wanglab/gogpt-training-data huggingface dataset:
Protein: Cullin 4B, putative (Q57XW2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA damage-binding protein 1
- COP9 signalosome complex subunit 5
- TATA-binding protein interacting
- RING-type domain-containing protein
- RING-type domain-containing protein
- COP9 signalosome complex subunit 3 N-terminal helical repeats domain-containing protein
- Ubiquitin, putative
- Cullin, putative
- COP9 signalosome complex subunit 4
- JAB1/MPN/MOV34 metalloenzyme domain-containing protein
Sequence:
MSSRTLYDQGVTQAQWGEQLLHTKPCVNIQLPQPEHSLHREASEAERDKALKSALGMLSAVLARSSGNTKAIVDSPAFVAKSVELLLQLLCTSSFPSLPHQHNPSASPAPLSTVPPIQQQRWLKIDFCDREYFVDSVCRNVRTLVELDCGPHLFAELEQCLKGYVTSMVELLTSSGEDGVTADVLFVRLAHAWGHYYLAVAELQEVWVYFDRWYVFKTHAVKSIEGLAIEILREGLLLHPWLLPRAQLGYLDCLSRDIVVHANSSVENSNGDGWNSRHELRLFTDLCAAVQVYFLRVEPEIVALVGKFYMEEADRMWSAGVPAGIFFARVEQFLLECRERVRVCLVSYSLPKLESVTQSSLLLTHGVAFLERDFANLAMEKKYDCFRLAWRLLASGKYVRLGKQCNAVFRAYILQQGLLVMQRFAARSVERDVFGTVKAMIELMHRGETIISEGFPEDSATFSIQLRDALTEVLQGHQMEFVEQLARYLDWVVRGSDTSTALGQSDHSESKPMATADGSSDVGGVLKLLDDIGRIYSLFPSKDIFEKLYWRDLARRLLHHPRGTPCVDVEGHFIQILREIVGTDAAKFEGMVNDLMSSQELNERFRLWVVNKHTEVPPLSPPPTSVANEEDDQTETPQPKAQHNNEGYEEEEENHEAVEAALAAVDVKLNVLTDGYWPKQTPLSTELPPQLRVLAKSMEVFYRKCFAKRRLIWLHQLSSAVVKSAVGNSRRQLSGTLVQANVLLALQEIIDAGMHSEQLCVSVGEICGQLGLDISLPDVVGAILGLCHPKFRLLLRAPGSGTDGSNQHGSDDASGYGSSVGVVAATLLGTDILRINHSFSVPSQFCRIPFLGARRRGGDGAVDERAADTDGEQTMEDIMKDRVHVVDAAIVRLMKQRRRASHEEVMEEVPKLVRFPVTASAVKESARRLTERGFLERGNTNEYIYIS
Protein: Cytochrome P450 2K22 (Zgc:55856) (Q802X8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MALVGALLPGLSFTVGMVVAFLLLFLVISYFSSSKDQGKYPPGPKPLPLLGNLHILDLKNTYMSLWKLSKQYGPVYTVHMGPRTVVVLSGYKAVKEALVNLSEEFGERDISPIFQDFNEGYGIVFSNGENWKEMRRFALSNLRDFGMGKKRGEELITEEIKYLKEEIERFGGKPFETKLPLAMAISNVIALIVYSIRFEYNSPKFHRAIVRANENAKLVGSPSVQLYNMFPWLRLFVINQKRVVDNVQESFKQIGEIVNGLKKTLNPQSPRGIADKFLIQQQKDKESGKTDSLYNSNNFLTTINNLFGAGIDTTVTTLRWGLLLIAKYPEIQAKVHDEIDSVIGERQPVPGDRKNLPYTDAVIHEIQRFADILPIGLLRQTSCDVHLNGYLIKKGTSVFPLIASVLRDENEWETPDSFNPKHFLNKQGQFVKKDAFMPFGAGRRLCIGESLARMELFLFFTSLLQHFCFTPPPGVSEDELDLTPVVGFTLSPMPHKLCAVKRF
Protein: Uncharacterized protein, isoform E (A8DZ25)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFDQPPENELQKSHDHNPGALSEHQLRVQASLQRLNIPDWFRHYNKGPEKAADGENACTSATGGGYRPGNFTRKRAQESGRWQGLNSKTTSLSSLGSQRSDRSPLLMSPSAHSHHGGQSSYSCGSTTIHGPAPVQIGMGATRWSTSHLNSTQMSPGASQRGSFTRGAPINSSFISVASGSGLLRNSYRQPYLGWRSTEKLSQRTPHERLANSLLTQRTAPPSTRAGNETRTLHSVSTEIQSSIKEVTSAIVHFVNDQQQSQHPRSRSTSPNSRCWLESSFVGTRTLDSPQTPVIDNSPPELARKQQQLHPHQVHLDVGLSPVVSAGQLPHRMNGINRIGNGGGESAIQV
Protein: Family with sequence similarity 49 member A (Uncharacterized protein LOC378872 isoform 3) (A0A0R4IMR9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}.
