wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger, MYND-type containing 8 (A0A0G2K9F7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
CLAEEEIKTEQEVVEGMDISTRSKDPGSTERTAQKRKVPSPPHSSNGHSPQDSSTSPIKKKKKPGLLNSSSKDQDGRNDFYCWVCHREGQVLCCELCPRVYHAKCLRLTSEPEGDWFCPECEKITVAECIETQSKAMTMLTIEQLSYLLKFAIQKMKQPGTDAFQKPVPLEQHPDYAEYIFHPMDLCTLEKNAKKKMYGCTEAFLADAKWILHNCIIYNGGNHKLTQIAKVVIKICEHEMNEIEVCPECYLAACQKRDNWFCEPCSNPHPLVWAKLKGFPFWPAKALRDKDGQVDARFFGQHDRAWVPVNNCYLMSKEIPFSVKKTKSIFNSAMQEMEVYVENIRKKFGVFNYSPFRTPYTPNSQYQMLLDPSNPSAGTAKTDKQEKVKLNFDMTASPKIILSKPLLSGGAGRRISLSDMPRSPTSTNSSVHTGSDVEQDPEKKAPSSHFSASEESMDFLDKSTASPASTKTGQAGSLSGSPKPFSPQAPTPIMTKPDKTSTATTGSILNLNLDRSKAEMDLKELSESVQQQSAPVPLISPKRQIRSRFQLNLDKTIESCKAQLGINEISEDVYTAVEHSDSEDSEKSESSDSEYVSDEEQKPKNEPEDPEDKEGSRVDKEAPAIKRKPKPSNQVEVKEEVKSNSPVGEKVDPAPAKDKASPEPEKDFAEKAKPSPHPTKDKLKGKDETDSPTVHLGLDSDSESELVIDLGEDPSGREGRKNKKEPKVPSPKQDAIGKPPPPTPAGNQSPPETPVLTRSATQAPAAGVTVAATTSTMSTVTVTAPATAAVTGSPVKKQRPLLPKETVPAVQRVVWNASTVQQKEVTQSPSTSTITLVTSTQPAALVSSSGSASTLASVINADLPIATASADVAADIAKYTSKMMDAIKGTMTEIYNDLSKNTTGSTIAEIRRLRIEIEKLQWLHQQELAEMKHNLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETKKKQWCANCKKEAIFYCCWNTSYCDYPCQQAHWPEHMKSCTQSATAPQQEADAEANQETGNKTSQGSSSNTQSAPSEPASTPKEKETSSSSSNSSSTEKSKDSNSTLDLSGSRETPSSILLGSNQGSVSKRYDKQPAYTPTTTDHQPHPNYPAQKYHSRSSKAGLWSSSEEKRGSSRSEHSAGTSTKNLMPKESRESRLDTFWD
Protein: Aldehyde dehydrogenase 1A1 (EC 1.2.1.19) (EC 1.2.1.28) (EC 1.2.1.3) (EC 1.2.1.36) (3-deoxyglucosone dehydrogenase) (ALDH-E1) (ALHDII) (Aldehyde dehydrogenase family 1 member A1) (Aldehyde dehydrogenase, cytosolic) (Retinal dehydrogenase 1) (RALDH 1) (RalDH1) (P24549)
Organism: Mus musculus (Mouse)
Function: Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid. Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid. This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (Probable). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:1935685}. Cell projection, axon {ECO:0000269|PubMed:26430123}.
Interaction partners:
- Cytochrome P450 26A1
- Alcohol dehydrogenase class-3
- Alcohol dehydrogenase 1
- Cytochrome P450 26B1
- Dehydrogenase/reductase SDR family member 4
- All-trans-retinol dehydrogenase [NAD
- All-trans-retinol dehydrogenase [NAD
- Cytochrome P450 26C1
- Aldehyde dehydrogenase, cytosolic 1
- Retinol dehydrogenase 5
Sequence:
MSSPAQPAVPAPLADLKIQHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKISQKNS
Protein: Rho GTPase-activating protein 22 (Rho-type GTPase-activating protein 22) (Q7Z5H3)
Organism: Homo sapiens (Human)
Function: Rho GTPase-activating protein involved in the signal transduction pathway that regulates endothelial cell capillary tube formation during angiogenesis. Acts as a GTPase activator for the RAC1 by converting it to an inactive GDP-bound state. Inhibits RAC1-dependent lamellipodia formation. May also play a role in transcription regulation via its interaction with VEZF1, by regulating activity of the endothelin-1 (EDN1) promoter (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytoplasmic. Some fraction is nuclear (By similarity). {ECO:0000250}.
Interaction partners:
- Transforming protein RhoA
- Cell division control protein 42 homolog
Sequence:
MLSPKIRQARRARSKSLVMGEQSRSPGRMPCPHRLGPVLKAGWLKKQRSIMKNWQQRWFVLRGDQLFYYKDKDEIKPQGFISLQGTQVTELPPGPEDPGKHLFEISPGGAGEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGGIFGQRLEETVHHERKYGPRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTIMEGTSLVQHLMTVLIRKHSQLFTAPVPEGPTSPRGGLQCAVGWGSEEVTRDSQGEPGGPGLPAHRTSSLDGAAVAVLSRTAPTGPGSRCSPGKKVQTLPSWKSSFRQPRSLSGSPKGGGSSLEVPIISSGGNWLMNGLSSLRGHRRASSGDRLKDSGSVQRLSTYDNVPAPGLVPGIPSVASMAWSGASSSESSVGGSLSSCTACRASDSSARSSLHTDWALEPSPLPSSSEDPKSLDLDHSMDEAGAGASNSEPSEPDSPTREHARRSEALQGLVTELRAELCRQRTEYERSVKRIEEGSADLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDAERRNQLLQREMEEFFSTLGSLTVGAKGARAPK
Protein: Histone-lysine N-methyltransferase (EC 2.1.1.355) (A0A8I6A3A4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR009343}.
Interaction partners:
Sequence:
PRAAGRRAYARERVLKRRLRPRAGKAALSDRYPFGFHGRRRKGRKKWNGPPSQNGGTGDSSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCVRILKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKGIRYNLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTTACRKYLF
Protein: P-type Ca(2+) transporter (EC 7.2.2.10) (M9PG15)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004326}.
Interaction partners:
- Calcium-transporting ATPase
Sequence:
