wanglab/gogpt-training-data huggingface dataset:
Protein: Cytoplasmic protein NCK2 (Growth factor receptor-bound protein 4) (NCK adaptor protein 2) (Nck-2) (SH2/SH3 adaptor protein NCK-beta) (O55033)
Organism: Mus musculus (Mouse)
Function: Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O43639}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O43639}.
Interaction partners:
- Ephrin-B1
- LIM and senescent cell antigen-like-containing domain protein 1
- Ephrin-B3
- Ephrin-B2
- Serine/threonine-protein kinase PAK 1
- Lymphocyte cytosolic protein 2
- SH2/SH3 adapter protein Nck1
- Serine/threonine-protein kinase PAK 2
- Serine/threonine-protein kinase PAK 3
- Serine/threonine-protein kinase PAK 4
Sequence:
MTEEVIVIAKWDYTAQQDQELDIRKNERLWLLDDSKTWWRVRNAANRTGYVPSNYVERKNSLKKGSLVKNLKDTLGLGKTRRKPSARDASPTPSTDAEYPANGSGADRIYDLNIPAFVKFAYVAEREDELSLVKGSRVTVMEKCSDGWWRGSFNGQIGWFPSNYVLEEADEAAAEAPSFLSLRRGTALSNGQGARVLHVVQTLYPFSSVTEEELSFEKGETMEVIEKPENDPEWWKCKNARGQVGLVPKNYVVVLSDGPALHPAHTPQISYTGPSASGRFAGREWYYGNVTRHQAECALNERGVEGDFLIRDSESSPSDFSVSLKASGRNKHFKVQLVDSVYCIGQRRFHSMDELVEHYKKAPIFTSEHGEKLYLVRALQ
Protein: Class E basic helix-loop-helix protein 22 (Class B basic helix-loop-helix protein 5) (Q7T301)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDSFRPTAGIDLSARDSQSPISCFEQNDPDPVQPGGRAGTLGLPTGSLCVKYGESANRTSGAESSGGEQSPDDDSDERCEMMLMTDGRTTVPGAKSEGGKKNKEQKMLRLNINARERRRMHDLNDALDELRAVIPYAHSPSVRKLSKIATLLLAKNYILMQAQALEEMRRLVAYLNQGQAISAASLPATTALTPGLSAYEQPAGYPFPAGVAASSCPDKCALFNNVTSSLCKQCTDKP
Protein: Protocadherin gamma A8 (Protocadherin gamma subfamily A, 8) (Q91XY0)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MAASKNQHRHGRLVLLCTLMGTLCKISVGQIRYSVPEETDKGTVVGNISKDLGLEPRELAERGVRIVSRGRSQLFSLNPRGGSLVTAGRIDREELCAQSTPCLVNINILVEEKGKLFGVEIEITDINDNNPKFHVGDLEVKINEIAAPGARYPLPEAVDPDVGINSLQSYQLSPNRHFSLHLQTGDDGTINPELVLERTLDREEEPTHHLVLTASDGGEPRRSSTALIQITVLDTNDNAPVFDQPVYRVKVLENVAPGTLLLTVRASDPDEGVNGKVTYKFRKINEKQSLLFHLHENTGEMTVAKNLDYEECSLYEMEIQAEDVGALLGRSKVIIMVEDVNDNRPEVTITSLFNPVLENSLPGTVIAFLNVHDQDSGKNGQVVCYTHDNLPFKLEKSIDNYYRLVTWKYLDREKVSTYNITVIASDLGAPPLSTETYIALTVADTNDNPPRFSHTSYTAYLPENNLRGASIFSLTAHDPDSQENAQVTYSVSEDTIQGVPLSSYISINSDTGILYALQSFDFEKIQDLQLLVIATDSGSPPLSSNVSLSLFVLDQNDNAPEILYPSFPTDGSTGVELAPRSAEPGYLVTKVVAVDKDSGQNAWLSYRLLKASEPGLFSVGLHTGEVRTARALLDRDALKQNLVMAVQDHGQPPLSATVTLTVAVANSIPEVLADLSSIMTPEVPEDSDLTLHLVVAVAVVSCVFLVFVIVLLALRLQRWQKSRQLQGSRSGLAPAPPSHFVGIDGVQAFLQTYSHEVSLTSGSQTSHIIFPQPNYADMLINQESCEKNDSLLTSIDFHENKDEDACAPQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Probable nucleoporin Nup54 (Q9V6B9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Essential for the nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner. Together with Nup58, required for transposable element silencing regulation in ovarian follicle cells. By interacting with the nuclear (Nxf1/Nxt1) and cytosolic (fs(1)Yb) components of the flamenco (flam) transcripts processing pathway, enables export and subsequent piRNA production.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17682050}.