Interaction partners:
Sequence:
MRAEEADVLIGISNPNLPKRIKEGVCNRNAVWWEGVYSRTRGCSKRKHTFSSRKGFAGMGNLLKVLTREIENYPHFFLDFENAQPTDCEREVWNQVNAVLQESESILSGLQAYKGAGQEIRDAIQNPNDMLLQERAWNSVCPLVIRLKKFYAFSLKLEQALQSLLESLTCPPYTPTQHLEREQALAKQFAEILHFTLRFDELKMRIPAIQNDFSYYRRTISRNRLNNMNLDIENEVNNEMANRMSLFYAEATPMLKTLSTATTNFVTENKTLPLENTTDCLSTMASVCKVMLETPEYTSRFNSEDTLLFCMRVMVGVIILYDHVHPNGAFNKSSKIDMKGCIKVLKDQPADNVEGLLNALKFTTKHLNDESTPKNIRTMLQ
Protein: Protein FAM222B (J3QKY8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLACLPGPGDLSFQLLSHTQMNTGLQKWDTTQKMRTAHYPTPAELDAYAKKVANNPLTIKIFPNSVKVPQRKHVRRTVNGLDTSAQRYSPYPTQAATKAGLLAIVKVPAKSILKDFDGTRARLLPEAIMNPPVAPYATVAPSTLAHPQAQALARQQALQHAQTLAHAPPQTLQHPQGIPPPQALSHPQSLQQPQGLGHPQPMAQTQGLVHPQALAHQGLQHPHNPLLHGGRKMPDSDAP
Protein: MATH domain-containing protein (A0A178UXI0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSRPIPIEEMVRLFKIRHTTSHLFKIDNFSLLKKHGIEKVESSVFDLAGHKWKLSVYPNGHKNAKGTHVSMFLVNQVPVNDMPTYELLVVSQLERKWHTHGRDEFDINPEPASEGFLRFISLADLERKGFLIGDCCMFGVKFHGIEPANPGTAECFSLIEKPLNHKVTWMMSKFSSFNPGKAHQSNEFVVGTRKWRLEVHPRGYMDEKDKSFSVYLSAEGFVNNAPMTKTYAKFKLRVLDQVSWNHVEESGLSWFDAEPSDQSGFADFMPLGKLNEPYLVKDKLYVGVEFEVVSTTYYC
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (Q9TZQ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
Sequence:
MLPFTPQVVKRLLALKKGNEDNSVEGKWSEKAVKNLVKKIKKQLEELERAISTQNCQTRCVTVPRSKPAPAGEHLRKGLPHVIYCRLWRWPDLQSQNELKPLDHCEYAFHLRKEEICINPYHYKKIELSILVPKSLPTPPDSIVDYPLDNHTHQIPNNTDYNAAIIRSASLSPPQYMELGGAGPVSVSSSASSTPATAAGGGGGPSSSSSSSSSAASAYQQQQQQLSFGQNMDSQSSVLSVGSSIPNTGTPPPGYMSEDGDPIDPNDNMNMSRLTPPADAAPVMYHEPAFWCSISYYELNTRVGETFHASQPSITVDGFTDPSNSERFCLGLLSNVNRNEVVEQTRRHIGKGVRLYYIGGEVFAECLSDSSIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLSQSVSQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDRVLTQMGSPRLPCSSMS
Protein: Cardiolipin synthase A (CL synthase) (EC 2.7.8.-) (P0A6H8)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00190, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:1663113, ECO:0000269|PubMed:19341704}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00190, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:1663113}.
