYQYADQPQIYNNFLDIMKEFKSHCIDTPGVIERVSTLFKGHTELIYGFNMFLPPGYKIEIHSDALGCSVPVVSMPSPPGAPTSTGTVHMLTGNSSMSGAGHIAIKTTNAATLTPAAGAGAAAAAAAVAQIQSAGAVNLMTHGGASLTQTTIHALQQATPPQSQSPGGGHVHVSVTNSTAANAVVPGQPGISVSAHNVPQNYSRDRERATITPTGQVAGAAANVNASASIVVGGPPTPNSLSELSPHGGAGGGPGAGAAQHNLHHIQQAHQSILLGETGQQNQPVEFNHAITYVNKIKNRFQNQPAKYKKFLEILHDYQREQKVMKEGSLNQGKMLTEQEVYTQVAKLFGQDEDLLREFGQFLPDATNHQSGQYMSKSASVHNDHGKRPTATLSGGAHITMSSASPAPSGSPLHLGATTLPQIDKSAHAAAIGNLSAVNTSVSIKTYNNNQQQQNHVIGSGLNATRNDILFEKDYHAGLQQQAHQRGAGVGGHHHLAGTAAGANIGRPGVGASVMVSYDKEHRNNHHVQKYVGHAPNQNLTHGHNAKKSPSYGIPSVIGSMPHISDNSLDRSSPGISYATPPLPSGPHGQHNSGSATRRPGDDSLVGHYASGAPPAKRPKPYCRDVSFSEASSKCTISDAAFFDKVRKALRSPEVYDNFLRCLTLFNQEIVSKTELLGLVSPFLMKFPDLLRWFTDFLGPPSGQPAGGLIDGMPLAATQRQGGGSSNSSHDRGTSHQSAAEYVQDVDLSSCKRLGASYCALPQSTVPKKCSGRTALCREVLNDKWVSFPTWASEDSTFVTSRKTQFEETIYRTEDERFELDLVIEVNSATIRVLENLQKKMSRMSTEELSKFHLDDHLGGTSQTIHQRAIHRIYGDKSGEIITGMKKNPFVAVPIVLKRLKVKEEEWREAQKTFNKQWREQNEKYYLKSLDHQAINFKPNDMKALRSKSLFNEIETLYDERHDQEDDAMEPFGPHLVLPYKDKTILDDAANLLIHHVKRQTGIQKQEKQKIKQIIRQFVPDLFFAPRQPLSDDERDDAFPFLVDDNTKMDVDSPLGRTESSTRNAKSTPSESASPARSNASTSSVTPAGIKKETDDSKATTGSFAPASSATASSATPVDDATPSTSSAAAAASAASSSTVSGTEGKPKDDPLSSHKEEGAGSTSSGVATSPRQAQDTAGAGVDVEIKLEHPADFSNPKLLPPHAHGQREDESYTLFFANNNWYLFLRLHAILCDRLHVMYERARLLAIEEERCRVNRRESTATALRLKPKPEIQVEDYYPTFLDMLKNVLDGNMDSNTFEDTMREMFGIYAYISFTLDKVVSNAVRQLQYCVTERAALDCVELFATEQRRGCTGGFCRDAHKTFDREMSYQRKAESILNEENCFKVYIYKIDCRVTIELLDSEPEEVDKPAALKAQKFSKYVERLANPALGGGGNTGRSDSALGNDSVVDGSDIKTEADEDTAEHTQSQQWTLLESENEKYIWSSPLKIHVQSY
Protein: Slit homolog 1 protein (Slit-1) (Multiple epidermal growth factor-like domains protein 4) (Multiple EGF-like domains protein 4) (O75093)
Organism: Homo sapiens (Human)
Function: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions (By similarity). SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Roundabout homolog 1
- Roundabout homolog 2
- Roundabout homolog 4
- Roundabout homolog 3
- SLIT-ROBO Rho GTPase-activating protein 1
- Netrin receptor DCC
- Netrin-1
- Homeobox protein Nkx-6.2
- Collagen alpha-5
- Homeobox protein Nkx-6.1
Sequence:
MALTPGWGSSAGPVRPELWLLLWAAAWRLGASACPALCTCTGTTVDCHGTGLQAIPKNIPRNTERLELNGNNITRIHKNDFAGLKQLRVLQLMENQIGAVERGAFDDMKELERLRLNRNQLHMLPELLFQNNQALSRLDLSENAIQAIPRKAFRGATDLKNLQLDKNQISCIEEGAFRALRGLEVLTLNNNNITTIPVSSFNHMPKLRTFRLHSNHLFCDCHLAWLSQWLRQRPTIGLFTQCSGPASLRGLNVAEVQKSEFSCSGQGEAGRVPTCTLSSGSCPAMCTCSNGIVDCRGKGLTAIPANLPETMTEIRLELNGIKSIPPGAFSPYRKLRRIDLSNNQIAEIAPDAFQGLRSLNSLVLYGNKITDLPRGVFGGLYTLQLLLLNANKINCIRPDAFQDLQNLSLLSLYDNKIQSLAKGTFTSLRAIQTLHLAQNPFICDCNLKWLADFLRTNPIETSGARCASPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYQLNSECNSDVVCPHKCRCEANVVECSSLKLTKIPERIPQSTAELRLNNNEISILEATGMFKKLTHLKKINLSNNKVSEIEDGAFEGAASVSELHLTANQLESIRSGMFRGLDGLRTLMLRNNRISCIHNDSFTGLRNVRLLSLYDNQITTVSPGAFDTLQSLSTLNLLANPFNCNCQLAWLGGWLRKRKIVTGNPRCQNPDFLRQIPLQDVAFPDFRCEEGQEEGGCLPRPQCPQECACLDTVVRCSNKHLRALPKGIPKNVTELYLDGNQFTLVPGQLSTFKYLQLVDLSNNKISSLSNSSFTNMSQLTTLILSYNALQCIPPLAFQGLRSLRLLSLHGNDISTLQEGIFADVTSLSHLAIGANPLYCDCHLRWLSSWVKTGYKEPGIARCAGPQDMEGKLLLTTPAKKFECQGPPTLAVQAKCDLCLSSPCQNQGTCHNDPLEVYRCACPSGYKGRDCEVSLDSCSSGPCENGGTCHAQEGEDAPFTCSCPTGFEGPTCGVNTDDCVDHACANGGVCVDGVGNYTCQCPLQYEGKACEQLVDLCSPDLNPCQHEAQCVGTPDGPRCECMPGYAGDNCSENQDDCRDHRCQNGAQCMDEVNSYSCLCAEGYSGQLCEIPPHLPAPKSPCEGTECQNGANCVDQGNRPVCQCLPGFGGPECEKLLSVNFVDRDTYLQFTDLQNWPRANITLQVSTAEDNGILLYNGDNDHIAVELYQGHVRVSYDPGSYPSSAIYSAETINDGQFHTVELVAFDQMVNLSIDGGSPMTMDNFGKHYTLNSEAPLYVGGMPVDVNSAAFRLWQILNGTGFHGCIRNLYINNELQDFTKTQMKPGVVPGCEPCRKLYCLHGICQPNATPGPMCHCEAGWVGLHCDQPADGPCHGHKCVHGQCVPLDALSYSCQCQDGYSGALCNQAGALAEPCRGLQCLHGHCQASGTKGAHCVCDPGFSGELCEQESECRGDPVRDFHQVQRGYAICQTTRPLSWVECRGSCPGQGCCQGLRLKRRKFTFECSDGTSFAEEVEKPTKCGCALCA
