wanglab/gogpt-training-data huggingface dataset:
Protein: Lectin 10 (MtLec10) (Agglutinin LEC10) (A9YWS7)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MALSNLKSNRTLSSSLITIFIISLFLQYHNIKSQSSWQSRQVPRSETVAFSITEFEKENPDIFLRGDTSISDGILRLTKTDQSGKPLPNTVGRATYLTPIHIWDKTSGELADFSTSFSFIVNTNDSDLHGDGFAFYLGPLHFDVPKNSSGGYLGLFDPENAFPPSKTPILAIEFDGFTNEWDPPSSFQSPHIGIDVGSIVSLEYAQWPINFVPRNALGEANINYNSESKRLSVFVAYPGTQWNSTRVSVVVDLRSVLPEWVRIGFSATTGELVETHDIINWSFESAL
Protein: Angio-associated migratory cell protein (Q13685)
Organism: Homo sapiens (Human)
Function: Plays a role in angiogenesis and cell migration. In smooth muscle cell migration, may act through the RhoA pathway.
Subcellular location: Cell membrane. Cytoplasm.
Interaction partners:
- Large ribosomal subunit protein uL16
- Nucleotide-binding oligomerization domain-containing protein 2
- Epidermal growth factor receptor
- Thromboxane A2 receptor
- Ribosomal protein uL16-like
- Glutamate-rich WD repeat-containing protein 1
- Apoptosis-enhancing nuclease
- mRNA turnover protein 4 homolog
- 60S ribosomal export protein NMD3
- Transducin beta-like protein 3
Sequence:
MESESESGAAADTPPLETLSFHGDEEIIEVVELDPGPPDPDDLAQEMEDVDFEEEEEEEGNEEGWVLEPQEGVVGSMEGPDDSEVTFALHSASVFCVSLDPKTNTLAVTGGEDDKAFVWRLSDGELLFECAGHKDSVTCAGFSHDSTLVATGDMSGLLKVWQVDTKEEVWSFEAGDLEWMEWHPRAPVLLAGTADGNTWMWKVPNGDCKTFQGPNCPATCGRVLPDGKRAVVGYEDGTIRIWDLKQGSPIHVLKGTEGHQGPLTCVAANQDGSLILTGSVDCQAKLVSATTGKVVGVFRPETVASQPSLGEGEESESNSVESLGFCSVMPLAAVGYLDGTLAIYDLATQTLRHQCQHQSGIVQLLWEAGTAVVYTCSLDGIVRLWDARTGRLLTDYRGHTAEILDFALSKDASLVVTTSGDHKAKVFCVQRPDR
Protein: Alginate biosynthesis protein AlgX (Probable alginate O-acetyltransferase AlgX) (EC 2.3.1.-) (Q51372)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Plays two roles in the biosynthesis of the exopolysaccharide alginate: protects alginate from degradation as the polymer traverses the periplasm, and also plays a role in its O-acetylation. Acetylation of alginate causes the cells in the biofilm to adhere better to lung epithelium, form microcolonies, and resist the effects of the host immune system and/or antibiotics. Displays a low acetylesterase activity in vitro using a pseudosubstrate, 3-carboxyumbelliferyl acetate. Probably has acetyltransferase activity in vivo.
Subcellular location: Periplasm {ECO:0000269|PubMed:15489449, ECO:0000269|PubMed:16376476}.
Interaction partners:
- Alginate lyase
- Mannuronan C5-epimerase
- Alginate biosynthesis protein AlgK
- Mannuronan synthase
- Alginate production protein AlgE
- Mannuronan synthase
- Probable alginate O-acetylase AlgI
- GDP-mannose 6-dehydrogenase
- Alginate biosynthesis protein AlgF
- Alginate biosynthesis protein AlgA
Sequence:
MKTRTSRLFRLSALAAGLCLAQAALAADPGAAPSYQALPAGNLCPAAAYDSRYNTKYLGFFTHLVQAQDDWLFRTTYDLRTDFGTSAEGWRELRALRDELKRKGIELVVVYQPTRGLVNREKLSPAEKAGFDYELAKKNYLATIARFRQAGIWTPDFSPLFDEKEEHAYYFKGDHHWTPHGARRSAKIVAETLKQVPGFEEIPKKQFESKRVGLLSKLGTFHKAAAQLCGNSYATQYVDRFETEPVGASDSGDLFGDGGNPQIALVGTSNSGPAYNFAGFLEEFSGADILNNAVSGGGFDSSLLAYMTSEEFHKNPPKILIWEFATHYDMAQKSFYRQAMPLVDNGCSGRKTVLSRKVKLRQGRNEVLLNSAALPIRSGSYVADVTYSDPSVHELKNTIWYMNGRREQLKIEQSKAVDTGGRYVFQLRNDSDWADQQFLSLEIEAPEDMPQGLEVQASICQAAPAKASQSVAGR
Protein: Uroporphyrinogen decarboxylase (UPD) (URO-D) (EC 4.1.1.37) (P29680)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00218}.
Interaction partners:
- Porphobilinogen deaminase
- Oxygen-dependent coproporphyrinogen-III oxidase
- Uroporphyrinogen-III synthase
- Ferrochelatase
- Oxygen-independent coproporphyrinogen III oxidase
- Delta-aminolevulinic acid dehydratase
- Glutamyl-tRNA reductase
- Endonuclease V
- Siroheme synthase
- Glutamate-1-semialdehyde 2,1-aminomutase
Sequence:
MTELKNDRYLRALLRQPVDVTPVWMMRQAGRYLPEYKATRAQAGDFMSLCKNAELACEVTLQPLRRYPLDAAILFSDILTVPDAMGLGLYFEAGEGPRFTSPVTCKADVDKLPIPDPEDELGYVMNAVRTIRRELKGEVPLIGFSGSPWTLATYMVEGGSSKAFTVIKKMMYADPQALHALLDKLAKSVTLYLNAQIKAGAQAVMIFDTWGGVLTGRDYQQFSLYYMHKIVDGLLRENDGRRVPVTLFTKGGGQWLEAMAETGCDALGLDWTTDIADARRRVGNKVALQGNMDPSMLYAPPARIEEEVATILAGFGHGEGHVFNLGHGIHQDVPPEHAGVFVEAVHRLSEQYHR
Protein: Elongation factor for RNA polymerase II 3 (C9JHD8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRILEESAERRWRWWPSPVAPVLLALELVAMEELQEPLRGQLRLCFTQAARTSLLLLRLNDAALRALQECQRQQVRPVIAFQGHRGYLRLPGPGWSCLFSFIVSQCCQEGAGGSLDLVCQRFLRSGPNSLHCLGSLRERLIIWAAMDSIPAPSSVQGHNLTEDARHPESWQNTGGYSEGDAVSQPQMALEEVSVSDPLASNQGQSL
Protein: DNA polymerase zeta catalytic subunit (EC 2.7.7.7) (Protein reversionless 3-like) (AtREV3) (Q766Z3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of the error prone DNA polymerase zeta. Involved in damage-tolerance mechanisms through translesion DNA synthesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA polymerase delta small subunit
- DNA polymerase eta
- DNA polymerase zeta processivity subunit