Interaction partners:
- Phosphatidylglycerophosphatase A
- Cardiolipin synthase C
- Cardiolipin synthase B
- Phosphatidylglycerophosphatase C
- Phosphatidylglycerophosphatase B
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidylserine decarboxylase proenzyme
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
- Phosphatidate cytidylyltransferase
Sequence:
MTTVYTLVSWLAILGYWLLIAGVTLRILMKRRAVPSAMAWLLIIYILPLVGIIAYLAVGELHLGKRRAERARAMWPSTAKWLNDLKACKHIFAEENSSVAAPLFKLCERRQGIAGVKGNQLQLMTESDDVMQALIRDIQLARHNIEMVFYIWQPGGMADQVAESLMAAARRGIHCRLMLDSAGSVAFFRSPWPELMRNAGIEVVEALKVNLMRVFLRRMDLRQHRKMIMIDNYIAYTGSMNMVDPRYFKQDAGVGQWIDLMARMEGPIATAMGIIYSCDWEIETGKRILPPPPDVNIMPFEQASGHTIHTIASGPGFPEDLIHQALLTAAYSAREYLIMTTPYFVPSDDLLHAICTAAQRGVDVSIILPRKNDSMLVGWASRAFFTELLAAGVKIYQFEGGLLHTKSVLVDGELSLVGTVNLDMRSLWLNFEITLAIDDKGFGADLAAVQDDYISRSRLLDARLWLKRPLWQRVAERLFYFFSPLL
Protein: Nucleolar protein 12 (O13741)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in pre-25S rRNA processing.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Ribosome biogenesis protein brx1
- ATP-dependent RNA helicase dbp9
- Uncharacterized WD repeat-containing protein C17D11.16
- Ribosome production factor 2 homolog
- Uncharacterized RNA-binding protein C4F6.14
- Probable metalloprotease arx1
- Ribosome biogenesis protein erb1
- Uncharacterized protein C4F10.09c
- Probable rRNA-processing protein ebp2
- AdoMet-dependent rRNA methyltransferase spb1
Sequence:
MGETNSSLDNENTSFVGKLSSSSNVDPTLNLLFSQSKPIPKPVAKETTVLTKKDVEVEEANGVEEAAETIESDTKEVQNIKPKSKKKKKKLNDSSDDIEGKYFEELLAEEDEEKDKDSAGLINDEEDKSPAKQSVLEERTSQEDVKSEREVAEKLANELEKSDKTVFVNNLPARVVTNKGDYKDLTKHFRQFGAVDSIRFRSLAFSEAIPRKVAFFEKKFHSERDTVNAYIVFRDSSSARSALSLNGTMFMDRHLRVDSVSHPMPQDTKRCVFVGNLAFEAEEEPLWRYFGDCGSIDYVRIVRDPKTNLGKGFAYIQFKDTMGVDKALLLNEKKMPEGRTLRIMRAKSTKPKSITRSKRGDEKTRTLQGRARKLIGKAGNALLQQELALEGHRAKPGENPLAKKKVNKKRKERAAQWRNKKAESVGKKQKTAAGKKDK
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit C (EC 2.4.1.198) (Phosphatidylinositol-glycan biosynthesis class C protein) (O64761)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis (Probable). Required for pollen germination and pollen tube growth.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Dolichol-phosphate mannose synthase subunit 2
- Phosphatidylinositolglycan-like protein
- N-acetylglucosaminyl transferase component family protein / Gpi1 family protein
- Phosphatidylinositol N-acetylglucosaminyltransferase, GPI19/PIG-P subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
- Mannosyltransferase APTG1
- N-acetylglucosaminylphosphatidylinositol deacetylase
- N-acetylglucosaminylphosphatidylinositol deacetylase
- GPI mannosyltransferase 1
Sequence:
MESNLAGDSIPGPKWRKVAYGGMQIGYDDNYTDESFLEEMVMNANVVRRDLLKVMKDSVSISQYLCIVALVVLVWVHTLESSLDENSLLLLDLSLLASGFLILLLTEEKMLSLSLLLRYLVNISFFTTGLYILAPIYQTLTRSISSDSIWAVTVSLLLLHLFLHDYSGSTIRAPGALKTPNLTSCISVNASIVASVFVASRLPSRLHVFAVMLFSLQVFLFAPLVTYCIKKFNFGLHLLFSFALMGLTLYSIYALHRLFFLVFLSLVLLVNVVCPYWLIRMQEYKFEINGPWDEAKLCFDITD
Protein: GPI-anchored protein LLG2 (LORELEI-like-GPI-anchored protein 2) (Q6NLF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FKT1}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
- Rapid alkalinization factor 23
- Receptor-like protein kinase FERONIA
- Receptor-like protein kinase ANXUR1
- Protein RALF-like 1
- Pollen-specific leucine-rich repeat extensin-like protein 4
- Receptor-like protein kinase ANXUR2
- Probable receptor-like protein kinase At2g21480
- Putative respiratory burst oxidase homolog protein H
- G-type lectin S-receptor-like serine/threonine-protein kinase RLK1
- Receptor-like protein kinase HERK 1
Sequence:
MEISPYCLLSLLPIFLLSGFSLSYDEFDGHAATSRALLQTRTTCKEDFANKNYTIITSRCKGPNYPANVCCSAFKDFACPFAEVLNDEKNDCASTMFSYINLYGRYPPGIFANMCKEGKEGLDCTDVTQSASATSDSIPRASTTASLAVLSTFLVLCLLFLSS
Protein: Taste receptor type 2 member 39 (T2R39) (Taste receptor type 2 member 57) (T2R57) (P59534)
Organism: Homo sapiens (Human)
Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Taste receptor type 1 member 2
- Taste receptor type 1 member 3
- Guanine nucleotide-binding protein G
- Taste receptor type 1 member 1
- Taste receptor type 2 member 1
Sequence:
MLGRCFPPDTKEKQQLRMTKLCDPAESELSPFLITLILAVLLAEYLIGIIANGFIMAIHAAEWVQNKAVSTSGRILVFLSVSRIALQSLMMLEITISSTSLSFYSEDAVYYAFKISFIFLNFCSLWFAAWLSFFYFVKIANFSYPLFLKLRWRITGLIPWLLWLSVFISFSHSMFCINICTVYCNNSFPIHSSNSTKKTYLSEINVVGLAFFFNLGIVTPLIMFILTATLLILSLKRHTLHMGSNATGSNDPSMEAHMGAIKAISYFLILYIFNAVALFIYLSNMFDINSLWNNLCQIIMAAYPASHSILLIQDNPGLRRAWKRLQLRLHLYPKEWTL
Protein: ECF RNA polymerase sigma factor SigD (ECF sigma factor SigD) (Alternative RNA polymerase sigma factor SigD) (RNA polymerase sigma-D factor) (Sigma-D factor) (P9WGG9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis.
Interaction partners:
- Anti-sigma-D factor RsdA
- ECF RNA polymerase sigma factor SigM
- ECF RNA polymerase sigma factor SigH
- RNA polymerase sigma factor SigF
- ECF RNA polymerase sigma factor SigG
- RNA polymerase sigma factor SigB
- Possible conserved transmembrane alanine and glycine rich protein
- Probable ECF RNA polymerase sigma factor SigI
- LuxR family transcriptional regulator
- Exported repetitive protein
Sequence:
MVDPGVSPGCVRFVTLEISPSMTMQGERLDAVVAEAVAGDRNALREVLETIRPIVVRYCRARVGTVERSGLSADDVAQEVCLATITALPRYRDRGRPFLAFLYGIAAHKVADAHRAAGRDRAYPAETLPERWSADAGPEQMAIEADSVTRMNELLEILPAKQREILILRVVVGLSAEETAAAVGSTTGAVRVAQHRALQRLKDEIVAAGDYA
Protein: Phosphatidate cytidylyltransferase 5, chloroplastic (EC 2.7.7.41) (CDP-DAG synthase 5) (CDP-DG synthase 5) (CDP-diacylglycerol synthase 5) (CDS 5) (CDP-diglyceride pyrophosphorylase 5) (CDP-diglyceride synthase 5) (CTP:phosphatidate cytidylyltransferase 5) (Q9M001)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the synthesis of minor phospholipids and in modulation of IP3-mediated signal transduction. Promotes the biosynthesis of plastidial phosphatidylglycerol (PG) which is required for structure and function of thylakoid membranes and, hence, for photoautotrophic growth.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:20442275}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Cardiolipin synthase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 1, chloroplastic/mitochondrial
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- Phosphatidate phosphatase PAH1
- Diacylglycerol kinase 5
- Phospholipase D zeta 1
- Phospholipase D zeta 2
Sequence:
MAPFVEVCRYKPLPLSLSSLCTCPCRSSPRKYLILPQFSEKYPKPLLSHSRFTPISVNRRVITAVARAESNQIGDDANSKEEHNIDQELQNVEEDSSLDDQKQKSRSQFKKRVTFGLGIGLSVGGIVLAGGWVFTVAVAAAVLLSAREYFELVRSKGIAQGMTPPPRYLSRVCSIICALMPILTLYFGHIDISITSAAFVVAMALLLQRGNPRFSQLSSTMFGLFYCGYLPCFWVKLRCGLTAPVLNTGIGRSWPTILGGQAHWTVGLVAILISFCGIIASDTFAFLGGKAFGRTPLISISPKKTWEGAFAGLVGCISITILLSKSLSWPQSLVSTIAFGVLNFFGSVFGDLTESMIKRDAGVKDSGSLIPGHGGILDRVDSYIFTGALAYSFVRLHGV
Protein: SMC5-SMC6 complex localization factor protein 2 (Smc5/6 localization factor 1) (Q8IX21)
Organism: Homo sapiens (Human)
Function: Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance. The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks. Promotes the recruitment of the SMC5-SMC6 complex to DNA lesions.
Subcellular location: Nucleus {ECO:0000269|PubMed:24561620, ECO:0000269|PubMed:25931565}. Nucleus, PML body {ECO:0000269|PubMed:36373674}. Note=Mainly localizes in the nucleus (PubMed:24561620). Colocalizes with PCNA on replication sites (PubMed:24561620). Associates with chromatin (PubMed:25931565). Accumulates with RAD18 and the SMC5-SMC6 complex at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner (PubMed:25931565). {ECO:0000269|PubMed:24561620, ECO:0000269|PubMed:25931565}.