MSKTPKPLTSKRRTSPASPGSTVLIESPTTSSGVRNRRSKIKGVDSKPNPQRTISHVKDSRAVPQNVKPGKVADMKDCKEPDEDNVDQQNGNIIQTGLTLTPEMLLSTSESSTHSASEVAGRLQVDVRTGLKWTEAKYRAKIIGHNELLLVAEDPTWKKYIEQFRNPLILLLLGSALVSVIMKQFDDAVSITIAILIVVTVAFIQEYRSEKSLEELKKLVPPECHCLREGRLDTFLARELVPGDIVHLNVGDRVPADVRLFEAVDLSIDESSFTGETEPARKITDVLLNNTNVKDHSNMKNIAFMGTLVRCGNGKGIVVSTGERSEFGEVFKMMQAEEAPKTPLQKSMDILGAQLSFYSFLIIGVIMLLGWLQGKPLSEMFNISVSLAVAAIPEGLPIVVTVTLALGVMRMAKRNSIVKKLPTVETLGCVNVICSDKTGTLTKNEMTATIIITSDGYMADVTGAGYNDQGEIHIRHCNNVEMAKTNITNLLEIGAVCNNAYIQNGTLLGQPTEGALVAVAMKNGMYATAENYVRIQEYPFSSEQKMMAVKCIHKYNNNKEEIFFAKGALETLLPQCTKYQFGTQTVPLTKQNEAEFLAEAYEIGRKGLRVLALAKGRSMQDLIYCGLVGITDPPRPLVRESIEMLMQSGVRVKMVTGDAQETALAIDPSRRLQAVPTHAIPAWPTAGGVPLCSASACCSTNCLENAMKEIYLTALAQQGLPLVTANLIGIDTIHHQTLSGQEMDQMNEHQLDKVANNVSVFYRVSPRHKLEIVKSLQRSGNIVGMTGDGVNDGVALKKADIGIAMGKNGTDVCKEAADMILVNDDFHTIIAAIEEGKGIFYNIRNFVRFQLSTSIAALALIALATLMDIANPLNAMQILWINIIMDGPPAQSLGVEPVDHDVLKQKPRNVKQPMITKSVVVNVLLSASIIVLGTLWVFQREMADGTLGKTKRDTTMTFTCFVFFDMFNALSCRSQTKSVFTIGLTTNRMFLLAVAFSIIGQMLVVYFPPLQMVFQTEALTPYDIFFLVSLTSSVLVVSEIKKWFERTMERKMYSTRSELDFV
Protein: Elastin microfibril interfacer 3 (F1SDV5)
Organism: Sus scrofa (Pig)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGRRRLPVWLCAVAALLSGAQAKGTPLLARPVQPGASRYSLYTTGWRPRLRPGPHKALCAYVVHRNVTCVLQEGAESYIKAEYRQCRWGPKCPGTVTYRTVFRPKYKVGYKTVTDLAWRCCPGLTGEGCPKHLADHGATPPQPAPEPQIPSGQVGPGPRPLPSSRVAPSPHGRKAPGLFGERLERLEADVQRLAQAYGTLSGLVASHEDPNKKTGGPRVPATPVGFGVIPEGFVNPGETTGGLLTPPLHEILSKVTEVSNTLRTKVQLLDEVHGLALGHEAHLQRLREAPPSPLTSLALLDEYVDRRLHRLWGSLLDGFEQKLQGVQSACDLRVQEVRQQCEEGQAASRRLHQSLDGRELALRRELSQLGTRLQGLSVAGGGSCCGQLALLSARMDSLERNLQVVTEAQRGHSPPSRDDLTRLSAAMLEGGMAGLLEGLETINGTEGGARGCCRGMGEGGWGVRGYQAMLEERVQRLEERLVTLAGDLSHDSAPPGRSARPLVQTELAVLEQRLVSLETSCTPSTTSAILDNLVAEVKAWQSRSEALLRQVASHAILLQQLNGTVAEVQGQLAEATGSSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAANTSLDERERKVEAEVQAIQEQVSSQGSQLRAGHRQVLSLRGELEQLKAGVASVAGGLSRCQDTAQALQHAVGHFDQRVARVEGACGRLGLLAAGLDSLPADSLGPREGLWGHVDQLNRTLTQHAKDIARLRDDLLDCQAQLAEQVRPGQAD
Protein: Uncharacterized CCDC90 family protein C3H1.08c, mitochondrial (Q10073)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MIIRKQIFPFLSQNRPWTIINRIQSERYSASYEPSPELLKQSSRRLEQAGYSVKNAETITNLMRTITGEALTELEKNIGFKAKQESVSFQQKRTFLQIRKYLETIEENEFDKVRKSSDKLINEIEKTKSSLREDVKTALSEVRLNLNLEKGRMKDAATSRNTNIHENETKILNEVDILHKEINDMKIQTNQWFTGFVGVVSSVVLIILFYF
Protein: Cytochrome b6-f complex subunit 5 (Cytochrome b6-f complex subunit PetG) (Cytochrome b6-f complex subunit V) (P0C390)
Organism: Oryza sativa (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00432}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00432}.
