wanglab/gogpt-training-data huggingface dataset:
Protein: N-alpha-acetyltransferase 50 (EC 2.3.1.258) (N-acetyltransferase NAT13) (N-epsilon-acetyltransferase 50) (EC 2.3.1.-) (NatE catalytic subunit) (Q6PGB6)
Organism: Mus musculus (Mouse)
Function: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (By similarity). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (By similarity). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (By similarity). Autoacetylates in vivo (By similarity). The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (By similarity). Component of N-alpha-acetyltransferase complexes containing NAA10 and NAA15, which has N-alpha-acetyltransferase activity (By similarity). Does not influence the acetyltransferase activity of NAA10 (By similarity). However, it negatively regulates the N-alpha-acetyltransferase activity of the N-terminal acetyltransferase A complex (also called the NatA complex) (By similarity). The multiprotein complexes probably constitute the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (By similarity). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16484612}. Nucleus {ECO:0000250|UniProtKB:Q9GZZ1}. Note=Localizes to the cytoplasm in interphase cells. {ECO:0000250|UniProtKB:Q9GZZ1}.
Interaction partners:
- Huntingtin-interacting protein K
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 10
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
- N-alpha-acetyltransferase 11
- N-terminal amino-acid N
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 25, NatB auxiliary subunit
- N-alpha-acetyltransferase 40
- N-alpha-acetyltransferase 30
Sequence:
MKGSRIELGDVTPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKLAYFNDIAVGAVCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYKRIEPADAHVLQKNLKVPSGQNAETQKTDN
Protein: FERM domain-containing protein 7 (Q6ZUT3)
Organism: Homo sapiens (Human)
Function: Plays a role in neurite development, may be through the activation of the GTPase RAC1. Plays a role in the control of eye movement and gaze stability.
Subcellular location: Cell projection, neuron projection {ECO:0000250|UniProtKB:A2AD83}. Cell projection, growth cone {ECO:0000250|UniProtKB:A2AD83}. Note=In undifferentiated neurons, located in the actin-rich regions of the cell body. In differentiated neurons, located in the actin-rich regions of the cell body and primary neurite processes but is almost absent from secondary extensions arising from the primary neurite. Also found at the actin-rich distal end of growth cones (By similarity). {ECO:0000250|UniProtKB:A2AD83}.
Interaction partners:
- Peripheral plasma membrane protein CASK
- G-protein coupled receptor 143
- Nyctalopin
- Long-wave-sensitive opsin 1
Sequence:
MLHLKVQFLDDSQKIFVVDQKSSGKALFNLSCSHLNLAEKEYFGLEFCSHSGNNVWLELLKPITKQVKNPKEIVFKFMVKFFPVDPGHLREELTRYLFTLQIKKDLALGRLPCSDNCTALMVSHILQSELGDFHEETDRKHLAQTRYLPNQDCLEGKIMHFHQKHIGRSPAESDILLLDIARKLDMYGIRPHPASDGEGMQIHLAVAHMGVLVLRGNTKINTFNWAKIRKLSFKRKHFLIKLHANILVLCKDTLEFTMASRDACKAFWKTCVEYHAFFRLSEEPKSKPKTLLCSKGSSFRYSGRTQRQLLEYGRKGRLKSLPFERKHYPSQYHERQCRSSPDLLSDVSKQVEDLRLAYGGGYYQNVNGVHASEPVLESRRRNSALEVTFATELEHSKPEADPTLLHQSQSSSSFPFIYMDPVFNTEPNPNPDPRDIFSERSSLSSFQTSCKFSGNHMSIYSGLTSKVRPAKQLTYTDVPYIPCTGQQVGIMPPQVFFYVDKPPQVPRWSPIRAEERTSPHSYVEPTAMKPAERSPRNIRMKSFQQDLQVLQEAIARTSGRSNINVGLEEEDPNLEDAFVCNIQEQTPKRSQSQSDMKTIRFPFGSEFRPLGPCPALSHKADLFTDMFAEQELPAVLMDQSTAERYVASESSDSESEILKPDYYALYGKEIRSPMARIRLSSGSLQLDEEDEDAYFNTPTAEDRTSLKPCNYFLA
Protein: ABC1 protein, putative (Q389E8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTLWSATRMFKRTSTRFSASITQWLYMNCRNRCFSQCSASMRRGSRALAWGRRMLLCAVAVTTSYVFIDYATAQSITRSMRALITTARVVYMYKGATPETSEERSNLHRAAALSLLNLCLRNEGLYIKLGQSLTAMNHILPWEYIDVLTVLLDRAPVVPLDEVRRIIQEETGRSCEELFVRFDPNPIASASIAQVHRALMQPSDPIQSPVEVCVKVQKPHIRRQVFWDLQTYRFVLHVLGAAFNIPVAWMKETVVEGIRREVDFSIEARNATRIRQDFADRRDLYVPEVYGDLVTPRLLVMEWVDGVKLVDVVAVREQFDEVKVLQTVFGAFGDMIFKSGFVHCDPHGANILVRPQPYPMEEEASGKSKELRQPGGRCCNPQVVLLDFGLCCPESERFRLEYALLLKAMIMQDMVTVRKIVYSWGVDDEKTFSTLQLRRSYASLHRRNCGEMTREEAMHMHNEERERIMNVLKREEQLPCELVLVGRSIDILHGVNRLYGGLVNHMRVFGRRAVSALGRLNTYEDIQLYLTHLVGLSNGNAGEEAIPPCCSGKLLSLFDPTLEHQRREEAAAVLKFRSGVTAAFRYRVWEGIISLLMLFQFELALLFLDAYHMFIRWYSKVFEVSIWNWMDARWQRFIKAGCCGKKENKFYSIR
Protein: Surface presentation of antigens protein SpaO (Q6XVW5)
Organism: Shigella flexneri
Interaction partners:
Sequence:
MLRIKHFDANEKLQILYAKQLCERFSIQTFKNKFTGSESLVTLTSVCGDWVIRIDTLSFLKKKYEVFSGFSTQESLLHLSKCVFIESSSVFSIPELSDKITFRITNEIQYATTGSHLCCFSSSLGIIYFDKMPVLRNQVSLDLLHHLLEFCLGSSNVRLATLKRIRTGDIIIVQKLYNLLLCNQVIIGDYIVNDNNEAKINLSESNGESDHTEVSLALFNYDDINVKVDFILLEKKMTINELKMYVENELFKFPDDIVKHVNIKVNGSLVGHGELVSIEDGYGIEISSWMVKE
Protein: PH domain-containing protein (Q20329)
Organism: Caenorhabditis elegans
Interaction partners:
- Thioredoxin domain-containing protein
- Uncharacterized protein F15G9.5
- C2 domain-containing protein
- RING finger protein nhl-1
- Probable dynactin subunit 2
- F-actin-capping protein subunit beta
- Dynactin subunit 6
- Dynactin subunit 5
- Dynactin subunit 1
- cAMP-dependent protein kinase, catalytic subunit-like
Sequence:
MPDLEINGVEMENGVGRSDSLKAEEANALREWDPKHLLKALYEISYEPRVETKRNRFVTMEGHVEVPADEVTKSDGLDNEGWMKQYIRMKEGRLQIFASHYAGEAPAQELVLSGADVDANKDERTLTIHGGREHVKYYCRVPSAVFDKWRQSFLSHCASSLIDAYVKPIPRAFQHLTERILILELGSCSIRAGVLTTEPSLPQSFFPAIAVRTDDGKIFVGEDAYRPEIRHNGDFVRPISATDPSVERYSIDKDVLKAVIGKVTKELKVEPWKYKVLLSIPQNIPTVLIGELLQICLEDIKFQSAGITRQPSLILYAYDVTTGVVVDIGERVNIVPVIDGYVVESAICSIPYGSQQMGDSLRASLSAHNKGLYAFQSPVEKLILRFALEQTTYVPEDYQKEEKSENKETRISLDAFTPSPGMQTRFDIDNSRFLCTEGLFKPKKWGLDTKGLHQLIHEAILQCPIDSRRTLYRNIYLAGGASLMPGIAEKLEQELSTVVPNTIHTQVNISPWRYNAAYLGAQIVASASTFEDSCISLQQLPKFLAQLQSSSF
Protein: Actin maturation protease (EC 3.4.11.-) (Actin aminopeptidase ACTMAP) (J3QPC3)
Organism: Mus musculus (Mouse)