Interaction partners:
- SMC5-SMC6 complex localization factor protein 1
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 6
- Non-structural maintenance of chromosomes element 1 homolog
- E3 ubiquitin-protein ligase RAD18
- Non-structural maintenance of chromosomes element 3 homolog
- E3 SUMO-protein ligase NSE2
- Non-structural maintenance of chromosomes element 4 homolog A
- Twinkle mtDNA helicase
Sequence:
MTRRCMPARPGFPSSPAPGSSPPRCHLRPGSTAHAAAGKRTESPGDRKQSIIDFFKPASKQDRHMLDSPQKSNIKYGGSRLSITGTEQFERKLSSPKESKPKRVPPEKSPIIEAFMKGVKEHHEDHGIHESRRPCLSLASKYLAKGTNIYVPSSYHLPKEMKSLKKKHRSPERRKSLFIHENNEKNDRDRGKTNADSKKQTTVAEADIFNNSSRSLSSRSSLSRHHPEESPLGAKFQLSLASYCRERELKRLRKEQMEQRINSENSFSEASSLSLKSSIERKYKPRQEQRKQNDIIPGKNNLSNVENGHLSRKRSSSDSWEPTSAGSKQNKFPEKRKRNSVDSDLKSTRESMIPKARESFLEKRPDGPHQKEKFIKHIALKTPGDVLRLEDISKEPSDETDGSSAGLAPSNSGNSGHHSTRNSDQIQVAGTKETKMQKPHLPLSQEKSAIKKASNLQKNKTASSTTKEKETKLPLLSRVPSAGSSLVPLNAKNCALPVSKKDKERSSSKECSGHSTESTKHKEHKAKTNKADSNVSSGKISGGPLRSEYGTPTKSPPAALEVVPCIPSPAAPSDKAPSEGESSGNSNAGSSALKRKLRGDFDSDEESLGYNLDSDEEEETLKSLEEIMALNFNQTPAATGKPPALSKGLRSQSSDYTGHVHPGTYTNTLERLVKEMEDTQRLDELQKQLQEDIRQGRGIKSPIRIGEEDSTDDEDGLLEEHKEFLKKFSVTIDAIPDHHPGEEIFNFLNSGKIFNQYTLDLRDSGFIGQSAVEKLILKSGKTDQIFLTTQGFLTSAYHYVQCPVPVLKWLFRMMSVHTDCIVSVQILSTLMEITIRNDTFSDSPVWPWIPSLSDVAAVFFNMGIDFRSLFPLENLQPDFNEDYLVSETQTTSRGKESEDSSYKPIFSTLPETNILNVVKFLGLCTSIHPEGYQDREIMLLILMLFKMSLEKQLKQIPLVDFQSLLINLMKNIRDWNTKVPELCLGINELSSHPHNLLWLVQLVPNWTSRGRQLRQCLSLVIISKLLDEKHEDVPNASNLQVSVLHRYLVQMKPSDLLKKMVLKKKAEQPDGIIDDSLHLELEKQAYYLTYILLHLVGEVSCSHSFSSGQRKHFVLLCGALEKHVKCDIREDARLFYRTKVKDLVARIHGKWQEIIQNCRPTQGQLHDFWVPDS
Protein: Zinc finger protein with KRAB and SCAN domains 3 (Zinc finger and SCAN domain-containing protein 13) (Zinc finger protein 306) (Zinc finger protein 309) (Zinc finger protein 47 homolog) (Zf47) (Zfp-47) (Q9BRR0)
Organism: Homo sapiens (Human)
Function: Transcriptional factor that binds to the consensus sequence 5'-[GT][AG][AGT]GGGG-3' and acts as a repressor of autophagy. Specifically represses expression of genes involved in autophagy and lysosome biogenesis/function such as MAP1LC3B, ULK1 or WIPI2. Associates with chromatin at the ITGB4 and VEGF promoters. Also acts as a transcription activator and promotes cancer cell progression and/or migration in various tumors and myelomas.
Subcellular location: Nucleus. Cytoplasm. Note=Mainly localizes in the nucleus. Under starvation conditions translocates to the cytoplasm, allowing expression of target genes involved in autophagy and lysosome biogenesis/function.
Interaction partners:
- Zinc finger protein 396
- Zinc finger and SCAN domain-containing protein 32
- Zinc finger protein 397
- Zinc finger protein with KRAB and SCAN domains 4
- Integrin beta-4
- PiggyBac transposable element-derived protein 1
- Zinc finger and SCAN domain-containing protein 20
- Zinc finger protein 24
- Zinc finger protein 232
- Zinc finger protein 444
Sequence:
MARELSESTALDAQSTEDQMELLVIKVEEEEAGFPSSPDLGSEGSRERFRGFRYPEAAGPREALSRLRELCRQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWVREQHPESGEEVVVLLEYLERQLDEPAPQVSGVDQGQELLCCKMALLTPAPGSQSSQFQLMKALLKHESVGSQPLQDRVLQVPVLAHGGCCREDKVVASRLTPESQGLLKVEDVALTLTPEWTQQDSSQGNLCRDEKQENHGSLVSLGDEKQTKSRDLPPAEELPEKEHGKISCHLREDIAQIPTCAEAGEQEGRLQRKQKNATGGRRHICHECGKSFAQSSGLSKHRRIHTGEKPYECEECGKAFIGSSALVIHQRVHTGEKPYECEECGKAFSHSSDLIKHQRTHTGEKPYECDDCGKTFSQSCSLLEHHRIHTGEKPYQCSMCGKAFRRSSHLLRHQRIHTGDKNVQEPEQGEAWKSRMESQLENVETPMSYKCNECERSFTQNTGLIEHQKIHTGEKPYQCNACGKGFTRISYLVQHQRSHVGKNILSQ
Protein: Protein Shroom2 (Protein Apxl) (A2ALU4)
Organism: Mus musculus (Mouse)
Function: May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:16684770}. Cell junction, tight junction {ECO:0000269|PubMed:16684770}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16684770}. Note=Associates with cortical F-actin.
