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Q02818 (NUCB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleobindin-1
Alternative name(s):
CALNUC
Gene names
Name:NUCB1
Synonyms:NUC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major calcium-binding protein of the Golgi. May have a role in calcium homeostasis By similarity.

Subunit structure

Interacts with GNAI2 and GNAI3. Ref.7

Subcellular location

Golgi apparatuscis-Golgi network membrane; Peripheral membrane protein; Lumenal side By similarity. Cytoplasm By similarity. Note: A small fraction of the protein may be cytoplasmic By similarity.

Tissue specificity

Expressed both in fetal and adult heart, lung, liver, kidney and brain, and in adult skeletal muscle, placenta and pancreas.

Domain

The EF-hand domains are unfolded in the absence of Ca2+ and fold upon Ca2+ addition.

Post-translational modification

O-glycosylated. Ref.9

Miscellaneous

Discovered as DNA-binding protein in the serum of lupus-prone mice.

Sequence similarities

Belongs to the nucleobindin family.

Contains 2 EF-hand domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB83EBI-2622179,EBI-6927928From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 461435Nucleobindin-1
PRO_0000004162

Regions

Domain240 – 27536EF-hand 1
Domain292 – 32736EF-hand 2
DNA binding172 – 21847 Potential
Calcium binding253 – 264121 Ref.10
Calcium binding305 – 316122 Ref.10
Region42 – 5110O-glycosylated at one site
Region228 – 32194Binds to GNAI2 and GNAI3 By similarity
Coiled coil150 – 21869 Potential
Coiled coil341 – 40767 Potential
Compositional bias401 – 4077Poly-Gln

Amino acid modifications

Modified residue861Phosphoserine By similarity
Modified residue3691Phosphoserine By similarity

Natural variations

Natural variant13 – 142LP → S.
VAR_012151
Natural variant3381M → V.
Corresponds to variant rs35456905 [ dbSNP | Ensembl ].
VAR_061087
Natural variant3991R → Q. Ref.2
VAR_012152

Experimental info

Sequence conflict299 – 3002HV → QL in AAA36383. Ref.1
Sequence conflict3851Q → K in AAA36383. Ref.1
Sequence conflict3851Q → K in AAB60431. Ref.2
Sequence conflict390 – 3912QQ → LL in AAA36383. Ref.1
Sequence conflict390 – 3912QQ → LL in AAB60431. Ref.2

Secondary structure

............. 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02818 [UniParc].

Last modified March 7, 2006. Version 4.
Checksum: 913C4B87C2A644C5

FASTA46153,879
        10         20         30         40         50         60 
MPPSGPRGTL LLLPLLLLLL LRAVLAVPLE RGAPNKEETP ATESPDTGLY YHRYLQEVID 

        70         80         90        100        110        120 
VLETDGHFRE KLQAANAEDI KSGKLSRELD FVSHHVRTKL DELKRQEVSR LRMLLKAKMD 

       130        140        150        160        170        180 
AEQDPNVQVD HLNLLKQFEH LDPQNQHTFE ARDLELLIQT ATRDLAQYDA AHHEEFKRYE 

       190        200        210        220        230        240 
MLKEHERRRY LESLGEEQRK EAERKLEEQQ RRHREHPKVN VPGSQAQLKE VWEELDGLDP 

       250        260        270        280        290        300 
NRFNPKTFFI LHDINSDGVL DEQELEALFT KELEKVYDPK NEEDDMREME EERLRMREHV 

       310        320        330        340        350        360 
MKNVDTNQDR LVTLEEFLAS TQRKEFGDTG EGWETVEMHP AYTEEELRRF EEELAAREAE 

       370        380        390        400        410        420 
LNAKAQRLSQ ETEALGRSQG RLEAQKRELQ QAVLHMEQRK QQQQQQQGHK APAAHPEGQL 

       430        440        450        460 
KFHPDTDDVP VPAPAGDQKE VDTSEKKLLE RLPEVEVPQH L 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of nucleobindin, a novel DNA-binding protein that contains both a signal peptide and a leucine zipper structure."
Miura K., Titani K., Kurosawa Y., Kanai Y.
Biochem. Biophys. Res. Commun. 187:375-380(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Organization of the human gene for nucleobindin (NUC) and its chromosomal assignment to 19q13.2-q13.4."
Miura K., Hirai M., Kanai Y., Kurosawa Y.
Genomics 34:181-186(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS 13-LEU-PRO-14 DELINS SER AND GLN-399, SEQUENCE REVISION TO 299-300.
Tissue: Placenta.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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. expand/collapse author list , 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: Umbilical cord blood.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Lung.
[7]"Interaction of the protein nucleobindin with G alpha i2, as revealed by the yeast two-hybrid system."
Mochizuki N., Hibi M., Kanai Y., Insel P.A.
FEBS Lett. 373:155-158(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, INTERACTION WITH GNAI2.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Structural studies on the Ca2+-binding domain of human nucleobindin (Calnuc)."
de Alba E., Tjandra N.
Biochemistry 43:10039-10049(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 228-326, CALCIUM-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96824 mRNA. Translation: AAA36383.1.
U31342 expand/collapse EMBL AC list , U31336, U31337, U31338, U31340, U31341 Genomic DNA. Translation: AAB60431.1.
BT009828 mRNA. Translation: AAP88830.1.
AK315422 mRNA. Translation: BAG37811.1.
CH471177 Genomic DNA. Translation: EAW52411.1.
BC002356 mRNA. Translation: AAH02356.1.
CCDSCCDS12740.1.
RefSeqNP_006175.2. NM_006184.5.
UniGeneHs.631602.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SNLNMR-A228-326[»]
ProteinModelPortalQ02818.
SMRQ02818. Positions 228-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110978. 19 interactions.
IntActQ02818. 15 interactions.
MINTMINT-2805455.
STRING9606.ENSP00000263273.

PTM databases

PhosphoSiteQ02818.

Polymorphism databases

DMDM90110780.

Proteomic databases

MaxQBQ02818.
PaxDbQ02818.
PRIDEQ02818.

Protocols and materials databases

DNASU4924.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263273; ENSP00000263273; ENSG00000104805.
ENST00000405315; ENSP00000385923; ENSG00000104805.
ENST00000407032; ENSP00000385211; ENSG00000104805.
GeneID4924.
KEGGhsa:4924.
UCSCuc002pla.3. human.

Organism-specific databases

CTD4924.
GeneCardsGC19P049403.
HGNCHGNC:8043. NUCB1.
HPAHPA008176.
MIM601323. gene.
neXtProtNX_Q02818.
PharmGKBPA31825.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262100.
HOGENOMHOG000007216.
HOVERGENHBG052685.
InParanoidQ02818.
OMAMDAEQEP.
OrthoDBEOG7WQ7SZ.
PhylomeDBQ02818.
TreeFamTF323218.

Gene expression databases

ArrayExpressQ02818.
BgeeQ02818.
CleanExHS_NUCB1.
GenevestigatorQ02818.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNUCB1. human.
EvolutionaryTraceQ02818.
GeneWikiNUCB1.
GenomeRNAi4924.
NextBio18963.
PROQ02818.
SOURCESearch...

Entry information

Entry nameNUCB1_HUMAN
AccessionPrimary (citable) accession number: Q02818
Secondary accession number(s): B2RD64 expand/collapse secondary AC list , Q15838, Q7Z4J7, Q9BUR1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM