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Protein

Bicaudal D-related protein 1

Gene

CCDC64

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Component of secretory vesicle machinery in developing neurons that acts as a regulator of neurite outgrowth. Regulates the secretory vesicle transport by controlling the accumulation of Rab6-containing secretory vesicles in the pericentrosomal region restricting anterograde secretory transport during the early phase of neuronal differentiation, thereby inhibiting neuritogenesis (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Neurogenesis, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Bicaudal D-related protein 1
Short name:
BICD-related protein 1
Short name:
BICDR-1
Alternative name(s):
Coiled-coil domain-containing protein 64A
Gene namesi
Name:CCDC64
Synonyms:BICDR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:28095. CCDC64.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485416.

Polymorphism and mutation databases

BioMutaiCCDC64.
DMDMi313104078.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 573573Bicaudal D-related protein 1PRO_0000302858Add
BLAST

Proteomic databases

EPDiQ6ZP65.
PaxDbiQ6ZP65.
PeptideAtlasiQ6ZP65.
PRIDEiQ6ZP65.

PTM databases

iPTMnetiQ6ZP65.
PhosphoSiteiQ6ZP65.

Expressioni

Gene expression databases

BgeeiQ6ZP65.
CleanExiHS_CCDC64.
ExpressionAtlasiQ6ZP65. baseline and differential.
GenevisibleiQ6ZP65. HS.

Organism-specific databases

HPAiHPA043908.
HPA061116.

Interactioni

Subunit structurei

Interacts with KIF1C. Interacts with RAB6A and RAB6B; interaction is specific to Rab6 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi124955. 1 interaction.
IntActiQ6ZP65. 1 interaction.
STRINGi9606.ENSP00000380690.

Structurei

3D structure databases

ProteinModelPortaliQ6ZP65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili118 – 376259Sequence analysisAdd
BLAST
Coiled coili440 – 52586Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the BICDR family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IHTB. Eukaryota.
ENOG410ZH4K. LUCA.
GeneTreeiENSGT00560000077255.
HOGENOMiHOG000015285.
HOVERGENiHBG097778.
InParanoidiQ6ZP65.
KOiK16756.
OMAiCMELPAG.
OrthoDBiEOG7KSX8N.
PhylomeDBiQ6ZP65.
TreeFamiTF326671.

Family and domain databases

InterProiIPR006933. HAP1_N.
[Graphical view]
PfamiPF04849. HAP1_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZP65-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSAFCLGLVG RASAPAEPDS ACCMELPAAA GDAVRSPAAA AALIFPGGSG
60 70 80 90 100
ELELALEEEL ALLAAGERPS DPGEHPQAEP GSLAEGAGPQ PPPSQDPELL
110 120 130 140 150
SVIRQKEKDL VLAARLGKAL LERNQDMSRQ YEQMHKELTD KLEHLEQEKH
160 170 180 190 200
ELRRRFENRE GEWEGRVSEL ESDVKQLQDE LERQQIHLRE ADREKSRAVQ
210 220 230 240 250
ELSEQNQRLL DQLSRASEVE RQLSMQVHAL REDFREKNSS TNQHIIRLES
260 270 280 290 300
LQAEIKMLSD RKRELEHRLS ATLEENDLLQ GTVEELQDRV LILERQGHDK
310 320 330 340 350
DLQLHQSQLE LQEVRLSCRQ LQVKVEELTE ERSLQSSAAT STSLLSEIEQ
360 370 380 390 400
SMEAEELEQE REQLRLQLWE AYCQVRYLCS HLRGNDSADS AVSTDSSMDE
410 420 430 440 450
SSETSSAKDV PAGSLRTALN ELKRLIQSIV DGMEPTVTLL SVEMTALKEE
460 470 480 490 500
RDRLRVTSED KEPKEQLQKA IRDRDEAIAK KNAVELELAK CRMDMMSLNS
510 520 530 540 550
QLLDAIQQKL NLSQQLEAWQ DDMHRVIDRQ LMDTHLKERS QPAAALCRGH
560 570
SAGRGDEPSI AEGKRLFSFF RKI
Length:573
Mass (Da):64,841
Last modified:November 30, 2010 - v2
Checksum:iF514AF0264B13F09
GO
Isoform 2 (identifier: Q6ZP65-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-351: Missing.
     436-436: T → TGSRRLDDDSLEEQIRQTSEDSRALRELMEGERGKLRQSLEELQRLHSQ

