Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BUN5 (CC28B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coiled-coil domain-containing protein 28B
Gene names
Name:CCDC28B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in ciliogenesis. Regulates cilia length through its interaction with MAPKAP1/SIN1 but independently of mTORC2 complex. Modulates mTORC2 complex assembly and function, possibly enhances AKT1 phosphorylation. Does not seem to modulate assembly and function of mTORC1 complex. Ref.8 Ref.9

Subunit structure

Interacts with BBS1, BBS2, BBS4, BBS5, BBS6, BBS7 and TTC8/BBS8. Interacts with MAPKAP1/SIN1 isoform 1 and RICTOR. Ref.5 Ref.9

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: It localizes near centrosomes and basal bodies. Ref.5

Involvement in disease

Bardet-Biedl syndrome (BBS) [MIM:209900]: A syndrome characterized by usually severe pigmentary retinopathy, early-onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease.
Note: The gene represented in this entry acts as a disease modifier. Ref.5

Sequence caution

The sequence CAI22057.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseBardet-Biedl syndrome
Ciliopathy
Obesity
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcilium assembly

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from direct assay Ref.5. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BUN5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BUN5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     183-200: IQKLHLAENAEPEEQSAA → MYPFQGTRLC...RYRNLEFPQN

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200Coiled-coil domain-containing protein 28B
PRO_0000234094

Regions

Coiled coil158 – 18326 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7
Modified residue461Phosphoserine Ref.6

Natural variations

Alternative sequence183 – 20018IQKLH…EQSAA → MYPFQGTRLCVCVPERSVSS SPALQEYSHTTNFPTSCSPV RFSHRLPKPRYRNLEFPQN in isoform 2.
VSP_046552
Natural variant251R → W.
Corresponds to variant rs1407134 [ dbSNP | Ensembl ].
VAR_056776

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 13, 2009. Version 2.
Checksum: 3D6128251CF41148

FASTA20022,037
        10         20         30         40         50         60 
MDDKKKKRSP KPCLAQPAQA PGTLRRVPVP TSHSGSLALG LPHLPSPKQR AKFKRVGKEK 

        70         80         90        100        110        120 
CRPVLAGGGS GSAGTPLQHS FLTEVTDVYE MEGGLLNLLN DFHSGRLQAF GKECSFEQLE 

       130        140        150        160        170        180 
HVREMQEKLA RLHFSLDVCG EEEDDEEEED GVTEGLPEEQ KKTMADRNLD QLLSNLEDLS 

       190        200 
NSIQKLHLAE NAEPEEQSAA 

« Hide

Isoform 2 [UniParc].

Checksum: E0490FDCC778F887
Show »

FASTA24126,904

References

« Hide 'large scale' references
[1]"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] (ISOFORM 1).
Tissue: Skeletal muscle.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1 AND 2).
Tissue: Lung and Retinoblastoma.
[5]"Dissection of epistasis in oligogenic Bardet-Biedl syndrome."
Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S., Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.
Nature 439:326-330(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BBS1; BBS2; BBS4; BBS5; BBS6; BBS7 AND BBS8, SUBCELLULAR LOCATION, INVOLVEMENT AS MODIFIER GENE IN BBS.
[6]"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-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Characterization of CCDC28B reveals its role in ciliogenesis and provides insight to understand its modifier effect on Bardet-Biedl syndrome."
Cardenas-Rodriguez M., Osborn D.P., Irigoin F., Grana M., Romero H., Beales P.L., Badano J.L.
Hum. Genet. 132:91-105(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CILIOGENESIS.
[9]"The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2 function and interacts with SIN1 to control cilia length independently of the mTOR complex."
Cardenas-Rodriguez M., Irigoin F., Osborn D.P., Gascue C., Katsanis N., Beales P.L., Badano J.L.
Hum. Mol. Genet. 22:4031-4042(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPKAP1 AND RICTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK291904 mRNA. Translation: BAF84593.1.
AL049795 Genomic DNA. Translation: CAB75616.1.
AL049795 Genomic DNA. Translation: CAI22057.1. Sequence problems.
CH471059 Genomic DNA. Translation: EAX07564.1.
BC002462 mRNA. No translation available.
BC022848 mRNA. Translation: AAH22848.1.
CCDSCCDS354.2. [Q9BUN5-1]
RefSeqNP_077272.2. NM_024296.3. [Q9BUN5-1]
XP_006710955.1. XM_006710892.1. [Q9BUN5-3]
UniGeneHs.534482.

3D structure databases

ProteinModelPortalQ9BUN5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122560. 2 interactions.
DIPDIP-60361N.
STRING9606.ENSP00000362704.

PTM databases

PhosphoSiteQ9BUN5.

Polymorphism databases

DMDM261260055.

Proteomic databases

MaxQBQ9BUN5.
PaxDbQ9BUN5.
PRIDEQ9BUN5.

Protocols and materials databases

DNASU79140.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373602; ENSP00000362704; ENSG00000160050. [Q9BUN5-1]
ENST00000421922; ENSP00000413017; ENSG00000160050. [Q9BUN5-3]
GeneID79140.
KEGGhsa:79140.
UCSCuc001bul.1. human. [Q9BUN5-1]

Organism-specific databases

CTD79140.
GeneCardsGC01P032666.
HGNCHGNC:28163. CCDC28B.
HPAHPA028403.
HPA028589.
MIM209900. phenotype.
610162. gene.
neXtProtNX_Q9BUN5.
PharmGKBPA142672186.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40385.
HOGENOMHOG000231321.
HOVERGENHBG061498.
InParanoidQ9BUN5.
OMADVREMEG.
OrthoDBEOG7ZPNMD.
PhylomeDBQ9BUN5.
TreeFamTF323549.

Gene expression databases

ArrayExpressQ9BUN5.
BgeeQ9BUN5.
CleanExHS_CCDC28B.
GenevestigatorQ9BUN5.

Family and domain databases

InterProIPR025271. DUF4061.
[Graphical view]
PfamPF13270. DUF4061. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCCDC28B. human.
GeneWikiCCDC28B.
GenomeRNAi79140.
NextBio68021.
PROQ9BUN5.
SOURCESearch...

Entry information

Entry nameCC28B_HUMAN
AccessionPrimary (citable) accession number: Q9BUN5
Secondary accession number(s): A8K789, Q8TBV8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 13, 2009
Last modified: July 9, 2014
This is version 95 of the entry and version 2 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM