wanglab/gogpt-training-data huggingface dataset:
Protein: Potassium voltage-gated channel subfamily A member 6 (MK1.6) (Voltage-gated potassium channel subunit Kv1.6) (Q61923)
Organism: Mus musculus (Mouse)
Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (By similarity). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (By similarity). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (By similarity). Homotetrameric channels display rapid activation and slow inactivation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P17658}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Potassium voltage-gated channel subfamily A member 2
- Potassium voltage-gated channel subfamily A member 1
- Voltage-gated potassium channel subunit beta-2
- Voltage-gated potassium channel subunit beta-1
- Ubiquitin-like protein FUBI
- Voltage-gated potassium channel subunit beta-3
Sequence:
MRSEKSLTLAAPGEVRGPEGEQQDAGEFQEAEGGGGCCSSERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFMEEIRFYQLGEEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPQFRADGRGGSNEGSGTRLSPASRSHEEEDEDEDSYAFPGSIPSGGLGTGGTSSLSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKAAFFRNIMNIIDLVAIFPYFITLGTELVQRHEQQSVSGGSGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADDVDSLFPSIPDAFWWAVVTMTTVGYGDMYPMTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEQEEQGQYTHVTCGQPTPDLKATDNGLGKPDFAEASRERRPSYLPTPHRAYAEKRMLTEV
Protein: Signal recognition particle 19 kDa protein (SRP19) (Q943Z6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (By similarity). Binds directly to 7SL RNA (By similarity). Mediates binding of SRP54 to the SRP complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P09132}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P09132}.
Interaction partners:
- Signal recognition particle 14 kDa protein
- Signal recognition particle 9 kDa protein
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP54 3
- Signal recognition particle subunit SRP54, chloroplastic
- Signal recognition particle subunit SRP54 2
- Signal recognition particle subunit SRP54 1
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP72
- Cell division protein FtsY homolog, chloroplastic
Sequence:
MDSGTINIKKWVVIYPVYINSKKTVAEGRRISVSKSCENPNCIEISDCCKHLKLPSAVEIDKAYPRDFMQVGRVRVQLKREDGTLLNPAITSRKHLMQKIAELVPRHPERVKKQEAQKAKKQEPQATTSTSGTSSKSGKGGKKKR
Protein: Insulin-like peptide 17 (G5EFH1)
Organism: Caenorhabditis elegans
Function: Involved in the regulation of the larval diapause.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- INSulin related
- Probable insulin-like peptide beta-type 1
- Probable insulin-like peptide beta-type 5
- Ceinsulin-1
- INSulin related
- Probable insulin-like peptide beta-type 3
- INSulin related
Sequence:
MFSTRGVLLLLSLMAAVAAFGLFSRPAPITRDTIRPPRAKHGSLKLCPPGGASFLDAFNLICPMRRRRRSVSENYNDGGGSLLGRTMNMCCETGCEFTDIFAICNPFG
Protein: Membrane frizzled-related protein (F1QRG7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
- Serine protease 56
- Transmembrane protein 98
- C1q and TNF-related 5
- Carboxypeptidase Z.
Sequence:
MDGEDSAESQSAYENVFCNPAFEPDEDNEENTRSAQIHIYFEPAKEPAAVNVLTVRACLADHRAVLVSAAVLFVSTVLCITLIFLLKQVETTKEEVSPSDTWFGNRVSENLSLSPTALQPTYSPTVSVSGTEPTFTKCGGMLSGAGGTLSSPNHPGVYPPDSHCVWVIRVSPPSLVQIQVSSLAIEGPSPCLFDWLEVREETEKTSAATRFCGNVAPPTLNTNSSTVLVSFHSDGSIGGTGFIAQYHSILPGQRSCSREEFMCDSGHCLLPVFICDGQPNCQDHSDELNCSHKHRVCGGQITGEYGSLSSPNHPKPYPHQQMCTWQISVEDGQVIRLSFQNFSLEAQDVCKFDYVEVYDGAETALGRYCGSALPPDLTSSGPVLTVVFVADEGVADSGFYASFQAISLSERTCSPAQFACPTGECLHQDWLCDGWSDCADGADEHHCMNSTYPPFTSSCELIQVEMCRDLSYNLTSFPNIWLSLSDQREAASILHKYRVLVDLPCFESFRQLVCGMFLPRCSPQSGVLQLCQSVCSTAELQCSPALSLFSLNWPFNCLLLPDSHDPMECSLP
Protein: RNA-directed RNA polymerase (EC 2.7.7.48) (Q9FZT2)
Organism: Pseudomonas phage phi13
Interaction partners:
Sequence:
MTSRFGEDEQDAHHSEHVDLDVELGHTVSARSTGKPRAPWKRKLGYEGGAPVFDGSDAHVDALFRANNNNSAAKRNREAPFREGPIETMRDRMSWDESNLRVMDRLSTKLTDRFPASTDKLGRVGPNAIRANFLGLRHVPGLPMIPATFPLTDNTKKRNDAGLADGPINKQHELIFRATIRLFFSSLENQGLKIARGSSTGCPDFQKTMSAKVMTATRALANAEAAGKLYLKGAYREAFLLYDFGGCYYVVYREQMSDAVTVDEAGDFVAKVRQVATEEYAVSGGHKGKMIEASKDPSRLRDAGYYVPEGFFATRRRTAMACPFTSNAPIMVIAQSVRARVYHEYAYTLHHTTRSQKQEKVSDWNFAIATDVSDHDTFWPGWLLDLICDELAEMGFADWWIEILRTTMRLPVYVSAPGPDIGHVLFGDWENPQMNVGLPSGIGITDLMGSLLMVPCYTIMQLDHTAPHLWASVRDLPSACTWMDSYLRGNEEILQMSKSDDALLGWKRGPSSAAARKLLDKMQEGDKTLSPYMIISYEHGGAFLGDILTYDHTGDLADARFTGNVISYVVNMFCPEYSVDSKQPSREKRARPFAGLAVEAAPTVFGSAPHFDDINDVIEEVHHDMLGYSYRAFRQDILAEDKAALADWIRRRSSFESLGALSPIDHEVLADPSKMWWKFDILEINPAVVELVSSGLERSLTESFFNSVTRDVR
Protein: Nucleoporin NIC96 (Nuclear pore protein NIC96) (G0S024)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NIC96, which is localized to the core of the NPC and the distal ring of the nuclear basket, is required for de novo assembly of NPCs.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P34077}. Nucleus membrane {ECO:0000250|UniProtKB:P34077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P34077}; Cytoplasmic side {ECO:0000250|UniProtKB:P34077}. Nucleus membrane {ECO:0000250|UniProtKB:P34077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P34077}; Nucleoplasmic side {ECO:0000250|UniProtKB:P34077}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P34077}.