Interaction partners:
Sequence:
MIEVFLFGIVLGLIPITLAGLFVTAYLQYRRGDQLDL
Protein: Uncharacterized protein DDB_G0290685 (Q54G14)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MTIFDAVAKAIVPSVTHAIEENNKNREIQEKRQKETKDRNDRMVQNQKDRKEMIGLTNEKQTYSNSVKNAKTDNEKKIFQNLLDKTNSRITDIEKRQSGDISEYKRLVEENKNLEKNVKEFKEVMKPFEENDIIHNPKHVDEDTIEENKKKMEDIKEVLGFTKTAANGGLPPNHDEDNKKIAELKKKYDDVKNHGHSNSGGLVGSVFNAIVPSVKENLRNAELENIQKEIKQTEDKISNDDKFYNTYKLTDDERKQFGSNPGDPQATPTPTPTPTPTPTPTPTPTTTTTTTTTPKPTTTTTTTSTTTPTKTSTNTNDKPGIFETVGGGSGKVADALNPIRIVTGGAIFSDTMEKIGGGSGKLADEGVEAVGSGISNFAQSVGIIPKKQEPKKDENNNQSNNNNNNNQAGDDQNKNQNRDENNQGGENNQGGENNQDGENNQNGDENNQGGENNQGDENNQGGENNQGDQNNQDGGENNQDGGENNQDGHGNNQDGENNQDGGENNQDSGENNQDGGENNQDGGENNQDGGENNQDGGENNQDGGENNQDGGENNQDGENNQDGENNQENNRDGENNQDGGENNQDGGENNQDGENNQDGGENNQDDGENKQDGGENNQDGGENNQDDGENNQDGENNQDGGENNQDGDENNQDSGENNQDSGENNQDGGENNQDGDENNQDGGENNQDGENNQNGENNQDGGENNQDGENNQDGENNQDGGENNQDGGENNQDGGEDNQDGGENNQEGGEDNQDGGEDNQDGGEDNQDGGENNQGDENNQDVDENNQDGENNQDGDENNQDGENNQDGENNQDGDENNNQDGEQNQDGDENNQDGGENNQDGDENNNQDGDENNNQDGGENNQDGGENNQDGDENNNQDGGENNQDGENNQDGDENNNQDGEQNQDGDENNQEGDENNNQGDDENNNQDGDENNNQDGDENNQDGDENNQDGDENNQGNDENNQDGDQNNQGGDENNQDGDGENNQGDENNQDGGENNQDGGENNQDQDGSENNQGNNENNQGGDENNQDQDGGENNQGNDENNQGGDENNQGNENDQGGDENNQGGDENTNQEENGGNDE
Protein: DNA adenine methylase (EC 2.1.1.72) (DNA adenine methyltransferase) (Deoxyadenosyl-methyltransferase) (Orphan methyltransferase M.EcoKDam) (M.EcoKDam) (P0AEE8)
Organism: Escherichia coli (strain K12)
Function: An alpha subtype methylase that recognizes the double-stranded sequence 5'-GATC-3' and methylates A-2 on both strands (Probable). Although it shares sequence specificity with a number of type II restriction endonucleases and methylases, it is thought to act in methyl-directed mismatch repair, initiation of chromosome replication and gene expression.
Interaction partners:
- DNA mismatch repair protein MutH
- Phosphoglycolate phosphatase
- Tryptophan--tRNA ligase
- Ribulose-phosphate 3-epimerase
- Negative modulator of initiation of replication
- DNA adenine methyltransferase YhdJ
- Cell division protein DamX
- Uncharacterized protein YhfW
- Uncharacterized protein YhfY
- Uncharacterized protein YhfX
Sequence:
MKKNRAFLKWAGGKYPLLDDIKRHLPKGECLVEPFVGAGSVFLNTDFSRYILADINSDLISLYNIVKMRTDEYVQAARELFVPETNCAEVYYQFREEFNKSQDPFRRAVLFLYLNRYGYNGLCRYNLRGEFNVPFGRYKKPYFPEAELYHFAEKAQNAFFYCESYADSMARADDASVVYCDPPYAPLSATANFTAYHTNSFTLEQQAHLAEIAEGLVERHIPVLISNHDTMLTREWYQRAKLHVVKVRRSISSNGGTRKKVDELLALYKPGVVSPAKK
Protein: Artemin (Enovin) (Neublastin) (Q5T4W7)
Organism: Homo sapiens (Human)
Function: Ligand for the GFR-alpha-3-RET receptor complex but can also activate the GFR-alpha-1-RET receptor complex. Supports the survival of sensory and sympathetic peripheral neurons in culture and also supports the survival of dopaminergic neurons of the ventral mid-brain. Strong attractant of gut hematopoietic cells thus promoting the formation Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue.
Subcellular location: Secreted {ECO:0000269|PubMed:15204970}.
Interaction partners:
- GDNF family receptor alpha-3
- Proto-oncogene tyrosine-protein kinase receptor Ret
- GDNF family receptor alpha-1
- GDNF family receptor alpha-2
- GDNF family receptor alpha-4
- Glial cell line-derived neurotrophic factor
- Neurturin
- Syndecan-3
- High affinity nerve growth factor receptor
- Persephin
Sequence:
MELGLGGLSTLSHCPWPRQQPALWPTLAALALLSSVAEASLGSAPRSPAPREGPPPVLASPAGHLPGGRTARWCSGRARRPPPQPSRPAPPPPAPPSALPRGGRAARAGGPGSRARAAGARGCRLRSQLVPVRALGLGHRSDELVRFRFCSGSCRRARSPHDLSLASLLGAGALRPPPGSRPVSQPCCRPTRYEAVSFMDVNSTWRTVDRLSATACGCLG
Protein: Small ribosomal subunit protein uS19 (40S ribosomal protein S15) (Q54N17)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- 30S ribosomal protein S9
- Small ribosomal subunit protein eS17
- Small ribosomal subunit protein eS30
- Small ribosomal subunit protein uS9
- Ribosomal protein L9 domain-containing protein
- Small ribosomal subunit protein eS27
- Large ribosomal subunit protein uL3
- 60S ribosomal protein L39
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL1
Sequence:
MSEQIKKRTFKKFTYSGVALESLLDLKEEQLISLLRCRARRKLRRETPIKHVNFLKKCRASKAAVTQVGEKPALVKTHARNILIVPEMIGSVIGIYNGKVFNQVEVKPEMIGHYTGEFSLSYKSVNHGRPGIGATHSSRFIPLK
Protein: Uncharacterized protein, isoform I (M9PB71)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
Sequence:
MNKVEFKNKNKDQGPCARVRKIRPINMGGNVEQRPWTPTVRIGKIAAETTNPGPATVQLPTLIGSKVPDSKKKAAPSYSFGHKLGGKYDTSGPGPAQYNVTGMRAKGRDYPRAATLQSRPKELTRFSNPGPGEYDVVPAAKAVIDATPKYTFGQRPVALKTFQIPGPNYYQVVPLDVVKRRAPRYSFRIKVNVYLVNNPAPNSYCPEKVTQSKKNAPRYTFGRRTKIEHDQGTPAPGAYCPEKVKLNKTPEFSFGIKHHEQRPDYTPAPGTYKPEQVVLEHIPAYSFGLKTKHIQVSDTPAPGAYSPEKSRLHSAPAYSIAGKASQDVVDCTPAPGAYEPEKCVLSRTPAFSFGHRAELAKSSDTPAPGTYNPEKVRLDHTPAFTLSGRPETRSVSETPAPGSYAPEKYRNDRTPAFTFGGKHEQRLESSTPAPGDYCPEKVRHDHNPAFSFAGRHDLHKPSDTPAPGAYDTEKVRQDHNPAFSFAGRHDLHKPSETPAPGAYSPEKVRQDHNPAFSMAGKHSQKVTSDSPAPGDYCPEKVRLDHTPAYSFGVKSDPKVENNTPAPGDYHPEKVRQDHNPAYSFAGRHDLQKPDNTPAPGAYFPEKVRLDHNPAFSMAGKYDAKVTNDTPAPGDYSPEKVRQDTNPAYSFAGRHDLHKPSETPAPGAYSPEKVRLDHNPAFTMAGKHDQKILNGTPAPGDYSPEKCRLDHTPAYSFGGKNDPKVENNTPAPGDYHPEKVRLDHNPAYSFAGRHDLQKPSDTPAPGAYSPEKVRQDHNPAFSMAGKPVEKLTNGTPAPGDYSPEKVRLNHTPAYTFGGKNDPKVENNTPAPGDYHPEKVRQDHNPAFSFAGRHDLHKPNDTPAPGAYCPEKVRQDHNPAFSMAGKYTQKVANDTPAPGDYSPEKVRLDHTPAYTFGGKNDPKVESNTPAPGDYHPEKVRQDHNPAFSFAGRHNLQKPSDTPAPGAYSPEKVRQDHNPAFTMAGKHDPKVSNDTPAPGDYSPEKVRLDYTPSFTFAGKNNPKVENDTPAPGDYHPEKVRQDHNPAFSFAGRHDLHKPSDTPAPGAYSPEKVRQDHNPAFSMAGKYIEKITNGTPAPGDYCPEKVRLDHTPAFTFGGKNDPKVENNTPAPGDYHPEKVRQDHVPAFSFAGRHDLHKPNETPAPGAYSPEKVRQDHNPAFTMAGKHDPKVTHDTPAPGDYHPEKVRLDHNPAFSFAGRHDLHKPSETPAPGDYFPEKVRQDFNPAFTFAGKHDPRSLSESPAPGDYSPEKVRLDHAPAFSFGGKHDPKTEHLHPAPCDYAPEKVRLDHTPAYTIAGRPAADHVSQTPAPCDYHPEQCQVDSTPAFTFGMRLGRERISDTPAPSAYEPEKHSLHSTPAYSFGTKSDIRVTTDAPAPGHYHPEQCKLDSSPAYSFGLKTVPTASLPEPRGAYIEDRIVQRRERRLASPVRNNAECTTTTTNHTNNNAGSSTTTTTTTTTTTKTFINGVEQPELQKKETTKQVNGTHKELKSAPQAPLSNGNIVSNGNHSKMVSTTTRIQEVAHGQKESGNLKVVASGKSDASATKAAAVSHQTVVQADGAIVTSGQSSRMQTVKYAVEASSVQEKIISS
Protein: Vitronectin (Q3KR94)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MASLRPFFILALLALVSLADQESCKGRCTQGFMASKKCQCDELCTYYQSCCVDYMEQCKPQVTRGDVFTMPEDEYWSYDYPEETKNSTSTGVQSENTSLHFNLKPRAEETIKPTTPDPQEQSNTQEPEVGQQGVAPRPDTTDEGTSEFPEEELCSGKPFDAFTDLKNGSLFAFRGEYCYELDETAVRPGYPKLIQDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPDYPRNISEGFSGIPDNVDAALALPAHSYSGRERVYFFKGKQYWEYEFQQQPSQEECEGSSLSAVFEHFALLQRDSWENIFELLFWGRSSDGAKGPQFISRDWHGVPGKVDAAMAGRIYITGSTFRSVQAKKQKSGRRSRKRYRSRRGRGHSRSRSRSMSSRRPSRSVWFSLLSSEESGLGTYNYDYDMNWRIPATCEPIQSVYFFSGDKYYRVNLRTRRVDSVNPPYPRSIAQYWLGCPTSEK
Protein: Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1) (Q9DGD9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as c-Jun and ATF2 and thus regulates AP-1 transcriptional activity. May play a role in the regulation of the circadian clock.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P49185}. Nucleus {ECO:0000250|UniProtKB:Q91Y86}. Synapse {ECO:0000250|UniProtKB:P49185}.