Protein: Actin-related protein 2/3 complex subunit 5 (Q9VQD8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Actin-related protein 2/3 complex subunit
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 3
- LD35927p
- RE12101p
- WHAMM and JMY related, isoform B
Sequence:
MAKNTSSNAFRKIDVDQYNEDNFREDDGVESAAAGPDESEITTLLTQGKSVEALLSALQNAPLRCKNQNVKDHALNITLRVLLSIKSTQMDQAIDTLDQNDLIDVLMKYIYRGFEIPSEGSSGHLLQWHEKAFAKGGVGCIVRVLSDTNRA
Protein: Nuclear receptor subfamily 0 group B member 2 (Orphan nuclear receptor SHP) (Small heterodimer partner) (Q15466)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator that acts as a negative regulator of receptor-dependent signaling pathways (By similarity). Specifically inhibits transactivation of the nuclear receptor with which it interacts (By similarity). Inhibits transcriptional activity of NEUROD1 on E-box-containing promoter by interfering with the coactivation function of the p300/CBP-mediated transcription complex for NEUROD1. Essential component of the liver circadian clock which via its interaction with NR1D1 and RORG regulates NPAS2-mediated hepatic lipid metabolism (By similarity). Regulates the circadian expression of cytochrome P450 (CYP) enzymes (By similarity). Represses: NR5A2 and HNF4A to down-regulate CYP2C38, NFLI3 to up-regulate CYP2A5, BHLHE41/HNF1A axis to up-regulate CYP1A2, CYP2E1 and CYP3A11, and NR1D1 to up-regulate CYP2B10, CYP4A10 and CYP4A14 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:14752053, ECO:0000269|PubMed:28797635}. Cytoplasm {ECO:0000269|PubMed:14752053}. Note=Colocalizes with NEUROD1 in the nucleus.
Interaction partners:
- Nuclear receptor subfamily 5 group A member 2
- Hepatocyte nuclear factor 4-alpha
- Cyclic AMP-responsive element-binding protein 3
- Bile acid receptor
- Peroxisome proliferator-activated receptor gamma
- Cytochrome P450 7A1
- 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase
- Nuclear receptor subfamily 1 group I member 2
- Bile salt export pump
- Oxysterols receptor LXR-alpha
Sequence:
MSTSQPGACPCQGAASRPAILYALLSSSLKAVPRPRSRCLCRQHRPVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAEAPVPSILKKILLEEPSSSGGSGQLPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPDVPGLQAASHIGHLQQEAHWVLCEVLEPWCPAAQGRLTRVLLTASTLKSIPTSLLGDLFFRPIIGDVDIAGLLGDMLLLR
Protein: Plastidial pyruvate kinase 1, chloroplastic (PK1) (PKp1) (EC 2.7.1.40) (Pyruvate kinase II) (Pyruvate kinase isozyme A) (PKP-ALPHA) (Q9LIK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for plastidial pyruvate kinase activity. Involved in seed oil accumulation, embryo development and seed storage compounds mobilization upon germination.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:17557808, ECO:0000269|PubMed:17892448, ECO:0000269|PubMed:18431481}.
