wanglab/gogpt-training-data huggingface dataset:
Protein: Tubulin monoglycylase TTLL3 (EC 6.3.2.-) (HOTTL) (Tubulin--tyrosine ligase-like protein 3) (Q9Y4R7)
Organism: Homo sapiens (Human)
Function: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction (By similarity). Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases (By similarity). Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance (By similarity). Involved in microtubule glycylation of primary cilia in colon which controls cell proliferation of epithelial cells and plays an essential role in colon cancer development. Together with TTLL8, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25180231}. Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A4Q9E5}.
Interaction partners:
Sequence:
MNRLRNAKIYVERAVKQKKIFTIQGCYPVIRCLLRRRGWVEKKMVHRSGPTLLPPQKDLDSSAMGDSDTTEDEDEDEDEEFQPSQLFDFDDLLKFDDLDGTHALMVGLCLNLRNLPWFDEVDANSFFPRCYCLGAEDDKKAFIEDFWLTAARNVLKLVVKSEWKSYPIQAVEEEASGDKQPKKQEKNPVLVSPEFVDEALCACEEYLSNLAHMDIDKDLEAPLYLTPEGWSLFLQRYYQVVHEGAELRHLDTQVQRCEDILQQLQAVVPQIDMEGDRNIWIVKPGAKSRGRGIMCMDHLEEMLKLVNGNPVVMKDGKWVVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFSLKNLDNSVHLCNNSIQKHLENSCHRHPLLPPDNMWSSQRFQAHLQEMGAPNAWSTIIVPGMKDAVIHALQTSQDTVQCRKASFELYGADFVFGEDFQPWLIEINASPTMAPSTAVTARLCAGVQADTLRVVIDRMLDRNCDTGAFELIYKQPAVEVPQYVGIRLLVEGFTIKKPMAMCHRRMGVRPAVPLLTQRGSGEARHHFPSLHTKAQLPSPHVLRHQGQVLRRQHSKLVGTKALSTTGKALRTLPTAKVFISLPPNLDFKVAPSILKPRKAPALLCLRGPQLEVPCCLCPLKSEQFLAPVGRSRPKANSRPDCDKPRAEACPMKRLSPLKPLPLVGTFQRRRGLGDMKLGKPLLRFPTALVLDPTPNKKKQVKYLGLDSIAVGGSRVDGARPCTPGSTARA
Protein: Myosin light chain kinase 3 (EC 2.7.11.18) (Cardiac MyBP-C-associated Ca/CaM kinase) (Cardiac MLCK) (Q3UIZ8)
Organism: Mus musculus (Mouse)
Function: Kinase that phosphorylates MYL2 in vitro. Has been proposed to be calmodulin-dependent, although MYL2 phosphorylation has also been observed in the presence or absence of calmodulin. Promotes sarcomere formation in cardiomyocytes and increases cardiomyocyte contractility (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18202317}.
Interaction partners:
- Calmodulin-like protein 4
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin light chain 3
- Calmodulin-1
- Myosin, light chain 12A, regulatory, non-sarcomeric
- Myosin regulatory light polypeptide 9
- Myosin light chain 6B
- Myosin light chain 4
- Calmodulin-like protein 3
- Calmodulin-4
Sequence:
MSGVSEEDPEGLAPQGLPALGGACLATMDKKLNVLTEKVDRLLHFQEDVTEKLQCVCQGMDHLEQDLHRLEASRELSLAGSGSTPPTTAQAAWPEVLELVRAVRQEGAQHGARLEALFKMVVAVDRAITLVGSTFQNSKVADFIMQGTVPGRKGSLADGPEENKEQAEVAGVKPNHVLTTGGVQADASRTLWEESQKEDIPVRTVEGLPLIINTSLKGADLTQAGASLRQGVEVLGPGQVPLPTEAESRLPETASENTGATLELSVAIDRISEVLTSLKMSQGGGQETSSSKPDCWLSEEAMRLSSGPLPQPLGPLTPDSDIHSGDALPRIPINMQEMATPGELLETQSGSPIGSAEAPGLGTVLEDQIPKGARPFPPLPKRSSNNGGMSAEEEIGSGAEPMRGPSLATRDWRDETVGTTDLQQGIDPGAVSPEPGKDHAAQGPGRTEAGRLSSAAEAAIVVLDDSAAPPAPFEHRVVSIKDTLISAGYTVSQHEVLGGGRFGQVHRCTERSTGLALAAKIIKVKNVKDREDVKNEVNIMNQLSHVNLIQLYDAFESKSSFTLIMEYVDGGELFDRITDEKYHLTELDVVLFTRQICEGVHYLHQHYILHLDLKPENILCVSQTGHQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYEFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNFIVNCSWDFDADTFKGLSEEAKDFVSRLLVKEKSCRMSATQCLKHEWLSHLPAKASGSNVRLRSQQLLQKYMAQSKWKKHFHVVTAVNRLRKFPTCP