Interaction partners:
- Transcription factor Jun
- Cellular tumor antigen p53
- Dual specificity mitogen-activated protein kinase kinase 7
- mitogen-activated protein kinase kinase
- mitogen-activated protein kinase kinase
- Nuclear factor of activated T-cells, cytoplasmic 3 isoform X1
- Apoptosis regulator Bcl-2
- Transcription factor JunD
- C-Jun-amino-terminal kinase-interacting protein 2
- Protein c-Fos
Sequence:
MNRNKREKEYYSIDVGDSTFTVLKRYQNLRPIGSGAQGIVCSAYDHVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERLSYLLYQMLCGIKHLHAAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAATGLLMTPYVVTRYYRAPEVILGMGYQANVDVWSIGCIMAEMVRGSVLFPGTDHIDQWNKVIEQLGTPSQEFMMKLNQSVRTYVENRPRYAGYSFEKLFPDVLFPADSDHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEVEAPPPAITDKQLDEREHSVEEWKELIYKEVLEWEERTKNGVIRGQPASLAQVQQ
Protein: Protein S100-A13 (S100 calcium-binding protein A13) (Q99584)
Organism: Homo sapiens (Human)
Function: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity).
Subcellular location: Cytoplasm. Secreted. Note=Secretion is mediated by exposure to stress and requires copper ions.
Interaction partners:
- Synaptotagmin-1
- Fibroblast growth factor 1
- Interleukin-1 alpha
- Advanced glycosylation end product-specific receptor
- Protein polybromo-1
- Sphingosine kinase 1
- Protein S100-A6
- Cellular retinoic acid-binding protein 2
- Protein S100-A3
- Protein S100-A10
Sequence:
MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK
Protein: D-alanyl-D-alanine carboxypeptidase (P74474)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Cobalamin biosynthesis protein CobD
Sequence:
MKKSLFMVGTLAFFSGLPAGGAWGESLDNKVQTILDEHYQNRREPEFFSAIQLSTKVGDGDIKTYVVGTKSHAPNSPPIDAKSLFQIGSITKSFTSVLLLQAEAENKVNLGDDFTTYLPEYDHWNGVTITQLLNMTSGLPNYSDSPTLNYGFVQSPERIWQDKELVDVVYPQPNLPAPPLNTGYAYTNTAYTLGGLVLEKVYGQSYAELIDKKLLQPLELNNTFYPIPSYPPDILDRMVEGSSFNPYTNPELAGKPVANGNLSWAGAAGGLVANTEDIINWVRALFVEDQLLSTEQKTQLTRLVSLITGKLIDGTTSEEQRGFGLGVVQGYHEDWGQYWFYQGETIGHRSFYLYFPCNEVIISALFNSAVDDQNNDVKPLLVGVYEALLDDQPSLACKTK
Protein: Casein kinase I isoform epsilon (CKI-epsilon) (CKIe) (EC 2.7.11.1) (P49674)
Organism: Homo sapiens (Human)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates (Probable). Participates in Wnt signaling. Phosphorylates DVL1. Phosphorylates DVL2. Phosphorylates NEDD9/HEF1 (By similarity). Central component of the circadian clock. In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation (By similarity). Inhibits cytokine-induced granuloytic differentiation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Period circadian protein homolog 2
- Cryptochrome-1
- Basic helix-loop-helix ARNT-like protein 1
- Cryptochrome-2
- Period circadian protein homolog 1
- Period circadian protein homolog 3
- Circadian locomoter output cycles protein kaput