- DNA repair protein REV1
- DNA polymerase alpha subunit B
- DNA polymerase epsilon subunit B
- Probable DNA primase large subunit
- DNA primase
- DNA polymerase II subunit B4
- Proliferating cell nuclear antigen 2
Sequence:
MADSQSGSNVFSLRIVSIDYYMASPIPGYNICYSSFQGSEVNEVPVIRIYGSTPAGQKTCLHIHRALPYLYIPCSEIPLEHHKGVDGSTLALSLELEKALKLKGNAASKRQHIHDCEIVRAKKFYGYHSTEEAFVKIYLSYHPPDVARAASLLLAGAVLGKSLQPYESHIPFILQFLVDYNLYGMGHVHISKMKFRSPVPHHFRPRRFDLDDCPGQRIDEVAITKANSSAAASVSFPVWSLSTIPGQWMWNLSEESDTPLSQSQHRHQHHYRRQSLCELEGDATSSDILNQQFKMYNSLSQAQSDTNMVQSLVAIWEEEYERTGVHDAPIPPDPGKPSAADVLQTMSDYVGFGNMLKEMLNKVELSPPGMKPTAVSSAGPDMHAKPEITDLQALNHMVGTCSEFPASEQLSPLGEKSEEASMENDEYMKTPTDRDTPAQIQDAEALGLFKWFASSQAAEDINSDDEILRETILSPLLPLASINKVLEMASTDYVSQSQKECQDILDSQENLPDFGSSTKRALPSNPDSQNLRTSSDKQSLEIEVASDVPDSSTSNGASENSFRRYRKSDLHTSEVMEYKNRSFSKSNKPSNSVWGPLPFTLTKNLQKDFDSTNASDKLGLTKISSYPMNEMTDNYIVPVKEHQADVCNTIDRNVLAGCSLRDLMRKKRLCHGESPVSQHMKSRKVRDSRHGEKNECTLRCEAKKQGPALSAEFSEFVCGDTPNLSPIDSGNCECNISTESSELHSVDRCSAKETASQNSDEVLRNLSSTTVPFGKDPQTVESGTLVSSNIHVGIEIDSVQKSGREQESTANETDETGRLICLTLSKKPPSLDCLSAGLQDSAHSHEIHAREKQHDEYEGNSNDIPFFPLEDNKEEKKHFFQGTSLGIPLHHLNDGSNLYLLTPAFSPPSVDSVLQWISNDKGDSNIDSEKQPLRDNHNDRGASFTDLASASNVVSVSEHVEQHNNLFVNSESNAYTESEIDLKPKGTFLNLNLQASVSQELSQISGPDGKSGPTPLSQMGFRDPASMGAGQQLTILSIEVHAESRGDLRPDPRFDSVNVIALVVQNDDSFVAEVFVLLFSPDSIDQRNVDGLSGCKLSVFLEERQLFRYFIETLCKWDPDVLLGWDIQGGSIGFLAERAAQLGIRFLNNISRTPSPTTTNNSDNKRKLGNNLLPDPLVANPAQVEEVVIEDEWGRTHASGVHVGGRIVLNAWRLIRGEVKLNMYTIEAVSEAVLRQKVPSIPYKVLTEWFSSGPAGARYRCIEYVIRRANLNLEIMSQLDMINRTSELARVFGIDFFSVLSRGSQYRVESMLLRLAHTQNYLAISPGNQQVASQPAMECVPLVMEPESAFYDDPVIVLDFQSLYPSMIIAYNLCFSTCLGKLAHLKMNTLGVSSYSLDLDVLQDLNQILQTPNSVMYVPPEVRRGILPRLLEEILSTRIMVKKAMKKLTPSEAVLHRIFNARQLALKLIANVTYGYTAAGFSGRMPCAELADSIVQCGRSTLEKAISFVNANDNWNARVVYGDTDSMFVLLKGRTVKEAFVVGQEIASAITEMNPHPVTLKMEKVYHPCFLLTKKRYVGYSYESPNQREPIFDAKGIETVRRDTCEAVAKTMEQSLRLFFEQKNISKVKSYLYRQWKRILSGRVSLQDFIFAKEVRLGTYSTRDSSLLPPAAIVATKSMKADPRTEPRYAERVPYVVIHGEPGARLVDMVVDPLVLLDVDTPYRLNDLYYINKQIIPALQRVFGLVGADLNQWFLEMPRLTRSSLGQRPLNSKNSHKTRIDYFYLSKHCILCGEVVQESAQLCNRCLQNKSAAAATIVWKTSKLEREMQHLATICRHCGGGDWVVQSGVKCNSLACSVFYERRKVQKELRGLSSIATESELYPKCMAEWF
Protein: Glucagon receptor (GL-R) (Q61606)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12552113}; Multi-pass membrane protein {ECO:0000269|PubMed:12552113}. Note=Is rapidly internalized after ligand-binding. {ECO:0000250|UniProtKB:P47871}.
Interaction partners:
- Pro-glucagon
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Gastric inhibitory polypeptide
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Insulin-2
- Guanine nucleotide-binding protein G
- Dipeptidyl peptidase 4
- Guanine nucleotide-binding protein subunit beta-4
Sequence:
MPLTQLHCPHLLLLLLVLSCLPEAPSAQVMDFLFEKWKLYSDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPPNTTANISCPWYLPWYHKVQHRLVFKRCGPDGQWVRGPRGQPWRNASQCQLDDEEIEVQKGVAKMYSSQQVMYTVGYSLSLGALLLALVILLGLRKLHCTRNYIHGNLFASFVLKAGSVLVIDWLLKTRYSQKIGDDLSVSVWLSDGAMAGCRVATVIMQYGIIANYCWLLVEGVYLYSLLSLATFSERSFFSLYLGIGWGAPLLFVIPWVVVKCLFENVQCWTSNDNMGFWWILRIPVFLALLINFFIFVHIIHLLVAKLRAHQMHYADYKFRLARSTLTLIPLLGVHEVVFAFVTDEHAQGTLRSTKLFFDLFLSSFQGLLVAVLYCFLNKEVQAELMRRWRQWQEGKALQEERLASSHGSHMAPAGPCHGDPCEKLQLMSAGSSSGTGCVPSMETSLASSLPRLADSPT
Protein: Phosphatidylinositol 4-kinase beta 2 (PI4-kinase beta 2) (PtdIns-4-kinase beta 2) (EC 2.7.1.67) (Phosphatidylinositol 4-OH kinase beta2) (AtPI4Kbeta2) (PI-4Kbeta2) (Q0WPX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5-trisphosphate (By similarity). Necessary for proper organization of the trans-Golgi network (TGN) and post-Golgi secretion in root hairs. Together with PI4KB1, required during polarized root hair expansion and pollen tube elongation. Functions redundantly with PI4KB1 upstream of the cold response phosphoinositide-dependent phospholipase C (PI-PLC) pathway.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FMJ0}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9FMJ0}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9FMJ0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9FMJ0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9FMJ0}. Note=Associated to tip-localized membranes in growing root hairs. {ECO:0000250|UniProtKB:Q9FMJ0}.
Interaction partners:
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Phosphatidylinositol 4-kinase alpha 1
- Phosphoinositide phosphatase SAC7
- Phosphatidylinositol 4-kinase alpha 2
- Phosphatidylinositol 4-phosphate 5-kinase 2
- Phosphoinositide phosphatase SAC8
- Phosphoinositide phosphatase SAC6
- Phosphatidylinositol 4-phosphate 5-kinase 3
- 1-phosphatidylinositol-3-phosphate 5-kinase FAB1B
Sequence:
MQMAQFLSLVRGDSIESPREITSPSNLISESGSNGWLIRFFDSSFFCEWIAVSYLYKHQHSGVRDYLCNRMYTLPLSGIESYLFQICYLMVHKPSPSLDKFVIDICAKSLKIALKVHWFLLAELEDSDDNEGISRIQEKCQIAATLVGEWSPLMRPHNEPSTPGSKVLNKFLSSKQKLFSLTLSPPTQKSLLFSPTSGSNLQDDGSQLSADDNKIFKRLIPSPKVRDALLFRKSADKEDEECEKDGFFKRLLRDSRGEDDEQRSNSEGFFKRLLKDNKSEEEEISNNSEGFFKRLRSSKGDEEELTSSSDGFFKRLLRDNKGDEEELGANSEGFFKKLLRDSKNEDEEPNANTEGFFKKLFHESKNEDDKVSNAVDDEEKDGFLKKLFKEKFDEKRNGNERNETDETVYTDETSGEDNGREGFFKKLFKEKFEDKPNIGKADDGNESEDDESSEFSLFRRLFRRHPEDVKTTLPSENCSNGGFVESSPGTENFFRKLFRDRDRSVEDSELFGSKKYKEKCPGSPKPQNNTPSKKPPLPNNTAAQFRKGSYHESLEFVHALCETSYDLVDIFPIEDRKTALRESIAEINSHLAQAETTGGICFPMGRGVYRVVNIPEDEYVLLNSREKVPYMICVEVLKAETPCGAKTTSTSLKLSKGGIPLANGDAFLHKPPPWAYPLSTAQEVYRNSADRMSLSTVEAIDQAMTHKSEVKLVNACLSVETHSNSNTKSVSSGVTGVLRTGLESDLEWVRLVLTADPGLRMESITDPKTPRRKEHRRVSSIVAYEEVRAAAAKGEAPPGLPLKGAGQDSSDAQPMANGGMLKAGDALSGEFWEGKRLRIRKDSIYGNLPGWDLRSIIVKSGDDCRQEHLAVQLISHFFDIFQEAGLPLWLRPYEVLVTSSYTALIETIPDTASIHSIKSRYPNITSLRDFFDAKFKENSPSFKLAQRNFVESMAGYSLVCYLLQIKDRHNGNLLMDEEGHIIHIDFGFMLSNSPGGVNFESAPFKLTRELLEVMDSDAEGLPSEFFDYFKVLCIQGFLTCRKHAERIILLVEMLQDSGFPCFKGGPRTIQNLRKRFHLSLTEEQCVSLVLSLISSSLDAWRTRQYDYYQRVLNGIR
Protein: Neuregulin 1 (Pro-neuregulin-1, membrane-bound isoform isoform X5) (A0A0R4IFE6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKSEAAEDISAGLASQETPSDALSEVATKETPEEAGENVPGDGDSSERGPLGCVPLPAVACCCVCLELERVNNCVRSEKICILPILACLLSLALCTAGLKWVFVDKIFEYEPPTHLDLKRIGQDPIINSDFTQNPVSVSPSSVTLSVPGQPKVFVEGDTTAGPFEVPPSKVAGFTPTAAVTVHPNSVSPPSPKSTFRPVQNDTANQLPTLESNEIIPKTSATSTTPSAKTSSHVTPCNESEKEYCVNHGKCFTLEVTPGNIRRLCRCPPGFTGNRCQNRDPVRVVDHKQAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRKKLHDRLRQSLRERNAAAKGPQHPHPPPENLQLVNHYMPTNPVPAHMTDKEAETSLSTNEFTSPTHPSTAITHSSSQCWSNGKAESVVSDSHAVLMKPSAENCQHGTPSHRGRLNATGGVHQLNDYLKNSREAQGSNRDSPYSERYVSAMTTPTRLSPVGLLSPVTPSSPPSEMSAPLSSLATSVPSMLTSPSGEEERPLLFRTPPILRDKSASTQGRKSGHNLRNSAHYNHGLDIPSPPPSPLHIEEEIDCLEQYKSTSVPSSAPHSPSAARTQPSGQAAPEQAVSGSNSESSSSESETEDERVGEDTPFLGLQNPLAAGSLVLDGLEGSRTNPALHLSPQHELQNRLTAVMANQDPIAV
Protein: ADP-ribosylation factor-related protein 1 (A0A384P5U7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYTLLSGLYKYMFQKDEYCILILGLDNAGKTTFLEQSKTRFNKNYKGMSLSKITTTVGLNIGTVDVGKARLMFWDLGGQEELQSLWDKYYAECHGVIYVIDSTDEERLAESKQAFEKVVTSEALCGVPVLVLANKQDVETCLSIPDIKTAFSDCTSKIGRRDCLTQACSALTGKGVREGIEWMVKCVVRNVHRPPRQRDIT
Protein: Peptidyl-prolyl cis-trans isomerase-like 1 (PPIase) (EC 5.2.1.8) (Rotamase PPIL1) (Q9Y3C6)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as component of the spliceosome. PPIases accelerate the folding of proteins. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Catalyzes prolyl peptide bond isomerization in CDC40/PRP17. Plays an important role in embryonic brain development; this function is independent of its isomerase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
Interaction partners:
- SNW domain-containing protein 1
- Cell division cycle 5-like protein
- Pre-mRNA-processing-splicing factor 8
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-processing factor 17
- Protein BUD31 homolog
- Pre-mRNA-splicing factor SYF2
- RNA helicase aquarius
- Pre-mRNA-splicing factor SPF27
- Pre-mRNA-splicing factor RBM22
Sequence:
MAAIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARRGYYNGTKFHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDRPVDDVKIIKAYPSG
Protein: Methyl-CpG binding domain 4 DNA glycosylase (A0A8I6AH85)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MESPSLGDNNVPSVTAGKSLVSDPPWDRWQVFKPLSGLRGVSLVWVFLTFNTSKEDVAVGLGGVGEDGKDLVISSECGSLLQEPAASTLPSCTTVAECHKPVPCGWERVVKQRLSGKTAGRVDVYFISPQGSKFRSKRSLANYLLKTGETCLKPEDFDFTVLSKGGINPGYKHQSLSAPASQQPNEADISKLNLRTRSKWKTDVLPLPGGNSESPDSNSLSNSNSARLLLKEHKGIQDADSGKSRKPKIKVTVLKGIASQRTKQRCRKSPSDSTGRNRKRLCTVQKADTDSELVPQESRLHRTVCPADACARATVSLVREAKGLGEEKSPSSDLRFTQVTSSITNKLYSTEAAGEATREATREQTFLESEEIRSKGEEEEAHLHIDILQSGSETPSCSQAKKHLTSETFREDSIPRTQVEKRKTSLYFSSKYNKEALSPPRRKAFKKWTPPRSPFNLVQETLFHDPWKLLISTIFLNRTSGKMAIPVLWEFLEKYPSAEVARTADWRDVSELLKPLGLYDLRAKTIIKFSDEYLTKPWRYPIELHGIGKYGNDSYRIFCVNEWKQVHPEDHKLNKYHDWLWENHEKLSLS
Protein: Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin] (P28481)
Organism: Mus musculus (Mouse)
Function: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Collagen alpha-2
- Collagen alpha-1
- CD44 antigen
- Aggrecan core protein
- Platelet glycoprotein VI
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
- Collagen type V alpha 3 chain
- Transcription factor SOX-9
Sequence:
MIRLGAPQSLVLLTLLIAAVLRCQGQDAQEAGSCLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNPEIPFGECCPICPADLATASGKLGPKGQKGEPGDIRDIIGPRGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPAGPPGPPGPPGLSAGNFAAQMAGGYDEKAGGAQMGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPAGKPGDDGEAGKPGKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLTGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLAGAPGLRGLPGKDGETGAAGPPGPSGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKQGDQGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGANGNPGPAGPPGPAGKDGPKGVRGDSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIAGPQGPRGDKGESGEQGERGLKGHRGFTGLQGLPGPPGPSGDQGASGPAGPSGPRGPPGPVGPSGKDGSNGIPGPIGPPGPRGRSGETGPVGPPGSPGPPGPPGPPGPGIDMSAFAGLGQREKGPDPMQYMRADEADSTLRQHDVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPATVPRKNWWSSKSKEKKHIWFGETMNGGFHFSYGDGNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGAEQEFGVDIGPVCFL
Protein: Patatin-like protein 2 (AtPLP2) (EC 3.1.1.-) (Patatin-related phospholipase A IIalpha) (pPLAIIa) (Phospholipase A IIA) (AtPLAIIA) (O48723)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), and less efficiently the phoshpolipids phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidic acid (PA), phosphatidylserine (PS) and phosphatidylinositol (PI). Favors the release of fatty acid at the sn-1 position for PC or PE and the sn-2 position for PG, PA, PS and PI. Negatively affects disease resistance to the necrotic fungal pathogen Botrytis cinerea and the avirulent bacteria Pseudomonas syringae by promoting cell death and reducing the efficiency of the hypersensitive response, respectively. However, PLP2 contributes to resistance to cucumber mosaic virus (CMV), an obligate parasite inducing hypersensitive response. May negatively regulate oxylipin production, possibly via participating in membrane repair that includes removal of oxidatively modified lipids.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12226489, ECO:0000269|PubMed:16297072}.
Interaction partners:
- Patatin
- At3g48450 family protein)
Sequence:
MQMDSPKSPLQPPTYGNLVTILSIDGGGIRGLIPAVILGFLESELQKLDGEEARLADYFDVIAGTSTGGLVTAMLTAPNKEGRPLFAASEIKDFYLEQCPKIFPQDHFPFSAAKKLVKSLTGPKYDGKYLHQLIHAKLGDTKLSQTLTNVVIPTFDIKHLQPTIFSSYEVKNHPLKDATLADIAISTSAAPTYLPAHFFKVEDLNGNAKEYNLIDGGVAANNPALLAIGEVTNEISGGSSDFFPIRPNDYGRFLVLSLGTGNHKAEEKFNAKEVAGWGLLNWLTHDNSTPIIDAFSQASSDMVDFHLSAVFRALHSEANYIRIQDDTLTGDAASVDIATVENLDILAKTGDELLKKPVARVNLDSGCNENAYETTNEHALIKLAGILSKEKKIRDIRSPHAKAPIRI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q7ZVD7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- M-phase inducer phosphatase
- non-specific serine/threonine protein kinase
- ATR serine/threonine kinase
- Checkpoint kinase 2.
- Cellular tumor antigen p53
- CDC45 cell division cycle 45 homolog
- DNA replication licensing factor MCM4
- DNA repair protein RAD51 homolog
- ATR-interacting protein
- Cell cycle checkpoint protein RAD17
Sequence:
MAVPFVKDWDVVQTLGEGAYGEVRLLVNKKTEEAVAVKVVDMAKAKDCIENVKKEVCICKMLSHPNIVRFFGHSVGITHRDIKPENILLDDKDNLKISDFGLATMFRHRGRERALNRLCGTLPYVAPELMSRSSFNAQPADTWACGIVLTAMLAGELPWDQPSENCQEYLDWLERKTYLTPWKKIDAVPLSLLSKILLHNPEDRFTIPEIKKHRWFSRSFKSAVQRQGITPAAKIQRADSELRRKNSDDRAQISSSQPEPQGLWEEKEVTVHTDVSVSFSQPTCPDHMLLGTQLLGTPGASQSPWQRLVRRMTRFFTTENTEASCIALRDSCIALGHTWKQSCNNQATVSTMDRRNNKLIFIVHFLEMEERILVDFRLSKGDGLEFKRIFLKLKQKLSDIISNQKVLPLI
Protein: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (NDUFV1) (EC 7.1.1.2) (Complex I-51kD) (CI-51kD) (NADH dehydrogenase flavoprotein 1) (NADH-ubiquinone oxidoreductase 51 kDa subunit) (P25708)
Organism: Bos taurus (Bovine)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}; Peripheral membrane protein {ECO:0000305|PubMed:25209663}; Matrix side {ECO:0000305|PubMed:25209663}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Cytochrome b-c1 complex subunit 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- NADH-ubiquinone oxidoreductase chain 2
- Cytochrome c1, heme protein, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
Sequence:
MLAARRLLGGSLPARVSVRFSGDTTAPKKTSFGSLKDEDRIFTNLYGRHDWRLKGAQSRGDWYKTKEILLKGPDWILGEVKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEGEPGTCKDREIIRHDPHKLVEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAGLIGKNACGSGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPTTVANVETVAVSPTICRRGGAWFASFGRERNSGTKLFNISGHVNNPCTVEEEMSVPLKELIEKHAGGVTGGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALIQAQTGLGTAAVIVMDRSTDIVKAIARLIEFYKHESCGQCTPCREGVDWMNKVMARFVRGDARPAEIDSLWEISKQIEGHTICALGDGAAWPVQGLIRHFRPELEERMQQFAQQHQARQAAF
Protein: Collagen type II, alpha-1b (Collagen, type II, alpha 1b precursor) (L0S5L0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMKTSMMVRSAELLLCVAALGALLTGGAAQDEEQDPGGCSQDGQLYRDKDVWKPEPCRICVCDSGTVLCDEIVCEELRDCAKPEIPLGECCPVCASADASTPERLPGAKGQKGEPGDITDVVGPRGPSGPMGPPGEQGPRGDRGEKGEKGSPGPRGRDGEPGTPGNPGPPGPPGPNGPPGLGGNFASQMAGGFDDKAGAAQMGVMQGPMGPMGPRGPPGPNGAPGPQGFQGNPGEGGEPGSSGPMGPRGPPGPPGKPGDDGEPGKPGNGGERGPPGPQGARGFPGTPGLPGIKGHRGYTGLDGAKGESGATGAKGESGSPGESGAPGPMGPRGLPGERGRPGPSGASGARGNDGLPGGAGPPGPVGTAGSPGFPGSPGAKGEAGPTGARGPEGAQGPRGESGVPGASGPSGVSGNPGSDGMPGAKGSVGAPGIGGAPGFPGPRGPPGPQGATGPLGPKGQSGDSGLAGFKGEAGPKGEIGNAGLQGAPGPAGEEGKRGPRGEPGAAGPPGPTGERGTPGNRGFPGQDGLAGPKGAPGERGPAGVSGPKGAGGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGVRGQPGVMGFPGPKGGNGEAGKAGEKGLAGAPGLRGLPGKDGETGAAGPPGPAGSAGERGEQGQPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGGAGATGPRGERGFPGERGGAGPQGLQGPRGLPGTPGTDGPKGGVGPAGTAGAQGPPGLQGMPGERGTSGNPGPKGDRGDNGDKGPEGAPGKDGSRGLTGPIGPTGPAGPNGEKGESGPAGPSGVAGTRGVPGDRGETGPPGPAGFAGPPGADGQPGVKGEQGEGGQKGDAGAPGPQGPSGAPGPQGPTGVSGPKGARGAQGPPGATGFPGAAGRVGPPGPNGNPGPAGPAGPPGKDGPKGVRGDGGPPGRPGDAGLRGSAGPAGEKGDPGEDGPHGPDGPAGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGGPGDRGPPGPVGAPGLTGAAGEPGREGNPGSDGPPGRDGSAGIKGDRGDTGPAGAPGAPGGPGAPGPVGPTGKQGDRGEAGPHGPSGPPGPAGARGMPGPQGPRGDKGEGGDSGDRGQKGHRGFTGLQGLPGSPGQPGDQGASGPSGPGGARGPPGPVGPAGKDGANGLPGPIGPPGPRGRSGETGPSGPPGTPGPPGPPGPPGPGIDMSAFAGLSQLEKSPDPLRYMRADQAADGNHQHDAEVDATLKSLNNQMENIRRPDGTKKSPARTCRDLKQCHPDWKSGEYWIDPNQGCTVDAIKVFCNMETGESCIYPKPANIPRKNWWTTKGGDRKHIWFGEAMNGGFHFNYGDENLSPNTASIQMTFLRLLSTEASQNLTYHCRNSIAYMDESSGNLKKALLLRGSNDVEIRAEGNSRFTYSVLEDGCKKHTGQWSKTVIEYKSQKTSRLPLVDIAPVDIGGAHQEFGVDVGAVCFL