wanglab/gogpt-training-data huggingface dataset:
Protein: Dynamin-related protein 3A (F4JJ15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTIEEVSGETPPSTPPSSSTPSPSSSTTNAAPLGSSVIPIVNKLQDIFAQLGSQSTIALPQVVVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLVLQLLQTKSRANGGSDDEWGEFRHLPETRFYDFSEIRREIEAETNRLVGENKGVADTQIRLKISSPNVLNITLVDLPGITKVPVGDQPSDIEARIRTMILSYIKQDTCLILAVTPANTDLANSDALQIASIVDPDGHRTIGVITKLDIMDKGTDARKLLLGNVVPLRLGYVGVVNRCQEDILLNRTVKEALLAEEKFFRSHPVYHGLADRLGVPQLAKKLNQILVQHIKVLLPDLKSRISNALVATAKEHQSYGELTESRAGQGALLLNFLSKYCEAYSSLLEGKSEEMSTSELSGGARIHYIFQSIFVKSLEEVDPCEDLTDDDIRTAIQNATGPRSALFVPDVPFEVLVRRQISRLLDPSLQCARFIFEELIKISHRCMMNELQRFPVLRKRMDEVIGDFLREGLEPSEAMIGDIIDMEMDYINTSHPNFIGGTKAVEAAMHQVKSSRIPHPVARPKQDTVEPDRTSSSTSQVKSRSFLGRQANGIVTDQGVVSADAEKAQPAANASDTRWGIPSIFRGGDTRAVTKDSLLNKPFSEAVEDMSHNLSMIYLKEPPAVLRPTETHSEQEAVEIQITKLLLRSYYDIVRKNIEDSVPKAIMHFLVNHTKRELHNVFIKKLYRENLFEEMLQEPDEIAVKRKRTQETLHVLQQAYRTLDELPLEADSVSAGMSKHQELLTSSKYSTSSSYSASPSTTRRSRRAGDQHQNGYGF
Protein: Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (eIF-3-eta) (eIF3 p116) (Q8JZQ9)
Organism: Mus musculus (Mouse)
Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55884}. Note=Localizes to stress granules following cellular stress. {ECO:0000250|UniProtKB:P55884}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit D
Sequence:
MQDAENVAVPEAAEERAEPARQQPASESPPTDEAAGSGGSEVGQTEDAEEDAEAGPEPEVRAKPAAQSEEETATSPAASPTPQSAERSPSQEPSAPGKAEAVGEQARGHPSAGAEEEGGSDGSAAEAEPRALENGEADEPSFSDPEDFVDDVSEEELLGDVLKDRPQEADGIDSVIVVDNVPQVGPDRLEKLKNVIHKIFSKFGKIINDYYPEEDGKTKGYIFLEYASPAHAVDAVKNADGYKLDKQHTFRVNLFTDFDKYMTISDEWDIPEKQPFKDLGNLRYWLEEAECRDQYSVIFESGDRTSIFWNDVKDPVSIEERARWTETYVRWSPKGTYLATFHQRGIALWGGDKFKQIQRFSHQGVQLIDFSPCERYLVTFSPLMDTQDDPQAIIIWDILTGHKKRGFHCESSAHWPIFKWSHDGKFFARMTLDTLSIYETPSMGLLDKKSLKISGIKDFSWSPGGNIIAFWVPEDKDIPARVTLMQLPTRQEIRVRNLFNVVDCKLHWQKNGDYLCVKVDRTPKGTQGVVTNFEIFRMREKQVPVDVVEMKETIIAFAWEPNGSKFAVLHGEAPRISVSFYHVKSNGKIELIKMFDKQQANTIFWSPQGQFVVLAGLRSMNGALAFVDTSDCTVMNIAEHYMASDVEWDPTGRYVVTSVSWWSHKVDNAYWLWTFQGRLLQKNNKDRFCQLLWRPRPPTLLSQDQIKQIKKDLKKYSKIFEQKDRLSQSKASKELVERRRTMMEDFRQYRKMAQELYMKQKNERLELRGGVDTDELDSNVDDWEEETIEFFVTEEVIPLGSQE
Protein: Voltage-dependent L-type calcium channel subunit alpha (Q8MQA1)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
Interaction partners:
- Guanylate kinase/L-type calcium channel beta subunit domain-containing protein
- Voltage-dependent calcium channel unc-36
- Voltage-dependent T-type calcium channel subunit alpha
- VWFA domain-containing protein
- Uncoordinated protein 79
- Ryanodine receptor
- Calcium-activated potassium channel slo-1
- Potassium voltage-gated channel protein shk-1
- SH3 domain-containing protein
- Caveolin-2
Sequence:
MSVLASMMSSGEDEEQAAADEQERTDLWQQTLQAAVAASSSQDATKKRPAQRKPLRQTNVVERSERSLLCLSLNNPIRKLCISIVEWKPFEFLILFMICANCIALAIYQPYPAQDSDYKNTLLETIEYVFIVVFTIECVLKIVAMGFMFHPSAYLRNAWNILDFIIVVIGLVSTILSKMSIQGFDVKALRAFRVLRPLRLVSGVPSLQVVLNAILRAMIPLLHIALLVLFVILIYAIIGLELFCGKLHSTCIDPATGQLAQKDPTPCGTDTEGSAFKCQPSDSLTNMGVRWECSSNTTWPGPNNGITNFDNFGLAMLTVFQCVSLEGWTDVMYWVNDAVGREWPWIYFVTLVILGSFFVLNLVLGVLSGEFSKEREKARARGLFQKFREKQQLEEDLKGYLDWITQAEDIEPVNEDEQEDEPVAQTVVGEEADEEGEERVEDVRPSKWAARMKRLEKLNRRCRRACRRLVKSQTFYWLVILLVLLNTLVLTSEHYGQSEWLDHFQTMANLFFVILFSMEMLLKMYSLGFTTYTTSQFNRFDCFVVISSILEFVLVYFDLMKPLGVSVLRSARLLRIFKVTKYWTSLRNLVSSLLNSLRSIISLLLLLFLFIVIFALLGMQVFGGKFNFNPQQPKPRANFDTFVQALLTVFQILTGEDWNTVMYHGIESFGGVGTLGVIVCIYYIVLFICGNYILLNVFLAIAVDNLADADSLTNAEKEEEQQEIEGEDEEFEEGEDEGEEHGMDEPEGDEEMTSARPRRMSEVPAASTVKPIPKASSLFILSHTNSFRVFCNMVVNHSYFTNAVLFCILVSSAMLAAEDPLQANSTRNMILNYFDYFFTSVFTVEITLKVIVFGLVFHKGSFCRNAFNLLDILVVAVSLTSFVLRTDAMSVVKILRVLRVLRPLRAINRAKGLKHVVQCVIVAVKTIGNIMLVTFMLQFMFAIIGVQLFKGTFFLCNDLSKMTEAECRGEYIHYEDGDPTKPVSKKRVWSNNDFNFDNVGDAMISLFVVSTFEGWPQLLYVAIDSNEEDKGPIHNSRQAVALFFIAFIIVIAFFMMNIFVGFVIVTFQNEGEREYENCELDKNQRKCIEFALKAKPHRRYIPRNRLQYRVWWFVTSRAFEYVIFLIIVMNTVSLACKHYPSSRGFEDFLDVFNLIFTGVFAFEAVLKIVALNPKNYISDRWNVFDLLVVVGSFIDITYGKLNPGGTNLISINFFRLFRVMRLVKLLSRGEGIRTLLWTFMKSFQALPYVALLIVLLFFIYAVIGMQFFGKVALDDSTSIHRNNNFHSFPAAILVLFRSATGEAWQDIMLSCSDREDVRCDPMSDDYHKGGLNESRCGNNFAYPYFISFFMLCSFLVINLFVAVIMDNFDYLTRDWSILGPHHLEEFVRLWSEYDPDAKGRIKHLDVVTLLRKISPPLGFGKLCPHRLACKRLVSMNMPLNSDGTVCFNATLFALVRTNLKIYTEGNIDEANEQLRSAIKRIWKRTHKDLLDEVVPPAGKEDDVTVGKFYATFLIQDYFRRFKKRKEMEAKGVLPAQTPQAMALQAGLRTLHEIGPELKRAISGNLETDFNFDEPEPQHRRPHSLFNNLVHRLSGAGSKSPTEHERIEKGSTLLPFQPRSFSPTHSLAGAEGSPVPSQMHRGAPINQSINLPPVNGSARRLPALPPYANHIHDETDDGPRYRDTGDRAGYDQSSRMVVANRNLPVDPDEEEQWMRSGGPSNRSDRRNPHLREPMLVARGAALALAGMSSEAYEGTYRPVGEGKSVRLPFSSRPVLRPAEDSRPVDRLIGQSLGLGRYADARIVGAARREIEEAYSLGEQEIDLAADSLAPLMQHVGMHDIRDINENSRSALLRPAENSSRQHDSRGGSQEDLLLVTTL
Protein: cAMP-responsive element modulator (Inducible cAMP early repressor) (ICER) (P27699)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator that binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. Isoforms are either transcriptional activators or repressors. Isoform 2, isoform 3 and isoform 4 are repressors, while isoform 1 is an activator. Plays a role in spermatogenesis and is involved in spermatid maturation. Binding of isoform 1 (activator) to CRE is increased by CREB3L4. The CREM isoform 1-CREB3L4 heterodimer functions through CRE and may recruit HIRA to CRE to regulate histone exchange.
Subcellular location: Nucleus {ECO:0000269|PubMed:23443664, ECO:0000269|PubMed:8252624}.; SUBCELLULAR LOCATION: [Isoform 11]: Cytoplasm. Nucleus.
Interaction partners:
- Cyclic AMP-responsive element-binding protein 1
- Cyclic AMP-responsive element-binding protein 3-like protein 4
- Cyclic AMP-dependent transcription factor ATF-2
- Cyclic AMP-dependent transcription factor ATF-4
- Apoptosis regulator Bcl-2
- Cyclic AMP-responsive element-binding protein 3
- Cyclic AMP-responsive element-binding protein 5
- Cyclic AMP-responsive element-binding protein 3-like protein 2
- Cyclic AMP-responsive element-binding protein 3-like protein 3
- Cyclic AMP-dependent transcription factor ATF-6 beta
Sequence:
MSKCGRKKYMRTNVRQMTMETVESQQDRSVTRSVAEHSSAHMQTGQISVPTLAQVSVAGSGTGRGSPAVTLVQLPSGQTVQVQGVIQTPHPSVIQSPQIQTVQVATIAETDDSADSEVIDSHKRREILSRRPSYRKILNELSSDVPGIPKIEEEKSEEEGTPPNIATMAVPTSIYQTSTGQYIAIAQGGTIQISNPGSDGVQGLQALTMTNSGAPPPGATIVQYAAQSADGTQQFFVPGSQVVVQDEETDLAPSHMAAATGDMPTYQIRAPTTALPQGVVMAASPGSLHSPQQLAEEATRKRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICSPKTD
Protein: Uncharacterized protein C16G5.19 (Q96VG0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative amidase PB8B6.03
- Uncharacterized mitochondrial membrane protein C800.14c
- Uncharacterized protein C685.08
- Putative uncharacterized protein C27E2.12
- Uncharacterized protein PB1A10.16
- Putative uncharacterized protein C23C4.04c
- Putative lysine N-acyltransferase C17G9.06c
- Fluoride export protein 2
- Probable circularly permuted 1,3-beta-glucanase P23A10.11c YJL171C
- Phospholipase D1
Sequence:
MCTFVFESLCAMISTLKVNKIERGYWFIQCLRYCFIYIIKKQHRQADLPRNFGMRSKALYIGRSVGKWIETFCLDSNYSTHVYSLWAKSFLIIQFENVDPFVDHF
Protein: Copine-7 (Copine VII) (Q9UBL6)
Organism: Homo sapiens (Human)
Function: Calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21087455}. Nucleus {ECO:0000269|PubMed:21087455}. Cell membrane {ECO:0000269|PubMed:21087455}. Note=Translocates to the cell membrane in a calcium-dependent manner (PubMed:21087455). {ECO:0000269|PubMed:21087455}.
Interaction partners:
Sequence:
MSAGSERGAAATPGGLPAPCASKVELRLSCRHLLDRDPLTKSDPSVALLQQAQGQWVQVGRTEVVRSSLHPVFSKVFTVDYYFEEVQRLRFEVYDTHGPSGFSCQEDDFLGGMECTLGQPAQKWLLQVVMRVSVDVLGPAGHCAKHFLCCTESSHLARTGPSFLLRYDDLCLPWATAGAVRWWTCRGGHTQGWQIVAQKKVTRPLLLKFGRNAGKSTITVIAEDISGNNGYVELSFRARKLDDKDLFSKSDPFLELYRVNDDQGLQLVYRTEVVKNNLNPVWEAFKVSLSSLCSCEETRPLKCLVWDYDSRGKHDFIGEFSTTFEEMQKAFEEGQAQWDCVNPKYKQKRRSYKNSGVVVLADLKFHRVYSFLDYIMGGCQIHFTVAIDFTASNGDPRNSCSLHYINPYQPNEYLKALVSVGEICQDYDSDKRFSALGFGARIPPKYEVSHDFAINFNPEDDECEGIQGVVEAYQNCLPRVQLYGPTNVAPIISKVARVAAAEESTGKASQYYILLILTDGVVTDMADTREAIVRASRLPMSIIIVGVGNADFTDMQVLDGDDGVLRSPRGEPALRDIVQFVPFRELKNASPAALAKCVLAEVPKQVVEYYSHRGLPPRSLGVPAGEASPGCTP
Protein: Epididymis secretory sperm binding protein (A0A384NPW1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCVEEPEPEPEAAEGDGDKKGNAEGSSDEEGKLVIDEPAKEKNEKGALKRRAGDLLEDSPKRPKEAENPEGEEKEAATLEVERPLPMEVEKNSTPSEPGSGRGPPQEEEEEEDEEEEATKEDAEAPGIRDHESL
Protein: Thyroid transcription factor 1-associated protein 26 (TTF-1-associated protein 26) (Coiled-coil domain-containing protein 59) (TTF-1-associated protein BR2) (Q9P031)
Organism: Homo sapiens (Human)
Function: Component of the transcription complexes of the pulmonary surfactant-associated protein-B (SFTPB) and -C (SFTPC). Enhances homeobox protein Nkx-2.1-activated SFTPB and SFTPC promoter activities.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription termination factor 1
- Protein LLP homolog
- Pulmonary surfactant-associated protein B
- Surfactant protein C
Sequence:
MAPVRRSAKWRPGGIEARGEGVSTVGYRNKNVRQKTWRPNHPQAFVGSVREGQGFAFRRKLKIQQSYKKLLRKEKKAQTSLESQFTDRYPDNLKHLYLAEEERHRKQARKVDHPLSEQVHQPLLEEQCSIDEPLFEDQCSFDQPQPEEQCIKTVNSFTIPKKNKKKTSNQKAQEEYEQIQAKRAAKKQEFERRKQEREEAQRQYKKKKMEVFKILNKKTKKGQPNLNVQMEYLLQKIQEKC
Protein: DUF7722 domain-containing protein (Q1G3G9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGIKFSQGPSNTTIHNRSHQDGEDQRNETATKINHDKPQNQSSSFQIPLHYPKYTKSDYEKMPEWQLDRLLREYGLPVIGDSYEKRKFAIGAFLWSSENEH
Protein: Phosphoinositide 3-kinase regulatory subunit 6 (Phosphoinositide 3-kinase gamma adapter protein of 87 kDa) (p84 PI3K adapter protein) (p84 PIKAP) (p87 PI3K adapter protein) (p87PIKAP) (Q3U6Q4)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of the PI3K gamma complex. Acts as an adapter to drive activation of PIK3CG by beta-gamma G protein dimers. The PIK3CG:PIK3R6 heterodimer is much less sensitive to beta-gamma G proteins than PIK3CG:PIK3R5 and its membrane recruitment and beta-gamma G protein dimer-dependent activation requires HRAS bound to PIK3CG. Recruits of the PI3K gamma complex to a PDE3B:RAPGEF3 signaling complex involved in angiogenesis; signaling seems to involve RRAS.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16476736}. Cell membrane {ECO:0000269|PubMed:19906996}; Peripheral membrane protein {ECO:0000269|PubMed:19906996}. Note=Translocated to the plasma membrane in a Ras-dependent manner (PubMed:19906996). {ECO:0000269|PubMed:19906996}.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphoinositide 3-kinase regulatory subunit 5
- Phosphoinositide 3-kinase regulatory subunit 4
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 3-kinase catalytic subunit type 3
Sequence:
MESSDVELDFQRSVQAVLRELNTPNPALQSNQGMWRWSLHKKVERNPGKSSILVRILLRELEKAESEDGRRVIIPLLLTLMSVLTKATGIPEDLYHRAYTFCTRLLTLPAPYSTVALDCAIRLKTETAVPGTLYQRTVIAEQNLISELYPYQERVFLFVDPELVSASVCSALLLEIQAAQEQQTPEACMRHVVSHALQAALGEACHTGALNRKLQASSRRVLEYYFHAVVAAIEQVASEDSPSRLGHLEKMEEIYCSLLGPATTRRHCVGDLLQDRLPSIPLPSPYITFHLWTDQEQLWKELVLFLRPRSQLRLSADLDALDLQGFRLDRDLARVSTDSGIERDLPLGSDELPDPSSSEMERAALQRKGGIKKRVWPPDFFMPGSWDGPPGLHRRTGRPSGDGELLPGVSRVHTARVLVLGDDRMLGRLAQAYYRLRKRETKKFCLTPRLSLQLYYIPVLAPQVTGQDPEASRKPELGELASFLGRVDPWYESTVNTLCPAILKLAEMPPYLDTSRTVDPFILDVITYYVRMGTQPIYFQLYKVKIFTSLSHDPTEDIFLTELKVKIQDSKSPKEGSSPRRRGAAEGTGAELSMCYQKALLSHRPREVTVSLRATGLVLKAIPAGDTEVSGFFHCTSPNAASATDCSCLHVSVTEVVKSSNLAGRSFTTSTNTFRTSSIQVQSQDQRLLTLWLDKDGRRTFRDVVRFEVSPCPEPCSRTQKSKTSALNSHGQETEKNMAKPNSLLMPINTFSGIIQ
Protein: Tiger protein B1 (Loose aggregate B1 protein) (Transmembrane, IPT, Ig, E-set, Repeat protein B1) (Q54V07)
Organism: Dictyostelium discoideum (Social amoeba)
Function: tgrB1 and tgrC1 are involved in kin discrimination. They play an essential role in aggregation and subsequent development.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Tiger protein C1
- Tiger protein D1
Sequence:
MKVIYIYLLLLLVCKFLFVKSSCSLKVGKIECTKELETFLLYNETVVNVKMDTNGVKYYFNALEFPYKNLLCDLNIDIKFTPEIPSFPNIPTTGGDFGFTFNFPCDYRRRVKRIEIERTILSLSFDTSKNQFVTYLNPGCGPFNISSSGIQILSTTYETGAIPNVPILDDDKGILTIQGSNLYNTSIKIYSNNILKDTNPSGALDASHSSVTFSAEEFLTPNNWTIEVSICGSFYKSYSFPYFPKLDKMEGVLNDNGGNMVFTGKHLRPKHNVTGTFGNKTIECLTSNSSKSITCTIPSRKNYGFLGYDIPVTITIDGEYKSNTIKISYDLPLIQSVSQRGNSQIFDVTGVYFSGVKNMTVITGKNMKTDIIQKKTATLEEPGFFIESNYTIFIFLPNNTQPGFMNLVVGDGGSETFTSPRYNFKITPTITAGQTFNSTTSGNDLEIKGIFMRTVDSDGRDVPLTVNSGSGGLVCNPLKDGDGLLFTCVLGPGFGSSHTMNVYYNLIPIGSFTVSYNPPYLGTSEQEKDGTIKMNGKDLGESVKDSIMTVVYSDGNTVNGTVIKSSHTSLIFRYPIGNRNTASYIFQLGDQKSNKAGPFTLKPIIENTDPAVPCGGGVVTINGHYFFNYTKDTTTITIGKVPCNISSISETTIECVIVPNLRSLSPYYTSGTKPLVISSSNPGTEKVYQLTPAGLNYKFAPPTITNTSAIDQTALITIYGTSFGDANLEILINDKPCTQPEINIHTYSSLTCNVTNYDEMKIYNYSNTKFNISISVDGQYFIADIFQFKYESGIIYSENKSTGFPNEMYLGFVVFVIFIALISFAAKNQIEKYFEERKSRKAFRSLDNLRLKLRQKHATEIAKHYTFGEQSAPKPDKSTFYDIRKKLSRLPLIRRCFKEHTD
Protein: Metalloendoproteinase 2-MMP (At2-MMP) (EC 3.4.24.-) (O04529)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (By similarity). Required for plant growth, morphogenesis, and development with particular relevance for flowering and senescence. Active on McaPLGLDpaAR-NH(2) (QF24) and myelin basic protein (MBP) and, to some extent, on beta-casein.
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}; Extracellular side {ECO:0000305}.
Interaction partners:
- 26S proteasome regulatory particle chain RPT6-like protein
- 26S proteasome regulatory particle chain RPT6-like protein
- Carboxypeptidase SOL1
- Cyclin-D1-1
Sequence:
MRFCVFGFLSLFLIVSPASAWFFPNSTAVPPSLRNTTRVFWDAFSNFTGCHHGQNVDGLYRIKKYFQRFGYIPETFSGNFTDDFDDILKAAVELYQTNFNLNVTGELDALTIQHIVIPRCGNPDVVNGTSLMHGGRRKTFEVNFSRTHLHAVKRYTLFPGEPRWPRNRRDLTYAFDPKNPLTEEVKSVFSRAFGRWSDVTALNFTLSESFSTSDITIGFYTGDHGDGEPFDGVLGTLAHAFSPPSGKFHLDADENWVVSGDLDSFLSVTAAVDLESVAVHEIGHLLGLGHSSVEESIMYPTITTGKRKVDLTNDDVEGIQYLYGANPNFNGTTSPPSTTKHQRDTGGFSAAWRIDGSSRSTIVSLLLSTVGLVLWFLP
Protein: Uncharacterized protein, isoform G (M9PC74)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPRNLPLLPLTLCAVALLAAVGPMPAHGAVANSHKHEKHLSKERVKDGIYAPRDAHHHGEDGEHNVEFDHEAIIGNTKEAQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRKLSEEEAADRFEEIDQDADERITWKEYLQDTYAMEDEDFKKETIDYDSYEDEQKMIKQDKEMFNAADTNKDGVLTLEEFVLFQNPEEHPQMLPILLEHTMQDKDADHDGKINFQEFVGDAASHHDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAIANDEVDHLFVSTDEDHDDRLSYLEILNNYDTFVGSEATDYGDHLQNINHLSDEL
Protein: Chromatin assembly factor 1 subunit B (CAF-1 subunit B) (Pombe CAF-1 first subunit) (O13985)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18761674, ECO:0000269|PubMed:38376141}. Note=Forms discrete foci in S-phase but not in G2-phase (PubMed:38376141). Localizes to replicating chromatin (PubMed:18761674). {ECO:0000269|PubMed:18761674, ECO:0000269|PubMed:38376141}.