Interaction partners:
- L-lactate dehydrogenase
- Cytosolic enolase 3
- Enolase 1, chloroplastic
- Bifunctional enolase 2/transcriptional activator
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
- D-lactate dehydrogenase [cytochrome], mitochondrial
- Malate dehydrogenase 1, cytoplasmic
- NADP-dependent glyceraldehyde-3-phosphate dehydrogenase])
- Inosine triphosphate pyrophosphatase
- Malate dehydrogenase 3, cytoplasmic
Sequence:
MSQSIQFSTPSHTPHLLHLPHSQFNRPLSSISFRRFPLTTIKYTSIRASSSSSPSPDLDSSSSSSSSQVLLSPNGTGAVKSDERSVVATAVTTDTSGIEVDTVTEAELKENGFRSTRRTKLICTIGPATCGFEQLEALAVGGMNVARLNMCHGTRDWHRGVIRSVRRLNEEKGFAVAIMMDTEGSEIHMGDLGGEASAKAEDGEVWTFTVRAFDSSRPERTISVSYDGFAEDVRVGDELLVDGGMVRFEVIEKIGPDVKCLCTDPGLLLPRANLTFWRDGSLVRERNAMLPTISSKDWLDIDFGIAEGVDFIAVSFVKSAEVINHLKSYLAARSRGGEIGVIAKIESIDSLTNLEEIILASDGAMVARGDLGAQIPLEQVPAAQQRIVQVCRALNKPVIVASQLLESMIEYPTPTRAEVADVSEAVRQRSDALMLSGESAMGQFPDKALTVLRTVSLRIERWWREEKRHESVPLQAIGSSFSDKISEEICNSAAKMANNLGVDAVFVYTTSGHMASLVSRCRPDCPIFAFTTTTSVRRRLNLQWGLIPFRLSFSDDMESNLNKTFSLLKSRGMIKSGDLVIAVSDMLQSIQVMNVP
Protein: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (6PF-2-K/Fru-2,6-P2ase) (AtF2KP) (PFK/FBPase) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] (Q9MB58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Synthesis and degradation of fructose 2,6-bisphosphate. Regulates carbon partitioning between sucrose versus starch during the diurnal cycle.
Subcellular location: Membrane {ECO:0000269|PubMed:18433157}; Lipid-anchor {ECO:0000269|PubMed:18433157}; Cytoplasmic side {ECO:0000269|PubMed:18433157}. Cytoplasm {ECO:0000269|PubMed:18433157}.
Interaction partners:
- fructose-bisphosphatase
- Fructose-1,6-bisphosphatase, cytosolic
- ATP-dependent 6-phosphofructokinase 2
- Fructose-1,6-bisphosphatase 1, chloroplastic
- Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 2
- ATP-dependent 6-phosphofructokinase 1
- Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 2
- Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 1
- Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 1
- ATP-dependent 6-phosphofructokinase 4, chloroplastic
Sequence:
MGSGASKNTEEDDDGSNGGGGQLYVSLKMENSKVEGELTPHVYGSLPLIGSWDPSKALPMQRESALMSELSFVVPPDHETLDFKFLLKPKNRNTPCIVEEGENRLLTGGSLQGDARLALFRLEGDVIVEFRVFINADRVSPIDLATSWRAYRENLQPSTVRGIPDVSINPDPKSAECPLESLELDLAHYEVPAPAPSANSYLVYAADNAENPRSLSASGSFRNDSTPKAAQRNSEDSGVTVDGSPSAKEMTIVVPDSSNIYSAFGEAESKSVETLSPFQQKDGQKGLFVDRGVGSPRLVKSLSASSFLIDTKQIKNSMPAAAGAVAAAAVADQMLGPKEDRHLAIVLVGLPARGKTFTAAKLTRYLRWLGHDTKHFNVGKYRRLKHGVNMSADFFRADNPEGVEARTEVAALAMEDMIAWMQEGGQVGIFDATNSTRVRRNMLMKMAEGKCKIIFLETLCNDERIIERNIRLKIQQSPDYSEEMDFEAGVRDFRDRLANYEKVYEPVEEGSYIKMIDMVSGNGGQIQVNNISGYLPGRIVFFLVNTHLTPRPILLTRHGESMDNVRGRIGGDSVISDSGKLYAKKLASFVEKRLKSEKAASIWTSTLQRTNLTASSIVGFPKVQWRALDEINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQRLEPVIIELERQRAPVVVISHQAVLRALYAYFADRPLKEIPQIEMPLHTIIEIQMGVSGVQEKRYKLMD