Interaction partners:
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup58
- Nuclear pore complex protein Nup154
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup75
- Nucleoporin seh1
- Nuclear pore protein
- Nuclear pore complex protein Nup153
Sequence:
MSFFGSNTSLGATSTPAKTTGGLFGSPFGGTAATSQPAPAFGAQATSTPAFGAQPATSAFGAGSAFGATAAAPAFGAATGTSAFGGSAFGSTPAFGAATTTTAGTGLGGGGFGGFGAAPATSQAGLFGAPATSAAPPAFSGFGQQAAASTAPASGFSGFGTTTTSAPAFGGFGTSQSTGFGGGAFGSTFGKPANTTVTPGFGGFGGTSFMLGQPQQQPAPISADEAFAQSILNVSIFGDERDKIVAKWNYLQATWGTGKMFYSQSAAPVDITPENVMCRFKAIGYSRMPGKDNKLGLVALNFCRELSAVKPHQQQVIQTLHSLFGSKPNMLVHIDSIKELENKKCQIVIYVEEKLQHAPNESKRILATELSNYLNQATLKPQLNNLGVVEALALVLPDEDQLREYLENPPRGVDPRMWRQANSDNPDPTLYIPVPMVGFNDLKWRVKCQEQETDTHALYIKKVESELTELKKRHATATAKILEHKRKLAELSHRILRIIVKQECTRKVGTSLTPEEEALRTKLQNMLAVVSAPTQFKGRLSELLSQMRMQRNQFAANGGAEYALDKEAEDEMKTFLTMQQRAMEVLSDTVNKDLRALDVIIKGLPELRQS
Protein: Stonin-1 (Stoned B-like factor) (Q9Y6Q2)
Organism: Homo sapiens (Human)
Function: May be involved in the endocytic machinery.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11381094}. Membrane {ECO:0000269|PubMed:11381094}. Note=Some fraction is membrane-associated.
Interaction partners:
- TFIIA-alpha and beta-like factor
- Transcription initiation factor IIA subunit 1
- Transcription initiation factor IIA subunit 2
Sequence:
MCSTNPGKWVTFDDDPAVQSSQKSKNFPLENQGVCRPNGLKLNLPGLREFPSGSSSTSSTPLSSPIVDFYFSPGPPSNSPLSTPTKDFPGFPGIPKAGTHVLYPIPESSSDSPLAISGGESSLLPTRPTCLSHALLPSDHSCTHPTPKVGLPDEVNPQQAESLGFQSDDLPQFQYFREDCAFSSPFWKDEGSDSHFTLDPPGSKKMFSSRNKEMPIDQKSLNKCSLNYICEKLEHLQSAENQDSLRSLSMHCLCAEENASSFVPHTLFRSQPKSGWSFMLRIPEKKNMMSSRQWGPIFLKVLPGGILQMYYEQGLEKPFKEIQLDPYCRLSEPKVENFSVAGKIHTVKIEHVSYTEKRKYHSKTEVVHEPDIEQMLKLGSTSYHDFLDFLTTVEEELMKLPAVSKPKKNYEEQEISLEIVDNFWGKVTKEGKFVESAVITQIYCLCFVNGNLECFLTLNDLELPKRDESYYEKDSEKKGIDILDYHFHKCVNVQEFEQSRIIKFVPLDACRFELMRFKTLYNGDNLPFSLKSVVVVQGAYVELQAFVNMASLAQRSSYAGSLRSCDNIRIHFPVPSQWIKALWTMNLQRQKSLKAKMNRRACLGSLQELESEPVIQVTVGSAKYESAYQAVVWKIDRLPDKNSSLDHPHCLSYKLELGSDQEIPSDWYPFATVQFSVPDTCASRTEVRSLGVESDVQPQKHVQQRACYNIQVEIEKKWIKIDGEDPDKIGDCITQ
Protein: LexA repressor (EC 3.4.21.88) (A0QVY5)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- DNA polymerase IV
- DNA polymerase IV
- DNA polymerase IV
- Regulatory protein RecX
- Arginine repressor
- Error-prone DNA polymerase
- Holliday junction branch migration complex subunit RuvA
- UvrABC system protein C
