wanglab/gogpt-training-data huggingface dataset:
Protein: Vinculin (Metavinculin) (MV) (P18206)
Organism: Homo sapiens (Human)
Function: Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P12003}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12003}; Cytoplasmic side {ECO:0000250|UniProtKB:P12003}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P12003}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P12003}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P85972}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q64727}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q64727}; Cytoplasmic side {ECO:0000250|UniProtKB:Q64727}. Cell projection, podosome {ECO:0000250|UniProtKB:Q64727}. Note=Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions. {ECO:0000250|UniProtKB:P12003}.
Interaction partners:
- Sorbin and SH3 domain-containing protein 1
- Catenin alpha-1
- Alpha-actinin-4
- Zyxin
- Vasodilator-stimulated phosphoprotein
- Talin-2
- Talin-1
- Alpha-actinin-1
- Vinexin
- Paxillin
Sequence:
MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPSASPGDAGEQAIRQILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGSSPVAMQKAQQVSQGLDVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNGGPEGEEQIRGALAEARKIAELCDDPKERDDILRSLGEISALTSKLADLRRQGKGDSPEARALAKQVATALQNLQTKTNRAVANSRPAKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQDLLAKCDRVDQLTAQLADLAARGEGESPQARALASQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGKLGATAEKAAAVGTANKSTVEGIQASVKTARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEQLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKPGIPAAEVGIGVVAEADAADAAGFPVPPDMEDDYEPELLLMPSNQPVNQPILAAAQSLHREATKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ
Protein: Serine repeat antigen 9 (EC 3.4.22.2) (Q8I3C0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Uncharacterized protein
- Dipeptidyl aminopeptidase 1
Sequence:
MKVSFTLFFIIYIILNCDVLKCEVESSDSTSFLNLISGQSSSNSDDTVSSSDSRGVVASVSGTVDSDVSRTDSTGNVNSKNSELSETRQNSVEQNNNSNSSDNSIKIKSAFLKENVGVKITGPCDEGFGLVMVPHIIINVDTRNTDIQLGKKSSEINYGIKLRKKGKDEYEEKVGIDLLKNVCETGKNFKFVAYIKGDELIIKWKVIEEGNIPIDIKKFKIKRMSPPITSIQVFSSMSDEKSFVLENKNYVVTNNMPEKCEALATNCFLSGNIDIEKCYQCSLLVENDSKSDVCYNFISRENKEKLNEERFKVKGSTEYEESVESELKGAIDLLISSFYKSDGENGENVLISFEDLNSTLEDDIINFCSLLKLVDLSGTFMNHQIGTTADAFNNIVKLLKEHKEEDEFVLRTKLRNPALCMKNVDDWVKSRCGLLTSDDSYVVIKKNSDTNGKNENNESNDEEYDGVIDLSTNENGNVKSIQFNDDIYCNDDYCNRWKNENNCISKIGVEDQGNCASSWAFASKLHFETLRCMKGYDHLGISALYLTNCSKGKISKRCTEGGNPSEFLEIVSNSGFLPTEFDYPYFYALVENSCPSGLNKWINLWEDVKLFDYKYEPNSIGSKGYSVYKSEMFKDNMDEYVKMIKSEIKNKGSVIAYINAQSVLTYDFNGKNILNMCGSKTTDHSINVIGYGHYKNKEGEEKSYWLVRNSWGYYWGDEGNFKVDMYGPSNCNYHFINTVLVFNIDIPMMNNNENNKKGLYNYFPKYTHEFYHNFYDQNFGSDNKISLINSNGSNKNDVNNAYTVHGQSGETEVQPSQLRSTANQDSNRGAVTSDPLRTQPETTSTSVKKMDVFQVLKHVKNSKIKVGLIKYDNDDEIGAHHSCTRAYSFDPEKYDECVEFCRKNWEQCKDKPSPGFCLTKLDESKGCFFCYV
Protein: Signal transducer and activator of transcription 2 (p113) (P52630)
Organism: Homo sapiens (Human)
Function: Signal transducer and activator of transcription that mediates signaling by type I interferons (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In addition, has also a negative feedback regulatory role in the type I interferon signaling by recruiting USP18 to the type I IFN receptor subunit IFNAR2 thereby mitigating the response to type I IFNs. Acts as a regulator of mitochondrial fission by modulating the phosphorylation of DNM1L at 'Ser-616' and 'Ser-637' which activate and inactivate the GTPase activity of DNM1L respectively.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11150296, ECO:0000269|PubMed:23139419, ECO:0000269|PubMed:27782195}. Nucleus {ECO:0000269|PubMed:11150296, ECO:0000269|PubMed:23139419}. Note=Translocated into the nucleus upon activation by IFN-alpha/beta. {ECO:0000269|PubMed:11150296, ECO:0000269|PubMed:23139419}.
