wanglab/gogpt-training-data huggingface dataset:
Protein: Sodium/hydrogen exchanger (Q9U624)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.
Interaction partners:
Sequence:
MLLIVGFALCVLAPGCSATDTDIALDAKATLNHRIQSLDLLVFVFLLALTVLTIWLFKHHRVSWLHETGLAVIYGLIVGAIIRYAGTSGTLDHMQVEPQGVPTYSDKLPPDTLWFRYPVNQTNGTKPPEGIKTYAYVFRGQVHDVDENEIDLKATFDPEVFFNIILPPIIFYAGYCLKKKYFFRNLGAILTFAIVGTTLSAFLIGGFMYGCVKLMPKYLSSSFTFLDSLYFGALISPTDPLTILAIFNDLRVDVNLYALVLGESVLNDAVAIVLSGAIQNYGEHYSNTGEFETTAFLRSLSDFFSIFLLSLMIGAAMGCLTALMTKFTRVRDFPLLESALFVLMSYSTFLLAEATELTGVVAVLFCGICQAHYTYNNLSEDSRQRTKQIFELLNFLAENFIFSYIGVSMFTFPKHHFDAGFIITAFICAAIGRAVNVYPLSWLLNIKRKPKISTNFQHMLFFAGLRGAMSFALAIRNTVSDERQTMLTATSLIVIFTVVIQGGAANFLLNWLKIPVGVDDETEQLNNYQVHSSDGYLQDVEGGGVNRNKMRLSGGTDTNLDTPVDGTNGSLGGASGGRRRNSHEKAILARIWGNFDTKYMKPLLTHSRPTLLETLPVCCNPIARLLTTTQQLTQDGSEFRRVDSDSDICIDNDTGNGLSQDGSGAAPGVGRRNSLSRVGGDHRNAYI
Protein: Mesencephalic astrocyte-derived neurotrophic factor precursor (Zgc:153327) (Q08CA7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLYLSGLSVAFALALVPSCSDALKDGECEVCVGFLQRLYQTIQENNVKFDSDSIEKALLKSCKDAKGKENRFCYYIGATSDAATKITNEVSKPMSYHVPVEKICEKLKKKDSQICELKYDKQVDLSSVDLKKLKVKDLKKILEEWGESCKGCVEKSDFIRKINELMPKYAPSAAKARTDL
Protein: Transcription factor HES-7 (mHes7) (Hairy and enhancer of split 7) (bHLH factor Hes7) (Q8BKT2)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor. Represses transcription from both N box- and E box-containing promoters. May with HES1, cooperatively regulate somite formation in the presomitic mesoderm (PSM). May function as a segmentation clock, which is essential for coordinated somite segmentation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
- Mesoderm posterior 2
Sequence:
MVTRERAENRDGPKMLKPLVEKRRRDRINRSLEELRLLLLERTRDQNLRNPKLEKAEILEFAVGYLRERSRVEPPGVPRSPGQDAEALASCYLSGFRECLLRLAAFAHDASPAARSQLFSALHGYRRPKPPRPEAVDPGLPAPRPPLDPASPILGPALHQRPPVHQGPPSPRLAWSPSHCSSRAGDSGAPAPLTGLLPPPPPPYRQDGAPKAPSLPPPAFWRPWP
Protein: Decorin (Bone proteoglycan II) (B5X3L8)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|PIRNR:PIRNR002490, ECO:0000256|RuleBase:RU364097}.
