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DNAJC2

Gene
DNAJC2
Protein
DnaJ homolog subfamily C member 2
Organism
Bos taurus
Length
621 amino acids
Function
Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3' (By similarity).
Mass
71.786 kDa
Sequence
MLLLPSAADGQGTAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASASFQELEDKKELSEESEDEELQLEEFPMLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEGDNDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSVPSKSEAKDNFFEVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDAFYSFWYNFDSWREFSYLDEEEKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKADAKRKEQEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNLCKTWNHFSDSEAERVKMMEEVEKLCDRLELSSLQCLNETLTSSTKEVGKAALEKQIEEINEQIRKEKEEAEARMRQASKNAEKSAGGGGNGSKHWSEDDLQLLIKAVNLFPAGTNSRWEVIANYMNIHSSSGVKRTAKDVIGKAKSLQKLDPHQKDDINKKAFDKFKKEHGVVPQADNATPSERFEGPCTDFTPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMKRYKELVEMVKAKKAAQEQVLNASRGKK

Gene
DNAJC2
Protein
DnaJ homolog subfamily C member 2
Organism
Homo sapiens
Length
621 amino acids
Function
Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'.
Mass
71.996 kDa
Sequence
MLLLPSAADGRGTAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASASFQELEDKKELSEESEDEELQLEEFPMLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEGDNDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSVPSKSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEEEKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKTWNHFSDNEAERVKMMEEVEKLCDRLELASLQCLNETLTSCTKEVGKAALEKQIEEINEQIRKEKEEAEARMRQASKNTEKSTGGGGNGSKNWSEDDLQLLIKAVNLFPAGTNSRWEVIANYMNIHSSSGVKRTAKDVIGKAKSLQKLDPHQKDDINKKAFDKFKKEHGVVPQADNATPSERFEGPYTDFTPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMKRYKELVEMVKAKKAAQEQVLNASRAKK

Gene
DNAJC2
Protein
DnaJ homolog subfamily C member 2
Organism
Macaca fascicularis
Length
621 amino acids
Function
Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3' (By similarity).
Mass
71.931 kDa
Sequence
MLLLPSPADGRGTAITHALTSASTLCRVEPVGRWFEAFVKRRNRNASASFQELEDKKELSEESEDEELQLEEFAMLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEGDNDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSVPSKSEAKDNFFEVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEEEKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDLQKKAIKKERQKLRNSCKTWNHFSDNEAERVKMMEEVEKLCDRLELASLQCLNETLTSCTKEVGKAALEKQIEEINEQIRKEKEEAEAHMRQASKNTEKSAGGGGNGSKNWSEDDLQLLIKAVNLFPAGTNSRWEVIANYMNIHSSSGVKRTAKDVIGKAKSLQKLDPHQKDDINKKAFDKFKKEHGVVPQADNAAPSERFEGPYTDFTPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMKRYKELVEMVKAKKAAQEQVLNASRAKK

Gene
Dnajc2
Protein
DnaJ homolog subfamily C member 2
Organism
Mus musculus
Length
621 amino acids
Function
Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation (By similarity). Specifically binds DNA sequence 5'-GTCAAGC-3'.
Mass
71.722 kDa
Sequence
MLLLPSAAEGQGTAITHALTSASSVCQVEPVGRWFEAFVKRRNRNASTSFQELEDKKELSEESEDEELQLEEFPMLKTLDPKDWKNQDHYAVLGLGHVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEGDNDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSVPSKSEAKDNFFQVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDAFYSFWYNFDSWREFSYLDEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEARRKEQEAKEKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKSWNHFSDNEADRVKMMEEVEKLCDRLELASLQGLNEILASSTREVGKAALEKQIEEVNEQMRREKEEADARMRQASKNAEKSTGGSGSGSKNWSEDDLQLLIKAVNLFPAGTNSRWEVIANYMNIHSSSGVKRTAKDVISKAKSLQKLDPHQKDDINKKAFDKFKKEHGVASQADSAAPSERFEGPCIDSTPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMRRYKELVEMVKAKKAAQEQVLNASRARK