Interaction partners:
- Interferon alpha/beta receptor 1
- Interferon regulatory factor 9
- Signal transducer and activator of transcription 1-alpha/beta
- Non-receptor tyrosine-protein kinase TYK2
- Interferon alpha/beta receptor 2
- CREB-binding protein
- Tyrosine-protein kinase JAK1
- Signal transducer and activator of transcription 6
- Tyrosine-protein kinase JAK2
- Tyrosine-protein kinase JAK3
Sequence:
MAQWEMLQNLDSPFQDQLHQLYSHSLLPVDIRQYLAVWIEDQNWQEAALGSDDSKATMLFFHFLDQLNYECGRCSQDPESLLLQHNLRKFCRDIQPFSQDPTQLAEMIFNLLLEEKRILIQAQRAQLEQGEPVLETPVESQQHEIESRILDLRAMMEKLVKSISQLKDQQDVFCFRYKIQAKGKTPSLDPHQTKEQKILQETLNELDKRRKEVLDASKALLGRLTTLIELLLPKLEEWKAQQQKACIRAPIDHGLEQLETWFTAGAKLLFHLRQLLKELKGLSCLVSYQDDPLTKGVDLRNAQVTELLQRLLHRAFVVETQPCMPQTPHRPLILKTGSKFTVRTRLLVRLQEGNESLTVEVSIDRNPPQLQGFRKFNILTSNQKTLTPEKGQSQGLIWDFGYLTLVEQRSGGSGKGSNKGPLGVTEELHIISFTVKYTYQGLKQELKTDTLPVVIISNMNQLSIAWASVLWFNLLSPNLQNQQFFSNPPKAPWSLLGPALSWQFSSYVGRGLNSDQLSMLRNKLFGQNCRTEDPLLSWADFTKRESPPGKLPFWTWLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTMSGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEVLQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQERRKYLKHRLIVVSNRQVDELQQPLELKPEPELESLELELGLVPEPELSLDLEPLLKAGLDLGPELESVLESTLEPVIEPTLCMVSQTVPEPDQGPVSQPVPEPDLPCDLRHLNTEPMEIFRNCVKIEEIMPNGDPLLAGQNTVDEVYVSRPSHFYTDGPLMPSDF
Protein: Claudin-10 (Q9Z0S6)
Organism: Mus musculus (Mouse)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in the regulation of paracellular epithelia permeability to ions in multiple organs. It acts as a paracellular ion channel probably forming permselective pores; isoform 1 appears to create pores preferentially permeable to cations and isoform 2 for anions. In sweat glands and in the thick ascending limb (TAL) of Henle's loop in kidney, it controls paracellular sodium permeability which is essential for proper sweat production and renal function.
Subcellular location: [Isoform 1]: Cell junction, tight junction {ECO:0000269|PubMed:16804102, ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:20460438}. Cell membrane {ECO:0000269|PubMed:16804102, ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:20460438}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell junction, tight junction {ECO:0000269|PubMed:16804102, ECO:0000269|PubMed:19383724, ECO:0000305|PubMed:35031570}. Cell membrane {ECO:0000269|PubMed:16804102, ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:35031570}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 3]: Endoplasmic reticulum {ECO:0000269|PubMed:19383724}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell junction, tight junction {ECO:0000269|PubMed:19383724}. Cell membrane {ECO:0000269|PubMed:19383724}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 5]: Endoplasmic reticulum {ECO:0000269|PubMed:19383724}.; SUBCELLULAR LOCATION: [Isoform 6]: Endoplasmic reticulum {ECO:0000269|PubMed:19383724}.
Interaction partners:
- Claudin-8
- Claudin-13
- Occludin
- Tight junction protein 1
- Claudin-23
- Tight junction protein ZO-3
- Claudin-16
- Claudin-11
- Claudin-5
- Claudin-9
Sequence:
MASTALEIVAFVVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYFANLWKICVTDSTGVANCKEFPSMLALDGYIQACRGLMIAAVSLGFFGSIFALFGMKCTKVGGSDQAKAKIACLAGIVFILSGLCSMTGCSLYANKITTEFFDPLYMEQKYELGAALFIGWAGASLCIIGGVIFCFSISDNNKTPRMGYTYNGPTSAMSSRTKYQGGEGDFKTTGPSKQFDKNAYV
Protein: Beta-glucosidase 13 (AtBGLU13) (EC 3.2.1.21) (Q9LU02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- (R)-mandelonitrile lyase-like (Hydroxynitrile lyase-like) ((R)-oxynitrilase-like)
- Beta-fructofuranosidase, insoluble isoenzyme CWINV6
- Beta-glucosidase 12
- Beta-glucosidase 20
- Beta-fructofuranosidase, insoluble isoenzyme CWINV2
Sequence:
MRTKYFSLLVFIIVLASNEVIAKKHSSTPKLRRSDFPKDFIFGAATSAYQVEGAAHEDGRGPSIWDTFSEKYPEKIKDGTNGSIASDSYHLYKEDVGLLHQIGFGAYRFSISWSRILPRGNLKGGINQAGIDYYNNLINELLSKGIKPFATIFHWDTPQSLEDAYGGFFGAEIVNDFRDYADICFKNFGDRVKHWMTLNEPLTVVQQGYVAGVMAPGRCSKFTNPNCTAGNGATEPYIVGHNLILAHGEAVKVYREKYKASQKGQVGIALNAGWNLPYTESAEDRLAAARAMAFTFDYFMEPLVTGKYPVDMVNNVKDGRLPTFTAKQSKMLKGSYDFIGINYYSSSYAKDVPCSSENVTLFSDPCASVTGEREGVPIGPKAASDWLLIYPKGIRDLLLYAKYKFKDPVMYITENGRDEASTGKIDLKDSERIDYYAQHLKMVQDAISIGANVKGFFAWSLLDNFEWATGYSVRFGLVYVDFNDGRKRYPKKSAKWFRKLLSEKKRN
Protein: Glycine--tRNA ligase alpha subunit (EC 6.1.1.14) (Glycyl-tRNA synthetase alpha subunit) (GlyRS) (P00960)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm.
Interaction partners:
- Glycine--tRNA ligase beta subunit
- Histidine--tRNA ligase
- Valine--tRNA ligase
- Phenylalanine--tRNA ligase alpha subunit
- Isoleucine--tRNA ligase
- Methionine--tRNA ligase
- Alanine--tRNA ligase
- Aspartate--tRNA ligase
- Phenylalanine--tRNA ligase beta subunit
Sequence:
MQKFDTRTFQGLILTLQDYWARQGCTIVQPLDMEVGAGTSHPMTCLRELGPEPMAAAYVQPSRRPTDGRYGENPNRLQHYYQFQVVIKPSPDNIQELYLGSLKELGMDPTIHDIRFVEDNWENPTLGAWGLGWEVWLNGMEVTQFTYFQQVGGLECKPVTGEITYGLERLAMYIQGVDSVYDLVWSDGPLGKTTYGDVFHQNEVEQSTYNFEYADVDFLFTCFEQYEKEAQQLLALENPLPLPAYERILKAAHSFNLLDARKAISVTERQRYILRIRTLTKAVAEAYYASREALGFPMCNKDK
Protein: Zinc finger protein with KRAB and SCAN domains 7 (Zinc finger protein 167) (Zinc finger protein 448) (Zinc finger protein 64) (Q9P0L1)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Transcription intermediary factor 1-beta
- Histone-lysine N-methyltransferase SETDB1
- Zinc finger protein with KRAB and SCAN domains 4
Sequence:
MTTAGRGNLGLIPRSTAFQKQEGRLTVKQEPANQTWGQGSSLQKNYPPVCEIFRLHFRQLCYHEMSGPQEALSRLRELCRWWLMPEVHTKEQILELLVLEQFLSILPGELRTWVQLHHPESGEEAVAVVEDFQRHLSGSEEVSAPAQKQEMHFEETTALGTTKESPPTSPLSGGSAPGAHLEPPYDPGTHHLPSGDFAQCTSPVPTLPQVGNSGDQAGATVLRMVRPQDTVAYEDLSVDYTQKKWKSLTLSQRALQWNMMPENHHSMASLAGENMMKGSELTPKQEFFKGSESSNRTSGGLFGVVPGAAETGDVCEDTFKELEGQTSDEEGSRLENDFLEITDEDKKKSTKDRYDKYKEVGEHPPLSSSPVEHEGVLKGQKSYRCDECGKAFNRSSHLIGHQRIHTGEKPYECNECGKTFRQTSQLIVHLRTHTGEKPYECSECGKAYRHSSHLIQHQRLHNGEKPYKCNECAKAFTQSSRLTDHQRTHTGEKPYECNECGEAFIRSKSLARHQVLHTGKKPYKCNECGRAFCSNRNLIDHQRIHTGEKPYECSECGKAFSRSKCLIRHQSLHTGEKPYKCSECGKAFNQNSQLIEHERIHTGEKPFECSECGKAFGLSKCLIRHQRLHTGEKPYKCNECGKSFNQNSHLIIHQRIHTGEKPYECNECGKVFSYSSSLMVHQRTHTGEKPYKCNDCGKAFSDSSQLIVHQRVHTGEKPYECSECGKAFSQRSTFNHHQRTHTGEKSSGLAWSVS
Protein: Cortactin-binding protein 2 (CortBP2) (B9EJA2)
Organism: Mus musculus (Mouse)
Function: Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}. Cell projection, dendritic spine {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}. Note=Remains associated with dendritic spines even after glutamate stimulation. {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}.
Interaction partners:
- Striatin-3
- Striatin-interacting protein 1
- Striatin-interacting proteins 2
- Striatin
- Striatin-4
- Serine/threonine-protein kinase 24
- Programmed cell death protein 10
- Serine/threonine-protein kinase 26
- Serine/threonine-protein kinase 25
- T-complex protein 1 subunit epsilon
Sequence:
MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDGTFNNATDSCIGLGTSSIRSIMLGSMPWSTGQSFSQSPWDFLKKKKVEQVLALLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIANQLALCMKYRQMAAGFPCEIVRAEVDSGFSKEQLVDVFIRNACLIPVKQFPVKKKIIVILENLEKSSLSELLGDFLAPLENRSTESPCTFQKGNGTSECYYFHENCFLVGTIAKACLQGSDLLVQQHFRWVQLRWDCEPIQGLLQRFLRRKVVSKFRGQLPAPCDPVCKIVDWALSVWRQLNSCLARLGTPEALLGPKYFLSCPVVPGHAQATVKWMSKLWNAVIAPRVQEAILSRASMNKQPGTGQTASKKYPSQGQQAVVRAALSILLNKAVLHGCPLPRAELDQQIADFKGGSFPLSIVSSYSKKKVESGAWRKVNTSPRKKPGHFSSPTWNKPDPKREGMRNKTIPHLNTNRNSSLSKQQSLENDLSVTLTLDHRLSLGSDDEADLVKELQSMCSSKSESDISKIADSRDDLRKFDSSRTNPGTSAPLNLRTPVPQKEASPPSSRQTAECSNSKSKTEMGVSSVKSFLPVPRSKVAQCSQNTKRNSSSSNTRQLEINNNSKEENWTLDKHEQVEKPNK
Protein: Mucin-like protein 1 (Protein BS106) (Small breast epithelial mucin) (Q96DR8)
Organism: Homo sapiens (Human)
Function: May play a role as marker for the diagnosis of metastatic breast cancer.