Interaction partners:
Sequence:
MRSACLSLLLVTACWSLPFRQSGFLDFMMEDEAGSGLPEVPIEPSVDIPTMPEGPKCPFRCQCHLRVVQCSDLGLKSVPDEIPADSTLLDLQNNKITEIKENDFKTLKGLQTLILVNNQITIIHPKAFIPLGKLQRLYLSKNHLKEMPANMPKSLQELRIHENKITKIKKASFEGMAQVIVMELGSNPLKSAGVEAGAFGALKKVSYIRIADTNLTEIPKGLPSSLSELHLDSNKITKVQADNLKGLKNLAKLGLSYNEISQVENGSLAMVPHLRELHLDNNALTTVPAGLPDHKYIQVIYLHSNKIGVVGTQDFCPPGYNTKKAMYSGISLFSNPVPYWEVQPITFRCVFDRSAIQLGNYRKK
Protein: Collagen alpha-1(IX) chain (P20849)
Organism: Homo sapiens (Human)
Function: Structural component of hyaline cartilage and vitreous of the eye.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-3
- Collagen alpha-2
- Collagen alpha-1
- CD44 antigen
- Platelet glycoprotein VI
- Matrilin-3
- Hyaluronan and proteoglycan link protein 1
- Sulfate transporter
- Collagen alpha-1
- Integrin alpha-2
Sequence:
MKTCWKIPVFFFVCSFLEPWASAAVKRRPRFPVNSNSNGGNELCPKIRIGQDDLPGFDLISQFQVDKAASRRAIQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGSTLKKNWNIWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLSSLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPRGPIDIDGFAVLGKLADNPQVSVPFELQWMLIHCDPLRPRRETCHELPARITPSQTTDERGPPGEQGPPGPPGPPGVPGIDGIDGDRGPKGPPGPPGPAGEPGKPGAPGKPGTPGADGLTGPDGSPGSIGSKGQKGEPGVPGSRGFPGRGIPGPPGPPGTAGLPGELGRVGPVGDPGRRGPPGPPGPPGPRGTIGFHDGDPLCPNACPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGTKGEPGKPGPPGDAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSLGSPGLPGLPGPPGLPGMKGDRGVVGEPGPKGEQGASGEEGEAGERGELGDIGLPGPKGSAGNPGEPGLRGPEGSRGLPGVEGPRGPPGPRGVQGEQGATGLPGVQGPPGRAPTDQHIKQVCMRVIQEHFAEMAASLKRPDSGATGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPGRGPNGLPGAIGLPGDPGPASYGRNGRDGERGPPGVAGIPGVPGPPGPPGLPGFCEPASCTMQAGQRAFNKGPDP
Protein: Nuclear autoantigen Sp-100 (Nuclear dot-associated Sp100 protein) (Speckled 100 kDa) (O35892)
Organism: Mus musculus (Mouse)
Function: Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. May also play a role in infection by viruses through mechanisms that may involve chromatin and/or transcriptional regulation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P23497}. Nucleus, PML body {ECO:0000250|UniProtKB:P23497}. Nucleus, nuclear body {ECO:0000250|UniProtKB:P23497}. Cytoplasm {ECO:0000250|UniProtKB:P23497}. Note=Accumulates in the cytoplasm upon FAS activation. {ECO:0000250|UniProtKB:P23497}.
Interaction partners:
- Death domain-associated protein 6
- Transcriptional regulator ATRX
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 2
- SUMO-conjugating enzyme UBC9
- Nuclear pore membrane glycoprotein 210
- Interferon regulatory factor 7
- Protein PML
- Nibrin
- Double-strand break repair protein MRE11
Sequence:
MEGSDGSPRMSTEQENTEMHLIECMLKHFKTQKVAISNAIRSTFPFLESLRDHEFITGKMYEDLLDSCRSLVPVDKVIYRALEELEKKFDMTVLCELFNEVNMEKYPDLNLIRRSFGCVFPNELCFQGIDGGNPNSQLSLEQGPGASYSQGSPNGSSLDLSASEGWRSNDRRNSNLMQANQTENHQLAESPGHLDSCELQVQLNNRDATPESCSLLPQNEERAVQLNYELQINPCFVQLVDVKKENSSFSLAGNQQTRARTNQNEDSEIIELSSGDSDNGENFSEATTTVPSQPAPAYSRKPPTLRRDRGGDTSDTESSIIIRRRKRTGRKKRERLGSYLIRNIKIPMKPSWKTAFLARSANPSSQRRRKRGPRIPREENADFGGAELPVVCGNAQGFLDKEKFKQGIYVRSIRGKTGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVLQDPPRKKKETPRNPRQTRRQVNAL
Protein: Solute carrier family 23 member 2 (Na(+)/L-ascorbic acid transporter 2) (Sodium-dependent vitamin C transporter 2) (SVCT-2) (mSVCT2) (Yolk sac permease-like molecule 2) (Q9EPR4)
Organism: Mus musculus (Mouse)
Function: Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9UGH3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UGH3}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Uridine 5'-monophosphate synthase
Sequence:
MMGIGKNTASKSVEAGGSTEGKYEEEAKHSNFFTLPVVINGGATSSGEQDNEDTELMAIYTTENGIAEKSSLAETLDSTGSLDPQRSDMIYTIEDVPPWYLCIFLGLQHYLTCFSGTIAVPFLLADAMCVGDDQWATSQLIGTIFFCVGITTLLQTTFGCRLPLFQASAFAFLAPARAILSLDKWKCNTTEITVANGTAELLEHIWHPRIQEIQGAIIMSSLIEVVIGLLGLPGALLRYIGPLTITPTVALIGLSGFQAAGERAGKHWGIAMLTIFLVLLFSQYARNVKFPLPIYKSKKGWTAYKFQLFKMFPIILAILVSWLLCFIFTVTDVFPSNSTDYGYYARTDARKGVLLVAPWFKVPYPFQWGMPTVSAAGVIGMLSAVVASIIESIGDYYACARLSCAPPPPIHAINRGIFVEGLSCVLDGIFGTGNGSTSSSPNIGVLGITKVGSRRVIQYGAALMLGLGMVGKFSALFASLPDPVLGALFCTLFGMITAVGLSNLQFIDLNSSRNLFVLGFSIFFGLVLPSYLRQNPLVTGITGIDQILNVLLTTAMFVGGCVAFILDNTIPGTPEERGIKKWKKGVSKGSKSLDGMESYNLPFGMNIIKKYRCFSYLPISPTFAGYTWKGFGKSENSRSSDKDSQATV
Protein: Mast/stem cell growth factor receptor (EC 2.7.10.1) (A0A0G2JTL4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU000311}.
Interaction partners:
Sequence:
PLCKPHHKDRPPSLGTSQPSASPGEPSPPSIQPAQSELIVEAGDTIRLTCTDPAFVKWTFEILDVRIENKQSEWIREKAEATHTGKYTCVSGSGLRSSIYVFVRDPAVLFLVGLPLFGKEDNDALVRCPLTDPQVSNYSLIECDGKSLPTDLKFVPNPKAGITIKNVKRAYHRLCIRCAAQREGKWMRSDKFTLKVRAAIKAIPVVSVPETSHLLKEGDTFTVICTIKDVSTSVDSMWIKLNPQPQSKAQVKRNSWHQGDFNYERQETLTISSARVNDSGVFMCYANNTFGSANVTTTLKVVEKGFINIFPVKNTTVFVTDGENVDLVVEFEAYPKPEHQQWIYMNRTPTNRGEDYVKSDNQSNIRYVNELRLTRLKGTEGGTYTFLVSNSDVSASVTFDVYVNTKPEILTYDRLMNGRLQCVAAGFPEPTIDWYFCTGAEQRCTVPVPPVDVQIQNASVSPFGKLVVQSSIDSSVFRHNGTVECKASNAVGKSSAFFNFAFKGNSKEQIQPHTLFTPLLIGFVVTAGLMGIIVMVLAYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSFIFSKQEEQADAALYKNLLHSKESSCDSSNEYMDMKPGVSYVVPTKTDKRRSARIDSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAAMYEVMKTCWDADPLKRPTFKQVVQLIEKQISDSSKHIYSNLANCNPNPENPVVVDHSVRVNSVGSSTSSTQPLLVHEDA
Protein: Homeobox protein goosecoid (ZGSC) (P53544)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus.
Interaction partners:
- Chordin
- T-box transcription factor T-A
- RRP15-like protein
- MOB-like protein phocein
- TAR DNA-binding protein 43
- Pre-mRNA-splicing factor ISY1 homolog
- Centrosomal protein 20
- WD repeat-containing protein 26
- Tektin 2
- Zinc finger protein 330.
Sequence:
MPAGMFSIDSILAGRPSCKDSVLLHRNAPVVFSNLTESLYTAAGDFNGLYSHTGPPAPNLQSVNGRIGYNNYYYGQLHVQGPTGPACCGAIPTLGSQQCPCIPTGYDSAGSVLISPVPHQMMSYMNVGTLSRTELQLLNQLHCRRKRRHRTIFTDEQLEALENLFQETKYPDVGTREQLARKVHLREEKVEVWFKNRRAKWRRQKRSSSEESENSQKWNKSTKTTSEKIEEGKSDVDSDS
Protein: Dampened, isoform A (Dampened, isoform B) (GM04147p) (Q7K2J4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Fates-shifted
Sequence:
MVSTRQMCSGGGTSASEGVSPFGGAGSGSASGTGMASGSAVSSGSGTGVQEPPESTANRSSVLRRTTSYQGNQAHSSYRVVSAGSLAESASAVTRLHSYTMQMQRQRPPTATTTTTTSAPSLYDLPNELIEKILSYVDYKKVSNLRLVSHRMNDICMAMLNTAFTKQIKTTLSRFQAIKASMPRRESHRRNHPLACECDIIETCYMRLSLLQMSMGKHIERGHCCFFPGAILDEVQAILNYISITPRLQRPYRVTDELFDLSTMAMEYFKDRIEATLPGLAYFNKDFYTLPTTTKRPTLAISSDLEDSASNSPPQNHMVLRKGIRKIKQGMKMYNNQLSVLRTELRTCKRKAAEQSKQLAEQSNLISEQQKQTLEYANRLDENDKKNEEMSRKFSTLLQELNKCKTELQFWRSKSPAIPAVCSSCNQKVAPVVPPEDFQALVNQGVDPEHFIIINEDVDAESDVSVGELKEFASPDESTTAKLLAVSTAAKNLKRKMPSESQSNAIASTSKAAEVAQSQSQPMATGNAGAAKAAGGYSPKLFYGNHQRSGVIVSPVSQNLGVAATTDNVAPGSEALEEPEEAKKARRVQKANRYVNTPGKRSK
Protein: Uncharacterized protein YEL067C (P39978)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MAFTTIRSLTIFSGSSFDMPTFFVLAKGGDGSGVFFISLHSSILYARFPLLNILSQHSPVYCSRRFPPDNDLITGLGNIRCGQLVKKALRRVCNVPPDHQLIASVRSIGYARVAFVFCTCTSECRDNLQSVTRTSGHQTTISQPCTDIQSTRKCSTIFVSAVMQTGTITFFWTFHFPIPLQRIVNQKQPPPQSYV
Protein: Nuclear factor 1 A-type (NF1-A) (Nuclear factor 1/A) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/A) (NF-I/A) (NFI-A) (TGGCA-binding protein) (Q02780)
Organism: Mus musculus (Mouse)
Function: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor SOX-9
Sequence:
MKLADSVMAGKASDGSIKWQLCYDISARTWWMDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKEEERAVKDELLSEKPEVKQKWASRLLAKLRKDIRPEYREDFVLTVTGKKPPCCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKSPQCSNPGLCVQPHHIGVSVKELDLYLAYFVHAADSSQSESPSQPSEADIKDQPENGHLGFQDSFVTSGVFSVTELVRVSQTPIAAGTGPNFSLSDLESSSYYSMSPGAMRRSLPSTSSTSSTKRLKSVEDEMDSPGEEPFYTGQGRSPGSGSQSSGWHEVEPGLPSPSTLKKSEKSGFSSPSPSQTSSLGTAFTQHHRPVITGPRASPHATPSTLHFPTSPIIQQPGPYFSHPAIRYHPQETLKEFVQLVCPDAGQQAGQVGFLNPNGSSQGKVHNPFLPTPMLPPPPPPPMARPVPLPMPDTKPPTTSTEGGAASPTSPTYSTPSTSPANRFVSVGPRDPSFVNIPQQTQSWYLG
Protein: Histone H3.3 (P10651)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H4
- Histone H2B-alpha
- Chromo domain-containing protein 1
- Histone H3.1/H3.2
- Histone H2A-beta
- Histone H2A.Z
- Histone H2A-alpha
- FACT complex subunit spt16
- Histone chaperone cia1
- CENP-A histone chaperone scm3
Sequence:
MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPPTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS
Protein: FHA domain-containing protein FhaA (P71590)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Regulates cell growth and peptidoglycan synthesis by binding to MviN. May inhibit the late stages of peptidoglycan synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22275220}. Note=Localizes at the cell poles and at the septum.
Interaction partners:
- Probable peptidoglycan biosynthesis protein MviN
- Serine/threonine-protein kinase PknB
- Multifunctional 2-oxoglutarate metabolism enzyme
- FHA domain-containing protein FhaB
- Serine/threonine-protein kinase PknA
- Serine/threonine protein phosphatase PstP
- Peptidoglycan D,D-transpeptidase PbpA
- Peptidoglycan glycosyltransferase RodA
- N-acetylmuramoyl-L-alanine amidase CwlM
- Serine/threonine-protein kinase PknE
Sequence:
MGSQKRLVQRVERKLEQTVGDAFARIFGGSIVPQEVEALLRREAADGIQSLQGNRLLAPNEYIITLGVHDFEKLGADPELKSTGFARDLADYIQEQGWQTYGDVVVRFEQSSNLHTGQFRARGTVNPDVETHPPVIDCARPQSNHAFGAEPGVAPMSDNSSYRGGQGQGRPDEYYDDRYARPQEDPRGGPDPQGGSDPRGGYPPETGGYPPQPGYPRPRHPDQGDYPEQIGYPDQGGYPEQRGYPEQRGYPDQRGYQDQGRGYPDQGQGGYPPPYEQRPPVSPGPAAGYGAPGYDQGYRQSGGYGPSPGGGQPGYGGYGEYGRGPARHEEGSYVPSGPPGPPEQRPAYPDQGGYDQGYQQGATTYGRQDYGGGADYTRYTESPRVPGYAPQGGGYAEPAGRDYDYGQSGAPDYGQPAPGGYSGYGQGGYGSAGTSVTLQLDDGSGRTYQLREGSNIIGRGQDAQFRLPDTGVSRRHLEIRWDGQVALLADLNSTNGTTVNNAPVQEWQLADGDVIRLGHSEIIVRMH
Protein: Retinoic acid early transcript 1G (C9JAK3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAAASPAFLLRLPLLLLLSSWCRTGLADPHSLCYDITVIPKFRPGPRWCAVQGQVDEKTFLHYDCGSKTVTPVSPLGKKLNVTTAWKAQNPVLREVVDILTEQLLDIQLENYIPKEPLTLQARMSCEQKAEGHGSGSWQLSFDGQIFLLFDSENRMWTTVHPGARKMKEKWENDKDMTMSFHYISMGDCTGWLEDFLMGMDSTLEPSAGGNRRKRNGDLQ
Protein: Crystaline entomocidal protoxin (S5VRK7)
Organism: Bacillus thuringiensis
Interaction partners:
Sequence:
MILLVQLSDLLPSYYNVLASPPTILDANQDWFPTGNDFKSVINELKDAFTKFQKDFHTSDLINTIQSIYNSYGSQGMDWVNVAQAVITFAFGFVPGGSLVSAGLNKIIGIFFPKDPNPTVFDQIKAAVEQLILNSFITYDIQGDITELNKLKDYSGILANSIQVALGQSQFQEFQQVNPTGPPTNCTHTPSCTLDPTNPIPPNCSCLLNFVYQNYNNHTSDINTVLLQIEGSIPKIFALINQSTTATTAQKNQLKSDYLQAYLPLYVMGATLEMIYYRTYIQFAETFQYGLSEQNSTTLTAMHNLRLTISRRTTFLFNNFLPFLPSITSNTKGDLNSYIQYTRRITINALDTAVFWTLLDPFDYPVSANQTLSRIIFNDIVGPVECKAGNQNSNNLLFNFYNVDGQPLPNNSITNYFYNNMQLRGLQFQIYKYSSTSTYFSTTSDIPIGFKASYRTNGSDKNIDHTRSLPYGLKGSTTTLTDDIYITNPSFNIINMNSSQTSGQIATDVSQILYTPISDIKQNCFSQNSPYLGNNRIQAIYPLQPTNPNTYNAYGSTDKLGFLTTLISNDTTTNLVFTSDPIYTFPAEQATVLSGTKLVEYVNGTASVQLQNGQNAQYTIDNTTRIAGPTQFQLRVHVATDPAVTDPNVLGQLAITIDNQRTQYLTIPNTNVDYSNPITLLNGQQLNQLRVKGTQGAYMLVPASNLNNINDRNTNVFTLNPNASMNVNIQNTGNLTVILDRIEFVPIDSTVIIPAQTLYSNQAYTLWESTNGLIGKQALLVVDDYLHFTVQYYYQSQLVHSNEQNIYDVNYIGLFDKITASTIADTLVNLTNGIVYLTTNTTPTPTPAVPSPIPPISNQNIGAGFEYTVWDGNNKTGNTVNFQGFAAPNSGSEGLLFQYKYNDQVIDTDQVSNQFSIQRKLAGTINKITATGGTPNGVYLTINNGGSVSTT
Protein: Serine/threonine-protein kinase Nek8 (EC 2.7.11.1) (Never in mitosis A-related kinase 8) (NimA-related protein kinase 8) (Nima-related protein kinase 12a) (Q86SG6)
Organism: Homo sapiens (Human)
Function: Required for renal tubular integrity. May regulate local cytoskeletal structure in kidney tubule epithelial cells. May regulate ciliary biogenesis through targeting of proteins to the cilia (By similarity). Plays a role in organogenesis and is involved in the regulation of the Hippo signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18199800}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91ZR4}. Cell projection, cilium {ECO:0000269|PubMed:18199800}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18199800}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:26967905}. Note=Predominantly cytoplasmic. Localizes to the proximal region of the primary cilium and is not observed in dividing cells. {ECO:0000250|UniProtKB:Q91ZR4}.
