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Q9HB71 (CYBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. 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:
Calcyclin-binding protein

Short name=CacyBP
Short name=hCacyBP
Alternative name(s):
S100A6-binding protein
Siah-interacting protein
Gene names
Name:CACYBP
Synonyms:S100A6BP, SIP
ORF Names:PNAS-107
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1). Ref.20

Subunit structure

Homodimer. Interacts with proteins of the S100 family S100A1, S100A6, S100B, S100P and S100A12 in a calcium-dependent manner By similarity. Component of some large E3 complex at least composed of UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts directly with SIAH1, SIAH2 and SKP1. Ref.12 Ref.20

Subcellular location

Nucleus. Cytoplasm. Note: Cytoplasmic at low calcium concentrations. In neuroblastoma cells, after a retinoic acid (RA) induction and calcium increase, it localizes in both the nucleus and cytoplasm. The nuclear fraction may be phosphorylated. Ref.13

Post-translational modification

Phosphorylated on serine residues. Phosphorylated upon induction by RA or at high calcium concentrations. Ref.13

Sequence similarities

Contains 1 CS domain.

Contains 1 SGS domain.

Sequence caution

The sequence AAG23817.1 differs from that shown. Reason: Frameshift at position 203.

The sequence BAG52713.1 differs from that shown. Reason: Frameshift at position 3.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HB71-1)

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: Q9HB71-2)

Also known as: SIP-S; S;

The sequence of this isoform differs from the canonical sequence as follows:
     73-80: VKISNYGW → DGISQISL
     81-228: Missing.
Isoform 3 (identifier: Q9HB71-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10 Ref.11
Chain2 – 228227Calcyclin-binding protein
PRO_0000185389

Regions

Domain73 – 16795CS
Domain168 – 22861SGS
Region2 – 8079Interaction with SIAH1
Region73 – 228156Interaction with SKP1
Region154 – 22875Interaction with S100A6 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.11 Ref.14 Ref.16 Ref.18 Ref.19
Modified residue81N6-acetyllysine Ref.16
Modified residue191N6-acetyllysine Ref.16
Modified residue851N6-acetyllysine Ref.16
Modified residue1181N6-acetyllysine Ref.16

Natural variations

Alternative sequence1 – 4343Missing in isoform 3.
VSP_046862
Alternative sequence73 – 808VKISNYGW → DGISQISL in isoform 2.
VSP_010171
Alternative sequence81 – 228148Missing in isoform 2.
VSP_010172

Experimental info

Mutagenesis23 – 264KRVR → AAVA: Abolishes interaction with SIAH1. Ref.20
Mutagenesis641V → N: Abolishes interaction with SIAH1; when associated with N-66. Ref.20
Mutagenesis661P → N: Abolishes interaction with SIAH1; when associated with N-64. Ref.20
Sequence conflict441M → V in AAG23817. Ref.4
Sequence conflict1771E → K in AAG23817. Ref.4
Sequence conflict1831T → P in AAG23817. Ref.4
Sequence conflict2261T → P in AAG23817. Ref.4

Secondary structure

.................................. 228
Helix Strand Turn

Details...

Sequences

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

Last modified April 26, 2004. Version 2.
Checksum: 88C822FB14A7EF89

FASTA22826,210
        10         20         30         40         50         60 
MASEELQKDL EEVKVLLEKA TRKRVRDALT AEKSKIETEI KNKMQQKSQK KAELLDNEKP 

        70         80         90        100        110        120 
AAVVAPITTG YTVKISNYGW DQSDKFVKIY ITLTGVHQVP TENVQVHFTE RSFDLLVKNL 

       130        140        150        160        170        180 
NGKSYSMIVN NLLKPISVEG SSKKVKTDTV LILCRKKVEN TRWDYLTQVE KECKEKEKPS 

       190        200        210        220 
YDTETDPSEG LMNVLKKIYE DGDDDMKRTI NKAWVESREK QAKGDTEF 

« Hide

Isoform 2 (SIP-S) (S) [UniParc].

Checksum: 13A2FAC2429FA9FD
Show »

FASTA808,956
Isoform 3 [UniParc].

Checksum: 99286837B26B2395
Show »