Interaction partners:
- Chromatin assembly factor 1 subunit A
- Histone-binding protein pcf3
- Histone chaperone cia1
- Proliferating cell nuclear antigen
- Meiotically up-regulated gene 183 protein
- RbAp48-related WD40 repeat-containing protein prw1
- Histone acetyltransferase type B subunit 2
- Histone H4
- Histone H3.1/H3.2
- Histone H3-like centromeric protein cnp1
Sequence:
MRAEVLQIRWHYDANDDHTPIYSVDFQKNSLNKFATCGGDSKIRIWQLITSESSTKVEYLSTLSRHTQAVNVVRFNPEGNILATAGDEGTIMLWVPTNTPITTLADDAEELALAKEYWKVKIVCRSMGSEIYDLCWSVDSNFLIAGAMDNSLRLYDAHTGQLLTQKFDHSHYVQGVCWDPLNQYIVSESSDRSICLYEIQEEKKNPKKFQLVLKSRICRIEYNVTKFELISVTKPLNNDESSGISEPIETSNNNESPVSKHEALSSTANIVKDGSLERTEPPNSLNSKISYSLYCNETLVSFFRRPAFSPDGLLLVTPAGRLRPHGQPNFEVPYTAYIYTRGSITKQPVACLNGFKKPVIAVRFSPIHYELNSFSNFSFTSVSFNLPYRMVFAVACQDAVYIYDTQTCKPFYRAVNLHYSNLTDIAWNDDGNVLLMTSIDGFCSVITFEPGELGVKSQHKISLPEKRSASPSSIDDSQDNTAGGPATTTLIPRKVESSKVSKKRIAPTPVYP
Protein: Protein VASP homolog (DdVASP) (Q5TJ65)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as lamellipodial and filopodial dynamics in migrating cells. Plays a crucial role in filopodia formation, cell-substratum adhesion, and proper chemotaxis. Nucleates and bundles actin filaments. When complexed with fotH in filopodial tips, may support formin-mediated filament elongation by bundling nascent actin filaments.
Subcellular location: Cytoplasm, cell cortex. Cell projection, filopodium. Cytoplasm, cytoskeleton. Note=Localizes to the leading edge of migrating cells and to the tips of filipodia. Translocates to the cell cortex in response to cAMP chemoattractant stimulation.
Interaction partners:
- Profilin-1
- Profilin-2
- Profilin-3
- Calponin homology and LIM domain-containing protein
- Probable vinculin
- Cofilin-1A
- Formin-H
- Ras GTPase activation domain-containing protein
- Neurofibromin-A
- LIM domain-containing protein DDB_G0271356
Sequence:
MSETAIFNATGQVFTYSPQTRNWVPSSNVPATLQMYFNSGANTYRVIGRAGDDPNNFLINFAVKSEVVYSRASEIFHQFTDQRTHFGINFTSKQDADTFGGGFENVLRSLKGGPQQPPPQVPKPQPQQPPQPQQPPQRPPSTVIAKPVAPQAPVAPPQAPAAAPQAPAPPAAPPAPPKPPGPPPPPPAPKPPAAGGGTGRNALLGSIENFSKGGLKKTVTVDKSAGVPTKTTPSANSAASNAGSEPSSGGSTPAPAPKSSGGGGGGDLMAEVMAKRAKMKAAASQPKEESSAPTPAPTPAPTPAPTPSSTSFKPPQSFSKPATKTAAANKPPSPSLSAPLPSTVANEDLQSLKEEILTEVRKEIQKAKDEILEAIRASQH
Protein: Inositol-tetrakisphosphate 1-kinase 1 (GmItpk1) (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase 1) (Inositol-triphosphate 5/6-kinase 1) (Ins(1,3,4)P(3) 5/6-kinase 1) (EC 2.7.1.159) (Inositol-hexakisphosphate 5-kinase) (EC 2.7.4.21) (A7X657)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3. May participate in an inositol lipid-independent pathway of InsP6 synthesis. Able to add a beta-phosphate to InsP6 to yield 5-InsP7, thus exhibiting InsP6 kinase activity. Has also some Ins(1,3,4,5,6)P5 phosphatase activity.
