wanglab/gogpt-training-data huggingface dataset:
Protein: Condensin-2 complex subunit D3-L (Q6GN08)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000255|PIRNR:PIRNR036508}.
Interaction partners:
Sequence:
MGDREAVLLEALSRCGLRGLSQAWVDSVWELDFTETEPLDSRIEAEITENGLETFSSLHENLLAFASEDPENSRSVWLLFSENDICRNSLVALLSHFIQAAANKKANAIQRILALNAAGLYFLLLEIPGSVANQVFHPVLFDKSVNALEKCWPRDPNASRKRKKDTLKSSQGDNRGGRKRPRPPRRDEQEMEDLSEEEQDEEEVYFSTRDLMHIRDSIFLVLKNFLRLLPKFSLKEKPQSVLHCIQIFINLTSFESVPQEMPFSDAVSVNHMKYVPELAYHGLWLLCLPIHGEGNQTVRRLFQRLLSVILMMKGGEGSNSALLVISPPVISARNQAIRFISFLVNELKEGTIPVLNILLQHICVKFPDKADYRVYAAQALVKLMENLPNAEYAIFIEWLYKYSKNSKISYRVFALEVVVALLDLPEREADVSLPHENLNFLQHKFLLQHMVFSRCSDKAPTVRSKALSCLAQCLEKNSTTAIDGVQELLQGSSCRTVFGTNITETTGNGTVYASNANEATTHPQKTMATLKIIEVSDTGDTLSSDGKEVLTMLRYRAGDEKTNVRKSALQVLVNVLKCHLIPCSSEDLSTLQDRCRDPAVSVRKQALTSLTELLLAQPHSVLIQKAWLTGLIPVVLDTESSVQEKALECLDQLLLQSITHYKRFKQDDERQKLTWDLLTLLTSESQDLSRYLTKAFHLWSKQDKFSSTFITNLISHTETEHTAPAWMILSKVAGSSPKLDYTKILQSWERVSRQTDADINTTGHILCVIGHIAKHLPADTRTHLIDHVKSWLKEFKSSPEVISPAVEALQKLCHAQTDKPEDVQDLLNDVCGEIVSACEHHISSVVMADCKDEPLDQDLLVKHLFTLGEVAQLCPAKVEKRVLLLVQSILASSVTTEQNSCHSDAEDPPVSQPLSQFKGSNMPSLIRAHAFITLGKLCLQHEDLAKKCIPALARELEVCDDVAIRNNVIIVICDLCIRYTTMVDRYIPNVSVCLRDRDPFIRKQTLIMLTNLLQEEFVKWKGSLFFRFVSVLVDPDPEIAKFGEFCLVHLLLKRNPVMFSQHFIECIFHFNCYEKHEKYNKFAQTKRERTLFSLKGKENKDKRMKIYKFLLEHFTDEQRFNLTTKISHNVLACFVDGILPIDMEANELLSDIFDIMSSKEIKLSAMRSKPGEDVGADDDEMAMANAVMQAAQKKLISQVQKKNFVENIIPIITSLKGFLEQHRIPAVRDLMNYLREMMQDYRDEIKDFFAADKQLAAELEYDMKKYEEQLEREQEENVQNPPSAESTGSPKGSPRAVNAISSPRSPNAPKSPLSTNAQTPGGAAPCTPITTPRVSILKGQGPRPRQMSLSTLAILNSARKAAQDNKKQRSKSIGAQPSTPSPARTTSSKQVTFRSEDQQSDSSLVGRMISTPDVTIENVTFGAGVSYISASQTPLSGRRGSIGSHEKERDVLCIMSPDKPAPQPRKWNVESPVQRRSIRQRISGKAPLKPSN
Protein: Cytochrome c2 (P86323)
Organism: Rhodoplanes tepidamans (Rhodoplanes cryptolactis)
Function: Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
Subcellular location: Periplasm {ECO:0000269|PubMed:20697695}.
Interaction partners:
Sequence:
QQVAAGAVSFRKCTPCHNIGEGATNKVGPVLDGLEGRHSGSIPGFNYSEANKKSGLTWDKATFKSYIADPRAKIPGTKMVFAGIKNEKEQEDLWAFLTQYGPDGKKK
Protein: T cell receptor beta variable 19 (A0A075B6N1)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of T cell receptor (TR) beta chain that participates in the antigen recognition. Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens. Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation. The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity.
Subcellular location: Cell membrane {ECO:0000303|PubMed:20452950}.
Interaction partners:
Sequence:
MSNQVLCCVVLCLLGANTVDGGITQSPKYLFRKEGQNVTLSCEQNLNHDAMYWYRQDPGQGLRLIYYSQIVNDFQKGDIAEGYSVSREKKESFPLTVTSAQKNPTAFYLCASSI
Protein: Probable guanine deaminase (Guanase) (Guanine aminase) (EC 3.5.4.3) (Guanine aminohydrolase) (GAH) (Q07729)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Purine nucleoside phosphorylase
- Adenine phosphoribosyltransferase 2
- Adenine phosphoribosyltransferase 1
- Hypoxanthine-guanine phosphoribosyltransferase
- Uridine nucleosidase
- Adenine deaminase
- Adenylosuccinate lyase
- Cytidine deaminase
- Phosphate metabolism protein 8
- S-methyl-5'-thioadenosine phosphorylase
Sequence:
MTKSDLLFDKFNDKHGKFLVFFGTFVDTPKLGELRIREKTSVGVLNGIIRFVNRNSLDPVKDCLDHDSSLSPEDVTVVDIIGKDKTRNNSFYFPGFVDTHNHVSQYPNVGVFGNSTLLDWLEKYTFPIEAALANENIAREVYNKVISKTLSHGTTTVAYYNTIDLKSTKLLAQLSSLLGQRVLVGKVCMDTNGPEYYIEDTKTSFESTVKVVKYIRETICDPLVNPIVTPRFAPSCSRELMQQLSKLVKDENIHVQTHLSENKEEIQWVQDLFPECESYTDVYDKYGLLTEKTVLAHCIHLTDAEARVIKQRRCGISHCPISNSSLTSGECRVRWLLDQGIKVGLGTDVSAGHSCSILTTGRQAFAVSRHLAMRETDHAKLSVSECLFLATMGGAQVLRMDETLGTFDVGKQFDAQMIDTNAPGSNVDMFHWQLKEKDQMQEQEQEQGQDPYKNPPLLTNEDIIAKWFFNGDDRNTTKVWVAGQQVYQI
Protein: Phosphatidylserine synthase 2 (PSS-2) (PtdSer synthase 2) (EC 2.7.8.29) (Serine-exchange enzyme II) (O08888)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Catalyzes the conversion of phosphatatidylethanolamine and does not act on phosphatidylcholine. Shows a substrate specificity for phosphatatidylethanolamine and does not act on phosphatidylcholine (By similarity). Can utilize both phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate and the latter is six times better utilized, indicating the importance of an ester linkage at the sn-1 position (By similarity). Although it shows no sn-1 fatty acyl preference, exhibits significant preference towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at the sn-2 position (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z1X2}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:12912985}. Note=Highly enriched in the mitochondria-associated membrane (MAM). {ECO:0000250|UniProtKB:Q9Z1X2}.
Interaction partners:
Sequence:
MRRAERRVAGGSGSGSPLLEGRRSTESEVYDDGTNTFFWRAHTLTVLFILTCSLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPRLGVPLPERDYGGNCLIYDADNKTDPFHNIWDKLDGFVPAHFIGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLICNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSWVRFEWKPASSLHRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGVAMREIYDFMDELKPHRKLGQQAWLVAAITVTELLIVVKYDPHTLTLSLPFYISQCWTLGSILVLTWTVWRFFLRDITMRYKETRRQKQQSHQGRAINNGDGHPGPDDDLLGTGTAEEEGSTNDSVPAEKEGASAAS
Protein: Uncharacterized WD repeat-containing protein C63.06 (Q9Y7T2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MVTASSSVRVSNEDECFIYDIEQLKDNVVVSYSTGSWSCFDKGTLLEIFKVPKAHTNITGIISCDQLNGVITCGSEGEIHLWDIRSQAKSAVRSWTQQSTPFTCIALNKKNQFATGSELTRSLASVQLWDVRSEQKLIRQWNDAHNDDITHLQFHPKDNELLLTGSVDGLVSLLDTTKEEDSTDPEEDPLLHVINHGASIHLAKFVSKKRVMVLSHMESYAMYKLKRDKDEKTWSSNELFSIDDLRAELSCSYVINEVSTSDKQFCALAFGDFSNHETKFVLVDTSTGELKKEPTKLERASEEICRAISFDVKNDVYYSGGEDGLLQAFRV
Protein: 4-aminobutyrate aminotransferase (EC 2.6.1.19) (GABA aminotransferase) (Gamma-amino-N-butyrate transaminase) (A0A1D8PH55)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Succinate-semialdehyde dehydrogenase
- Succinate-semialdehyde dehydrogenase
- Glutamate decarboxylase
- Aldehyde dehydrogenase
- methylmalonate-semialdehyde dehydrogenase
- Aldehyde dehydrogenase
- Glutamate decarboxylase
- Aldehyde dehydrogenase domain-containing protein
- Aldehyde dehydrogenase domain-containing protein
- 3-hydroxyisobutyrate dehydrogenase
Sequence:
MSSKSVSSLYFPEEPKEPVVVDSHAKSKEIADRLGKVFDNRGVYFVADYEKSVGNYIADVDGNVYLDVYAQIASIPLGYNNPALIETAKSDKMIRAIVDRPAIGNFPGKDTDEIVSEILKVAPKGQDKVWSGLSGADANELAFKAAFFYYQAKKRGYTTQFSEEEMKSVMQNEAPGSPELAILSFERGFHGRLFASGSTTCSKPIHKLDMPSFKWPKAQFPSYKYPLDKYAEENKKEDERCLKIVDDIIQNNKIPVAAVLVEPIQSEGGDNHASAEFFQGLRDITLKHGSLLIMDEVQTGVGATGVMWAHERFNLQPPPDLVTFSKKFQSAGYFFHDPEIIPNFAYRQFNTWCGDPARMILAGAIGQEILKHDLVKRAAEVGDYLFKKLEQLQEKYPKYIKDLRGKDRATFIAWSLESGEARNKFLSDMKTVGVNIGGCAEDSVRLRPTLVFEEQHADILVSAIDKLLGSY
Protein: mRNA interferase toxin HigB (EC 3.1.-.-) (Endoribonuclease HigB) (Toxin HigB) (P64578)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system. A probable translation-dependent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome by subsequent expression of antitoxin HigA. Overexpression causes cleavage of a number of mRNAs in a translation-dependent fashion, suggesting this is an mRNA interferase.
Interaction partners:
- Antitoxin HigA
- Endoribonuclease toxin MazF
- mRNA interferase toxin YafQ
- mRNA interferase toxin RelE
- Toxin YoeB
- mRNA interferase toxin MqsR
- Probable mRNA interferase toxin HicA
- Antitoxin YefM
- Antitoxin HicB
- Antitoxin RelB
Sequence:
MHLITQKALKDAAEKYPQHKTELVALGNTIAKGYFKKPESLKAVFPSLDNFKYLDKHYVFNVGGNELRVVAMVFFESQKCYIREVMTHKEYDFFTAVHRTKGKK
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IFQ5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MVPPGGRQGGSGEDGIDDKDAKHLLDSIGKIVHEQVKNDAKTYKGELEGKLSLATTIGELNYTKDPCIFDYSKLINGSGSGGVTARDDPCGNGSGKGEDVSRFSDKEGAQCANSKIHGNSKGSNGGACAPLRRLHLCNKNMEKIATSTAKHDLLVDVCMAANYEAQSLIRDHPQHKRTNPDSKICTELARSFADIGDIVRGRDLYRGNKKENKQREKLEENLRKIFENIYEGLSNNGVKARYEGDKENFYQLREDWWALNRDQVWKALTCSDDLKDASYFRPTCSDRKGSCSQAKDNCRCDGSNTDQVPTYFDYVPQFLRWFEEWAEDFCRKKKKKLEKLEQQCRGVYEGKERYCSRNGFDCEKTVNARGKVRMGKGCTDCFFACNPYIDWIEKQKEQFDKQKQKYDEEIKKYTKVASSSSGGRAKRAARGGSNVNGYEKIFYKKLKDSGYESVGEFLDLLSKEEVCKNFKEKEEGKIDFKTVKSSSAKNSDDSNKTFCRTKYCQPCPLCGMKKNNNGEWEHKKKGKCTSGNLYRPIDGAIHTDINFLYSGDRHDDIEKKLNRFCDETNGDTINSVAGVSGTGVVAGSNSRSKELYQEWKCYKGKDVEKVKDGKDEDDEDYEDDYHKEVENAGGLCILENNDGKEKVNKQKTYNDFFYYWVAHMLKDSIHWKKKLEKCLKNGTKTRCKNNKCNRECGCFQKWVEQKKKKEWGKIIEHFYKQEGIPPGTHDITLEGVLKKEVLLTSLQEGYGNAEDIEHIKQLLEEEENEENEGTPGADNKNKNTIDKLLDHEEGIAKECQQKQNECPKKPPKKTPGGPDRALKPEEVDASSEDHYDEEGGEDEEEEEDKEEEGEDGEDVQDDVAEEDTAKEEGSSTTETQLPDACNIVKTLFESTKNFEDACRQKYGPKAPTSWKCVPTTGDKDGATGKSDGSICVPPRRRRLYIHKVDDNVKDDASLRKWFIESSAVETFFLWHEYKMEKKREDIEKQKANEKVVDTSNVGEELQNDLEGNGTIPEEFKRQMFYTLGDYKDIFEGKSIEVGDEKDKQKMKEIEKKIQAHINSGSSSPPHGTPGQPNSVTTPQQTWWSRNAPSIWKGMICALTYKEDGEKSTDDKTTLKRNDDVYEKIFGKPPNNDNPQNPNNGTFHKKYHYDSVRLKDDDDQSGDKLQSTSAPSDTPTLNNPKLSDFVLRPTYFRYLEEWGESFCGTRKRMLEQLEKVCRSGETGKEHCSGDGHVCEKDYLNHNNMFADSYCPDCKKACRKYKKWIEKKLEEFQKQKDKYKGELDKLTKDKSGGDKKFCEEIKNHSSAANFLKELKHGKDNQGNSDQDNKLDFENIPQTFSRSTYCKTCPPNKVNCSSGSKSRTSGGTNRCTEVKKNGETWEKVFDKIAKNNGKTTTIDVHMIDRRAPFIKKYLENSKNSEESNNSLFKDSYLFKSVRDQNWECKFENENKDVCKLKNFNDKIDLNQYTTFKVLLIYWLEDFIEGYYILKKRKVFEQCKENGENTCSEESKNYCACVKVWLEKKKNEWDQIKKHFKDRKSDDGDTVVSKVRNFLETLIPRIAPKKNNGEVTELSDLEKSLGCNCAGRAENSKEDEKEDVVLCLLTKLEDKANKCKEDQKPNGENQAQTCEKSAPVEDEDDEPLEEENPVTQPNICPKVETTEETVDEGKCEEDTVTPSLGPKDDSEKDEKKEENSEDTTAAEGEENGAPGSSGTPPPPPAAPPSTPAKTKESKKPKSTKKPRIKTLNVLDHPAVIPALMSSTIMWSIGIGFATFTYFYLKKKTKSSVRNLFQILQIPKGDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSESEYEEMDINDIYVPGSPKYKTLIEVVLEPSKSNGNTLGDDMVPTTNTFTDEEWNELKHDFISNMLQNQPNDYKSEDIPLNTQPNTLYFNKPEEKPFITSIHDRNLYSGEEYSYNINMSTNSMDDIPINRDNNVYSGIDLINDTLSGNQHIDIYDEVLKRKENELFGTKHHTKRTSTQNVAKPARDDPIHNQLDLFHKWLDRHRDMCKKWNNKEGLLDKLKEEWNKDTNSGKLSDNIHSDNKPGDIPSDNHVLNSDVSIQIDMGNPKYINQFTCVDSNPNLTLRSNPNLMGNQNPNLNLVENNINPNHQNQNQVGDTNFVDTPTNPTNVQIEMDVNTKLVKEKYPIGDVWDI
Protein: Appetite-regulating hormone (Growth hormone secretagogue) (Growth hormone-releasing peptide) (Motilin-related peptide) (Protein M46) [Cleaved into: Ghrelin-27; Ghrelin-28 (Ghrelin); Obestatin] (Q9UBU3)
Organism: Homo sapiens (Human)
Function: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
Subcellular location: Secreted.
Interaction partners:
- Growth hormone secretagogue receptor type 1
- Leptin
- Membrane-bound ghrelin O-acyltransferase MBOAT4
- G-protein coupled receptor 39
- Pro-neuropeptide Y
- Insulin
- Pro-glucagon
- Agouti-related protein
- Peptide YY
- Cholecystokinin
Sequence:
MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQQRKESKKPPAKLQPRALAGWLRPEDGGQAEGAEDELEVRFNAPFDVGIKLSGVQYQQHSQALGKFLQDILWEEAKEAPADK
Protein: tRNA-dihydrouridine(20/20a) synthase (EC 1.3.1.-) (EC 1.3.1.91) (U20-specific dihydrouridine synthase) (U20-specific Dus) (tRNA-dihydrouridine synthase A) (P32695)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs.
Interaction partners:
- tRNA pseudouridine synthase B
- tRNA-cytidine
- tRNA
Sequence:
MHGNSEMQKINQTSAMPEKTDVHWSGRFSVAPMLDWTDRHCRYFLRLLSRNTLLYTEMVTTGAIIHGKGDYLAYSEEEHPVALQLGGSDPAALAQCAKLAEARGYDEINLNVGCPSDRVQNGMFGACLMGNAQLVADCVKAMRDVVSIPVTVKTRIGIDDQDSYEFLCDFINTVSGKGECEMFIIHARKAWLSGLSPKENREIPPLDYPRVYQLKRDFPHLTMSINGGIKSLEEAKAHLQHMDGVMVGREAYQNPGILAAVDREIFGSSDTDADPVAVVRAMYPYIERELSQGTYLGHITRHMLGLFQGIPGARQWRRYLSENAHKAGADINVLEHALKLVADKR
Protein: Forkhead box O4 (A0A096MJF0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MEPENKKSATEAAAIIDLDPDFEPQSRPRSCTWPLPRPELATEPPEPSEVEPSLGQKAIESAPEKRLTLAQIYEWMVRTVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIKVHNEATGKSSWWMLNPDGGKGGKAPRRRAASMDSSSKLLRGRSKGPKKKPSVLPAPPEGATPRSPLGHFAKWSSSPCPRNREEADVWTTFRPRSSSNASTVSTRLSPMRPESEVLAEEEMPASASSYAGGVPPTLSEDLELLDGLNLASPHSLLSRSNLSSFSLQHPGLAGPLHSYGASLFGPIDGSLSAGEGCFSSSQSLEALLTSDTPPPPADVLMTQVDPILSQAPTLLLLGGMPSSSKLATGVSLCPTPLEGPGPSNLVPTLSVMAPPPVMPGAPIPKVLGTPVLASPTEDFSHDRMPQDLDLDMYMENLECDMDNIISDLMDGEGLDFNFEPDP
Protein: tRNA (cytosine(38)-C(5))-methyltransferase (EC 2.1.1.204) (DNA (cytosine-5)-methyltransferase-like protein 2) (Q9VKB3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- tRNA
- 28S rRNA
- Queuine tRNA-ribosyltransferase catalytic subunit
- Methyl-CpG binding domain protein-like, isoform C
- Endoribonuclease Dcr-2
- tRNA
- Pseudouridylate synthase 7 homolog
- N
- S-adenosylmethionine synthase
- G/T mismatch-specific thymine DNA glycosylase
Sequence:
MVFRVLELFSGIGGMHYAFNYAQLDGQIVAALDVNTVANAVYAHNYGSNLVKTRNIQSLSVKEVTKLQANMLLMSPPCQPHTRQGLQRDTEDKRSDALTHLCGLIPECQELEYILMENVKGFESSQARNQFIESLERSGFHWREFILTPTQFNVPNTRYRYYCIARKGADFPFAGGKIWEEMPGAIAQNQGLSQIAEIVEENVSPDFLVPDDVLTKRVLVMDIIHPAQSRSMCFTKGYTHYTEGTGSAYTPLSEDESHRIFELVKEIDTSNQDASKSEKILQQRLDLLHQVRLRYFTPREVARLMSFPENFEFPPETTNRQKYRLLGNSINVKVVGELIKLLTIK
Protein: Sister chromatid cohesion protein PDS5 homolog D (Precocious dissociation of sisters protein 5-D) (AtPDS5D) (A8MRD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex. Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication (By similarity). Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
Sequence:
MTAIVGFDQLSKALIDAGTNLLSPPSSTDDLLTLLDETESLLKNVEQDQPLSMQSALIPSRNALVSVDLLSHPDSDVRVSVVSCLTEIVRITAPETPYSDDLMKEIFRLTIEAFEKLADASSRSYKKAEFVLDNVAKVKSCLVMLDLECYDLILQMFRNFFKFIRSDHPQLVFSSMELIMIAIIDETEQVSTDLLDSLLATVKKENQNVSPMSWSLAEKVLSRCARKLKPYIIEALKSRGTSLDMYSPVVSSICQSVFNTPKVHSPVNTKEHEEKLDLGHSRKENLSKSSSKRPARHETRGINEKEKVRNGNKSSLLKQSLKQVRSESTDAEITGKRGRKPNSLMNPEDYDISWLSGKRDPLKTSSNKKIQKKGSGGVSSLGKVPAKKTPLPKENSPATSSRSLTGSLKRSRVKMDESDYDSDSLSSPRLKKLASCFRDEEPNQEDDRKIGNSSKQTRSKNGLEKSQKTAKKKPVVEAKIVNSSGKRLSARSVAKRRNLERAPLDTLVPQSSKRKKMVSQVAARQLANESEEETPKSHPTRRRTVRKEVESDGFGEDLVGKRVNIWWPLDKTFYEGVIDSYCTRKKMHRVIYSDGDSEELNLTEERWELLEDDTSADEDKEIDLPESIPLSDIMQRQKVKKSKNVAVSVEPTSSSGVRSSSRTLMKKDCGKRLNKQVEKTREGKNLRSLKELNAETDRTAEEQEVSLEAESDDRSEEQEYEDDCSDKKEQSQDKGVEAETKEEEKQYPNSEGESEGEDSESEEEPKWRETDDMEDDEEEEEEEIDHMEDEAEEEKEEVDDKEASANMSEIEKEEEEEEEDEEKRKS
Protein: AP-2 complex subunit sigma (Adaptor protein complex AP-2 subunit sigma) (Adaptor-related protein complex 2 subunit sigma) (Clathrin assembly protein 2 sigma small chain) (Clathrin coat assembly protein AP17) (Clathrin coat-associated protein AP17) (Plasma membrane adaptor AP-2 17 kDa protein) (Sigma-adaptin 3b) (Sigma2-adaptin) (P62743)
Organism: Mus musculus (Mouse)
Function: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via Transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. May also play a role in extracellular calcium homeostasis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P63010}. Membrane, coated pit {ECO:0000250|UniProtKB:P53680}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53680}; Cytoplasmic side {ECO:0000250|UniProtKB:P53680}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000250|UniProtKB:P63010}.
Interaction partners:
- AP-2 complex subunit alpha-1
- AP-2 complex subunit alpha-2
- AP-2 complex subunit mu
- AP-2 complex subunit beta
- Intersectin-2
- Clathrin heavy chain 1
- Adaptin ear-binding coat-associated protein 2
- AP-4 complex subunit beta-1
- Clathrin light chain B
- F-BAR domain only protein 2
Sequence:
MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQSLE
Protein: S-phase kinase-associated protein 2 (Cyclin-A/CDK2-associated protein p45) (F-box protein Skp2) (F-box/WD-40 protein 1) (FWD1) (Q9Z0Z3)
Organism: Mus musculus (Mouse)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription (By similarity). Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, YTHDF2, and probably MYC, TOB1 and TAL1. Degradation of TAL1 also requires STUB1. Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destruction of CDH1 in a CK1-dependent manner, thereby regulating cell migration (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13309}. Nucleus {ECO:0000250|UniProtKB:Q13309}.