Gene
Dnajc2
Protein
DnaJ homolog subfamily C member 2
Organism
Rattus norvegicus
Length
621 amino acids
Function
Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3' (By similarity).
Mass
71.769 kDa
Sequence
MLLLPSAAEGQGTAITHALTSASAVCQVEPVGRWFEAFVKRRNRNASTSFQELEDKKELSEESEDEELQLEEFPMLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKTMVLKHHPDKRKAAGEPIKEGDNDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSVPSKSEAKENFFQVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDAFYSFWYNFDSWREFSYLDEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEGKAKKEAEKRAKAEARRKEQEAKEKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNSCKNWNHFSDNEADRVKMMEEVEKLCDRLELASLQCLNEILASSTREVGKAALEKQIEEVNELMRKEKEEADARMRQASKNAEKSTGGSGSGSKNWSEDDLQLLIKAVNLFPAGTNSRWEVIANYMNIHSSSGVKRTAKDVIGKAKSLQKLDPHQKDDINKKAFDKFKKEHGVAPQADSAAPSERFEGPCIDSIPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMRRYKELVEMVKAKKAAQEQVLNASRARK

Gene
dnajc2
Protein
DnaJ homolog subfamily C member 2
Organism
Xenopus tropicalis
Length
620 amino acids
Function
Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation (By similarity).
Mass
71.995 kDa
Sequence
MLIEAQAEQCTFVTRGLCAAAVLCQVEPVGRWFEAFIKRRNRNVSASFQELEDEKESSEESEDEEFQLEEFPLLKTLDPKDWKNQDHYAVLGLKNLRYKATQRQIKAAHKAMVLKHHPDKRKAAGEQIVEGDNDYFTCITKAYEILSDPIKRRAFNSIDPTFDNSIPSKSEGKDNFFDAFSPVFERNSRWSNKKNIPKLGDMNSCIEEVDGFYSFWYNFDSWREFSYLDEEEKEKAECRDERRWIEKQNRAARAQRKKEEMIRIRTLVDNAYSSDPRIKKFKEEEKARKEAEKKAKADARRKEQEEKERQKQAELEAVRLAKEKEEEEARQQALLIKKEKEIQKKAIKKERQRLRTSCKNWNYFSDNEAESVKMMEEIEKLCDRLELASLQSLNESLAVSSKEEGKSAVEKQIAEVNAQLKREKEQEEARMKQSTKGAENSAIGGGSGSKSWSEDDLQLLIKAVNLFPAGTNARWEVIANYMNLHSISGIKRTSKDVINKAKSLQKLDPQQKDDINKKAFDKFKKEHRVVPQSVDNAVPSERFEGPAADMSPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRSKKDCMKRYKELVEMVKAKKAAQEQVLNATKIKK

Gene
dnajc2
Protein
DnaJ homolog subfamily C member 2
Organism
Danio rerio
Length
618 amino acids
Function
Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation (By similarity).
Mass
71.598 kDa
Sequence
MLTEALEGQLTVVYNTVAASVQVQVEPVGRWFEAFLKRRNRNVSASFQELEEEEELSEEEEDEELQLEEYPMLKTLDPKDWKNQDHYAVLGLAHVRYKATQKQIKAAHKAMVLKHHPDKRKAAGEQIVEGDNDYFTCITKAIEILSDPVKRRAFDSVDPTFDNAVPTKAEGKENFFEVFAPVFERNARWSVKKHFPSLGTMESSFEDVDNFYSFWYNFDSWREFSYLDEEEKEKAECRDERRWIEKQNRASRAQRKKEEMNRIRTLVDTAYNADPRIKKFKEEEKARKESEKKAKVEAKKREQEEKERARQQQEEAARLLKEQQEEAARQAAQQAKKEKEAQKKAIKKERQKLRMTCKSQNYFTDNEADSVRMMEEVEKLCDRLELISLQTLNEALSAGNKEQSKAALEKQVQEVNMQLQKEKDAELQAQQAARGSEHSSAAGGQNNRGWSEEDLQLLIKAVNLFPAGTNARWEVIANYMNQHSSSGVRRTAKDVINKAKTLQKLDPHQKDEINRKAFEKFKKEHSAVPPTVDNAMPSERFDAVGADSNAAAWTTEEQKLLEQALKTYPVSTAERWERISEAVPGRSKKDCMKRYKELVEMIKAKKAAQEQVAAKNKK