Protein: CTD small phosphatase like 2 (H0YNW9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRLRTRKASQQSNQIQTQRTARAKRKYSEVDDSLPSGGEKPSKNETGLLSSIKKFIKGSTPKEERENPSKRSRIERDIDNNLITSTPRAGEKPNKQISRVRRKSQVNGEAGSYEMTN
Protein: Putative POM121-like protein 1 (Q3SYA9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSLWGPGAGSHPFGVHNSRLSPDLCPGKIVLRALKESGAGMPEQDKDPRVQENPGDQRRVPEVTGDAPSAFRPLRDNGGLSPFVPGPGPLQTDLHAQRSEIRYNQTSQTSWTSSCTNRNAISSSYSSTGGLPGLKRRRGPASSHCQLTLSSSKTVSEDRPQAVSSGHTQCEKVAEIAPGQTLALRNDSSRSEASRPSTRKFPLLPRRRGEPLMLPPPVELGYRVTAEDLDWEKEAAFQCIKSALQVEDKAISDCRPSRPSHTLSSLATGASGLPAVSKAPSMDAQQERHKSQDCLGLVAPLASATEVPSTAPMSGEKHRPPGPLFSSSDPLPATSSHSQDSAQVTSLIPAPFPAASMDAGMRRTRPGTSAPAAAAAAPPPSTLNRTLGSLLEWMEALHISGPQPQLQQVPRGQNQRSQTSRTSSCPK
Protein: Pituitary homeobox 2 (Homeobox protein PITX2) (Paired-like homeodomain transcription factor 2) (D6RFI4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
METNCRKLVSACVQLGVQPAAVECLFSKDSEIKKVEFTDSPESRKEAASSKFFPRQHPGANEKDKSQQGKNEDVGAEDPSKKKRQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERNQQAELCKNGFGPQFNGLMQPYDDMYPGYSYNNWAAKGLTSASLSTKSFPFFNSMNVNPLSSQSMFSPPNSISSMSMSSSMVPSAVTGVPGSSLNSLNNLNNLSSPSLNSAVPTPACPYAPPTPPYVYRDTCNSSLASLRLKAKQ
Protein: Calpastatin (Calpain inhibitor) (E9PDE4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNPTETKAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPPEPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSQSDKDLDDALDKLSDSLGQRQPDPDENKPMEDKVKEKAKAEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD
Protein: COP9 signalosome complex subunit 4 (D6RFN0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000256|ARBA:ARBA00004234}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAAVRQDLAQLMNSSGSHKDLAGKYRQILEKAIQLSGAEQLEALKAFVEAMVNENVSLVISRQLLTDFCTHLPNLPDSTAKEIYHFTLEKIQPRVISFEEQVASIRQHLASIYEKEEDWRNAAQVLVGIPLETGQKQYNVDYKLETYLKIARLYLEDDDPVQAEAYINRASLLQNESTNEQLQIHYKVCYARVLDYRRKFIEAAQRYNELSYKTIVHESERLEALKHALHCTILASAGQQRSRMLATLFKDERCQQLAAYGILEKMYLDRIIRGNQLQEFAAMLMPHQKATTADETGSLHFAQAGLELLGSSSSSHLGFPKCWDDRGSSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ
Protein: Mixed lineage kinase domain-like protein (Q9D2Y4)
Organism: Mus musculus (Mouse)
Function: Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process. Does not have protein kinase activity. Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. In addition to TNF-induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: following ZBP1 activation, which senses double-stranded Z-RNA structures, nuclear RIPK3 catalyzes phosphorylation and activation of MLKL, promoting disruption of the nuclear envelope and leakage of cellular DNA into the cytosol. Binds to highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which is essential for its necroptotic function (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32200799, ECO:0000269|PubMed:32296175}. Cell membrane {ECO:0000269|PubMed:32200799}. Nucleus {ECO:0000269|PubMed:32200799, ECO:0000269|PubMed:32296175}. Note=Localizes to the cytoplasm and translocates to the plasma membrane on necroptosis induction (By similarity). Localizes to the nucleus in response to orthomyxoviruses infection (PubMed:32200799). {ECO:0000250|UniProtKB:Q8NB16, ECO:0000269|PubMed:32200799}.