- ATP-dependent Clp protease ATP-binding subunit ClpX
Sequence:
MSDDTGEFTDGSTESPADADGAGRRRAVDNGLTERQRTILEVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRAADDPAAAAVVTTDVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGDSMVDAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRARGQVWLMPHNPAYDPIPGNEAAVLGKVVTVIRKI
Protein: Coiled-coil domain-containing protein 115 (Coiled-coil protein 1) (Ccp1) (Q8VE99)
Organism: Mus musculus (Mouse)
Function: Accessory component of the proton-transporting vacuolar (V)-ATPase protein pump involved in intracellular iron homeostasis. In aerobic conditions, required for intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. Necessary for endolysosomal acidification and lysosomal degradation (By similarity). May be involved in Golgi homeostasis (By similarity).
Subcellular location: Endosome {ECO:0000269|PubMed:16378758}. Lysosome {ECO:0000269|PubMed:16378758}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q96NT0}. Cytoplasmic vesicle, COPI-coated vesicle {ECO:0000250|UniProtKB:Q96NT0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96NT0}. Note=Seems not to be associated with recycling endosomes. {ECO:0000269|PubMed:16378758}.
Interaction partners:
- Vacuolar ATPase assembly protein VMA12
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d 2
- Renin receptor
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit E 1
- V-type proton ATPase 116 kDa subunit a 4
- V-type proton ATPase 16 kDa proteolipid subunit c
Sequence:
MAVQALREELDSKCLQLLSDLEELEAKRAALNARVEEGWLSLAKARYAMGAKSVGPLQYASRMEPQVCVRASEAQDGPQTFRVIKADAQTPEEVGPSEASLRRRKGPTKTKELGSAVVPQDPLNWFGILVPHSLRQAQASFRDGLQLAADIASLQTRINWGQSQLRGLQKKLKELDPGPA
Protein: Lipoprotein lipase (LPL) (EC 3.1.1.34) (Phospholipase A1) (EC 3.1.1.32) (Q06000)
Organism: Rattus norvegicus (Rat)
Function: Key enzyme in triglyceride metabolism (By similarity). Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (By similarity). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (By similarity). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P11151}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted {ECO:0000250|UniProtKB:P11151}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11151}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells. Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles. {ECO:0000250|UniProtKB:P11151}.
Interaction partners:
- Glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1
- Apolipoprotein C-II
- Angiopoietin-related protein 4
- Angiopoietin-related protein 3
- Prolow-density lipoprotein receptor-related protein 1
- Patatin-like phospholipase domain-containing protein 2
- Apolipoprotein C-III
- Apolipoprotein E
- Acylglycerol transacylase
- phosphatidate phosphatase
Sequence:
MESKALLLVALGVWLQSLTAFRGGVAAADGGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWLEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAEKGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNVGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTENDKQNNQAFEISLYGTVAESENIPFTLPEVATNKTYSFLIYTEVDIGELLMMKLKWKNDSYFRWSDWWSSPSFVIEKIRVKAGETQKKVIFCAREKVSHLQKGKDAAVFVKCHDKSLKKSG
Protein: Response regulator protein PmrA (Q9HV32)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Member of the two-component regulatory system PmrA/PmrB that plays a role in the regulation of resistance towards polymyxin B and cationic antimicrobial peptides in response to limiting concentrations of Mg(2+). Functions as a transcriptional activator by direct binding to a cis-acting sequence upstream of the target gene promoters including lipase lipA and pmrH promoters. Autoregulates also its own pmrAB operon under Mg(2+)-limiting conditions.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor protein kinase PmrB
- DUF155 domain-containing protein
- UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase aminotransferase)
- Polyamine aminopropyltransferase 2
- Two-component sensor PhoQ
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- histidine kinase
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
- UDP-3-O-acylglucosamine N-acyltransferase
Sequence:
MRILLAEDDLLLGDGIRAGLRLEGDTVEWVTDGVAAENALVTDEFDLLVLDIGLPRRSGLDILRNLRHQGLLTPVLLLTARDKVADRVAGLDSGADDYLTKPFDLDELQARVRALTRRTTGRALPQLVHGELRLDPATHQVTLSGQAVELAPREYALLRLLLENSGKVLSRNQLEQSLYGWSGDVESNAIEVHVHHLRRKLGNQLIRTVRGIGYGIDQPAP
Protein: EPN3 protein (Epsin 3) (I6L9I8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGIGIGSGQLGFSRRYGEDYSRSRGSPSSYNSSSSSPRYTSDLEQARPQTSGEEELQLQLALAMSREEAEKPVPPASHRDEDLQLQLALRLSRQEHEKEVRSWQGDGSPMANGAGAVVHHQRDREPEREERKEEEKLKTSQAPPTSEPRLPLPSTVLHPGLG
Protein: Nuclear polyadenylated RNA-binding protein 4 (Cleavage factor IB) (CFIB) (Heterogeneous nuclear ribonucleoprotein 1) (Q99383)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding protein, which is involved in the polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor CFIA complex and the cleavage and polyadenylation factor (CPF) complex. May be involved in regulation of poly(A) site selection. Is involved in nonsense-mediated mRNA decay. Seems to bind to an RNA downstream sequence element (DSE) located 3' of a nonsense codon and may mark the transcript for decay.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9334319, ECO:0000269|PubMed:9499403}. Nucleus {ECO:0000269|PubMed:23222640, ECO:0000269|PubMed:9334319, ECO:0000269|PubMed:9499403}. Cytoplasm, Stress granule {ECO:0000269|PubMed:18981231}.