Interaction partners:
- Cyclin-A2
- Cyclin-dependent kinase inhibitor 1B
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- Cyclin-dependent kinase 2
- S-phase kinase-associated protein 1
- Cyclin-A1
- Cyclin-dependent kinases regulatory subunit 1
- F-box/WD repeat-containing protein 1A
- Cyclin-dependent kinases regulatory subunit
Sequence:
MHRKHLQEIPDQSGNVTTSFTWGWDSSKTSELLSGMGVSALEKEEVDSENIPHGLLSNLGHPQSPPRKRVKGKGSDKDFVIIRRPKLSRENFPGVSWDSLPDELLLGIFSCLCLPELLRVSGVCKRWYRLSLDESLWQSLDLAGKNLHPDVTVRLLSRGVVAFRCPRSFMEQPLGESFSSFRVQHMDLSNSVINVSNLHKILSECSKLQNLSLEGLQLSDPIVKTLAQNENLVRLNLCGCSGFSESAVATLLSSCSRLDELNLSWCFDFTEKHVQAAVAHLPNTITQLNLSGYRKNLQKTDLCTIIKRCPNLIRLDLSDSIMLKNDCFPEFFQLNYLQHLSLSRCYDIIPDTLLELGEIPTLKTLQVFGIVPEGTLQLLREALPRLQINCAYFTTIARPTMDSKKNLEIWGIKCRLTLQKPSCL
Protein: Cation channel sperm-associated auxiliary subunit gamma (Q6ZRH7)
Organism: Homo sapiens (Human)
Function: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Cation channel sperm-associated protein 1
- Cation channel sperm-associated auxiliary subunit beta
- Cation channel sperm-associated auxiliary subunit delta
- Cation channel sperm-associated auxiliary subunit epsilon
- Cation channel sperm-associated protein 2
- Cation channel sperm-associated protein 3
- EF-hand calcium-binding domain-containing protein 9
- Cation channel sperm-associated auxiliary subunit zeta
- Cation channel sperm-associated protein 4
- Cation channel sperm-associated auxiliary subunit TMEM262
Sequence:
MCGPAMFPAGPPWPRVRVVQVLWALLAVLLASWRLWAIKDFQECTWQVVLNEFKRVGESGVSDSFFEQEPVDTVSSLFHMLVDSPIDPSEKYLGFPYYLKINYSCEEKPSEDLVRMGHLTGLKPLVLVTFQSPVNFYRWKIEQLQIQMEAAPFRSKEPCMAEEVCSMSWYTPMPIKKGSVVMRVDISSNGLGTFIPDKRFQMNINGFLKRDRDNNIQFTVGEELFNLMPQYFVGVSSRPLWHTVDQSPVLILGGIPNEKYVLMTDTSFKDFSLVELSIDSCWVGSFYCPHSGFTATIYDTIATESTLFIRQNQLVYYFTGTYTTLYERNRGSGSWIRVLASECIKKLCPVYFHSNGSEYIMALTTGKHEGYVHFGTIRDGQVSFEMLPRQWSVCEQIGVTTCSIIWSEYIAGEYTLLLLVESGYGNASKRFQVVSYNTASDDLELLYHIPEFIPEARGLEFLMILGTESYTSTAMAPKGIFCNPYNNLIFIWGNFLLQSSNKENFIYLADFPKELSIKYMARSFRGAVAIVTETEEIWYLLEGSYRVYQLFPSKGWQVHISLKLMQQSSLYASNETMLTLFYEDSKLYQLVYLMNNQKGQLVKRLVPVEQLLMYQQHTSHYDLERKGGYLMLSFIDFCPFSVMRLRSLPSPQRYTRQERYRARPPRVLERSGFHNENSLAIYQGLVYYLLWLHSVYDKPYADPVHDPTWRWWANNKQDQDYYFFLASNWRSAGGVSIEMDSYEKIYNLESAYELPERIFLDKGTEYSFAIFLSAQGHSFRTQSELGTAFQLHSQVDVGVVLADPGCIEASVKQEVLINRNSVLFSITLKDKKLCYDQGISGHHLMETSMTVNVVGSSGLCFQETHLGPHMQGNLMVPVFIGCPPGKRLAFDITYTLEYSRLKNKHYFDCVNVNPEMPCFLFRDIFYPFFLIQDLVTGDSGSFQGSYVLLVVGGGPTLDSLKDYSEDEIYRFNSPLDKTNSLIWTTRTTRTTKDSAFHIMSHESPGIEWLCLENAPCYDNVPQGIFAPEFFFKVLVSNRGVDTSTYCNYQLTFLLHIHGLPLSPKRALFIIMVSASVFVGLVIFYIAFCLLWPLVVKGCTMIRWKINNLIASESYYTYASISGISSMPSLRHSRMGSMFSSRMTEDRAEPKEAVERQLMT