Subcellular location: Secreted {ECO:0000305|PubMed:15880534}. Membrane {ECO:0000305|PubMed:15880534}.
Interaction partners:
- Mammaglobin-A
Sequence:
MKFLAVLVLLGVSIFLVSAQNPTTAAPADTYPATGPADDEAPDAETTAAATTATTAAPTTATTAASTTARKDIPVLPKWVGDLPNGRVCP
Protein: TARBP2 subunit of RISC loading complex (F8VZ57)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSKKAAKHKAAEVALKHLKGGSMLEPALEDSSSFSPLDSSLPEDIPVFTAAAAATPVPSVVLTRSPPMELQPPVSPQQSECNPVGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGCGLPPGWSSKPGPRLHLGFSTKFSRREDPVPPQLLPGLPGCPGPCLLPCPQ
Protein: Protein MEMO1 (C21orf19-like protein) (Hepatitis C virus NS5A-transactivated protein 7) (HCV NS5A-transactivated protein 7) (Mediator of ErbB2-driven cell motility 1) (Mediator of cell motility 1) (Memo-1) (Q9Y316)
Organism: Homo sapiens (Human)
Function: May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Is required for breast carcinoma cell migration.
Interaction partners:
- Large ribosomal subunit protein eL32
- Receptor tyrosine-protein kinase erbB-2
Sequence:
MSNRVVCREASHAGSWYTASGPQLNAQLEGWLSQVQSTKRPARAIIAPHAGYTYCGSCAAHAYKQVDPSITRRIFILGPSHHVPLSRCALSSVDIYRTPLYDLRIDQKIYGELWKTGMFERMSLQTDEDEHSIEMHLPYTAKAMESHKDEFTIIPVLVGALSESKEQEFGKLFSKYLADPSNLFVVSSDFCHWGQRFRYSYYDESQGEIYRSIEHLDKMGMSIIEQLDPVSFSNYLKKYHNTICGRHPIGVLLNAITELQKNGMNMSFSFLNYAQSSQCRNWQDSSVSYAAGALTVH
Protein: F-box protein SKIP28 (Protein MATERNAL EFFECT EMBRYO ARREST 11) (SKP1-interacting partner 28) (Q9ZU90)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Required during the endosperm development in embryos.
Interaction partners:
- Protein ARABIDILLO 1
- CCG-binding protein 1
- At5g50410
- F-box/LRR-repeat protein 17
Sequence:
MKTELEEEEEEEWRSVHEVLLIVLPYLHSLFELLSMIRVSRSLRDAIRDETALWTKLVIEPPLSSRLTDDILSEFSSKSAGKLKTLILRQCLMVTNKGLRRVVDANPLITKIIVPGCSGLTPEGIMECVESLSKNNHKLETLHINGVNGFTKQHLSALYTYLSSEGTIDLEVCPKCDEVRMIPSCSRESCNQKQRKCRGCWLCIPRCAECAVCLVGSDTESQEAACGNDDVLCLECWLVLPKCRFCNKPYCTNHSSRRHEIAITDAASRPSFECEACYYRAGTNPYEVDYQI
Protein: Osmotic avoidance abnormal protein 3 (Kinesin-like protein osm-3) (P46873)
Organism: Caenorhabditis elegans
Function: Kinesin motor protein which is required for the anterograde intraflagellar transport (IFT) along the middle segment of the sensory neuron cilia together with the kinesin II motor complex (composed of klp-11, klp-20 and kap-1) and on its own, is required for IFT along the distal segment. In addition, regulates the length of cilia. May have a role during neurogenesis and axonal transport.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:17420466, ECO:0000269|PubMed:28479320}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:27623382}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27623382}. Note=Localizes along the full cilium length. {ECO:0000269|PubMed:17420466, ECO:0000269|PubMed:27623382}.