Interaction partners:
- mRNA 3'-end-processing protein RNA15
- Nuclear polyadenylated RNA-binding protein NAB2
- mRNA 3'-end-processing protein RNA14
- Protein PCF11
- mRNA cleavage and polyadenylation factor CLP1
- Poly
- Endoribonuclease YSH1
- mRNA 3'-end-processing protein YTH1
- Protein CFT1
- Importin subunit beta-2
Sequence:
MSSDEEDFNDIYGDDKPTTTEEVKKEEEQNKAGSGTSQLDQLAALQALSSSLNKLNNPNSNNSSSNNSNQDTSSSKQDGTANDKEGSNEDTKNEKKQESATSANANANASSAGPSGLPWEQLQQTMSQFQQPSSQSPPQQQVTQTKEERSKADLSKESCKMFIGGLNWDTTEDNLREYFGKYGTVTDLKIMKDPATGRSRGFGFLSFEKPSSVDEVVKTQHILDGKVIDPKRAIPRDEQDKTGKIFVGGIGPDVRPKEFEEFFSQWGTIIDAQLMLDKDTGQSRGFGFVTYDSADAVDRVCQNKFIDFKDRKIEIKRAEPRHMQQKSSNNGGNNGGNNMNRRGGNFGNQGDFNQMYQNPMMGGYNPMMNPQAMTDYYQKMQEYYQQMQKQTGMDYTQMYQQQMQQMAMMMPGFAMPPNAMTLNQPQQDSNATQGSPAPSDSDNNKSNDVQTIGNTSNTDSGSPPLNLPNGPKGPSQYNDDHNSGYGYNRDRGDRDRNDRDRDYNHRSGGNHRRNGRGGRGGYNRRNNGYHPYNR
Protein: tRNA (guanine(9)-N(1))-methyltransferase (EC 2.1.1.221) (X6REK4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSEMLPAFIETSNVDKKQGINEDQEESQKPRLGEGCEPISKRQMKKLIKQKQWEEQRELRKQKRKEKRKRKKLERQCQMEPNSDGHDRKRVRRDVVHSTLRLIIDCSFDHLMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTSHGGQLKKNMDENDKGWVNWKDIHIKPEHYSELIKKEDLIYLTSDSPNILKELDESKAYVI
Protein: Octaprenyl pyrophosphate synthase (EC 2.5.1.32, EC 2.5.1.90) (O96130)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Bifunctional farnesyl/geranylgeranyl diphosphate synthase
- 4-hydroxybenzoate polyprenyltransferase, putative
- Alkyl transferase
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- NADH-cytochrome b5 reductase, putative
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MVHLSKRNNIKSFLNYCKAKYLNPLLINKNEDIIKETSILKNNNLYSRKESNVFIEILKSSFIKFRGQKINEEINNHNNIINNSSHNNNHNIYHDTNKKKKQQYEEKHNVFHTENMHKEVLLCMDVLQYEEDKVNRELHLLHSYFNKERTNIDPYTLCESKIKNIDEYIYNIIKTNYKNIDEFITYIYLYKGKRFRVILSILLKNILHHIDNVSKIKTNFKNRNIQRKFFKSNKLTSNYLSNKLKLYNLKITQKKNICEKTVLDNQCKIIAASEIIHMGSLLHDDVIDDSNKRRGVIALHKKFGNKISILSGDYLLARASSIFAGTGSPKICRSFSYVVESLIKGEFLQRNLKFNNVEEALKMYLIKSYHKTASLFSHLFACIAILSFKNDTIIQLCFNLGLHIGMAFQLYDDYLDYKIDDNTNKPILNDLKNNIKTAPLLFSYNYNPQVILQLINKNSYTNNDIENILYYIQHSNSMKKNELCSLLHIKKASDILYSLISHCNKPSTNKNNTKHDDIKQSSEALINLILNVLSRNVK
Protein: Transforming growth factor beta-1 (O02730)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
ALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
Protein: Kelch-like protein 6 (Q8WZ60)
Organism: Homo sapiens (Human)
Function: Involved in B-lymphocyte antigen receptor signaling and germinal center formation.
Interaction partners:
- Cullin-3
- Roquin-2
Sequence:
MLMAGQRGAWTMGDVVEKSLEGPLAPSTDEPSQKTGDLVEILNGEKVKFDDAGLSLILQNGLETLRMENALTDVILCVDIQEFSCHRVVLAAASNYFRAMFCNDLKEKYEKRIIIKGVDAETMHTLLDYTYTSKALITKQNVQRVLEAANLFQFLRMVDACASFLTEALNPENCVGILRLADTHSLDSLKKQVQSYIIQNFVQILNSEEFLDLPVDTLHHILKSDDLYVTEEAQVFETVMSWVRHKPSERLCLLPYVLENVRLPLLDPWYFVETVEADPLIRQCPEVFPLLQEARMYHLSGNEIISERTKPRMHEFQSEVFMIIGGCTKDERFVAEVTCLDPLRRSRLEVAKLPLTEHELESENKKWVEFACVTLKNEVYISGGKETQHDVWKYNSSINKWIQIEYLNIGRWRHKMVVLGGKVYVIGGFDGLQRINNVETYDPFHNCWSEAAPLLVHVSSFAATSHKKKLYVIGGGPNGKLATDKTQCYDPSTNKWSLKAAMPVEAKCINAVSFRDRIYVVGGAMRALYAYSPLEDSWCLVTQLSHERASCGIAPCNNRLYITGGRDEKNEVIATVLCWDPEAQKLTEECVLPRGVSHHGSVTIRKSYTHIRRIVPGAVSV
Protein: Beta-amyrin 28-monooxygenase (EC 1.14.14.126) (Beta-amyrin 28-oxidase) (Cytochrome P450 716A46) (K4CEE8)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Catalyzes the carboxylation of beta-amyrin at the C-28 position to form oleanolate. Catalyzes the carboxylation of alpha-amyrin at the C-28 position to form ursolate.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MELFYASLVCLFVLLLSLSFLFLFNKKNKSMILSCPLPPGNSGWPVIGETLEFLSTGWKGHPEKFIFDRISKYKSSIFKTHLLGEKAVVFCGASSNKFLFSNENKLVQTWWPSSVDKVFPSSTQTSSKEEAIKMRKMLPNFLKPEALQRYIRIMDHIAQKHFQSWENQQEVVVFPLAKRYTFWLACRLFVSVEDPNHVARLADPFDVLASGLISIPINLPGTPFNRAIKASNFIRKELVAIIKQRKIDLTEGKASDSQDILSHMLLTSDENGKFMHELDIADKILGLLIGGHDTASSACAFIVKYLAELPEIYDQVYKEQIEIAKSKGPGELLSWEDIKKMKYSWNVACEVLRLAPPLQGAFREALVDFTFNGFSIPKGWKIYWSANSTHINPEVFVDPLKFDPSRFEGNGPAPYTFVPFGGGPRMCPGKEYARLEILVFMHHLVKRFSWKKIIRDEKIVVNPMPIPANGLPIRLYPHHVKT
Protein: Putative pentatricopeptide repeat-containing protein At1g13800 (Q9LMH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MRVFPIPLLSHVRGLIRQGPSSRFYVVPALARTNLTISHSEQVKEGTFDYKALELNDIGVLRVLNSMKDDPYLALSFLKRIEGNVTLPSVQAYATVIRIVCGWGLDKKLDTFLFELVRRGDEGRGFSVMDLLKAIGEMEQSLVLLIRVSTALVKAYANLDMFDEAIDIFFRAYYSLGRAPDIKALNFLISRMIASGRSDMVVGFFWEIERLGLDADAHTYVLVVQALWRNDDKEELEKLLSRLLISETRNPCVFYLNFIEGLCLNQMTDIAYFLLQPLRDANILVDKSDLGIAYRKVVRGLCYEMRIEDAESVVLDMEKHGIDPDVYVYSAIIEGHRKNMNIPKAVDVFNKMLKKRKRINCVIVSSILQCYCQMGNFSEAYDLFKEFRETNISLDRVCYNVAFDALGKLGKVEEAIELFREMTGKGIAPDVINYTTLIGGCCLQGKCSDAFDLMIEMDGTGKTPDIVIYNVLAGGLATNGLAQEAFETLKMMENRGVKPTYVTHNMVIEGLIDAGELDKAEAFYESLEHKSRENDASMVKGFCAAGCLDHAFERFIRLEFPLPKSVYFTLFTSLCAEKDYISKAQDLLDRMWKLGVEPEKSMYGKLIGAWCRVNNVRKAREFFEILVTKKIVPDLFTYTIMINTYCRLNEPKQAYALFEDMKRRDVKPDVVTYSVLLNSDPELDMKREMEAFDVIPDVVYYTIMINRYCHLNDLKKVYALFKDMKRREIVPDVVTYTVLLKNKPERNLSREMKAFDVKPDVFYYTVLIDWQCKIGDLGEAKRIFDQMIESGVDPDAAPYTALIACCCKMGYLKEAKMIFDRMIESGVKPDVVPYTALIAGCCRNGFVLKAVKLVKEMLEKGIKPTKASLSAVHYAKLKAKGLR
Protein: Protein AimP [Cleaved into: Arbitrium peptide] (P0DOE2)
Organism: Bacillus phage phi3T (Bacteriophage phi-3T)
Function: Part of the latency-replication switch system which decides at the onset of infection whether to replicate and lyse the host or to lysogenize (latency) and keep the host viable.
Subcellular location: [Arbitrium peptide]: Secreted {ECO:0000269|PubMed:28099413}.
Interaction partners:
Sequence:
MKKVFFGLVILTALAISFVAGQQSVSTASASDEVTVASAIRGA
Protein: C-type lectin domain family 1 member B (C-type lectin-like receptor 2) (CLEC-2) (Q9P126)
Organism: Homo sapiens (Human)
Function: C-type lectin-like receptor that functions as a platelet receptor for the lymphatic endothelial marker, PDPN. After ligand activation, signals via sequential activation of SRC and SYK tyrosine kinases leading to activation of PLCG2.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Podoplanin
- Tyrosine-protein kinase SYK
- Platelet glycoprotein VI
- von Willebrand factor
- Killer cell lectin-like receptor subfamily F member 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Lymphocyte cytosolic protein 2
- NKG2-F type II integral membrane protein
- P-selectin
- Platelet glycoprotein Ib alpha chain
Sequence:
MQDEDGYITLNIKTRKPALISVGSASSSWWRVMALILLILCVGMVVGLVALGIWSVMQRNYLQGENENRTGTLQQLAKRFCQYVVKQSELKGTFKGHKCSPCDTNWRYYGDSCYGFFRHNLTWEESKQYCTDMNATLLKIDNRNIVEYIKARTHLIRWVGLSRQKSNEVWKWEDGSVISENMFEFLEDGKGNMNCAYFHNGKMHPTFCENKHYLMCERKAGMTKVDQLP
Protein: Cylicin-2 (Cylicin II) (Multiple-band polypeptide II) (Q14093)
Organism: Homo sapiens (Human)
Function: Possible architectural role during spermatogenesis. May be involved in spermatid differentiation.
Subcellular location: Cytoplasm, cytoskeleton, perinuclear theca, calyx {ECO:0000250|UniProtKB:A0A571BEE2}. Cytoplasm, cytoskeleton, perinuclear theca {ECO:0000250|UniProtKB:A0A571BEE2}. Note=Localizes to the subacrosomal layer of the perinuclear theca in round and elongating spermatids. Localizes to the calyx, also known as post-acrosomal region, in spermatozoa. {ECO:0000250|UniProtKB:A0A571BEE2}.
Interaction partners:
- Calicin
Sequence:
MSLPRFQRVNFGPYDNYIPVSELSKKSWNQQHFALLFPKPQRPGTKRRSKPSQIRDNTVSIIDEEQLRGDRRQPLWMYRSLMRISERPSVYLAARRQPLKPTRTVEVDSKAAEIGKKGEDKTTQKDTTDSESELKQGKKDSKKGKDIEKGKEEKLDAKKDSKKGKKDAEKGKDSATESEDEKGGAKKDNKKDKKDSNKGKDSATESEGEKGGTEKDSKKGKKDSKKGKDSAIELQAVKADEKKDEDGKKDANKGDESKDAKKDAKEIKKGKKDKKKPSSTDSDSKDDVKKESKKDATKDAKKVAKKDTEKESADSKKDAKKNAKKDAKKDAKKNAKKDEKKDAKKKGK
Protein: Protein FAM90A1 (Q86YD7)
Organism: Homo sapiens (Human)
