DNJC1_HUMAN » DnaJ homolog subfamily C member 1

DNJC1_HUMAN » DnaJ homolog subfamily C member 1
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Topology in Endoplasmic reticulum membrane
Topologylumenal side
cytoplasmic side
DNJC1_HUMAN » DnaJ homolog subfamily C member 1 » DnaJ protein homolog MTJ1
Hydrophobic Thickness 30.2 ± 2.4 Å
Tilt Angle 26 ± 9°
ΔGtransfer -22.3 kcal/mol
ΔGfold -14.6 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 151-172 (151-177)
Pathways

Protein processing in endoplasmic reticulum (KEGG)

PDB 2cqq (327-385), 2cqr (484-543)
OPM none
Complexes none
Interactions none
Domains

AA: 65-126, PDBID: 2CUG, Subunit A, Seq Identity:53%, DnaJ domain

AA: 494-548, PDBID: 2CQR, Subunit A, Seq Identity:100%, Myb-like DNA-binding domain

UniProt annotation for DNJC1_HUMAN » DnaJ homolog subfamily C member 1
FUNCTION: May modulate protein synthesis.

SUBUNIT: Interacts (via J domain) with HSPA5. Interacts (via cytosolic domain) with ribosomes (By similarity). Interacts (via SANT 2 domain) with SERPINA3; the interaction delays the formation of the covalent inhibitory complex SERPINA3-chymotrypsin, but does not alter the catalytic activity of SERPINA3. Interacts (via SANT 2 domain) with ITIH4 (via C-terminus); the interaction protects ITIH4 against in vitro cleavage by kallikrein.

UniProt features for DNJC1_HUMAN » DnaJ homolog subfamily C member 1
SIGNAL 1 47 Potential.
CHAIN 48 554 DnaJ homolog subfamily C member 1.
DOMAIN 65 129 J.
DOMAIN 325 379 SANT 1.
DOMAIN 492 547 SANT 2.
Amino Acid Sequence for DNJC1_HUMAN » DnaJ homolog subfamily C member 1
MTAPCSQPAQ LPGRRQLGLV PFPPPPPRTP LLWLLLLLLA AVAPARGWES GDLELFDLVE EVQLNFYQFL GVQQDASSAD IRKAYRKLSL TLHPDKNKDE NAETQFRQLV AIYEVLKDDE RRQRYDDILI NGLPDWRQPV FYYRRVRKMS NAELALLLFI ILTVGHYAVV WSIYLEKQLD ELLSRKKREK KKKTGSKSVD VSKLGASEKN ERLLMKPQWH DLLPCKLGIW FCLTLKALPH LIQDAGQFYA KYKETRLKEK EDALTRTELE TLQKQKKVKK PKPEFPVYTP LETTYIQSYD HGTSIEEIEE QMDDWLENRN RTQKKQAPEW TEEDLSQLTR SMVKFPGGTP GRWEKIAHEL GRSVTDVTTK AKQLKDSVTC SPGMVRLSEL KSTVQNSRPI KTATTLPDDM ITQREDAEGV AAEEEQEGDS GEQETGATDA RPRRRKPARL LEATAKPEPE EKSRAKRQKD FDIAEQNESS DEESLRKERA RSAEEPWTQN QQKLLELALQ QYPRGSSDRW DKIARCVPSK SKEDCIARYK LLVELVQKKK QAKS