Interaction partners:
- Nucleoporin NSP1
- Nucleoporin NUP188
- Nucleoporin NUP57
- Nucleoporin NUP49
- Nucleoporin NUP152
- Nucleoporin NUP192
- Nucleoporin NUP170
- Nucleoporin NUP145
- Nucleoporin NUP84
- Nucleoporin SEH1
Sequence:
MSLIGNGPSVPPSSTKASLFSSPTTSANPTGGLFGSTTGGSSLFAPKTAGSTTTSTTQPTSTTGLGTSLFGTSTTANTQNTANAARPSLFTAGNSIFGTSTTQPGLGASSLTTAATSNQQAQQQQQQRQQHQQAAPTGALFDSLLARNKKQAEGETALGELPSLQLGLADLRQRLRKLGPSSDRPIEPGKAHYFLAASGVDPGAAVRDLGALGLQAKTERTAASVGPAAGPSGVSTTGFGTGLGEVDVDTYLSNLQTKTTLSMIADGLERSARDFDAFLEENVTLEWEAQRKRIYQHFGIKPRDSSVAGTTTAQPTATPSKDGQGTFGRSRRKASQPPPGERPAQRMSILGRSTMMRSVIGTPTRIGAHAPEFSDVEARKDSSGAAVASVDDRFLREKQAKLAEKIREFNDARQRGTPFYICRDLADLESKSGDRHGPHIVEAYRAVMEMVGEHPDAGEAPRERQFAKMYLDPNTQSANALAMRKQILKGATTFLEKQFWNEVNSLIAKYPQDANLGGLPDVVSKIKAYIRLRIARKTLVPDNVELQQINGEYVWAIVFYLLRAGFVTEAAQYVNSNQAHFRAIDRTFSGYINSYASSEERRLKRQMQDRCMSEYNQRIRNAPEGSIDPFRMACYKIIGRCDLSNRSLDGLQTDVNDWIWLQFNLARETDRSLELAGESYGLAELQASIREIGLKHFPKTAAEDTNGSFGMFFYLQILAGMFEQAIAYLYPFSYVDAVHFAIALTYYGLLRPVDAASAGNELLSHNTRSMPQINFGRMLGYYTRDFRAANPAAAVDYLVLICLNADEAAGGQQAQAALCHEALRELVLESREFSRLIGDIRPDGRRIRGVIEERGPLIALGQEDDFIRTITLQAASFADDNGRTTDAVLLYHLAEDYDTVVSIVSRALSEAISLEIGEDPMRLIPVKPRVTNAEGQVEEAAPGSSLSLAAIDDPVELAKAMMGMYERDHMFWQKIREPNRVACSVLLQMADIKSLVEQGRWAECLDKIRALDILPLTARGDPGTIRSYAARFPSLAQPVAINVPNLLMWTVLCCMRQRERLAGGQFAGNESTARLMMDELKQMTVDLMAYTSQLRYRLPPHLHEALARASAD
Protein: RNA-binding post-transcriptional regulator csx1 (O13759)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulates global gene expression after oxidative stress. Interacts and stabilizes atf1 and pcr1 mRNAs after oxidative stress, thus controlling their turnover.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14633985, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Dual specificity protein kinase lkh1
- Iron-sulfur cluster biogenesis chaperone, mitochondrial
- Mitogen-activated protein kinase sty1
- Pre-mRNA-processing factor 39
- Transcription factor atf1
- Transcriptional repressor tup11
- ATP-dependent helicase upf1
Sequence:
MSIDCLYRRSSLFDTSFVPLHSSIPATSKMSASNSDVNAPISPVVDEGKSELVSPTLERLVAPFNCSPSSTPLQDVAGVGSKMSDTLWMGDLEPWMDATFIQQLWASLNEPVNVKVMRSKASSSETLISYCFVQFSSSAAAERALMKYNNTMIPGAHCTFKLNWATGGGIQHNNFVSRDPEFSIFVGDLLPTTEDSDLFMTFRSIYPSCTSAKIIVDPVTGLSRKYGFVRFSSEKEQQHALMHMQGYLCQGRPLRISVASPKSRASIAADSALGIVPTSTSNRQPNQDLCSMDPLNTTVFVGGLASNLSEKDLQVCFQPFGRILNIKIPFGKGCGFVQYSEKSAAEKAINTMQGALVGTSHIRLAWGHNTLPVSALSQSQSQVSDEGFDRTLSANQIFGMNQSVIGANSGSSNSSGSSLKSAPVSPRTAAAQSLLPNSVVSSINGMNSVNFSTISPPPLSRSASISPTLSGSGSGLTPLSSHFPSAATGLVGGQVYPQSSVLQSSKINGSAKVQPSVKLPEWLQPFSGNNHNSFATQDLLTRVSSLKLVDDEQPASLNGSAFQARASRPWNLGRERQSSLIDLRHELEQNENGLEKSGFGLNLRGRLPPRSYSTFNCTGQYLQPSLRLSRDS
Protein: GH26015p (Q7K3N4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Gastrulation defective protein 1 homolog
- LD40136p
- Cellular retinaldehyde binding protein
- Trehalose 6-phosphate phosphatase
Sequence:
MQVFDNNMRRASRRASLRRGSISALPQKSHEIPWDIFERLFMPFLFCQAAAIVTSHLLHALDISSISTFAVFVWFALATVGAVLFYHFVKVSASGKGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPIEESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHLPHGAEGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAGEFAPGNGWLNETELRDQAKQMWNQLSSEQKKTYGEDYYEAAMTSVEKYSRQAADIQPTLRVLIDAVTRTFPMARYTPVTSSERLQIFLAEHLAPSLYESLYGEQKKFVY
Protein: RE12330p (Tara 1A isoform) (Taranis, isoform A) (Q9VEX7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKMWTESNVNSAMGLQATAATKRKHELTFDSKDANTTYTGNCAPPPVKANKWAISNNNYLESLEEQQQQQQSPSEPAVESNNNHIVLEASMDALKPTEPSISNGHEVTTAVAAMKSQAEVPLPPTASAAIPEDSIARLEVVTSAVPCEPWTSNGPTTPSAVAGPAASAEPVDCISKLQAVAVPSDPWGSIATRSTLATTLLSADELDDDDDDFEDDYEEEESIIPTYCPMRYHPFVPHPHPHSHQLPSHPHQQQPQQLSQQQPHPQQQQLAQQQQQHPQQQRSYAPGYGSRQPNYYSEPFPQQNCSRTGGPQHMTQSPPTPQQARGFAPPQWATAGSSPANPSSGAQQFYEPTNGGAYAPPAAPQQTIRCAENGKSYLDLGCSSGASGNAGGSPISPPPSSAPVVPFAGLPLHGLPLKRCCDGRPGGWCSANRSCYKDTRLKIRNLSMFKLSRFRQVSEQSLYRSVLICNTLKRIDREIEAEAKELHQAAQQHHQQAAAAAAAAAAAAAQAAQYHPAYQQQQQQQQSPPAPLHPHTQQQMDYAPVLNCARLANMDHYQQLSFQPQHQQQQQPSQPHSYHERLDSQPAYRGAAAGAGSFATQPSNCDTSAGASSSNTSGNSNNSSATAASSNSSLHPYDHYPFRESQSGRATPFPACPTTTAAAAAASAAAAASSGGAATTLSSNISSSPASSSTSSNTTSSTVISSSSGNTVSSNGTTPVAPTASSSNCDTSDSGYADDDSTRSINWSSVLSLSSQSALDPLNNNDLFSILPSAATPTAVPVSVPASSSSSSSGSTLAFSGSFTTVQASGGSSSSCGSSSTTATFTTLSTISSATHSLTSSYVSSISSNVSAGANTWEYGFLDMEFGLGSEFTELVPSCKLSSEDLFKSGLGGQVVTASRLHDNELEHPAHIMVGS
Protein: B-cell differentiation antigen CD72 (Lyb-2) (CD antigen CD72) (P21854)
Organism: Homo sapiens (Human)
Function: Plays a role in B-cell proliferation and differentiation.
Subcellular location: Membrane; Single-pass type II membrane protein.