Interaction partners:
- Ret finger protein-like 4A
- Bromodomain-containing protein 3
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
Sequence:
MMARRDPKPGAKRLVRAQTLQKQRRAPVGPRAPPPDEEDPRLKCKNCEAFGHTARSTRCPMKCWKAALVPPNFGEKEGKENLKPWKPQVEANPGPLNKDKGEKEERPRPQDPQRKALLHIFSRKPPEKPLPNQKGSTESSDYLRVASGPMPVHTTSKRPRVDPVLSDRSATEMSDRGSVLASLSPLRKASLSSSSSLGPKERQTGAAADIPQTAVRHQGPEPLLVVKPTHSSPAGGCREVPQAASKTHGLLQAVSPQAQDKRPAVTSQPCPPAATHSLGLGSNLSFGPGAKRSAPAPIQACLNFPKKPRLGPFQIPESAIQGGELGAPENLQPPPAATELGPRTSPQTGTRTPAQVLSGDRQPPHSRPCLPTAQACTMSHHPAASHDGAQPLRVLFRRLENGRWSSSLLTAPSFHSPEKPGAFLAQSPHVSEKSEGPCVRVPPSVLYEDLQVPSSSEDSDSDLE
Protein: IKAROS family zinc finger 2 (Lymphoid transcription factor) (Q90W82)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEAEAADGYITSGDNELSPEREHSSMAIDLTSSTPNGQHTSPSHVASTNSVKVEMQSDEESDRKTFCQEDEVRVLDEGSSLEEPLTENNEMADNRKIQELSSEGGIRLPNGKLKCDVCGMVCIGPNVLMVHKRSHTGERPFHCNQCGASFTQKGNLLRHIKLHSGEKPFKCPFCSYACRRRDALTGHLRTHSVPGIEMALQEEIPVQRKPLNYSSELLYMSQDLLPSTMGKPHKCNYCGRSYKQRSSLEEHKERCHNYMQNVGMEAAGQVLSHHVPPMEDCKEQEPVMDNNIPMVPFERPAVIEKLTSNLGKRKSSTPQKFVGEKLMRLGYPDIHFDMNLSYEKESELIQSQMMDQAIHNAIAYLGADSLHPLMQHTPSTIAEVAPVSSSPYAQVYHPNRIERPISRETADSHENNMDGPISLIRPKSRTQDREGSPSNSCLDSTDSESSHEDRQSYQGNSALNPKRKPSPAYMKEDAKALDATKASKGSLKDIYKVINGEGEQIRAFKCEHCRVLFLDHVMYTIHMGCHGYRDPLECNICGYRSQDRYEFSSHIVRGEHTFH
Protein: B box and SPRY domain-containing protein (Q80YW5)
Organism: Mus musculus (Mouse)
Function: May regulate epithelial calcium transport by inhibiting TRPV5 activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16380433}. Membrane {ECO:0000269|PubMed:16380433}; Peripheral membrane protein {ECO:0000269|PubMed:16380433}. Note=Apical domain of kidney distal tubular cells.
Interaction partners:
Sequence:
MSADVSGTESGSESGPEPEPGPEPGPESRPESRPKPGPGPEPRPESGPEPGPRSGLRRGPKQGSERSQLCPEHFEPLSWFCLSERRPVCATCAGFGGRCHRHRIRRAEEHAEELRNKIVDQCERLQLQSAGISKYMAEVLQGKNQKAVVMASAARDLIIQRLSLVRSLCESEEQRLLEQVHGEEERAHQSILTQRAHWVDAVQKLDTLRTNMVDMITHLDDLQLIQREQEIFERAEEAEGILDPQDSEKLSFNEKCAWSPLLTQLWAASVLGSLSGVEEVLIDERTVSPLLHLSEDRRTLTFIAKKSKVCSDEPERFDHWPNALAATAFQTGLHAWIVNVKHSCAYKVGVASDQLPRKGSGNDCRLGHNAFSWVFSRYDQEFCFSHNGYHEPLPLLRCPAQLGMLLDLQAGELVFYEPASGTVLHIHRASFPQVLFPVFAVADQLISIVRGPLATVRLDSPPHHPCRSGHASR