Interaction partners:
- Rho-associated protein kinase 1
- Tight junction protein 1
Sequence:
MEGAEPRARPERLAEAEAPATDGVRLVEVQLSGGAPWGFTLKGGREHGEPLVITKIEEGSKAAAVDKLLAGDEIVAINDVSLSGFRQEAICLVKGSHKTLKLVVKRKSDPSWRPHSWHATKYFDVHPEPAASLFLNTSGSPSWKSQHQASSSSHDLSGSWEHTSLQRTSDHFSSMGSIDSLDHSSQLYPSGHLSSAKSNSSIDHLGGHSKRDSAYGSFSTCSSTPDHTLPKADASSTENILYKVGLWEASRPGSSRQSQSTGDPQGLQDRPSCFIPRVPGNSSKSPRPEDNVEPKIATHGRSNFGPVWYVPDKKKAPSPPPLGLPLRSDSFSVAARGHEKARGPPFSDLASMQHFITLPHVQPRGDHRMETTDRQWKLTHLSSGKEIGNVGYQSEGHLDCRWLCSDDRAGRPSGPPGRLQFSDVHFLKSYHGSQHQQQCSDESPRAPSSPRELLHITPGGGLQEPPEPSQDDNPTQVRWPGSAHQKLDDRGRSHYFPGSLRQPVQGSAQVVIPRGDYWHSDTTPVDLEYPLLRPVGQRTYLQQHEETPASHEKEGYHQLNAGIEGCCSGIQEPPRASRTVRTGLQCPSNDFKLVDGESGRISRQRTPMLHSLTQDGTWRPGNSKDCGNDKPPLFDAQVGKPTRRSDRFATTLRNEIQMRRAKLQKSKSTVTLAGDSEAEDCAGDWRADVGAVPEGSFPSTYKEHLKEAQTRVLKATSFQRRDLDPTPADQYSGPSEHRTFDHSASSSLSSFPGEPDSAPRFCETGLAKAPSSGVGVPHVLRIGGRKRFTAEQKLKSYSEPEKINEVGLSGDHRPHPTVRTPEDTVGTFADRWKFFEETSKSLLQKAGHRQVHCGLPREKAERPQTGHHECESTEPWFQKRSLATSCGEILSDRKVEKASEKLNPPRRLGTFAEYQASWKEQKKPLEARSSGRYHSADDILDAGLDQQQRPQYIHERSRSSPSTDHYSQEVPVEPNRQAEDSGDHKEAILCTLQAEEGCSAPSAQPQDSQHVNEDTTFPQPETQLSSKCQHLQTSAMETSRSPSPQFAPQKLTDKPPLLIHEDNSARIERVMDNNTTVKMVPIKIVHSESQPEKESRQSLACPAELPPLPSGLERDQIKTLSTSEQCYSRFCVYTRQEVEAPHRARPPEPRPPSTPAPPVRDSCSSPPSLNYGKAKEKTMDDLKSEELAREIVGKDKSLADILDPSVKIKTTMDLMEGIFPKDEYLLEEAQQRRKLLPKVPLPRVTEDKKQDPGMPGVVSLATNSTYYSTSAPKAELLIKMKDLQEPEEYSAGDLDHDLSVKKQELIDSISRKLQVLREARESLLEDIQANNALGDEVEAIVKDVCKPNEFDKFRMFIGDLDKVVNLLLSLSGRLARVENALNNLDDNPSPGDRQSLLEKQRVLTQQHEDAKELKENLDRRERIVFDILATYLSEENLADYEHFVKMKSALIIEQRELEDKIHLGEEQLKCLFDSLQPERSK
Protein: Transketolase 1 (TK 1) (EC 2.2.1.1) (P27302)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Thus, catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate.