- Axin-1
- Glycogen synthase kinase-3 beta
- Casein kinase I isoform delta
Sequence:
MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGAARNPEDVDRERREHEREERMGQLRGSATRALPPGPPTGATANRLRSAAEPVASTPASRIQPAGNTSPRAISRVDRERKVSMRLHRGAPANVSSSDLTGRQEVSRIPASQTSVPFDHLGK
Protein: Formyl peptide receptor 3 (D4A8L8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Annexin A1
- fMet-Leu-Phe receptor
Sequence:
METNYSIPMSGSEVMVNDSTISRVLWILTMVVLSITFVLGVLGNGLVIWVAGFRMAHTVTTTCYLNLALADFFFTATLPFFIISTAMEGKWPFGWFLCKLLYIIADVNGIGSIFLITLIALDRCICVVHPVWAQNHRTVSLARKVVIGPWIFGLILSLHIFIFISTYRVSGGDVYCVYYFPSWGNTDEEMLNTVFIFTTALGIIKFIIIFIIPMSIVSICYGLIAVKIQRRALVNSSRASRVLKAVVASFFICWFPFQLVALLSLVWFKERLLNDEYKIIDMLIMPTNSLAFFNSCLNPILYVFFGQDFRKRLIHSLPSSLERALSEDSGQTSNTGTNSALPSANIEMMST
Protein: Endoplasmic reticulum membrane adapter protein XK (Kell complex 37 kDa component) (Kx antigen) (Membrane transport protein XK) (XK-related protein 1) (P51811)
Organism: Homo sapiens (Human)
Function: Recruits the lipid transfer protein VPS13A from lipid droplets to the endoplasmic reticulum (ER) membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:32845802, ECO:0000269|PubMed:9593744}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Kell blood group glycoprotein
- Intermembrane lipid transfer protein VPS13A
- Endothelin-3
Sequence:
MKFPASVLASVFLFVAETTAALSLSSTYRSGGDRMWQALTLLFSLLPCALVQLTLLFVHRDLSRDRPLVLLLHLLQLGPLFRCFEVFCIYFQSGNNEEPYVSITKKRQMPKNGLSEEIEKEVGQAEGKLITHRSAFSRASVIQAFLGSAPQLTLQLYISVMQQDVTVGRSLLMTISLLSIVYGALRCNILAIKIKYDEYEVKVKPLAYVCIFLWRSFEIATRVVVLVLFTSVLKTWVVVIILINFFSFFLYPWILFWCSGSPFPENIEKALSRVGTTIVLCFLTLLYTGINMFCWSAVQLKIDSPDLISKSHNWYQLLVYYMIRFIENAILLLLWYLFKTDIYMYVCAPLLVLQLLIGYCTAILFMLVFYQFFHPCKKLFSSSVSEGFQRWLRCFCWACRQQKPCEPIGKEDLQSSRDRDETPSSSKTSPEPGQFLNAEDLCSA
Protein: Coproporphyrin III ferrochelatase (EC 4.99.1.9) (P9WNE3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III. Has weaker activity with coproporphyrin I, protoporphyrin IX, deuteroporphyrin, 2,4 hydroxyethyl and 2,4 disulfonate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}.
Interaction partners:
- Coproporphyrinogen III oxidase
- Uroporphyrinogen decarboxylase
- Coproheme decarboxylase
- Uncharacterized protein Rv2850c
- Bacterioferritin BfrA
- Protoheme IX farnesyltransferase
- Possible magnesium chelatase
- Multicopper oxidase MmcO
- Bacterioferritin BfrB
- Enoyl-[acyl-carrier-protein] reductase
Sequence:
MQFDAVLLLSFGGPEGPEQVRPFLENVTRGRGVPAERLDAVAEHYLHFGGVSPINGINRTLIAELEAQQELPVYFGNRNWEPYVEDAVTAMRDNGVRRAAVFATSAWSGYSSCTQYVEDIARARRAAGRDAPELVKLRPYFDHPLFVEMFADAITAAAATVRGDARLVFTAHSIPTAADRRCGPNLYSRQVAYATRLVAAAAGYCDFDLAWQSRSGPPQVPWLEPDVTDQLTGLAGAGINAVIVCPIGFVADHIEVVWDLDHELRLQAEAAGIAYARASTPNADPRFARLARGLIDELRYGRIPARVSGPDPVPGCLSSINGQPCRPPHCVASVSPARPSAGSP