Interaction partners:
- Semaphorin-4D
- T-cell surface glycoprotein CD5
- Tyrosine-protein phosphatase non-receptor type 6
- B-cell receptor CD22
- Plexin-B1
- Low affinity immunoglobulin gamma Fc region receptor II-b
- B-cell antigen receptor complex-associated protein beta chain
- B-lymphocyte antigen CD19
- B-cell antigen receptor complex-associated protein alpha chain
- Pre-B lymphocyte protein 3
Sequence:
MAEAITYADLRFVKAPLKKSISSRLGQDPGADDDGEITYENVQVPAVLGVPSSLASSVLGDKAAVKSEQPTASWRAVTSPAVGRILPCRTTCLRYLLLGLLLTCLLLGVTAICLGVRYLQVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQSEEQQRRALEQKLSNMENRLKPFFTCGSADTCCPSGWIMHQKSCFYISLTSKNWQESQKQCETLSSKLATFSEIYPQSHSYYFLNSLLPNGGSGNSYWTGLSSNKDWKLTDDTQRTRTYAQSSKCNKVHKTWSWWTLESESCRSSLPYICEMTAFRFPD
Protein: Citrate lyase, beta subunit, putative (P95083)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTSMYEQVDTNTADPVAGSRIDPVLARSWLLVNGAHGDRFESAAHSRADIVVLDIEDAVAPKDKHAARDNAVRWFGDGNADWVRINGFGTPWWADDLAMLADSPVGGVMLAMVESVDHVTETAKRLPNVPIVALVETARGLERINEIAAAKGTFRLAFGIGDFRRDTGFGEDPATLAYARSRFTIAARAAGLPSAIDGPTIGSNALKLIEATAVSAEFGMTGKICLSPDQCPVVNEGLSPSQDEIVWAKEFFAEFARDGGEIRNGSDLPRIARATKILDLARAYGIEVSDFEDEPVHMPAPTDTYHY
Protein: Polycystin cation channel PKD1/PKD2 domain-containing protein (Q8WSP3)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}.
Interaction partners:
Sequence:
MSRRSTTDRSDFNDNASNASSNASRRPTINFQEIMEDLPHHERETGERLRRHLQFFFMNPMEKWKVRHQLPYKLVLQVLKIVFVTMQLILFAEMRMSHVDFLEDTTTVMRHRFLKEWNDDRDALQYPPAEGRYSVYDDQGLSEHLSFLINSYYSIRNDSFASFSYDVVSHPSGNLGAQISFESIPPIEVLIDRISNVTVNNNTYNFDIREVKDTKRLNLTETEVFQIGQSDDAVRDILATRGITFLPEDALKISTVQFKFRLRTIHYSPTAGDQKPECYKISVSIKFDNSRHTGQVHVTLSTVVSYVNVCNGRIIKGVGWSFDTLLIGGTDIFVLILCILSLILCCRALIKAHLLQIKTSDYFENVLKNKITVTDQLDFLNLWYVMIVVNDALIIIGTVAKISIEFQFNKNTFTTRNDFDNSLFTLTSIFLGMGALLVYVGVLRYFGFFSQYNILMLTLKRSAPNIMRFMTCAIVLYAGFLIAGWVIIGPYSMKFRTLAESSEALFSLLNGDDMFATFYTINDSNTVIKVFGTVYIYLFVSLFIYVVLSLFIAIIMDAYEVVKDRYSDGLRAIEKRGCLRDFVESNPPPSELGSPTTRSAYAPSNLLNLGRCVPVEVTRIFLCSGFLHTFSFFLHLCTPNKLGC
Protein: Small ribosomal subunit protein eS17B (40S ribosomal protein S17-B) (RP51B) (P14127)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS6A
- Small ribosomal subunit protein uS2B
- Small ribosomal subunit protein eS28A
- Small ribosomal subunit protein eS28B
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS19B
- Small ribosomal subunit protein eS25A
- Small ribosomal subunit protein eS1B
- Small ribosomal subunit protein uS11A
- Small ribosomal subunit protein RACK1
Sequence:
MGRVRTKTVKRASKALIERYYPKLTLDFQTNKRLCDEIATIQSKRLRNKIAGYTTHLMKRIQKGPVRGISFKLQEEERERKDQYVPEVSALDLSRSNGVLNVDNQTSDLVKSLGLKLPLSVINVSAQRDRRYRKRN
Protein: Caveolin-3 (Q2KI43)
Organism: Bos taurus (Bovine)
Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. May also regulate voltage-gated potassium channels. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress. Mediates the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P56538}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250|UniProtKB:P51637}; Peripheral membrane protein {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P51637}. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). {ECO:0000250}.