Interaction partners:
- Kinesin-associated protein
- Intraflagellar transport protein 52 C-terminal domain-containing protein
- Cytoplasmic dynein 2 heavy chain 1
- Intraflagellar transport protein 122 homolog
- Intraflagellar transport protein 88 homolog
- CHE-2 protein
- WD_REPEATS_REGION domain-containing protein
- Tetratricopeptide repeat protein 30 homolog
- Intraflagellar transport protein osm-1
- Intraflagellar transport protein che-13
Sequence:
MAESVRVAVRCRPFNQREKDLNTTLCVGMTPNVGQVNLNAPDGAAKDFTFDGAYFMDSTGEQIYNDIVFPLVENVIEGYNGTVFAYGQTGSGKTFSMQGIETIPAQRGVIPRAFDHIFTATATTENVKFLVHCSYLEIYNEEVRDLLGADNKQKLEIKEQPDRGVYVAGLSMHVCHDVPACKELMTRGFNNRHVGATLMNKDSSRSHSIFTVYVEGMTETGSIRMGKLNLVDLAGSERQSKTGATGDRLKEATKINLSLSALGNVISALVDGKSKHIPYRDSKLTRLLQDSLGGNTKTIMIACVSPSSDNYDETLSTLRYANRAKNIKNKPTINEDPKDALLREYQEEIARLKSMVQPGAVGVGAPAQDAFSIEEERKKLREEFEEAMNDLRGEYEREQTSKAELQKDLESLRADYERANANLDNLNPEEAAKKIQQLQDQFIGGEEAGNTQLKQKRMKQLKEAETKTQKLAAALNVHKDDPLLQVYSTTQEKLDAVTSQLEKEVKKSKGYEREIEDLHGEFELDRLDYLDTIRKQDQQLKLLMQIMDKIQPIIKKDTNYSNVDRIKKEAVWNEDESRWILPEMSMSRTILPLANNGYMQEPARQENTLLRSNFDDKLRERLAKSDSENLANSYFKPVKQINVINKYKSDQKLSTSKSLFPSKTPTFDGLVNGVVYTDALYERAQSAKRPPRLASLNPK
Protein: RNA polymerase II assembly factor rtp1 (O42977)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the cytoplasmic assembly and the nuclear import of RNA polymerase II.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDANQKLLDFAKLLNQKNDSRPVIEKLKDNISGDLLNYFLNLLEEISKLDTDQPLSVTSLRCLQLFVHLTFLLGVYTQLPKEMLSQAKIKALPIYTPKKNLVQIYNILLPLLLTPSLLQGPLNLHYADLLLLHLYLLNCHEQGSLIEEPRPLFLDPSWKEKVTSIMSPQMVDPSKMISSCLSLLQPNVDNWLQDKLKHYLTTCLCRETGVQGFLKVYMQAQPNSIERARQAAHLISSVPKDISPQKYFSCILPQVWSLFSTQPRLASQLIIAVTNTHCDIVTSFLLKKLQILEAPKVIDLSPFENALDVLQVLVYIQNDDIIRICESCVPSLLHLQENTTLRSKVQDILLRIISVCGTKSLLRNLTNAKHLRIFCERLTKSQLAMFLPNLLEIWVQQPPDKRLELLELVQYALSNVDSDEIPSNVMLSVCTNLINEVASQNKYSSTEISQITTNREVEEENEEILLVLLNIISSVIGRNAELDLENPISSLLPALEQLSNYSNREISDLAKDVYKTLIQSKDDYSLALSYTQSDLVPVRGQGVYMLRKLIEKKDDRINPVRVLHVLINLLRDENSYVHLNVISAVVSLCDKYDDSLIRLLKEYTNTNKFTVDETLLIGQAIYQTMERQGELVAKFYGQIEQTCLSMLNNENTDIKISSLNIARLLCQMTSSDAFIESAKNILILEMGSDKQFLRRAAVQLLDSCKHLPDSVITTLSYVGSHDKDDFIKESCLNILANQADAAKYYLQ
Protein: Ras-related protein Rab-39A (Rab-39) (Q14964)
Organism: Homo sapiens (Human)