Interaction partners:
- Ribulose-phosphate 3-epimerase
- Transaldolase B
- Transaldolase A
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase class 2
- Ribose-5-phosphate isomerase A
- Phosphoenolpyruvate synthase
- Triosephosphate isomerase
- Pyruvate kinase I
- Fructose-1,6-bisphosphatase class 1
Sequence:
MSSRKELANAIRALSMDAVQKAKSGHPGAPMGMADIAEVLWRDFLKHNPQNPSWADRDRFVLSNGHGSMLIYSLLHLTGYDLPMEELKNFRQLHSKTPGHPEVGYTAGVETTTGPLGQGIANAVGMAIAEKTLAAQFNRPGHDIVDHYTYAFMGDGCMMEGISHEVCSLAGTLKLGKLIAFYDDNGISIDGHVEGWFTDDTAMRFEAYGWHVIRDIDGHDAASIKRAVEEARAVTDKPSLLMCKTIIGFGSPNKAGTHDSHGAPLGDAEIALTREQLGWKYAPFEIPSEIYAQWDAKEAGQAKESAWNEKFAAYAKAYPQEAAEFTRRMKGEMPSDFDAKAKEFIAKLQANPAKIASRKASQNAIEAFGPLLPEFLGGSADLAPSNLTLWSGSKAINEDAAGNYIHYGVREFGMTAIANGISLHGGFLPYTSTFLMFVEYARNAVRMAALMKQRQVMVYTHDSIGLGEDGPTHQPVEQVASLRVTPNMSTWRPCDQVESAVAWKYGVERQDGPTALILSRQNLAQQERTEEQLANIARGGYVLKDCAGQPELIFIATGSEVELAVAAYEKLTAEGVKARVVSMPSTDAFDKQDAAYRESVLPKAVTARVAVEAGIADYWYKYVGLNGAIVGMTTFGESAPAELLFEEFGFTVDNVVAKAKELL
Protein: Lactaldehyde reductase (EC 1.1.1.77) (Propanediol oxidoreductase) (P0A9S1)
Organism: Escherichia coli (strain K12)
Interaction partners:
- L-fuculose phosphate aldolase
- Glycerol dehydrogenase
- Acetaldehyde dehydrogenase
- Lactaldehyde dehydrogenase
- Aldehyde reductase Ahr
- Alcohol dehydrogenase, propanol-preferring
- L-fuculokinase
- Putative 2-dehydro-3-deoxy-D-gluconate aldolase YagE
- L-fucose isomerase
- Oxidoreductase UcpA
Sequence:
MANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAGEEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELYHTAW
Protein: NAD(P)-binding domain-containing protein (Q54U38)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- NADH-ubiquinone oxidoreductase subunit 9
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase 23 kDa subunit
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase 49 kDa subunit
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- Cytochrome c1, heme protein, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4
- NADH dehydrogenase flavoprotein 2, mitochondrial
Sequence:
MKKFYFILITSIAFIFQYIYNNSGYFINTISENSEISNYKPYNFKYYNMSQGAKCIVIGGTGATGKHLIRELIDSKFVQVTSLVRKEDLSIQNEKLKQVVVDFDKLEDYKEEFKDKDAAFNVLGTTRKQAGSAERFREIELGISSKFADLSKESGVRSMHLLTSTGSNPNSFFLYPKVKGEIEEKMKKEGFHYLSIFRPGFLDRGVGDRWIENVFIKVVSPMKVSTLAKAMRIEAENELLNSPPSNTVKIYSNKEIYEIVGEK