Interaction partners:
- Caveolin-2
- Tyrosine-protein kinase
- Caveolin-1
- Dysferlin
- Tyrosine-protein kinase Fyn
- Calmodulin-like protein 4
- CALML5 protein
- Receptor protein-tyrosine kinase
- Integrin beta
- EF-hand calcium-binding domain-containing protein 11
Sequence:
MMAEEHTDLEAQIVKDIHFKEIDLVNRDPKNINEDIVKVDFEDVIAEPVGTYSFDGVWKVSYTTFTVSKYWCYRLLSTLLGVPLALLWGFLFACISFCHIWAVVPCIKSYLIEIQCISHIYSLCIRTFCNPLFAALGQVCSNIKVMLRKEV
Protein: Pericentriolar material 1 (A0A5H1ZRS1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATGGGPFEDGMNDQDLPNWSNENVDDRLNNMDWGAQQKKANRSSEKNKKKFGVESDKRVTNDISPESSPGVGRRRTKTPHTFPHSRYMSQMSVPEQAELEKLKQRINFSDLDQRSIGSDSQGRATAANNKRQLSENRKPFNFLPMQINTNKSKDASTNPPNRETIGSAQCKELFASALSNDLLQNCQVSEEDGRGEPAMESSQIVSRLVQIRDYITKASSMREDLVEKNERSANVERLTHLIDHLKEQEKSYMKFLKKILARDPQQEPMEEIENLKKQHDLLKRMLQQQEQLRALQGRQAALLALQHKAEQAIAVMDDSVVAETAGSLSGVSITSELNEELNDLIQRFHNQLRDSQPPAVPDNRRQAESLSLTREVSQSRKPSASERLPDEKVELFSKMRVLQEKKQKMDKLLGELHTLRDQHLNNSSSSPQRSVDQRSTSAPSASVGLAPVVNGESNSLTSSVPYPTASLVSQNESENEGHLNPSEKLQKLNEVRKRLNELRELVHYYEQTSDMMTDAVNENRKDEETEESEYDSEHENSEPVTNIRNPQVASTWNEVNSHSNAQCVSNNRDGRTVNSNCEINNRSAANIRALNMPPSLDCRYNREGEQEIHVAQGEDDEEEEEEAEEEGVSGASLSSHRSSLVDEHPEDAEFEQKINRLMAAKQKLRQLQDLVAMVQDDDAAQGVISASASNLDDFYPAEEDTKQNSNNTRGNANKTQKDTGVNEKAREKFYEAKLQQQQRELKQLQEERKKLIDIQEKIQALQTACPDLQLSAASVGNCPTKKYMPAVTSTPTVNQHETSTSKSVFEPEDSSIVDNELWSEMRRHEMLREELRQRRKQLEALMAEHQRRQGLAETASPVAVSLRSDGSENLCTPQQSRTEKTMATWGGSTQCALDEEGDEDGYLSEGIVRTDEEEEEEQDASSNDNFSVCPSNSVNHNSYNGKETKNRWKNNCPFSADENYRPLAKTRQQNISMQRQENLRWVSELSYVEEKEQWQEQINQLKKQLDFSVSICQTLMQDQQTLSCLLQTLLTGPYSVMPSNVASPQVHFIMHQLNQCYTQLTWQQNNVQRLKQMLNELMRQQNQHPEKPGGKERGSSASHPPSPSLFCPFSFPTQPVNLFNIPGFTNFSSFAPGMNFSPLFPSNFGDFSQNISTPSEQQQPLAQNSSGKTEYMAFPKPFESSSSIGAEKPRNKKLPEEEVESSRTPWLYEQEGEVEKPFIKTGFSVSVEKSTSSNRKNQLDTNGRRRQFDEESLESFSSMPDPVDPTTVTKTFKTRKASAQASLASKDKTPKSKSKKRNSTQLKSRVKNIRYESASMSSTCEPCKSRNRHSAQTEEPVQAKVFSRKNHEQLEKIIKCNRSTEISSETGSDFSMFEALRDTIYSEVATLISQNESRPHFLIELFHELQLLNTDYLRQRALYALQDIVSRHISESHEKGENVKSVNSGTWIASNSELTPSESLATTDDETFEKNFERETHKISEQNDADNASVLSVSSNFEPFATDDLGNTVIHLDQALARMREYERMKTEAESNSNMRCTCRIIEDGDGAGAETPVIENRSSQQPVSEVSTIPCPRIDTQQLDRQIKAIMKEVIPFLKEHMDEVCSSQLLTSVRRMVLTLTQQNDESKEFVKFFHKQLGSILQDSLAKFAGRKLKDCGEDLLVEISEVLFNELAFFKLMQDLDNNSITVKQRCKRKIEATGVIQSCAKEAKRILEDHGSPAGEIDDEDKDKDETETVKQTQTSEVYDGPKNVRSDISDQEEDEESEGCPVSINLSKAETQALTNYGSGEDENEDEEMEEFEEGPVDVQTSLQANTEATEENEHDEQVLQRDFKKTAESKNVPLEREATSKNDQNNCPVKPCYLNILEDEQPLNSAAHKESPPTVDSTQQPNPLPLRLPEMEPLVPRVKEVKSAQETPESSLAGSPDTESPVLVNDYEAESGNISQKSDEEDFVKVEDLPLKLTIYSEADLRKKMVEEEQKNHLSGEICEMQTEELAGNSETLKEPETVGAQSI