Interaction partners:
- Ankyrin repeat and SAM domain-containing protein 6
- Nephrocystin-3
- Inversin
- Ankyrin repeat and SAM domain-containing protein 3
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Nephrocystin-4
- Polycystin-1
- Polycystin-2
- Sorcin
- Nephrocystin-1
Sequence:
MEKYERIRVVGRGAFGIVHLCLRKADQKLVIIKQIPVEQMTKEERQAAQNECQVLKLLNHPNVIEYYENFLEDKALMIAMEYAPGGTLAEFIQKRCNSLLEEETILHFFVQILLALHHVHTHLILHRDLKTQNILLDKHRMVVKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMSGTFAPISDRYSPELRQLVLSLLSLEPAQRPPLSHIMAQPLCIRALLNLHTDVGSVRMRRAEKSVAPSNTGSRTTSVRCRGIPRGPVRPAIPPPLSSVYAWGGGLGTPLRLPMLNTEVVQVAAGRTQKAGVTRSGRLILWEAPPLGAGGGSLLPGAVEQPQPQFISRFLEGQSGVTIKHVACGDFFTACLTDRGIIMTFGSGSNGCLGHGSLTDISQPTIVEALLGYEMVQVACGASHVLALSTERELFAWGRGDSGRLGLGTRESHSCPQQVPMPPGQEAQRVVCGIDSSMILTVPGQALACGSNRFNKLGLDHLSLGEEPVPHQQVEEALSFTLLGSAPLDQEPLLSIDLGTAHSAAVTASGDCYTFGSNQHGQLGTNTRRGSRAPCKVQGLEGIKMAMVACGDAFTVAIGAESEVYSWGKGARGRLGRRDEDAGLPRPVQLDETHPYTVTSVSCCHGNTLLAVRSVTDEPVPP
Protein: Snake venom metalloproteinase atroxlysin-1 (SVMP) (EC 3.4.24.-) (Atroxlysin-I) (P85420)
Organism: Bothrops atrox (Barba amarilla) (Fer-de-lance)
Function: Snake venom zinc metalloproteinase that acts on fibrinogen, fibrin, fibronectin (FN1), type I collagen, type IV collagen, integrin alpha-7/beta-1 (ITGA7/ITGB1) and integrin alpha-1/beta-1 (ITGA1/ITGB1). Binds to fibronectin (FN1), fibrinogen and, weakly, to type I collagen and laminin. Cleaves Xaa-Leu bonds. Inhibits ADP- and collagen-induced platelet aggregation both in the presence (IC(50)=1.4 uM for collagen) and in the absence (IC(50)=2.2 uM for collagen) of cofactors. Has hemorrhagic activity.
Subcellular location: Secreted {ECO:0000269|PubMed:20102699}.