Function: Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in vesicular trafficking. Plays a role in the fusion of phagosomes with lysosomes. Negatively regulates LPS-induced autophagosome formation in macrophages possibly by implicating PI3K. May be involved in multiple neurite formation (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:24349490}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Lysosome {ECO:0000269|PubMed:24349490}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
Sequence:
METIWIYQFRLIVIGDSTVGKSCLLHRFTQGRFPGLRSPACDPTVGVDFFSRLLEIEPGKRIKLQLWDTAGQERFRSITRSYYRNSVGGFLVFDITNRRSFEHVKDWLEEAKMYVQPFRIVFLLVGHKCDLASQRQVTREEAEKLSADCGMKYIETSAKDATNVEESFTILTRDIYELIKKGEICIQDGWEGVKSGFVPNTVHSSEEAVKPRKECFC
Protein: Large ribosomal subunit protein uL4 (50S ribosomal protein L4) (P9WH85)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Interaction partners:
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein bS16
- Large ribosomal subunit protein bL35
- Small ribosomal subunit protein bS1
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL5
Sequence:
MAAQEQKTLKIDVKTPAGKVDGAIELPAELFDVPANIALMHQVVTAQRAAARQGTHSTKTRGEVSGGGRKPYRQKGTGRARQGSTRAPQFTGGGVVHGPKPRDYSQRTPKKMIAAALRGALSDRARNGRIHAITELVEGQNPSTKSARAFLASLTERKQVLVVIGRSDEAGAKSVRNLPGVHILAPDQLNTYDVLRADDVVFSVEALNAYIAANTTTSEEVSA
Protein: TrwE protein (O50337)
Organism: Escherichia coli
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MFGRKKGDVIDAGAELERAEQERIEGEYGASELASERRPHTPGARTLLMVLLCVIAVVLVTLSYKAYKVRGVVEDDDAQPQQVVRQVIPGYTPRPIRPEPENVPEPPQPTTSVPAIQPAPVTQPVRPQPTGPREKTPYELARERMLRSGLTAGSGGGEDLPRPQGGDVPAGGLMGGGGGGGELAEKLQPMRLSGSSAGRLGNRDMLITQGTQLDCVLETRLVTTQPGMTTCHLTRDVYSTSGRVVLLDRGSKVVGFYQGGLRQGQARIFVQWSRIETPSGVVINLDSPGTGPLGEAGLGGWIDRHFWERFGGAIMISLIGDLGDWASRQGSRQGNNSIQFSNTANGVESAAAEALRNSINIPPTLYKNQGERVNILVARDLDFSDVYSLESIPTK
Protein: Large ribosomal subunit protein uL6 (50S ribosomal protein L6) (P9WH81)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Interaction partners:
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein bL19
- Small ribosomal subunit protein bS18A
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein bL34
- Small ribosomal subunit protein bS6
- Large ribosomal subunit protein uL16
Sequence:
MSRIGKQPIPVPAGVDVTIEGQSISVKGPKGTLGLTVAEPIKVARNDDGAIVVTRPDDERRNRSLHGLSRTLVSNLVTGVTQGYTTKMEIFGVGYRVQLKGSNLEFALGYSHPVVIEAPEGITFAVQAPTKFTVSGIDKQKVGQIAANIRRLRRPDPYKGKGVRYEGEQIRRKVGKTGK