wanglab/gogpt-training-data huggingface dataset:
Protein: Neuroligin-1 (Q8N2Q7)
Organism: Homo sapiens (Human)
Function: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Required to maintain wakefulness quality and normal synchrony of cerebral cortex activity during wakefulness and sleep (By similarity). The protein is involved in nervous system development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28841651}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62765}. Postsynaptic density {ECO:0000250|UniProtKB:Q62765}. Synaptic cleft {ECO:0000250|UniProtKB:Q62765}. Synaptic cell membrane {ECO:0000250|UniProtKB:Q62765}. Note=Enriched in synaptic plasma membranes and clustered in synaptic clefts and postsynaptic densities. Colocalized with DLG4/PSD-95 and GRIN1/NMDAR1. {ECO:0000250|UniProtKB:Q62765}.
Interaction partners:
- Neurexin-1
- Disks large homolog 4
- Neurexin-2
- SH3 and multiple ankyrin repeat domains protein 3
- Neurexin-3
- Nucleoredoxin
- Disks large-associated protein 1
- SH3 and multiple ankyrin repeat domains protein 1
- SH3 and multiple ankyrin repeat domains protein 2
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
Sequence:
MALPRCTWPNYVWRAVMACLVHRGLGAPLTLCMLGCLLQAGHVLSQKLDDVDPLVATNFGKIRGIKKELNNEILGPVIQFLGVPYAAPPTGERRFQPPEPPSPWSDIRNATQFAPVCPQNIIDGRLPEVMLPVWFTNNLDVVSSYVQDQSEDCLYLNIYVPTEDVKRISKECARKPGKKICRKGGPLTKKQTDDLGDNDGAEDEDIRDSGGPKPVMVYIHGGSYMEGTGNLYDGSVLASYGNVIVITVNYRLGVLGFLSTGDQAAKGNYGLLDLIQALRWTSENIGFFGGDPLRITVFGSGAGGSCVNLLTLSHYSEGNRWSNSTKGLFQRAIAQSGTALSSWAVSFQPAKYARMLATKVGCNVSDTVELVECLQKKPYKELVDQDIQPARYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGLKFVENIVDSDDGISASDFDFAVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRHNPETRRKTLLALFTDHQWVAPAVATADLHSNFGSPTYFYAFYHHCQTDQVPAWADAAHGDEVPYVLGIPMIGPTELFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVAWTRYSQKDQLYLHIGLKPRVKEHYRANKVNLWLELVPHLHNLNDISQYTSTTTKVPSTDITFRPTRKNSVPVTSAFPTAKQDDPKQQPSPFSVDQRDYSTELSVTIAVGASLLFLNILAFAALYYKKDKRRHDVHRRCSPQRTTTNDLTHAQEEEIMSLQMKHTDLDHECESIHPHEVVLRTACPPDYTLAMRRSPDDVPLMTPNTITMIPNTIPGIQPLHTFNTFTGGQNNTLPHPHPHPHSHSTTRV
Protein: WAPL domain-containing protein (Q7JP75)
Organism: Caenorhabditis elegans
Interaction partners:
- Ras-like GTP-binding protein rhoA
- Profilin-3
- FH2 domain-containing protein
- Protein ECT2
- Actin
- Profilin-1
- Anillin-like protein 1
- Myosin-11
- Profilin-2
- Formin-homology and zinc finger domains protein 1
Sequence:
MSSDDYESIDTPRVASLADMNRLPTQSRHSSYSTDDDEDVTPTPSASNSAPKNTILDPLQAQFLHPNSENSDIDEPRVQLREKKKATRAQDATVSHFLEDQVPNQKFKRRSAERHSMLAGAADFASRRSPFHLSGANGSGRWTDLFSSSRFKRKQRQKLNNVPSSSYSNNDYGTYAGTQSIGGFSIASNSSGESFALSGTEDEIREEFRKIMLDKGLPEADKIISNTPLDQMKMMIENSRKQDNQAKGRSPEWVVRVLGEILKTKNIPECKQDIVTVRVQLVGQGVSFLNKFAVEVHDESGRTGADLICCLYSLVLKRLRSSEVGSKYELDLIDFLQEIVRCVRTLINTHVGLVLVLRRNSPVYSLLIQTLCVLNRREQNDHEAAEIRAIRVDVVRTCYTLIFVQHDTLSTPIEMTGQQKMFMELSLIAKAESKRLNEPVSRFRPLISCIDFLESRDPKQGMYVLLMINMMINGVDRNISDDQMWTEETMWQARMRLRSEAAKDKLHKYIEKFTTSETVNSQIRDVAQNMLTEHNADLETLMGKLENVKGEYDTLDGCFELLAANSEATGTETVLLSILQLMTLTNEDMSTKRSYMKLIETAISDILLHRTPIDPQADYKFVFEVPVAEIIDKMQDEEMAKKVRQATSAKQEAVAMQGEYWKTLCDFQKEAEELRKHINDPKIPLPPPTKMNLSAPSTSAGGSSALPPITGGPPPPPGLPPITGGPPPPPPPGGLPPITGGPPPPPPPGGLPPISGGPPPPPPPPGGCPPPPPPPPPGGFKGGPPPPPPPGMFAPMAPVIPDYLPPKKVPKVDGPMRKFPWGAHTINPRDIPRESFWVGTNEEQLTSDRMFDRLRTKFATKPAANSGTLGGVLNSKKKVKTAQVIHDDKLLQKLGILQGSIKMSHSELKLAILEVNEKVLTVGFLEQLRSAMPVEKELIDKLRAVNKAQFEEMPEGEQFVTRLLQIQGLPLRLDLVLFKMRFSEVLNELKPAMSSVMEACEEVRASEGFRTFLKLVLATGNFMGGATKNYSSAYAFDMRMLTRLVDTKDVDNRHTLLHHLIEEMKRIDPRRARFALTDFHHCIESSRVNADEIRKTVQLTENNIKKLENCLKVYKIQGERDLFDEKMRPFHEKAVKEFSTVSSMCGKMKNDWESLVKYYAFNDKKYPMEEFFADIRTFSEQYSNAWKELDAEAEAKRKEAEFETQKRKQLQQSQQERKPLQERQAINRVPRTPAAMIRVSTAADKAGVLDELERATGNADFLQTLMSATNSRTPRSGLPARTRGGGRLGGGLDRQRSRHQNALGQLQDLTGCASEPVLSGQFARSRNVPQNDLQRQNMELPSSVKPTTALDRAKAFGVGLPIGQNELKVRVRRKGQPAVPVTNINGTSQISPTHKENDPTGSSSTSSGPASSNTATSSSSGTVVPSTDDLLARLNDF
Protein: Alanine--tRNA ligase (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Q8ID31)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03133}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03133}.
Interaction partners:
- Anaphase-promoting complex subunit 10, putative
- Anaphase-promoting complex subunit 11, putative
- tryptophan--tRNA ligase
- Protein kinase domain-containing protein
- Tryptophan--tRNA ligase
- glycine--tRNA ligase
- threonine--tRNA ligase
- 40S ribosomal protein S18, putative
- isoleucine--tRNA ligase
- glutamine--tRNA ligase
Sequence:
MIVYSFSFLIFLYFCLYLNIKESIILGNCKIILSRPFKEEKKKKDIYFFFNSGKNLLKRKKSTFDLLPLHSNKRRRINLFINNDKKKKIKSNSNNNNSNNNSNNNNSNNNNSNNNNNNSSSIKRECGEPFFSFYSYENILTVHNNKILKDQNNNYVLLHLCKKIKKKYKKEKNKKREYCNHYKFMYLNSIKRKDIFIKLNKINNKSHFYKDIHKSNKCIKTFIYSSSHNFHNSNYSSLNAFSFKSLFTKNTYNRSFLNFLKYTTKNNLKEKKNIKDFFSFSIKLGKDKNINLDNLKKGYYKDINTNNRSNHNKHNNNKYNYNNNNCSSNHFCSNHFCSNHFCSNHFCINMDMNDKLNNRNNWSNTNNPKDDNIKNTNCSTNDEGQKKYMSAEEVRNNFINYFHKKNHTIIESSSVVPYNDNTLLFTNAGMNQFKKIFLGNADKNSDLGKLKRAVDTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGNWSFGDYFKEESISFAWDLLTNVYKINPDRLYVTYFGGDENLSTCPADHETKKIWMKYISEDRILPFGLKENFWEMAETGPCGPCSEIHYDRIGNRDASSLVNKDDPSVLEIWNIVFMQYNKDENKNMNKLPFPCIDTGMGLERITSILQNVDSNYDTDLFQPIFKQIKELFPYLPNYEGKINEQDVDKIDTAYRVISDHIRCVTVAISDGCLPSNEGRNYVIRRIIRRAIRFGKQVFNIKSNVLWFYKLVDSVCFILGNTFKDLQNPDKINFIKNTIKQEEMVFNKTLEKGVEQFHKIIKKNTKNNIFSGKDAFDLYTSFGFPIDLIQIMCEEKSFNLDLQEFNDLFKKHQLVSDTNNFKINKFFDIPVEKSHELKNVHNINPTVDHFKYEWNNNCANDGDNKDIKFETYVQVIYDGNNFLDNFTLPSNNDEQVLEKEKSIEENKKKYALILKETNFYYENGGQIYDTGIIQNDNMKFQVLNVQKINEYVLHIGVFLKGYVSKNDKVQTIVDFDRRKLVACNHTATHMLNFMLRKVLTEKYTNSGKSSKTHEGNNEKHEMSENDINSNNNYDNNKEEKGFSIFTCEQKGSLVDDEKLRFDFSFIENINIDAITKIENEINKLIKEELNVTVKTMDLDESKKIKGIRAIFEEDYADKVNVVFINKDVNNILNNMNIDYTYLHSIELCGGTHIGNTKLIRKFLVTSEESIGKGIYRITAVTNKKADEIEKTFNDLYDKYKHVLQEPNENKLADVQNYKRTLKENKFLPYIKKYHILQELEQIEKTIVEKTKNMQKELFNKATNIGKDYAVQDKNNILLDIKFFDEIKGNQKVLEKIVQSYSKNNKNLSYFFIICDENNTYCVLEVKEALKNKNVQADLFMKEIMKSVLGHSGGSKNKAFGSVEKDKGMVIKEHAEEMLKNINK
Protein: Uncharacterized peptide chain release factor-like protein C1105.18c, mitochondrial (Q9Y811)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Meiotically up-regulated gene 82 protein
- Large ribosomal subunit protein bL12m
- Meiotic fizzy-related protein 1
- Putative peptide chain release factor 1, mitochondrial
- Exoribonuclease II, mitochondrial
Sequence:
MLCAARKCLNKTFISVRLNAFSCLAELNFRHTWYCSKKETPYQLERLQEEDIEETFICGKGPGGQKINKTSIVAQVKHIPTGIIVRSQDTRSREQNRCIARKRLTEKVDEFKHGNDSLLARKVQRIVKKKKQREKKSKRKYGNKIDDQDSSLNNNEAKQDVI
Protein: Kallikrein 1-related peptidase b27 (EC 3.4.21.-) (Glandular kallikrein K27) (mGK-27) (Tissue kallikrein 27) (mKlk27) (Q9JM71)
Organism: Mus musculus (Mouse)
Function: Serine protease with chymotrypsin-like cleavage specificity. Shows activity towards casein, gelatin, IGFBP3 and fibronectin but not towards laminin or collagens I and IV. Does not hydrolyze kininogin to release Lys-bradykinin.
Interaction partners:
Sequence:
MRFLILFLALSLGGIDAAPPVQSRIIGGFKCKKNSQPWHVAVLRSNKYICGGVLLDPNWVLTAAHCYGNDTSQHNVWLGKNKLFQREPSAQHRWVSKSFPHPDYNMSLLNDHIPHPEDKSNDLMLLRLSKPADITDAVKPIDLPTEEPKLGSTCLASGWGSITPTKYQIPNDLQCVFIKLLPNENCAKAYVHKVTDVMLCVGETGGGKGTCKGDSGGPLICDGVLHGITSWGSIPCAKPNAPGVFTKLIKFTSWIKDTMAKNP
Protein: Endolysin B (Gene 12 protein) (Gp12) (Mycolylarabinogalactan esterase) (EC 3.1.-.-) (O64205)
Organism: Mycobacterium phage D29 (Mycobacteriophage D29)
Function: Endolysin that degrades the junction between mycolic acid and peptidoglycans in the host cell wall and participates with the holin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the mycolic acid-rich outer membrane. Cleaves the ester linkage joining the mycolic acid-rich outer membrane to arabinogalactan, releasing free mycolic acids.