FASTA18521,228

References

« Hide 'large scale' references
[1]"Cloning and expression of human calcyclin binding protein (hCacyBP) gene."
Liu W.X., Wu J., Zhao Z., Zhou Y., Peng X.Z., Yuan J.G., Qiang B.Q.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:181-186(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"Amplification and overexpression of the gene encoding the human calcyclin binding protein on chromosome 1q24-q25 in advanced lung carcinomas."
Petersen S., Schluens K., Dietel M., Petersen I.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Rhodes S.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Human acute promyelocytic leukemia cell line NB4's apoptosis related genes."
Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Promyelocytic leukemia.
[5]"Identification of a human growth inhibition gene 5 (GIG5)."
Kim J.W.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"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] (ISOFORMS 1 AND 3).
Tissue: Skeletal muscle and Testis.
[7]"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].
[8]Mural R.J., Istrail S., Sutton 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].
[9]"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] (ISOFORM 1).
Tissue: Brain and Skin.
[10]Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14; 34-41; 112-118 AND 124-143, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma.
[11]Bienvenut W.V., Heiserich L., Gottlieb E.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-19 AND 112-118, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[12]"Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses."
Matsuzawa S., Reed J.C.
Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2), SUBUNIT OF A COMPLEX WITH UBE2D1; SIAH1; SKP1; APC AND TBL1X, INTERACTION WITH SIAH1; SIAH2 AND SKP1.
[13]"Translocation and phosphorylation of calcyclin binding protein during retinoic acid-induced neuronal differentiation of neuroblastoma SH-SY5Y cells."
Wu J., Tan X., Peng X.Z., Yuan J.G., Qiang B.Q.
J. Biochem. Mol. Biol. 36:354-358(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[14]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-8; LYS-19; LYS-85 AND LYS-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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].
[18]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex."
Santelli E., Leone M., Li C., Fukushima T., Preece N.E., Olson A.J., Ely K.R., Reed J.C., Pellecchia M., Liddington R.C., Matsuzawa S.
J. Biol. Chem. 280:34278-34287(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 1-70, SUBUNIT, MUTAGENESIS OF 23-LYS--ARG-26; VAL-64 AND PRO-66, FUNCTION, INTERACTION WITH SIAH1.
[21]"Solution structure of the core domain of calcyclin binding protein; SIAH-interacting protein (SIP)."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 63-176.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF057356 mRNA. Translation: AAC21458.1.
AF314752 mRNA. Translation: AAG34170.1.
AL035305 mRNA. Translation: CAA22910.1.
AF275803 mRNA. Translation: AAG23817.1. Frameshift.
AY423723 mRNA. Translation: AAS00486.1.
AK093425 mRNA. Translation: BAG52713.1. Frameshift.
AK313278 mRNA. Translation: BAG36086.1.
Z99127 Genomic DNA. Translation: CAI18938.1.
Z99127 Genomic DNA. Translation: CAQ52581.1.
CH471067 Genomic DNA. Translation: EAW90982.1.
BC005975 mRNA. Translation: AAH05975.1.
BC022352 mRNA. Translation: AAH22352.1.
BC078151 mRNA. Translation: AAH78151.1.
RefSeqNP_001007215.1. NM_001007214.1.
NP_055227.1. NM_014412.2.
XP_005245149.1. XM_005245092.1.
UniGeneHs.508524.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X5MNMR-A63-176[»]
2A25X-ray2.20B58-70[»]
2A26X-ray1.20A/B/C1-47[»]
ProteinModelPortalQ9HB71.
SMRQ9HB71. Positions 1-47, 61-180, 188-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118001. 31 interactions.
IntActQ9HB71. 16 interactions.
MINTMINT-200516.
STRING9606.ENSP00000356652.

PTM databases

PhosphoSiteQ9HB71.

Polymorphism databases

DMDM46576651.

2D gel databases

UCD-2DPAGEQ9HB71.

Proteomic databases

PaxDbQ9HB71.
PRIDEQ9HB71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367679; ENSP00000356652; ENSG00000116161. [Q9HB71-1]
ENST00000367681; ENSP00000356654; ENSG00000116161. [Q9HB71-3]
ENST00000405362; ENSP00000385771; ENSG00000116161. [Q9HB71-3]
ENST00000406752; ENSP00000384139; ENSG00000116161. [Q9HB71-2]
GeneID27101.
KEGGhsa:27101.
UCSCuc001gki.1. human. [Q9HB71-1]

Organism-specific databases

CTD27101.
GeneCardsGC01P174968.
HGNCHGNC:30423. CACYBP.
HPAHPA025753.
HPA057038.
MIM606186. gene.
neXtProtNX_Q9HB71.
PharmGKBPA134894213.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247905.
HOGENOMHOG000238284.
HOVERGENHBG003242.
InParanoidQ9HB71.
KOK04507.
OMAYAWDQSD.
OrthoDBEOG7K9K4J.
PhylomeDBQ9HB71.
TreeFamTF323891.

Gene expression databases

ArrayExpressQ9HB71.
BgeeQ9HB71.
CleanExHS_CACYBP.
GenevestigatorQ9HB71.

Family and domain databases

Gene3D2.60.40.790. 1 hit.
InterProIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007699. SGS.
IPR015120. Siah-Interact_N.
[Graphical view]
PfamPF04969. CS. 1 hit.
PF05002. SGS. 1 hit.
PF09032. Siah-Interact_N. 1 hit.
[Graphical view]
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS51203. CS. 1 hit.
PS51048. SGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCACYBP. human.
EvolutionaryTraceQ9HB71.
GeneWikiCACYBP.
GenomeRNAi27101.
NextBio49757.
PROQ9HB71.
SOURCESearch...

Entry information

Entry nameCYBP_HUMAN
AccessionPrimary (citable) accession number: Q9HB71
Secondary accession number(s): B2ZWH2 expand/collapse secondary AC list , B3KSF1, O60666, Q5R370, Q5R371
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: April 16, 2014
This is version 120 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

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 chromosome 1

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