Protein: Stage IV sporulation protein A (EC 3.6.1.-) (Coat morphogenetic protein SpoIVA) (Q81SW4)
Organism: Bacillus anthracis
Function: ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Directs the assembly of the coat and exosporium to an area around the forespore.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P35149}. Note=Localized on spore coat surrounding the forespore. {ECO:0000250|UniProtKB:P35149}.
Interaction partners:
- Stage II sporulation protein D
- Stage III sporulation protein D
- Stage VI sporulation protein D
- Stage III sporulation protein AA
- Spore coat protein E.
- Spore coat protein CotJC
- Stage 0 sporulation protein A
- Stage II sporulation protein P
- Stage II sporulation protein R
- Germination protease
Sequence:
MEKVDIFKDIAERTGGDIYFGVVGAVRTGKSTFIKKFMELVVIPNIENESDRQRAQDELPQSAAGRTIMTTEPKFVPNQAVSIEVDEGLEVNIRLVDCVGYTVPGAKGYEDENGPRMINTPWYEEPIPFHEAAEIGTRKVIQEHSTIGVVITTDGTIGEIPRRDYIEAEERVVNELKEVGKPFIMIINTVQPYHPDTEQLRQSLSEEYDIPVIAMSVESLRETDVYNVLREALFEFPVLEVNVNLPSWVMVLNEGHWLRQSYQEAVQETVKDIKRLRDVDRVVWQFSQYEFIDRASLAGIDMGQGVAEIDLYAPDELYDQILKEVVGVEIRGKDHLLKLMLDLSHAKIEYDQVADALRMVKQTGYGVAAPALADMSLDEPEIIRHGSRFGVKLKAVAPSIHMIKVDVESTFEPIIGTEKQSEELVRYLMQDFEDDPLSIWNSDIFGRSLSSIVREGIQAKLSLMPENARYKLKETLERIINEGSGGLIAIIL
Protein: LIM domain binding 1 (A0A8I5ZVT6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKEAFHSNFVSLDCDQGSMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQQPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQVPVSISAFFSSGLPHCSPLTPV
Protein: Transport permease protein (O67182)
Organism: Aquifex aeolicus (strain VF5)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361157}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361157}.
Interaction partners:
- ABC transporter
- Mannosyltransferase A
- Polysaccharide biosynthesis protein
- Polysaccharide biosynthesis protein
- DUF4214 domain-containing protein
Sequence:
MNLSLILELVRQEIKNRYADTVLGIWWAFLWPILLVLIYTLIFSHLIGAKLGHENTVYAYSIYLSSGIFPWFFFSNSLSRITGIFTEKKFLFTKIPIRLEVFPVVVIISELINYLIGISLVTLISFITLGFEGIKYFYLFPVALYLMIVYSFSIGMVLGTLNVFFRDIKEIIGVFLQIFFWFTPIVYTLDILPPFVKKLIYYNPMYPVVSIHHLVFVNYLDLHLYSLLGFLLASPLVFFVSYYFFKKLEKDIKDFA
Protein: Nuclear pore complex protein Nup160 homolog (Nuclear pore protein 160) (Q9VKJ3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions as a component of the nuclear pore complex (NPC). Involved in poly(A)+ RNA transport (By similarity). Required for nuclear import of Mad. May play a role in double strand break DNA repair. Essential for nephrocyte development.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:19197064}.