Interaction partners:
Sequence:
MSKPWLFTVHGTGQPDPLGPGLPADTARDVLDIYRWQPIGNYPAAAFPMWPSVEKGVAELILQIELKLDADPYADFAMAGYSQGAIVVGQVLKHHILPPTGRLHRFLHRLKKVIFWGNPMRQKGFAHSDEWIHPVAAPDTLGILEDRLENLEQYGFEVRDYAHDGDMYASIKEDDLHEYEVAIGRIVMKASGFIGGRDSVVAQLIELGQRPITEGIALAGAIIDALTFFARSRMGDKWPHLYNRYPAVEFLRQI
Protein: Putative redox protein FMP46, mitochondrial (EC 1.-.-.-) (Found in mitochondrial proteome protein 46) (P36141)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Putative mitochondrial redox protein which could be involved in the reduction of small toxic molecules.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
Sequence:
MSFWKTLQRQPRTISLFTNDIASNIKSQKCLQLLKGDVSHRFDVEIANRFPTWDQLQYMRTSCPQGPVSLQRQIPKLDSVLKYKHTDPTFGMDLQKCVQRGLWNPKEALWVDWENKLVGNEPADIDKYIIQRK
Protein: ATP synthase F(1) complex catalytic subunit beta, mitochondrial (EC 7.1.2.2) (ATP synthase F1 subunit beta) (P10719)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00829}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00829}; Matrix side {ECO:0000250|UniProtKB:P00829}.
Interaction partners:
- ATP synthase F
- LRRGT00139
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- Uncharacterized protein
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
Sequence:
MLSLVGRVASASASGALRGLNPLAALPQAHLLLRTAPAGVHPARDYAAQSSAAPKAGTATGQIVAVIGAVVDVQFDEGLPPILNALEVQGRESRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFIEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGDYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS
Protein: LD41490p (Q960P5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTVAIAANRLSCAESDDELLNLLDVIHRKSNRLREEVEHLQSYERQHGDAQKTGGEGQGASKEGMTAQQFREQVERLNREDIKQLRKERDRLLDKLAEMEAETLTGRIKAAKMSDQVEELVGVKKDLEEQLKLAMAQKLELSSRVQQLQQQQQSKSSSSGSQSDYSSQRNFLSSATTVLSNGSRPSSNVISNNTFQPVVLDQPAQEAFHQSPGSDIPLRKQQQQSLGRLDGIVSTPGTRNSKCRLTDSKRFAAILLETNVLELQRHLLTLTVQNQVLAQKLESSSKSKTLLAKRLDKNSEEFEHLRYQLEEKNIELEGTKAQLRLVESRLQASNSTSNSYLHSSQHDYETNRSSASTTLMLSRRGVSDSVDSTSTAMPAPPVTQISTPSMKAMVPLAMDELQQHSSSTESAHEHENQGLQTPNSTSSPLSKTIINASPCPVGSSTPSNIAARVMSISVGGVSPFEAMTPPPRQNAFRKFGSASKPSKIPLPGSKAAAYFSGKPPTGRPSTAGRSPPSANNSSSTSYGSKSSLSRSTGNLQSLRRAETSASNHSLSTNTSRSSTSSSIPLATTPYSSGSTGNRSQPTAATTPSPRVLQNSPLPKLKRDTISSRVRHLDSLSRAQQTPEGLKGTTTNSTSIAAQLSSTLRKDLQLSGNGTGAPYNQHHLNHRRSGHSPASNSSGSGVSRRYSSASTGGSGGRAIGRDQGEPTTPTSSYGGDSDSGKIQATYPNKRQATLRK
Protein: ORF3a protein (ORF3a) (Accessory protein 3a) (Protein 3a) (Protein U274) (Protein X1) (P0DTC3)
Organism: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
Function: Plays a role in viral egress via lysosomal trafficking. Forms homotetrameric ion channels (viroporins) localized at endosomes and lysosomes, that may induce deacidification of lysosomes, allowing safe egress of virions via lysosomal trafficking. Also blocks autolysosome formation by binding and sequestering the host component VPS39 for homotypic fusion and protein sorting (HOPS) on late endosomes. This prevents fusion of autophagosomes with lysosomes, disrupting autophagy and facilitating virus egress. Induces host RETREG1/FAM134B-dependent reticulophagy by interacting with host HMGB1 and enhancing the association between HMGB1 and host BECN1. This induces endoplasmic reticulum stress and inflammatory responses and facilitates viral infection.
Subcellular location: Virion {ECO:0000250|UniProtKB:P59632}. Host cell membrane {ECO:0000250|UniProtKB:P59632, ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:34158638}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P59632, ECO:0000269|PubMed:34158638}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:35239449}; Multi-pass membrane protein {ECO:0000269|PubMed:34158638}. Secreted {ECO:0000250|UniProtKB:P59632}. Host cytoplasm {ECO:0000250|UniProtKB:P59632, ECO:0000269|PubMed:33060197}. Host endosome {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:33422265}. Host lysosome {ECO:0000269|PubMed:33422265}. Note=The cell surface expressed protein can undergo endocytosis. The protein is secreted in association with membranous structures. {ECO:0000250|UniProtKB:P59632}.
Interaction partners:
Sequence:
MDLFMRIFTIGTVTLKQGEIKDATPSDFVRATATIPIQASLPFGWLIVGVALLAVFQSASKIITLKKRWQLALSKGVHFVCNLLLLFVTVYSHLLLVAAGLEAPFLYLYALVYFLQSINFVRIIMRLWLCWKCRSKNPLLYDANYFLCWHTNCYDYCIPYNSVTSSIVITSGDGTTSPISEHDYQIGGYTEKWESGVKDCVVLHSYFTSDYYQLYSTQLSTDTGVEHVTFFIYNKIVDEPEEHVQIHTIDGSSGVVNPVMEPIYDEPTTTTSVPL
Protein: CRISPR-associated endonuclease Cas1 (EC 3.1.-.-) (Q99ZW1)
Organism: Streptococcus pyogenes serotype M1
Interaction partners:
Sequence:
MAGWRTVVVNTHSKLSYKNNHLIFKDAYKTELIHLSEIDILLLETTDIVLSTMLVKRLVDENVLVIFCDDKRLPTAMLMPFYGRHDSSLQLGKQMSWSETVKSQVWTTIIAQKILNQSCYLGACSYFEKSQSIMDLYHGLENFDPSNREGHAARIYFNTLFGNDFSRDLEHPINAGLDYGYTLLLSMFAREVVVSGCMTQFGLKHANQFNQFNFASDIMEPFRPLVDKIVYENRNQPFPKIKRELFTLFSDTFSYNGKEMYLTNIISDYTKKVVKALNNEGKGVPEFRI
Protein: GH26494p (Q8IH39)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
NVEAARALITSHFVNLNQFDGMLRDCMDNGNNYVAISFGIALLERLIMDDRVINIVSDNEFMATVELLGRLTQHRHRYPECIVNAIDTLWSGNFNSSSDYSPFNGNDRYLSGASHYIHSGMHHSCDTDDPPGLQEKTEFLLKDWVALYTQQNQQSTRDARNFGAFVQKMNTYGILKTDDLITRFFRQATHICTDVVYRMFAEPSLPINQAKNKIFQWIDAFVHLIAMLVRHSGEAGNPTTKINLLNKVLGIVLGTLIKDHEMRGVSFQQVGYHRFFMMLFMELCTADVILESLMHSIVSAFAYTYHLLNPSVAPGFCFAWLELISHRVFLGRILVQIPGQKGWPLYAQLLQDLFKYLAPFLRNTELGKPVQLLYKGTLRVLLVLLHDFPEFLCDYHFGFCDTIPPNCVQMRNIILSAFPRNMRLPDPFTPNLKVDMLSDSSNAPKVLSSYIMNIQPANFKKDLDSYLKARAPVTFLSELRGHLQVTSEPGTRYNMALMNALVMYVGTQAIALIRNKNFVPNTSNIAHSAHMDIFQNLAVDLDTEGRYLFLNAIANQLRYPNSHTHYFSCAVLHLFAEANSEAIQEQITRVLLERLIVNRPHPWGLLITFIELIKNPIYKFWDHDFVHCAPEITKLFESVARSCLAKSNVTQQLNMPVVDGEGQEVATIN
Protein: C10orf11 homolog (H. sapiens) (Leucine-rich melanocyte differentiation-associated) (Leucine-rich melanocyte differentiation-associated protein isoform X1) (Q501Y0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Small nuclear ribonucleoprotein E
- Splicing factor 3a, subunit 3.
- Small nuclear ribonucleoprotein Sm D2
- Splicing factor 3B subunit 1
- Splicing factor 3B subunit 3
- Pre-mRNA-splicing factor SYF1
- Elongation factor Tu GTP-binding domain-containing 2.
- Small nuclear ribonucleoprotein G
- Splicing factor 3B subunit 2
- Splicing factor 3A subunit 1
Sequence:
MAHNESMVVVNGSQVSCIGHDWEDIPDFLGTKYGQMARRLDLSFNQLRSLTGLKAFSQLEELIVDNNLLGNDLRLPRLPRLHTLTLNKNQLTDIEALLEHLVEVTPALEYLSLLGNEACPNQLVSMDKDEDDYQRYRYFVLHKLTNLKFLDTRRVTQWERSEAQARGAFMKVVKPKNDQDTASDTRSESIATPYTPLPRGSRDARNHKGVFTKCRYVYYGKHSEGNRFIRNDQL
Protein: Versican core protein (Chondroitin sulfate proteoglycan core protein 2) (Large fibroblast proteoglycan) (PG-M) (A0A2R8Q3K1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000256|ARBA:ARBA00004504}. Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix {ECO:0000256|ARBA:ARBA00004593}.
Interaction partners:
- Hyaluronan synthase 2
- Bone morphogenetic protein 4.
- Decorin
- Brevican.
- T-box transcription factor TBX2b
- CD166 antigen homolog A
- Myosin light chain 2 Mlc2a
Sequence:
MRPVSGLLSGKVTLPCYFSIMPTIGPRNKDASGYDYLRIKWTRIDGGVESTVLVTQNGVIKIGSGYRSRVSVQSHPEDIGDASLTMVKLRASDAGTYRCEVMFGIEDTQDTVNLNVDGVVFHYRSKVSRYILNYAQAVQACSDVGATIATSEQLRAAYEDGFDQCDAGWIADQTVRYPITRPRPGCFGNLPGKPGVRSYGKRKPTETYDVFCYVDKLEGNVFFAPTLQKMTFDEAKAVCESNNAELASPGQLHAAWRQGLDRCDYGWLSDGSARHPVSVPRSQCGGGLLGVRTMYRYRNQTGFPDPSMRLGAYCFQGVHSCSDAVCLNGGTCIKTGGAQICICQPGYSGEQCEIDIDECHTNPCRNGGTCIDGLNSFTCLCLPSYAGALCEQDTETCSYGWHKFQGHCYKYFPHRRNWDTAERECRLQGAHLASVLSHDEQQYINRLGHDYQWIGLNDKMFENDFRWTDGRVVQYENWRPNQPDSFFSSGEDCVVMIWHEDGQWNDVPCNYHLTFTCKKGTVSCSQPPIVHNARTFGQPRPRYEINSLIRYQCMDGFIQRHVPTIRCRGDGLWDSPRISCMSPSNYQRSYTRRLQRYSVYRNNRKRSAEHSVDVHRRRHHHHHHHHGGKHIRTKQ
Protein: Spectrin beta chain, erythrocytic (Beta-I spectrin) (P15508)
Organism: Mus musculus (Mouse)
Function: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Interaction partners:
- Ankyrin-1
- Spectrin alpha chain, erythrocytic 1
- Spectrin alpha chain, non-erythrocytic 1
- Ankyrin-2
- Ankyrin-3
- Protein 4.1
- Band 3 anion transport protein
Sequence:
MTSATEFENVGNQPPFSRINARWDAPDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRISDLYKDLRDGRMLIKLLEVLSGEMLPRPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGREQRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFDVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQTISVLNSRKFANSLSGVQQQLQAFSTYRTVEKPPKFQEKGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYQRELALRSELIRQEFDRKAAMRETWLNENQRLVTQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVKALEDLAQELEKENYHDQKRIIARKDNILRLWSYLQELLRSRRQRLEATLALQKLFQDMLHSIDWMDEIKAHILSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLQFAEGKGYQPCDPQVIQDRVSHLEQCFSELSNMAAGRKAQLEQSKRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLKQIFQEADDMVAQKQFGHPQIETRVKEVSAQWDHLKELAAFRKKDLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKEFLEELEESRGVMEHLEHQAQGFPEEFRDSPDVTNRLQALRKLYQQVLTQAELRGHKLQEALDLYTVFGESDACELWMTEKGKWLDQMDIPNTLEDLEVVQHRFDILDQEMKTLMAQIDGVNLAANNLVESGHPRSGEVKQYQDRLNKRWQAFQAVVSEQREAVDSALRVNNYCVDCEETSKWIMDKTKVVESTKDLGQDLAGVIAIQRKLSGLERDVLAIRDRVSALERESQYLMESHPEQKEDIGQRQADVEKLWKGLQDALQGQELSLGEASKLQAFLQDLDDFKAWLSMAQKAVASEDMPESLPEAEQLLQQHAAIKEEIDAHRDDYHRVKASGEKVIEGQTDPDYQLLGQRLEGLDTDWDALRRMWESRGNTLTQCLGFQEFQKDAKQAEAILSNQEYTLAHLEPPDSLAAAEAGIRKFEDFLVSMENNRDKILSPVDSGNKLVAEGNLYSNKIMEKVQLIEDRHKKNNEKAQEATVLLKDNLELQNFLQNCKELTLWINDKLLTSPDVSYDEARNLHNKWMKHQAFMAELASHQGWLENIDAEGRQLMAEKPQFKDVVSERLEALHKLWEELQSTAKAKAEQLSAARSSDLRLQTHADLNKWIGAMEDQLRSDDLGKDLTTVNRMLAKLKRVEEQVNLRKEELEELFADAPSLGAEAGDTDMSIEKRFLDLLEPLGRRKKQLELSKAKLQISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHAPRVEDVLRRGQELVKAAEIDCQDIEERLGHLQSSWDTLREAAAGRLQRLRDAHEAQQYYLDAGEAEAWISEQELYVFSDEPPKDEEGAIVMLKRHLRQQRTVEEYGRNIKQLAGRAQSLLSAGHPEGEQIIRLQGQVDKQYAGLKDMAEERRRRLENMYHLFQLKREADDLEQWITEKEMVASSQEMGQDFDHVTMLRDKFRDFARETGAIGQERVDNVTIIERLIDAGHSEAATIAEWKDGLNDMWADLLELIDTRMQLLAASYDLHRYFYTGTEILGLIDEKHRELPEDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEKADAIQSKEQEVSAAWQALLDACAGRRAQLVDTADKFRFFSMVRDLLSWMESIIRQIETQERPRDVSSVELLLKYHQGIKAEINTRAKNFSTCLELGESLLQRQHQASDEIREKLQQVISRRQEMNDKWEARSDRLHMLLEVCQFSRDASVAEAWLIAQEPYLASRDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEKPTTLELKERQTPERPTEEPGPQEEEGETAGEAPQVHHAATERTSPVSFMSRLSSSWESLLPEPAHPF
Protein: ATPase expression protein 1, mitochondrial (Nuclear control of ATPase messenger RNA expression protein 1) (P32493)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for translation of the mitochondrial OLI1 transcript encoding subunit 9 of mitochondrial ATP synthase.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ATPase expression protein 2
- Nuclear control of ATPase protein 2
Sequence:
MITTVQEISKWRNLCFIRMQSRKWYPVLKKTPLVADGRKIIKHADKVPHPEEIIHPFYQPTAIEQFTACATEYNPSLLDGKKIAPSLIKHPVSLKTILVDSKLKFDDIRGVNKWLMEFVARRQHQRNIVLTPASKSVRSFHVLHLSSTDIAKLRGLENILSEIENTNDLQSRVESVNNELQNIFDRDSKQTRLFCENILAYLIKNYGNSTEKLILLINVTEMQLYSRLDQMKAMNIILYNILCKVEANENPPYSPTLVTALENLLAAINNRFFPGRCENSLHPIVIEQLLSYFIKTGNLNESKNFLGHLIKKGILPEATIINRYLEAIDVHFDKSTKIFDIRSKFAFIADLAPIIENYGTIDLFKFLIPMCRHFDELCSLLNIIRKSNNAKRAVDSTLPIFIKKVLTFTKDPMINSGNLSTVFNIVSPIYGQNVPSEFVEKFILSFALQGNYTMMAHMIDTYKIKLSHKYQLQIIRALKNSERNHALKNTGAVGYNKEFKKYFIEKYLNCTEREALRP
Protein: Tudor domain-containing protein 5 (Q5VCS6)
Organism: Mus musculus (Mouse)
Function: Required during spermiogenesis to participate in the repression transposable elements and prevent their mobilization, which is essential for the germline integrity. Probably acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for chromatoid body (CB) assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21383078}. Note=Localizes to chromatoid body (CB) and pi-body (also called intermitochondrial cementin), 2 cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis.
Interaction partners:
- Piwi-like protein 2
- Piwi-like protein 1
- Putative ATP-dependent RNA helicase TDRD12
- RNA helicase Mov10l1
- Torsin-1A-interacting protein 1
- ATP-dependent RNA helicase TDRD9
Sequence:
MSEQERIQDCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVILKAIPDESTKGIASLVAKQRRSHKVRNSMPKGRPSICSGRVPYRGRVPPILPAVVKSELKDLLALSPVLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLTLKKSVSEDKQRGWPAGKVFTQPFRMKQQGSYSTGFPVMKAHFSQPISNMEPPKQVLSMAKTPTFNSVEASRLNHTEKLNQLESTFKSVIAQIGPGGTVDPELKRKIQFVVSKFPQGLFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLLVFDADLKPLPSGGPLSSVRNSCLVQPDKKTEANPWTSSLSRNSLSTVAVKKTTWDCPLKNQKEPEQKIYKKPNLVVKPLQLQVETNKPQLSLSVANHDIPPDAVRAKKLCRLPPLDTSTLVGVFVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPAEEHWTARAILHFQKLCGLKPLVGVVDEYIDGILNIFLCDTSSNEDVYFHHVLRTEGHAIVCRENAPSKGFRDFNPPALYTNASSAGDMVLTDLGHPAQQHYLNEDQEILQQAQQDINDGKCISYLKSAPKELLKDSKLSSLKTHKSCEEDPRWSILQPKDLKEENEDEVPTGMPCLESVTIGDDVWDENWLPLQAKMGKAGSPASQLFTSNLVGKKQYQTGGEMAQKDWCFSTSKDIWDDSWQPLGLANDVKGGIHTPEGPIAQEKNTSTTRIQQQPDLQYPLDSSTLPKLEEFYISLIKSQQSAERSQSEPASIQTHAGRAASKALSSTPAVGDSPENHSGSVESSPGSLKKEDVSNSRAEATAKDKSQGAIDQLSFILSPQHQISQKLYIPRSTATAVLGAAARLATSRSLLHWYPSVKGGKLEAERDGVK
Protein: Protein kinase, putative (Q388C6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- WW domain-containing protein
Sequence:
MPAGMCSVDVAELNQITMGKKLGSGSFGSVYAGILPSGQFVAVKELELAEDSPTNTEVEVHKKLVHENVIRYLHSRIDNESTPKRLYLYLEFVTGGSVSSLMKTLPNGHLPYPVVRVYSRQMFSGLEYLHRNKVAHRDIKGDNLLISMDTGIAKLADFDQAKVMTTYGTLRQAATSTLAGTPYWMAPEVITDENGYDPFKADIWSAGCTVAEMITGRAPWTPMANVMHIMNKLAMSTGWPDAIPKDPNALGSQEAYDFLDLCFRRTVAERPDAATLLQHPFLKV
Protein: Amino acid transporter, putative (Q57WK6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MRATKKHPNDGKGATTDPFVDGSDPIPSEVAAFDPSQQEHVDVVKEVKPSLFTVLLEKFIPHGGLWSCALNLASATLGAGICSLPAGFNLSGIVMSCIYLVCVAVGTVYSLNLLAKVAVKTGSRNYGEAAKAVMGPLAGYYTAALMIVMCFGGSVAYIIIIGIILKAVLNRDGVPEYLKSESGNRLMTSMVWLVIILPMCIPKQVNSLRHLSFVGVMFIVYFSCVVIGHSINKIINEGVADGIVYMRTGNSALDGLSLFLFSFICQPNAFEIFREMKHRSPQRFTIYGTVGMSMCAVLYFLVGLFGYLEFGGDAIDTVLSLYDPGENVAVAIAYIGVAAKVCVAFALHIIPMRDALYHCTGWHVDTVPYWKHSLIVTSITLAALLMGLFIPKASTVFGLVGAFCGGHIGLVLPPLFYMYSGGFTREKVGNIDFFGTYLLLFVGVVAVVFGTVSTIYNTVP