Interaction partners:
- Receptor-interacting serine/threonine-protein kinase 3
- Receptor-interacting serine/threonine-protein kinase 1
- Serine/threonine-protein phosphatase PGAM5, mitochondrial
- Tumor necrosis factor
- FAS-associated death domain protein
- Caspase-8
- NACHT, LRR and PYD domains-containing protein 3
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 3
- Heat shock protein HSP 90-alpha
Sequence:
MDKLGQIIKLGQLIYEQCEKMKYCRKQCQRLGNRVHGLLQPLQRLQAQGKKNLPDDITAALGRFDEVLKEANQQIEKFSKKSHIWKFVSVGNDKILFHEVNEKLRDVWEELLLLLQVYHWNTVSDVSQPASWQQEDRQDAEEDGNENMKVILMQLQISVEEINKTLKQCSLKPTQEIPQDLQIKEIPKEHLGPPWTKLKTSKMSTIYRGEYHRSPVTIKVFNNPQAESVGIVRFTFNDEIKTMKKFDSPNILRIFGICIDQTVKPPEFSIVMEYCELGTLRELLDREKDLTMSVRSLLVLRAARGLYRLHHSETLHRNISSSSFLVAGGYQVKLAGFELSKTQNSISRTAKSTKAERSSSTIYVSPERLKNPFCLYDIKAEIYSFGIVLWEIATGKIPFEGCDSKKIRELVAEDKKQEPVGQDCPELLREIINECRAHEPSQRPSVDGRSLSGRERILERLSAVEESTDKKV
Protein: Inosine triphosphate pyrophosphatase (ITPase) (Inosine triphosphatase) (EC 3.6.1.9) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase) (Putative oncogene protein hlc14-06-p) (Q9BY32)
Organism: Homo sapiens (Human)
Function: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148, ECO:0000269|PubMed:11278832}.
Interaction partners:
- Adenine phosphoribosyltransferase
- Thiopurine S-methyltransferase
- Bifunctional purine biosynthesis protein ATIC
- Inosine-5'-monophosphate dehydrogenase 2
- GMP synthase
- AMP deaminase 1
- Adenylosuccinate synthetase isozyme 2
- Nucleoside diphosphate kinase homolog 7
- Nucleoside diphosphate kinase 6
- Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
Sequence:
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFALSTGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYFGSLAA
Protein: Sequestosome 1 (F7GSB8)
Organism: Macaca mulatta (Rhesus macaque)
Subcellular location: Cytoplasm, myofibril, sarcomere {ECO:0000256|ARBA:ARBA00004204}. Cytoplasmic vesicle, autophagosome {ECO:0000256|ARBA:ARBA00004419}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- TNF receptor-associated factor 6
- GABA type A receptor-associated protein
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Microtubule associated protein 1 light chain 3 alpha
- Kelch-like ECH-associated protein 1
- Gamma-aminobutyric acid receptor-associated protein
- Serine/threonine-protein kinase TBK1
- Microtubule associated protein 1 light chain 3 beta
- Next to BRCA1 gene 1 protein
- Receptor-interacting serine/threonine-protein kinase 1
Sequence:
MASLTVKAYLLGKEDAAREIRRFSFCFSPEPEAEAEDAAGPGPCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVKDDIFRIYIKEKKECRRDHRPPCAQEAPRNMVHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHQGHTKLAFPSPFGHLSEGFSHSRWLRKLKHGHFGWPGWEMGPPGNWSPRPPRAGDARPGPTVESAAGPSEDPSVNFLKNVGESVAAALSPLGIEVDIDVEHGGKRSRLTPASPESSSTEEKNSSQPSSCCSDPSKLGGNVEGATQSLAEQMRKIALESEGRPEEQMESDNCSGGDDDWTHLSSKEVDPSTGELQSLQMPESEGPSSLDPSQEGPTGLKEAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHSPPL
Protein: Protein kinase A catalytic subunit (EC 2.7.11.1) (Q388U5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein kinase A regulatory subunit
- Cyclic nucleotide-binding domain-containing protein
- cAMP binding protein
Sequence:
MKSDGCLTRKDVSSWKLQDLEIRETIGTGTFGRVRLCRHRASGQYVVLKILKKQEILRMKQVDHILAESSILQELSHPFIVTMYKGFMDDDRLYLLLEYVVGGELFSHLRKAGKFPNDVAKFYSAEVVLAFEYIHECGIVYRDLKPENVLLDKQGNIKITDFGFAKRVRDRTYTLCGTPEYLAPEIIQSKGHDRAVDWWTLGILLYEMLVGYPPFFDESPFRTYEKILEGKLQFPKWVEMRAKDLIKSFLTIEPTKRLGSVKRGVQDVKRHKFYSGVNWNVLLQRGVAAPIHVRLNNDGDTRYFDRYPESPRHPLQPLTEAQQELFSGFCDGEYTRI
Protein: LIM domain-containing protein 2 (Q9BT23)
Organism: Homo sapiens (Human)
Function: Acts as an activator of the protein-kinase ILK, thereby regulating cell motility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24590809}. Nucleus {ECO:0000269|PubMed:24590809}. Note=Mainly found in cytoplasm, concentrated in membrane ruffles and in streaks reminiscent of focal adhesion plaques (PubMed:24590809). Also found in nucleus (PubMed:24590809). {ECO:0000269|PubMed:24590809}.
Interaction partners:
Sequence:
MFQAAGAAQATPSHDAKGGGSSTVQRSKSFSLRAQVKETCAACQKTVYPMERLVADKLIFHNSCFCCKHCHTKLSLGSYAALHGEFYCKPHFQQLFKSKGNYDEGFGRKQHKELWAHKEVDPGTKTA
Protein: Astrotactin 2 (H0Y3A8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
QTHNSVIGVPIRETPILDDYDCEEDEEPPRRANHVSREDEFGSQVTHTLDSLGHPGEEKVDFEKKAAAEATQETVESLMQKFKESFRANTPIEIGQLQPPLRSTSAGKRKRRSKSRGGISFGRAKGTSGSEADDETQLTFYTEQYRSRRRSKGLLKSPVNKTALTLIAVSSCILAMVCGSQMSCPLTVKVTLHVPEHFIADGSSFVVSEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPETGECSCHEGYAPDPVHRHLCVRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILSLGQGLWLPVSKSFVVPPVELSINPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNGGCTRNFKCVSDRQVDSSGCVCPEELKPMKDGSGCYDHSKGIDCSDGFNGGCEQLCLQQTLPLPYDATSSTIFMFCGCVEEYKLAPDGKSCLMLSDVCEGPKCLKPDSKFNDTLFGEMLHGYNNRTQHVNQGQVFQMTFRENNFIKDFPQLADGLLVIPLPVEEQCRGVLSEPLPDLQLLTGDIRYDEAMGYPMVQQWRVRSNLYRVKLSTITLAAGFTNVLKILTKESSREELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQQLWLQYQKETTELGSKKELKSMPFITYLSGLLTAQMLSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNGTKEAFKSALMSSYWCSGKGDVIDDWCRCDLSAFDANGLPNCSPLLQPVLRLSPTVEPSSTVVSLEWVDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLSFADDLLSGLGTSCVAAGRSHGEVPEVSIYSVIFKCLEPDGLYKFTLYAVDTRGRHSELSTVTLRTACPLVDDNKAEEIADKIYNLYNGYTSGKEQQMAYNTLMEVSASMLFRVQHHYNSHYEKFGDFVWRSEDELGPRKAHLILRRLERVSSHCSSLLRSAYIQSRVETVPYLFCRSEEVRPAGMVWYSILKDTKITCEEKMVSMARNTYGESKGR