Interaction partners:
Sequence:
TPEQQRYVDLFIVVDHGMFMKYNGNSDKIRRRIHQMVNIMKEAYSTMYIDILLTGVEIWSNKDLINVQPAAPQTLDSFGEWRKTDLLNRKSHDNAQLLTSTDFNGPTIGLAYVGSMCDPKRSTGVIQDHSEQDLMVAITMAHELGHNLGISHDTGSCSCGGYSCIMSPVLSHEPSKYFSDCSYIQCWDFIMKENPQCILNKR
Protein: DNA ligase (EC 6.5.1.1) (Q5U2M4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTLAFKTLFPRNLCALGRKELCLFSEQHHWPAIRQFSQWSETNLLCGCCLLQRRKPVLSFQRGHLRPRATHLISWSGSHVGLCTGPCEMAEQRFCVDYAKRGTAGCKKCKEKIVKGVCRIGKVVPNPFSESGGDMKEWYHIKCMFEKLERARATTKKIEDLTELEGWEELEDNEKEQISQHIADLSSKTAATPKKKATVQAKLTTTGQVTSPVKGASFITSTNPRKFSGFSAAKPNNSEQDPSSPAPKTSLSASKCDPKHKDCLLREFRKLCAMVAENPSYNTKTQIIHDFLQKGSTGDGFRGDVYLTVKLLLPGVIKSVYNLNDKQIVKLFSRIFNCNPDDMARDLEQGDVSETIRVFFEQSKSFPPAAKSLLTIQEVDAFLLHLSKLTKEDEQQQALQDIASRCTANDLKCIIRLIKHDLKMNSGAKHVLDALDPNAYEAFKASRNLQDVVERVLHNEQEVEKDPGRRRALSVQASLMTPVQPMLAEACKSIEYAMKKCPNGMFSEIKYDGERVQVHKKGDHFSYFSRSLKPVLPHKVAHFKDYIPKAFPGGQSMILDSEVLLIDNNTGKPLPFGTLGVHKKAAFQDANVCLFVFDCIYFNDVSLMDRPLCERRKFLHDNMVEIRNRIMFSEMKQVTKASDLADMINRVIREGLEGLVLKDVKGTYEPGKRHWLKVKKDYLNEGAMADTADLVVLGAFYGQGSKGGMMSIFLMGCYDPDSQKWCTVTKCAGGHDDATLARLQKELDMVKISKDPSKIPSWLKINKIYYPDFIVPDPKKAAVWEITGAEFSRSEAHTADGISIRFPRCTRIRDDKDWKSATNLPQLKELYQLSKDKADFAVVAGDEGSSTTGGSNGENEGTAGSTVPRKGPKGPPSKSSASAKKTEQKLNDPSSRGGEKLAVKSSPVKVGMKRKAADETPGLTKRRRASRQRGRRAMRTGRR
Protein: Frizzled-7 (Fz-7) (hFz7) (FzE3) (O75084)
Organism: Homo sapiens (Human)
Function: Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by WNT8 induces expression of beta-catenin target genes (By similarity). Following ligand activation, binds to CCDC88C/DAPLE which displaces DVL1 from FZD7 and leads to inhibition of canonical Wnt signaling, activation of G-proteins by CCDC88C and triggering of non-canonical Wnt responses. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27386966}; Multi-pass membrane protein {ECO:0000269|PubMed:27386966}. Endosome membrane {ECO:0000269|PubMed:27386966}; Multi-pass membrane protein {ECO:0000269|PubMed:27386966}. Note=Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2). Localized in recycling endosomes in other conditions. {ECO:0000269|PubMed:27386966}.
Interaction partners:
- Protein Wnt-5a
- Protein Wnt-11
- Protein Wnt-7a
- Segment polarity protein dishevelled homolog DVL-1
- Low-density lipoprotein receptor-related protein 6
- Proto-oncogene Wnt-1
- Syndecan-4
- Proto-oncogene Wnt-3
- Protein Wnt-7b
- Segment polarity protein dishevelled homolog DVL-2
Sequence:
MRDPGAAAPLSSLGLCALVLALLGALSAGAGAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGPGGGPTAYPTAPYLPDLPFTALPPGASDGRGRPAFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFSDDGYRTVAQGTKKEGCTILFMVLYFFGMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDLLSGVCYVGLSSVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVLACYFYEQAFREHWERTWLLQTCKSYAVPCPPGHFPPMSPDFTVFMIKYLMTMIVGITTGFWIWSGKTLQSWRRFYHRLSHSSKGETAV
Protein: Protein MODIFYING WALL LIGNIN-1 (MWL-1) (A2RVU1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with MWL2, contributes to secondary cell wall biology, specifically lignin biosynthesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26930070}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- At4g27438
- At1g52910
- Protein DESIGUAL 2
- E3 ubiquitin-protein ligase WAV3
- Glutamate receptor 2.8
- 7-dehydrocholesterol reductase-like protein
- Cysteine-rich receptor-like protein kinase 19
- Calcium-transporting ATPase 9, plasma membrane-type
Sequence:
MFIFLFGLAAFFLCLSAEFQKAKALLRAQVFLKGKDLKWDGESCYLPENRAFGLGIAALVCVSVAQIVGNVVICRGFTKTDKTRTTIFCIILLLFSWVNFAVAVTLISVGASMNREQIYGKGWLNRECYLVKDGVFAASGFLSVTTMAAILGAFAFKVKPSLQVENHDKRHTQNV