Interaction partners:
- Inositol-pentakisphosphate 2-kinase
- Inositol-pentakisphosphate 2-kinase
- Uncharacterized protein
- 3'
- Inositol polyphosphate multikinase
- Inositol polyphosphate-related phosphatase domain-containing protein
- Inositol-pentakisphosphate 2-kinase
- Multiple inositol polyphosphate phosphatase 1
- Multiple inositol polyphosphate phosphatase 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
Sequence:
MAEKRFGVIGYALAPKKQNSFIRDSLVSLAKSRGIELVRVDSDKPLADQGPFDCVLHKLYGDDWKRQLQEFHTLYPNAVILDAPEAIERLHNRISMLQVVSELRIEDRPETFGIPKQIVIYDKATLLDPQAWESLKFPVIAKPLVADGSAKSHKMALVFTRDALNKLKPPIVLQEFVNHGGVIFKVYVVGEHVRCVKRKSLPDVSDEEKALGGVSEDLMSFSQVSNLATVNDCDGYYRLMHLDDDTEMPPDAFVVDIAGGLRRALKLNLFNFDVIRDARYGNRYLIIDINYFPGYAKMPGYEAVLTQFFCEVMLKKKQQEEQQQEEGNAPKEKEESLQA
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 (EC 3.1.4.11) (Phosphoinositide phospholipase C-zeta-1) (Phospholipase C-zeta-1) (PLC-zeta-1) (Testis-development protein NYD-SP27) (Q86YW0)
Organism: Homo sapiens (Human)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronucleus at interphase following meiosis and mitosis (By similarity). {ECO:0000250|UniProtKB:Q8K4D7}.
Interaction partners:
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Protein kinase C alpha type
- Inositol polyphosphate multikinase
- Inositol polyphosphate-5-phosphatase A
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Protein kinase C gamma type
- Protein kinase C beta type
- 1-phosphatidylinositol 3-phosphate 5-kinase
Sequence:
MEMRWFLSKIQDDFRGGKINLEKTQRLLEKLDIRCSYIHVKQIFKDNDRLKQGRITIEEFRAIYRIITHREEIIEIFNTYSENRKILLASNLAQFLTQEQYAAEMSKAIAFEIIQKYEPIEEVRKAHQMSLEGFTRYMDSRECLLFKNECRKVYQDMTHPLNDYFISSSHNTYLVSDQLLGPSDLWGYVSALVKGCRCLEIDCWDGAQNEPVVYHGYTLTSKLLFKTVIQAIHKYAFMTSDYPVVLSLENHCSTAQQEVMADNLQATFGESLLSDMLDDFPDTLPSPEALKFKILVKNKKIGTLKETHERKGSDKRGDNQDKETGVKKLPGVMLFKKKKTRKLKIALALSDLVIYTKAEKFKSFQHSRLYQQFNENNSIGETQARKLSKLRVHEFIFHTRKFITRIYPKATRADSSNFNPQEFWNIGCQMVALNFQTPGLPMDLQNGKFLDNGGSGYILKPHFLRESKSYFNPSNIKEGMPITLTIRLISGIQLPLTHSSSNKGDSLVIIEVFGVPNDQMKQQTRVIKKNAFSPRWNETFTFIIHVPELALIRFVVEGQGLIAGNEFLGQYTLPLLCMNKGYRRIPLFSRMGESLEPASLFVYVWYVR