Protein: MAP kinase phosphatase (MkpA protein) (Q9GV71)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Ubiquitin domain-containing protein
Sequence:
MGNTIGVSVSPPQLDDLFKVHDLKSFQNSTITPNLNTTNTKLKNTITTTTTTTTTTINNCNNSNSSSSNSSNNSVSSSCSNNNNNNNNNNKNKCKNSPLVVSIPTTIINHNIHHHHLFNNINNNNNNNNINNNNNNNSNISSNSNSNSNGGGSSYSNLVTPTSTPIAEIFGSYLFIWKVLVDQNSDSIIQFQSVDLLHYKNYNQSECYIILHVFNSNQNNVNKSYISSPRSLNNILSHDPLFSYFDSNNKLLHDLYTWNGKNSDSLSRAFCLSKALEFSKALKFSESLAVKQSPSSSSSSSPLLSPTSSSSSTTSLSSSSSASFSSSSAASSSLQPQTISESSFSSLTTAAITNNNNNNNNINININNHNNINININNHNYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNNNNNNNNNNNINNNNTQTTSYDSNKYWKLPNNSSQIIQKLFEKRIGVNSNLNSNNNIDYLVDNNNNNINNNNSNFVNFSPISNYFIDNDFSLFDGELIPFENSIQFQSEDGDDSIPNKNFFNFCKHFIKNNFQPTFLKTNFNINTFCNNNQDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSQNITNNGNNIPSSVQVITQPSTILNISNIFVNLKTINQYNHSNNDNNSQNNQNNNNNNHNQNNNNNNNNNGNNHNNGNFNSNNSNFSNSNNYNNNNNSSGDDNNNNNPNNLNNLNKKDESQSNTVKKKESSQPPSPSQQQQQQQQQQQQQQQQQQQQQQQQQQQPPSLPITNGDNTSINTKPLFEVLKKLSFSPPTSPSSSSSSPSPLFLPIPIADSKSGSTQPQHSPTKTINVTSSPPPTTTTTTTTIIPKIQIPKGKIPSLSLPLQQPITQHQEQPPPSSSSSQEPIQQEKLIKPIMVPKLSLNLSNTKSNGNGVSSSTTTTTTTTSTNNQITNASKKVVPSLNFGKQMSMSSMPLPSSSTSSSSSSTTTTTTTTTNNTNWVKKSLKLPDLNSLRITPPSTPRGTIPPNLSHLNSYHNNNNNNNNIMIPPSVSHRIDQCQEEFQHLSQKELILFFEPTLNRIVDELYLGSRIPASNLQLLKGEGITHILNCAGMVCPNHFQDHFVYKTLFISDGNGEDISCLFYEILDFIQDATKTNGKVYIHCHQGISRSSAFVILYLMWINKWSFQQAHEFTKKRRYISNPNPGFTGQLMYWNKFLLKHLQHPSVKEQPLLYRMVQLLDGLIVPKRVQTVSYLSLDARCCFILRVTDCIYIWSGEGCVGKLGDLFLESAKLAISRFQRYENDSTNIIELRQGHEDDKFWDHLGGEGGVGLVFAYDKDFKTQQYSISDFINNHNGTTNNNNNNNNNNSTTTTTTITTTTTTEQLVNNNSKNNNNNNNNNNNNNNNNNNNNINNSNGNGNGRAYLYRFIKEENSWEEYDVFDCEDLADDGLFILISKYDRILYVWIGKDINYTQFYNSFIKNNENNFNNSNNEINNINNNNNCDQKLLYINEDENSLEIKKEIGNFMANQFIQNNNLNNLKFSNTIIITHASQETDDFLDNFY
Protein: Protocadherin-12 (Vascular cadherin-2) (Vascular endothelial cadherin-2) (VE-cad-2) (VE-cadherin-2) [Cleaved into: Protocadherin-12, secreted form] (O55134)
Organism: Mus musculus (Mouse)
Function: Cellular adhesion molecule that may play an important role in cell-cell interactions at interendothelial junctions. Acts as a regulator of cell migration, probably via increasing cell-cell adhesion (By similarity). Promotes homotypic calcium-dependent aggregation and adhesion and clusters at intercellular junctions. Unable to bind to catenins, weakly associates with the cytoskeleton.
Subcellular location: [Protocadherin-12]: Cell membrane {ECO:0000250|UniProtKB:Q9NPG4}; Single-pass type I membrane protein {ECO:0000255}. Cell junction {ECO:0000269|PubMed:9651350}.; SUBCELLULAR LOCATION: [Protocadherin-12, secreted form]: Secreted {ECO:0000250|UniProtKB:Q9NPG4}. Note=The secreted form is produced following cleavage by ADAM10. {ECO:0000250|UniProtKB:Q9NPG4}.