Function: Actin maturation protease that specifically mediates the cleavage of immature acetylated N-terminal actin, thereby contributing to actin maturation. Cleaves N-terminal acetylated methionine of immature cytoplasmic beta- and gamma-actins Actb and Actg1 after translation. Cleaves N-terminal acetylated cysteine of muscle alpha-actins Acta1, Actc1 and Acta2 after canonical removal of N-terminal methionine.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:36173861}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D2
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm5
- Small nuclear ribonucleoprotein G
- U6 snRNA-associated Sm-like protein LSm6
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein Sm D1
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm8
Sequence:
MTSPCSFPLKPTISPIIHETPDTNIPPPLPLNPPDLALPSPPCSLHTSISSPLPPPPPPPAPPPPPPPPPLPSAVEPVLPHVYGLKNSQLLKEALEKAGPAPKGKEDVKRLLKLHKDRFRSDLQWILFCADLPSCIQEGPQCGLVALWMAEALLSTPDSVSLERLVQVAKERGYTAQGEMFSVADMAKLAQETLDCQAELLCGGLGGPNRERVLQHLITGHPLLIPYDEDFNHEPCQKKGHKAHWAVSAGVLIGVQNVPSPGYIEDSELPGLFHPVPGAPHQPPSFPEESSPGALFLLSKQGKSWHYQLWDYSQVRESNLQLTDFSPARAADGQVYVVPAGGVEAGLCGQALLLRPQEGSH
Protein: Calcium homeostasis modulator protein 2 (Protein FAM26B) (Q9HA72)
Organism: Homo sapiens (Human)
Function: Pore-forming subunit of a voltage-gated ion channel.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8VEC4}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAALIAENFRFLSLFFKSKDVMIFNGLVALGTVGSQELFSVVAFHCPCSPARNYLYGLAAIGVPALVLFIIGIILNNHTWNLVAECQHRRTKNCSAAPTFLLLSSILGRAAVAPVTWSVISLLRGEAYVCALSEFVDPSSLTAREEHFPSAHATEILARFPCKENPDNLSDFREEVSRRLRYESQLFGWLLIGVVAILVFLTKCLKHYCSPLSYRQEAYWAQYRANEDQLFQRTAEVHSRVLAANNVRRFFGFVALNKDDEELIANFPVEGTQPRPQWNAITGVYLYRENQGLPLYSRLHKWAQGLAGNGAAPDNVEMALLPS
Protein: U5 small nuclear ribonucleoprotein TSSC4 (Tumor-suppressing STF cDNA 4 protein) (Tumor-suppressing subchromosomal transferable fragment candidate gene 4 protein) (Q9Y5U2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:34131137}. Cytoplasm {ECO:0000269|PubMed:34131137}. Note=Shuttles between the cytoplasm and the nucleus, associated with the U5 snRNP. {ECO:0000269|PubMed:34131137}.
Interaction partners:
- Pre-mRNA-processing-splicing factor 8
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Protein AAR2 homolog
- Tetraspanin-32
- U5 small nuclear ribonucleoprotein 40 kDa protein
- Zinc finger HIT domain-containing protein 2
- E2F-associated phosphoprotein
- Pleckstrin homology-like domain family A member 2
- CD2 antigen cytoplasmic tail-binding protein 2
- 116 kDa U5 small nuclear ribonucleoprotein component
Sequence:
MAEAGTGEPSPSVEGEHGTEYDTLPSDTVSLSDSDSDLSLPGGAEVEALSPMGLPGEEDSGPDEPPSPPSGLLPATVQPFHLRGMSSTFSQRSRDIFDCLEGAARRAPSSVAHTSMSDNGGFKRPLAPSGRSPVEGLGRAHRSPASPRVPPVPDYVAHPERWTKYSLEDVTEVSEQSNQATALAFLGSQSLAAPTDCVSSFNQDPSSCGEGRVIFTKPVRGVEARHERKRVLGKVGEPGRGGLGNPATDRGEGPVELAHLAGPGSPEAEEWGSHHGGLQEVEALSGSVHSGSVPGLPPVETVGFHGSRKRSRDHFRNKSSSPEDPGAEV
Protein: Disco interacting protein isoform TO67 (Q9NIH3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPLQAANVQEQQSSPVALYPTSASPVAVQSPQDAFLAVQSPGAPAPVQLANSSDQQNNPDADAIASKLPMPVIIKEEPISVNDEPSVDNIEDNTSASTSASGIGGKIPFKKIFQKRKKSSERTRDKKLRQNRQLRKSMLPKNALMALNEVKGVTISDFTIDSNTDGGFTAVVTVNSNQYEGKGTSKMTAKNAACEKAWRDFIIAKMTPKPPRIHQVEMGSEPMDINEDEADAPDDDLPMLNLASFAIYKLFAEWEREGYVVPEMHPSANAAQQAGGDAGTPVPPVPKEPKKPPVRTELPSGWETMHPATILCIMRPGLNYVDYGSSGDKTNGMQHLGIMVDNQEFHANGRSKKIARRNVAVKVCNSLFGTNFTY
Protein: Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I] (G5BQH5)
Organism: Heterocephalus glaber (Naked mole rat)
Function: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Phosphatidylcholine-sterol acyltransferase
- P-type phospholipid transporter
- Apolipoprotein B-100
- Apolipoprotein E
- Apolipoprotein A-II
- Apolipoprotein C-III
- Apolipoprotein A-IV
Sequence:
MKAVVLAVAVLFLTGSQARHFWQGDEPQTSWDRMKDFAALYVDAIQESGKDCAAQLDASALGKQLNLNLLANWNTLTSTFNNLREQLGSVTKEFWDNLGEDTVWLRQQMNKDLEEVKQKVQSYLDNFQKKVNEEVERYRDKVQPLGKELHKDAQQKLKELQEKLAPLGQDIRQRAREYVDALRTHLGSYTQGMRQGLAKRLEALKESAPVSEYQVKASKHLKTFSEKAKPALEDLRQGLMPVMESLKASFLSSIDQASKQLSAQ
Protein: Protein argonaute PNH1 (Protein PINHEAD homolog 1) (OsPNH1) (Q69VD5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probably involved in the RNA silencing pathway. May bind to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them (By similarity). Plays a role in the maintenance of the indeterminate state of the stem cells in the shoot apical meristem (SAM). Regulates leaf formation through vascular development and may be involved in determining the central domain of the leaf founder region.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12000455}.
Interaction partners:
- Os02g0152700 protein
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit
- Endoribonuclease Dicer homolog 1
- Endoribonuclease Dicer homolog 4
- Os03g0121901 protein
- Endoribonuclease Dicer homolog 2b
- Ribonuclease 3-like protein 3
- Ribonuclease 3-like protein 2
- Endoribonuclease Dicer homolog 2a
Sequence:
MLEVLDMAPPRHQPAAGKAGGGRGHGHGHGHGGGGGGPAARKQPLQSSMAQPKAETAAATAAVAPPEGGKKCGGGGGRRRGGRGRGGRAGAGPGPGLAAAPAVVVAPAARAVIGPPVASKGLSFCRRPGFGTVGARCVVKANHFLAELPDKDLTQYDVKITPEVSSRSVNRAIMSELVRLYHDSDLGGRLPAYDGRKNLYTAGTLPFDAREFVVRLTDDDDGTGVPPREREYRVAIKFAARADLHHLRQFIAGRQADAPQEALQVLDIVLRELANRRYVSIGRSFYSPDIRKPQRLGDGLQSWCGFYQSIRPTQMGLSLNIDMSSTAFIEPLPVIEFVAQILGKDVISRPLSDANRIKIKKALRGVKVEVTHRGNVRRKYRISGLTTQPTHELIFPIDDQMNMKSVVEYFKEMYGFTIQHPHLPCLQVGNQKKANYLPMEACKIVEGQRYTKRLNEKQITSLLKVTCRRPREQEMDILQTVQQNGYEQDPYAKEFGINISEKLTSVEARVLPAPWLKYHDTGKEKECLPQVGQWNMVNKKVINGCKVNHWACINFSRSVQETTARGFCQELAQMCQISGMEFNSEPVIPIYSARPDQVEKALKHVYNMSLNKLKGKELELLLAILPDNNGSLYGDIKRICETDLGLISQCCLTKHVFKISKQYLANVSLKINVKMGGRNTVLLDAISWRIPLVSDIPTIIFGADVTHPETGEDSSPSIAAVVASQDWPEVTKYAGLVCAQAHRQELIQDLYKTWHDPQRGTVTGGMIRELLISFRKATGQKPLRIIFYRDGVSEGQFYQVLLYELDAIRKACASLEPNYQPPVTFVVVQKRHHTRLFANNHKDRSSTDKSGNILPGTVVDSKICHPSEFDFYLCSHAGIQGTSRPAHYHVLWDENNFTADEMQTLTNNLCYTYARCTRSVSVVPPAYYAHLAAFRARFYMEPEMSENQTTSKSSTGTNGTSVKPLPAVKEKVKRVMFYC
Protein: Transcobalamin-2 (TC-2) (Transcobalamin II) (TC II) (TCII) (P20062)
Organism: Homo sapiens (Human)
Function: Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells.
Subcellular location: Secreted {ECO:0000269|PubMed:3782074, ECO:0000269|PubMed:8443384}.
Interaction partners:
- CD320 antigen
- E3 ubiquitin-protein ligase CBL
- Lactotransferrin
- Lysosomal cobalamin transport escort protein LMBD1
- Methylmalonyl-CoA mutase, mitochondrial
- Low-density lipoprotein receptor-related protein 2
- Dihydrofolate reductase 2, mitochondrial
- Methionine synthase reductase
- Dihydrofolate reductase
- Methionine synthase
Sequence:
MRHLGAFLFLLGVLGALTEMCEIPEMDSHLVEKLGQHLLPWMDRLSLEHLNPSIYVGLRLSSLQAGTKEDLYLHSLKLGYQQCLLGSAFSEDDGDCQGKPSMGQLALYLLALRANCEFVRGHKGDRLVSQLKWFLEDEKRAIGHDHKGHPHTSYYQYGLGILALCLHQKRVHDSVVDKLLYAVEPFHQGHHSVDTAAMAGLAFTCLKRSNFNPGRRQRITMAIRTVREEILKAQTPEGHFGNVYSTPLALQFLMTSPMRGAELGTACLKARVALLASLQDGAFQNALMISQLLPVLNHKTYIDLIFPDCLAPRVMLEPAAETIPQTQEIISVTLQVLSLLPPYRQSISVLAGSTVEDVLKKAHELGGFTYETQASLSGPYLTSVMGKAAGEREFWQLLRDPNTPLLQGIADYRPKDGETIELRLVSW
Protein: D-3-phosphoglycerate dehydrogenase 1, chloroplastic (EC 1.1.1.95) (Protein EMBRYO SAC DEVELOPMENT ARREST 9) (O49485)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the plastidial phosphorylated pathway of serine biosynthesis (PPSB). Required for mature pollen development.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:24058165, ECO:0000269|PubMed:24368794}.
Interaction partners:
- Phosphoserine aminotransferase 2, chloroplastic
- Phosphoserine aminotransferase 1, chloroplastic
- Phosphoserine phosphatase, chloroplastic
- D-glycerate 3-kinase, chloroplastic
- D-3-phosphoglycerate dehydrogenase 2, chloroplastic
- Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
- Phosphoglycerate mutase-like protein 4
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2
Sequence:
MSATAAASSSIAVATNSLRNVTLSSRSPLPSAISVAFPSRGRNTLQRRLVLVSCSTGDGSKPTILVAEKLGDAGIKLLEDVANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVNAPMVSAEVLTELKPYVVLAEKLGRLAVQLVAGGSGVKNAKITYASARATDDLDTRLLRAMITKGIIEPISDVYVNLVNADFTAKQRGLRLSEERVLLDGSPESPLETITVQLSNVESKFASSLSESGEVKVEGKVKDGVPHLTKVGSFEVDVTLEGSIILCRQVDQPGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVEEFVFLKL
Protein: Galectin (J3QR96)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAFSGCQAPYLSPAVPFSGTIQGGLQDGFQITVNGAVLSCSGTRFAVDFQTGFSGNDIAFHFNPRFEDGGYVVCNTRQKGTWGPEERKMHMPFQKGMPFDLCFLVQSSDFKVMVNGSLFVQYFHRVPFHRVDTISVNGSVQLSYISFQPPSVRPANPAPITQTVIHTVQSASGQMFSTPAIPPMMYPHPAYPMPFITTIPGGLYPSKSIILSGTVLPSAQRCGSCVKLTASRWPWMVSTCLNTTIA
Protein: Thioredoxin-related transmembrane protein 4 (Thioredoxin domain-containing protein 13) (Q8C0L0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:31142202}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H1E5}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Thioredoxin-related transmembrane protein 2
- Protein disulfide-isomerase TMX3
Sequence:
MTGGFCVPVLLAAWLAAAAAEGLEQAALPAEESRVQPMTASNWTLVMEGEWMLKFYAPWCPSCQQTDSEWETFAKNGETLQISVGKVDVIQEPGLSGRFFVTTLPAFFHAKDGIFRRYRGPGIYEDLQNYILEKKWQSVEPLTGWKSPASLTMSGMAGLFSISGKIWHLHNYFTVTLGIPAWCSYVFFVIATLVFGLFMGLILVVISECFCVPLPRASSERCEQEQSTGEAQGAEQLQDAEEEKDDSNEEENKDSLVDDEEEKEDIGDEDEGEEDEEEDNLAGIMAEERSDTNERAVVKEGSVSPKEDGAHPADTQDVVEDALRQRKSQNANKGS
Protein: E3 ubiquitin-protein ligase ARIH2 (ARI-2) (Protein ariadne-2 homolog) (EC 2.3.2.31) (Triad1 protein) (O95376)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (By similarity). The initial ubiquitin is then elongated (By similarity). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the ECS complex. Mediates 'Lys-6', 'Lys-48'- and 'Lys-63'-linked polyubiquitination. May play a role in myelopoiesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16118314}. Cytoplasm {ECO:0000269|PubMed:19340006}.
Interaction partners:
- Cullin-5
- RING-box protein 2
- Ubiquitin-like protein NEDD8
- Elongin-B
- Ubiquitin/ISG15-conjugating enzyme E2 L6
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Elongin-C
- E3 ubiquitin-protein ligase RING1
- Protein AF-10
- Ankyrin repeat and SOCS box protein 9
Sequence:
MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEARVQPNPSKHVPTSHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVGVSCMAQDCPLRTPEDFVFPLLPNEELREKYRRYLFRDYVESHYQLQLCPGADCPMVIRVQEPRARRVQCNRCNEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKCNICIEKNGGCNHMQCSKCKHDFCWMCLGDWKTHGSEYYECSRYKENPDIVNQSQQAQAREALKKYLFYFERWENHNKSLQLEAQTYQRIHEKIQERVMNNLGTWIDWQYLQNAAKLLAKCRYTLQYTYPYAYYMESGPRKKLFEYQQAQLEAEIENLSWKVERADSYDRGDLENQMHIAEQRRRTLLKDFHDT
Protein: Heat shock protein beta-7 (Heat shock protein family, alpha-crystallin-related, b7) (Q5XJD0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSASNSSAYRSERSYHQTSSSSSSSSTSANPYMEKSRGLFADDFGSFMCPKDALGFPNRTGTVGNIKTLGDTYQFTVDVQDFSPEDVIVTTSNNQIEVHAEKLASDGTVMNTFTHKCRLPEDVDPTSVKSSLGADGTLTIKAQRNTAKLEHAQTFRTEIKI
Protein: Methyl-CpG binding domain protein 3 (A0A8I6ANN7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRRPPSRSPSGKKFRSKPQLARYLGGSMDLSTFDFRTGKMLMNKMNKSRQRVRYDSSNQVKGKPDLNTALPVRQTASIFKQPVTKITNHPSNKVKSDPQKAVDQPRQLFWEKKLSGLSAFDIAEELVRTMDLPKGLQGVGPGCTDETLLSAIASALHTSTLPITGQLSAAVEKNPGVWLNTAQPLCKAFMVTDDDIRKQEELVQQVRKRLEEALMADMLAHVEELARDGEAPLDKACAEEEEEEEEEEEEEPEPERV
Protein: Adhesion and penetration protein autotransporter (EC 3.4.21.-) [Cleaved into: Adhesion and penetration protein; Adhesion and penetration protein translocator] (P45387)
Organism: Haemophilus influenzae
Function: Probable protease; promotes adherence and invasion by directly binding to a host cell structure.
Subcellular location: [Adhesion and penetration protein autotransporter]: Periplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Adhesion and penetration protein]: Secreted. Cell surface.; SUBCELLULAR LOCATION: [Adhesion and penetration protein translocator]: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane. {ECO:0000250}.
Interaction partners:
Sequence:
MKKTVFRLNFLTACISLGIVSQAWAGHTYFGIDYQYYRDFAENKGKFTVGAQNIKVYNKQGQLVGTSMTKAPMIDFSVVSRNGVAALVENQYIVSVAHNVGYTDVDFGAEGNNPDQHRFTYKIVKRNNYKKDNLHPYEDDYHNPRLHKFVTEAAPIDMTSNMNGSTYSDRTKYPERVRIGSGRQFWRNDQDKGDQVAGAYHYLTAGNTHNQRGAGNGYSYLGGDVRKAGEYGPLPIAGSKGDSGSPMFIYDAEKQKWLINGILREGNPFEGKENGFQLVRKSYFDEIFERDLHTSLYTRAGNGVYTISGNDNGQGSITQKSGIPSEIKITLANMSLPLKEKDKVHNPRYDGPNIYSPRLNNGETLYFMDQKQGSLIFASDINQGAGGLYFEGNFTVSPNSNQTWQGAGIHVSENSTVTWKVNGVEHDRLSKIGKGTLHVQAKGENKGSISVGDGKVILEQQADDQGNKQAFSEIGLVSGRGTVQLNDDKQFDTDKFYFGFRGGRLDLNGHSLTFKRIQNTDEGAMIVNHNTTQAANVTITGNESIVLPNGNNINKLDYRKEIAYNGWFGETDKNKHNGRLNLIYKPTTEDRTLLLSGGTNLKGDITQTKGKLFFSGRPTPHAYNHLNKRWSEMEGIPQGEIVWDHDWINRTFKAENFQIKGGSAVVSRNVSSIEGNWTVSNNANATFGVVPNQQNTICTRSDWTGLTTCQKVDLTDTKVINSIPKTQINGSINLTDNATANVKGLAKLNGNVTLTNHSQFTLSNNATQIGNIRLSDNSTATVDNANLNGNVHLTDSAQFSLKNSHFSHQIQGDKGTTVTLENATWTMPSDTTLQNLTLNNSTITLNSAYSASSNNTPRRRSLETETTPTSAEHRFNTLTVNGKLSGQGTFQFTSSLFGYKSDKLKLSNDAEGDYILSVRNTGKEPETLEQLTLVESKDNQPLSDKLKFTLENDHVDAGALRYKLVKNDGEFRLHNPIKEQELHNDLVRAEQAERTLEAKQVEPTAKTQTGEPKVRSRRAARAAFPDTLPDQSLLNALEAKQAELTAETQKSKAKTKKVRSKRAVFSDPLLDQSLFALEAALEVIDAPQQSEKDRLAQEEAEKQRKQKDLISRYSNSALSELSATVNSMLSVQDELDRLFVDQAQSAVWTNIAQDKRRYDSDAFRAYQQQKTNLRQIGVQKALANGRIGAVFSHSRSDNTFDEQVKNHATLTMMSGFAQYQWGDLQFGVNVGTGISASKMAEEQSRKIHRKAINYGVNASYQFRLGQLGIQPYFGVNRYFIERENYQSEEVRVKTPSLAFNRYNAGIRVDYTFTPTDNISVKPYFFVNYVDVSNANVQTTVNLTVLQQPFGRYWQKEVGLKAEILHFQISAFISKSQGSQLGKQQNVGVKLGYRW
Protein: Meiosis-specific serine/threonine-protein kinase MEK1 (EC 2.7.11.1) (P24719)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable protein kinase required for meiotic recombination.
Interaction partners:
- Protein RED1
- Meiosis-specific protein HOP1
- Meiotic recombination protein DMC1
- Synaptonemal complex protein ZIP1
- DNA repair and recombination protein RAD54
- Meiosis-specific protein SPO11
- Meiosis-specific transcription factor NDT80
- Meiosis-specific protein SPO13
- Meiotic recombination protein REC8
- Serine/threonine-protein kinase RCK2
Sequence:
MRPLYSCNLATKDDIEMAGGVAPAHLEVNVGGYNTEQTIPIVKHQLVKVGRNDKECQLVLTNPSISSVHCVFWCVFFDEDSIPMFYVKDCSLNGTYLNGLLLKRDKTYLLKHCDVIELSQGSEENDIKKTRLVFMINDDLQSSLDPKLLDQMGFLREVDQWEITNRIVGNGTFGHVLITHNSKERDEDVCYHPENYAVKIIKLKPNKFDKEARILLRLDHPNIIKVYHTFCDRNNHLYIFQDLIPGGDLFSYLAKGDCLTSMSETESLLIVFQILQALNYLHDQDIVHRDLKLDNILLCTPEPCTRIVLADFGIAKDLNSNKERMHTVVGTPEYCAPEVGFRANRKAYQSFSRAATLEQRGYDSKCDLWSLGVITHIMLTGISPFYGDGSERSIIQNAKIGKLNFKLKQWDIVSDNAKSFVKDLLQTDVVKRLNSKQGLKHIWIAKHLSQLERLYYKKILCNNEGPKLESINSDWKRKLPKSVIISQAIPKKKKVLE