Note: No experimental confirmation available.
Show »
Length:270
Mass (Da):30,943
Checksum:i879683EF4FDD3DF0
GO

Sequence cautioni

The sequence AAC83181.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAC85259.1 differs from that shown.Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 9719Missing in BAC85259 (PubMed:14702039).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 351351Missing in isoform 2. 1 PublicationVSP_056941Add
BLAST
Alternative sequencei436 – 4361T → TGSRRLDDDSLEEQIRQTSE DSRALRELMEGERGKLRQSL EELQRLHSQ in isoform 2. 1 PublicationVSP_056942

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129960 mRNA. Translation: BAC85259.1. Sequence problems.
AK301580 mRNA. Translation: BAG63072.1.
AC004812 Genomic DNA. Translation: AAC83181.1. Sequence problems.
AC004815 Genomic DNA. No translation available.
CCDSiCCDS41845.1. [Q6ZP65-1]
RefSeqiNP_997194.2. NM_207311.2. [Q6ZP65-1]
UniGeneiHs.369763.

Genome annotation databases

EnsembliENST00000397558; ENSP00000380690; ENSG00000135127. [Q6ZP65-1]
GeneIDi92558.
KEGGihsa:92558.
UCSCiuc001txl.2. human. [Q6ZP65-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129960 mRNA. Translation: BAC85259.1. Sequence problems.
AK301580 mRNA. Translation: BAG63072.1.
AC004812 Genomic DNA. Translation: AAC83181.1. Sequence problems.
AC004815 Genomic DNA. No translation available.
CCDSiCCDS41845.1. [Q6ZP65-1]
RefSeqiNP_997194.2. NM_207311.2. [Q6ZP65-1]
UniGeneiHs.369763.

3D structure databases

ProteinModelPortaliQ6ZP65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124955. 1 interaction.
IntActiQ6ZP65. 1 interaction.
STRINGi9606.ENSP00000380690.

PTM databases

iPTMnetiQ6ZP65.
PhosphoSiteiQ6ZP65.

Polymorphism and mutation databases

BioMutaiCCDC64.
DMDMi313104078.

Proteomic databases

EPDiQ6ZP65.
PaxDbiQ6ZP65.
PeptideAtlasiQ6ZP65.
PRIDEiQ6ZP65.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397558; ENSP00000380690; ENSG00000135127. [Q6ZP65-1]
GeneIDi92558.
KEGGihsa:92558.
UCSCiuc001txl.2. human. [Q6ZP65-1]

Organism-specific databases

CTDi92558.
GeneCardsiCCDC64.
HGNCiHGNC:28095. CCDC64.
HPAiHPA043908.
HPA061116.
neXtProtiNX_Q6ZP65.
PharmGKBiPA143485416.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHTB. Eukaryota.
ENOG410ZH4K. LUCA.
GeneTreeiENSGT00560000077255.
HOGENOMiHOG000015285.
HOVERGENiHBG097778.
InParanoidiQ6ZP65.
KOiK16756.
OMAiCMELPAG.
OrthoDBiEOG7KSX8N.
PhylomeDBiQ6ZP65.
TreeFamiTF326671.

Miscellaneous databases

ChiTaRSiCCDC64. human.
GenomeRNAii92558.
PROiQ6ZP65.

Gene expression databases

BgeeiQ6ZP65.
CleanExiHS_CCDC64.
ExpressionAtlasiQ6ZP65. baseline and differential.
GenevisibleiQ6ZP65. HS.

Family and domain databases

InterProiIPR006933. HAP1_N.
[Graphical view]
PfamiPF04849. HAP1_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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 2).
    Tissue: Kidney and Mammary gland.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiBICR1_HUMAN
AccessioniPrimary (citable) accession number: Q6ZP65
Secondary accession number(s): A8MUC8
, B4DWL0, B5MDJ0, O95000
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 30, 2010
Last modified: July 6, 2016
This is version 85 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. 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.