Interaction partners:
- Cadherin-5
- Trophoblast-specific protein alpha
Sequence:
MMLLLPFLLGLLGPGSYLFISGDCQEVATVMVKFQVTEEVPSGTVIGKLSQELRVEERRGKAGDAFQILQLPQALPVQMNSEDGLLSTSSRLDREKLCRQEDPCLVSFDVLATGASALIHVEIQVLDINDHQPQFPKDEQELEISESASLHTRIPLDRALDQDTGPNSLYSYSLSPSEHFALDVIVGPDETKHAELVVVKELDRELHSYFDLVLTAYDNGNPPKSGISVVKVNVLDSNDNSPVFAESSLALEIPEDTVPGTLLINLTATDPDQGPNGEVEFFFGKHVSPEVMNTFGIDAKTGQIILRQALDYEKNPAYEVDVQARDLGPNSIPGHCKVLIKVLDVNDNAPSILITWASQTSLVSEDLPRDSFIALVSANDLDSGNNGLVHCWLNQELGHFRLKRTNGNTYMLLTNATLDREQWPIYTLTVFAQDQGPQPLSAEKELQIQVSDVNDNAPVFEKSRYEVSTWENNPPSLHLITLKAHDADLGSNGKVSYRIKDSPVSHLVIIDFETGEVTAQRSLDYEQMAGFEFQVIAEDRGQPQLASSISVWVSLLDANDNAPEVIQPVLSEGKATLSVLVNASTGHLLLPIENPSGMDPAGTGIPPKATHSPWSFLLLTIVARDADSGANGELFYSIQSGNDAHLFFLSPSLGQLFINVTNASSLIGSQWDLGIVVEDQGSPSLQTQVSLKVVFVTSVDHLRDSAHEPGVLSTPALALICLAVLLAIFGLLLALFVSICRTERKDNRAYNCREAESSYRHQPKRPQKHIQKADIHLVPVLRAHENETDEVRPSHKDTSKETLMEAGWDSCLQAPFHLTPTLYRTLRNQGNQGELAESQEVLQDTFNFLFNHPRQRNASRENLNLPESPPAVRQPLLRPLKVPGSPIARATGDQDKEEAPQSPPASSATLRRQRNFNGKVSPRGESGPHQILRSLVRLSVAAFAERNPVEEPAGDSPPVQQISQLLSLLHQGQFQPKPNHRGNKYLAKPGGSSRGTIPDTEGLVGLKPSGQAEPDLEEGPPSPEEDLSVKRLLEEELSSLLDPNTGLALDKLSPPDPAWMARLSLPLTTNYRDNLSSPDATTSEEPRTFQTFGKTVGPGPELSPTGTRLASTFVSEMSSLLEMLLGQHTVPVEAASAALRRLSVCGRTLSLDLATSGASASEAQGRKKAAESRLGCGRNL
Protein: Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase (EC 3.6.1.40) (Guanosine pentaphosphate phosphohydrolase) (pppGpp-5'-phosphohydrolase) (P25552)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. In vitro, can hydrolyze pppGp. Also has exopolyphosphatase activity, catalyzing the release of orthophosphate by processive hydrolysis of the phosphoanyhydride bonds of polyphosphate chains (1000 residues).
Interaction partners:
- GTP pyrophosphokinase
- Polyphosphate kinase
- Exopolyphosphatase
- Bifunctional
- Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase
Sequence:
MGSTSSLYAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWLERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLKQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLHLAVEQDIRSRTLRNIQRRFMIDIDQAQRVAKVAANFFDQVENEWHLEAISRDLLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATLLLNQTNPVDLSSLHQQNAVPPRVAEQLCRLLRLAIIFASRRRDDLVPEMTLQANHELLTLTLPQGWLTQHPLGKEIIAQESQWQSYVHWPLEVH
Protein: Nuclear poly(A) polymerase 1 (PAP(I)) (Poly(A) polymerase I) (EC 2.7.7.19) (Polynucleotide adenylyltransferase 1) (Q9LMT2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:19956626}.
Interaction partners:
- Nuclear poly
- Symplekin
- Cleavage stimulation factor subunit 77
- HEAT repeat-containing protein
- 30-kDa cleavage and polyadenylation specificity factor 30
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage stimulating factor 64
- FIP1[V]-like protein
- Cleavage and polyadenylation specificity factor subunit 3-I
- Cleavage and polyadenylation specificity factor subunit 1
Sequence:
MASVQQNGQRFGVSEPISMGGPTEFDVIKTRELEKHLQDVGLYESKEEAVRREEVLGILDQIVKTWIKTISRAKGLNDQLLHEANAKIFTFGSYRLGVHGPGADIDTLCVGPRHATREGDFFGELQRMLSEMPEVTELHPVPDAHVPLMGFKLNGVSIDLLYAQLPLWVIPEDLDLSQDSILQNADEQTVRSLNGCRVTDQILRLVPNIQNFRTTLRCMRFWAKRRGVYSNVSGFLGGINWALLVARICQLYPNALPNILVSRFFRVFYQWNWPNAIFLCSPDEGSLGLQVWDPRINPKDRLHIMPIITPAYPCMNSSYNVSESTLRIMKGEFQRGNEICEAMESNKADWDTLFEPFAFFEAYKNYLQIDISAANVDDLRKWKGWVESRLRQLTLKIERHFKMLHCHPHPHDFQDTSRPLHCSYFMGLQRKQGVPAAEGEQFDIRRTVEEFKHTVNAYTLWIPGMEISVGHIKRRSLPNFVFPGGVRPSHTSKGTWDSNRRSEHRNSSTSSAPAATTTTTEMSSESKAGSNSPVDGKKRKWGDSETLTDQPRNSKHIAVSVPVENCEGGSPNPSVGSICSSPMKDYCTNGKSEPISKDPPENVVAFSKDPPESLPIEKIATPQAHETEELEESFDFGNQVIEQISHKVAVLSATATIPPFEATSNGSPFPYEAVEELEVLPTRQPDAAHRPSVQQRKPIIKLSFTSLGKTNGK
Protein: BARP protein (Q38CV2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSITFHNLWLLLTVLCTAGIRADYIWNNCSVENSHPPLEEIRVLCRVAEQLRGLPETVSSAVETAAAASSKAFEAKVQAEEAVELAESRGLNVTKAKEAAVRATLAAEAAATAASNVEINAANIAAVPWLQPISDAGLENLSKCEHIDKYVQEAAAECSKKAEHVTAQSLSAALEGLENLFTDVSTREALRKETIEFHTELKSLEEHVEEAVRAQKRAEDAAAYANQTVGTNTGPVGNSVASPEGSVLLLMAGLFLGSVL
Protein: Monocarboxylate transporter 12 (MCT 12) (Solute carrier family 16 member 12) (D4A734)
Organism: Rattus norvegicus (Rat)
Function: Functions as a transporter for creatine and as well for its precursor guanidinoacetate. Transport of creatine and GAA is independent of resting membrane potential and extracellular Na(+), Cl(-), or pH. Contributes to the process of creatine biosynthesis and distribution.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6ZSM3}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:34075817}; Multi-pass membrane protein {ECO:0000255}. Note=Localized on the sinusoidal membrane of the hepatocyte. Colocalized with SLC6A13 in hepatocytes around the portal vein, (PubMed:34075817). Interaction with isoform 2 of BSG is required for its localization to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q6ZSM3, ECO:0000269|PubMed:34075817}.
Interaction partners:
Sequence:
MTKITRVGSASPPDGGWGWMIVAGCFLVTICTRAVTRCISIFFVEFQTYFAQDYSQTAWIHSIVDCMTMLCAPLGSVVSNQLSCQAGIMLGGLLASTGLILGSFATSLKHLYLSLGVLTGLGFALCYSPAIAMVGKYFSRRKAFAYGIAMSGSGIGTFILAPVVQLLIEQFSWRGALLILGGFVLNLCVCGALMRPITLKEDPSGPEKSHDRDAQREDCKQASPYSPLTKEWTETRLCCSLQQGYGFLLMSDFVVLAVSVLFMAYGCSPLFVYLVPYALSVGVSHHQAAFLMSILGVIDIVGNITFGWLTDRRCLKNYRYVCYLFAVALDGLCYLCLPMLQSFPLLVPFSCTFGYFDGAYVTLIPVVTAEIVGTTSLSSALGVVYFLHAVPYLVSPPIAGWLVDTTGSYTAAFLLCGFAMIFSSILLGFAKIAKRMKRTQVPFLVKDSDPKLHLWTNGSVAYSIAKELDQKDEESLAKARTGCNLT