Interaction partners:
- Nuclear pore complex protein Nup205
- Protein SEC13 homolog
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup107
- Nucleoporin 43kD
- Nucleoporin seh1
- Nuclear pore complex protein Nup75
- Nucleoporin Nup37
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup154
Sequence:
MPTSKLQANMSYREVIPRNLSPAEWIEVKINTGTQSTLQDLKTFETSGGYCYKNTKNVQTRNRFIYWRTYQDVLELSEVSLDISLQRNHLRLRFTDSAVLNVSLTEQGTSVTLLVVTVSSVHRYVFPLKVAGQEGGAASPEDLLSQSIFYDVNDKINDPSTYYVTDGFGTMPNAAVSYLTQDSQSAYFAVAYQSKLLLHVMKCSTGHTITHEIKEPKLMPWFLSNLKGALTGRSETLEAATSMAFSEIGGEIFILVLYRNNELRLWSVDNLQTVASINCSTELGQDSAAQGPQNSQLRKISDQNFCLFLSHNSRAEFICVSIMPDADDASVINLVQNMVPAPQTDLVDFDATSSHIWALWSNAEGDFHVSAAYFASNNAIKWVSAALEPPPDRYCLTMEQGVDPRETYCSYIFHPGRFDRNVIAKALYMFRRVNLQFDVKQLSMSVLKEQVCQAVEDEIQNELKDFVVTDEEYLEISTRLWDRFYSCCEQYHIKLSEPTGLAVLGGMDAVCLVRRQSFALLRPCEVLEHLLLIGEHNDEVATYVAPLFRNDPEMAKGFVELMNVVTLLDKLISEDIKIELDKQLYQRESPVEVISKLVARISMIDDNGPILPSNCVRQIQQKLQNIPNLEPALEMLLDVLCMIDPDEPPHDYSLSTRFLQSSGALMGSEYGLSILSETVKQMAMIRFSVCRNLLVLQYMAYGQNEMESENVLTNLNYLNSYYTLVWIAETPISSSTPAGFEASIQRLSRAQLFSGYNRPYSSHLKHNGNDQTTLLRLFLESKGLFSALTMLLKHDSLSLDSEQLNLRQSLLQLVGYINKMLWPGSPIYVFPEWLFGTCHHIIVQDYVRILSNWCSVQKHARRFMLAVSLLDCGEAHKAVHLFHEAESGIVEDDFLFEHVLKNTPLYGKLQNSVSRGDTISPEDTKLAIVHYYLKVIQLFEQHSALDYIIQLADMAIRVLQPDDPQLPMFQSIVFNNHLQLGHYVEAYTALVNNADISRRKDCLRQLVITLFQNKCLPLLMQFSYIGLQDEFESIVESRARSMSIDQNEVYNFLYAFHTNKGNMRKASTVMYEQAMRFQVDSDAPNALEKRCSSLLICLNCLHLVDSRYRWIAKPVLGDEQVITIDQDNDDGEPKCDEDKRGQEVVVLELADIRRELVHAEALRELSFYRKDTAAYERATPEELSYLLASSGLYTAALKLSRGHSFSVLPIFESLTSACVAATEDKSSDAWNWLQNNDMADLPHRSNAADMAWTLLQKLVVDNEAKDSTLIRKSVVQRLLGLNAFLPQWLINSYKLSHSRELLHLLVKHNRLLEAADLGCEIIAGMLGAGSEYFEFKHAVNIANPQLCFPISTIDLLLHGLKINGKDDLDYEMAYFKLEEEVQRYIETIKRTTDDKMSMAVLQMRTDLQEER