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Protein

DnaJ homolog subfamily C member 1

Gene

DNAJC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May modulate protein synthesis.By similarity

GO - Molecular functioni

  • ATPase activator activity Source: UniProtKB
  • DNA binding Source: UniProtKB-KW

GO - Biological processi

  • negative regulation of proteolysis Source: UniProtKB
  • positive regulation of ATPase activity Source: GOC
  • protein folding Source: Ensembl
  • regulation of protein secretion Source: UniProtKB
  • regulation of translation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily C member 1
Alternative name(s):
DnaJ protein homolog MTJ1
Gene namesi
Name:DNAJC1
Synonyms:HTJ1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:20090. DNAJC1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini48 – 153106LumenalBy similarityAdd
BLAST
Transmembranei154 – 17421HelicalSequence analysisAdd
BLAST
Topological domaini175 – 554380CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394706.

Polymorphism and mutation databases

BioMutaiDNAJC1.
DMDMi27805464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4747Sequence analysisAdd
BLAST
Chaini48 – 554507DnaJ homolog subfamily C member 1PRO_0000071042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei381 – 3811PhosphoserineCombined sources
Modified residuei430 – 4301PhosphoserineCombined sources
Modified residuei479 – 4791PhosphoserineCombined sources
Modified residuei480 – 4801PhosphoserineCombined sources
Modified residuei484 – 4841PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96KC8.
MaxQBiQ96KC8.
PaxDbiQ96KC8.
PRIDEiQ96KC8.

PTM databases

iPTMnetiQ96KC8.
PhosphoSiteiQ96KC8.

Expressioni

Gene expression databases

BgeeiQ96KC8.
CleanExiHS_DNAJC1.
ExpressionAtlasiQ96KC8. baseline and differential.
GenevisibleiQ96KC8. HS.

Organism-specific databases

HPAiHPA013432.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SERPINA3P010113EBI-296550,EBI-296557

Protein-protein interaction databases

BioGridi122105. 20 interactions.
IntActiQ96KC8. 6 interactions.
MINTiMINT-1036349.
STRINGi9606.ENSP00000366179.

Structurei

Secondary structure

1
554
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi332 – 34413Combined sources
Helixi352 – 3609Combined sources
Helixi364 – 37613Combined sources
Turni489 – 4913Combined sources
Helixi499 – 51113Combined sources
Beta strandi514 – 5163Combined sources
Helixi517 – 5237Combined sources
Helixi524 – 5263Combined sources
Beta strandi528 – 5303Combined sources
Helixi532 – 54312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQQNMR-A327-385[»]
2CQRNMR-A484-543[»]
ProteinModelPortaliQ96KC8.
SMRiQ96KC8. Positions 65-137, 327-385, 485-543.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96KC8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 12965JPROSITE-ProRule annotationAdd
BLAST
Domaini325 – 37955SANT 1PROSITE-ProRule annotationAdd
BLAST
Domaini492 – 54756SANT 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation
Contains 2 SANT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410INV7. Eukaryota.
COG2214. LUCA.
GeneTreeiENSGT00530000063419.
HOGENOMiHOG000231867.
HOVERGENiHBG051374.
InParanoidiQ96KC8.
KOiK09521.
OMAiTVSGGFW.
OrthoDBiEOG7XM2XM.
PhylomeDBiQ96KC8.
TreeFamiTF105161.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF46689. SSF46689. 2 hits.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51293. SANT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96KC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAPCSQPAQ LPGRRQLGLV PFPPPPPRTP LLWLLLLLLA AVAPARGWES
60 70 80 90 100
GDLELFDLVE EVQLNFYQFL GVQQDASSAD IRKAYRKLSL TLHPDKNKDE
110 120 130 140 150
NAETQFRQLV AIYEVLKDDE RRQRYDDILI NGLPDWRQPV FYYRRVRKMS
160 170 180 190 200
NAELALLLFI ILTVGHYAVV WSIYLEKQLD ELLSRKKREK KKKTGSKSVD
210 220 230 240 250
VSKLGASEKN ERLLMKPQWH DLLPCKLGIW FCLTLKALPH LIQDAGQFYA
260 270 280 290 300
KYKETRLKEK EDALTRTELE TLQKQKKVKK PKPEFPVYTP LETTYIQSYD
310 320 330 340 350
HGTSIEEIEE QMDDWLENRN RTQKKQAPEW TEEDLSQLTR SMVKFPGGTP
360 370 380 390 400
GRWEKIAHEL GRSVTDVTTK AKQLKDSVTC SPGMVRLSEL KSTVQNSRPI
410 420 430 440 450
KTATTLPDDM ITQREDAEGV AAEEEQEGDS GEQETGATDA RPRRRKPARL
460 470 480 490 500
LEATAKPEPE EKSRAKRQKD FDIAEQNESS DEESLRKERA RSAEEPWTQN
510 520 530 540 550
QQKLLELALQ QYPRGSSDRW DKIARCVPSK SKEDCIARYK LLVELVQKKK

QAKS
Length:554
Mass (Da):63,883
Last modified:December 1, 2001 - v1
Checksum:i65EAAB16C65E2B46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY225122 mRNA. Translation: AAP50497.1.
AK026062 mRNA. Translation: BAB15343.1.
AK027263 mRNA. Translation: BAB55004.1.
EF444973 Genomic DNA. Translation: ACA05978.1.
EF444973 Genomic DNA. Translation: ACA05979.1.
AL445431, AL359697 Genomic DNA. Translation: CAI13668.1.
AL359697, AL445431 Genomic DNA. Translation: CAH73412.1.
BC110894 mRNA. Translation: AAI10895.1.
CCDSiCCDS7136.1.
RefSeqiNP_071760.2. NM_022365.3.
UniGeneiHs.499000.

Genome annotation databases

EnsembliENST00000376980; ENSP00000366179; ENSG00000136770.
GeneIDi64215.
KEGGihsa:64215.
UCSCiuc001irc.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY225122 mRNA. Translation: AAP50497.1.
AK026062 mRNA. Translation: BAB15343.1.
AK027263 mRNA. Translation: BAB55004.1.
EF444973 Genomic DNA. Translation: ACA05978.1.
EF444973 Genomic DNA. Translation: ACA05979.1.
AL445431, AL359697 Genomic DNA. Translation: CAI13668.1.
AL359697, AL445431 Genomic DNA. Translation: CAH73412.1.
BC110894 mRNA. Translation: AAI10895.1.
CCDSiCCDS7136.1.
RefSeqiNP_071760.2. NM_022365.3.
UniGeneiHs.499000.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQQNMR-A327-385[»]
2CQRNMR-A484-543[»]
ProteinModelPortaliQ96KC8.
SMRiQ96KC8. Positions 65-137, 327-385, 485-543.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122105. 20 interactions.
IntActiQ96KC8. 6 interactions.
MINTiMINT-1036349.
STRINGi9606.ENSP00000366179.

PTM databases

iPTMnetiQ96KC8.
PhosphoSiteiQ96KC8.

Polymorphism and mutation databases

BioMutaiDNAJC1.
DMDMi27805464.

Proteomic databases

EPDiQ96KC8.
MaxQBiQ96KC8.
PaxDbiQ96KC8.
PRIDEiQ96KC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376980; ENSP00000366179; ENSG00000136770.
GeneIDi64215.
KEGGihsa:64215.
UCSCiuc001irc.4. human.

Organism-specific databases

CTDi64215.
GeneCardsiDNAJC1.
HGNCiHGNC:20090. DNAJC1.
HPAiHPA013432.
MIMi611207. gene.
neXtProtiNX_Q96KC8.
PharmGKBiPA128394706.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INV7. Eukaryota.
COG2214. LUCA.
GeneTreeiENSGT00530000063419.
HOGENOMiHOG000231867.
HOVERGENiHBG051374.
InParanoidiQ96KC8.
KOiK09521.
OMAiTVSGGFW.
OrthoDBiEOG7XM2XM.
PhylomeDBiQ96KC8.
TreeFamiTF105161.

Miscellaneous databases

ChiTaRSiDNAJC1. human.
EvolutionaryTraceiQ96KC8.
GeneWikiiDNAJC1.
GenomeRNAii64215.
NextBioi66123.
PROiQ96KC8.
SOURCEiSearch...

Gene expression databases

BgeeiQ96KC8.
CleanExiHS_DNAJC1.
ExpressionAtlasiQ96KC8. baseline and differential.
GenevisibleiQ96KC8. HS.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF46689. SSF46689. 2 hits.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51293. SANT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity."
    Kroczynska B., Evangelista C.M., Samant S.S., Elguindi E.C., Blond S.Y.
    J. Biol. Chem. 279:11432-11443(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SERPINA3.
    Tissue: Liver.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  3. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381 AND SER-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479; SER-480 AND SER-484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Solution structure of RSGI RUH-037, a Myb DNA-binding domain in human."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 327-385 AND 484-543.

Entry informationi

Entry nameiDNJC1_HUMAN
AccessioniPrimary (citable) accession number: Q96KC8
Secondary accession number(s): B0YIZ8, Q5VX89, Q9H6B8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: December 1, 2001
Last modified: March 16, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.