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P50991

- TCPD_HUMAN

UniProt

P50991 - TCPD_HUMAN

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Protein

T-complex protein 1 subunit delta

Gene

CCT4

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

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin.1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB
  3. unfolded protein binding Source: ProtInc

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: Reactome
  2. binding of sperm to zona pellucida Source: Ensembl
  3. cellular protein metabolic process Source: Reactome
  4. protein folding Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_17050. Folding of actin by CCT/TriC.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit delta
Short name:
TCP-1-delta
Alternative name(s):
CCT-delta
Stimulator of TAR RNA-binding
Gene namesi
Name:CCT4
Synonyms:CCTD, SRB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:1617. CCT4.

Subcellular locationi

Cytoplasm. Melanosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

GO - Cellular componenti

  1. cell body Source: Ensembl
  2. centrosome Source: MGI
  3. chaperonin-containing T-complex Source: Ensembl
  4. cytoplasm Source: HPA
  5. cytosol Source: Reactome
  6. extracellular vesicular exosome Source: UniProtKB
  7. microtubule Source: UniProtKB
  8. nucleus Source: HPA
  9. zona pellucida receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26181.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 539538T-complex protein 1 subunit deltaPRO_0000128332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211N6-acetyllysineBy similarity
Modified residuei288 – 2881N6-acetyllysine1 Publication
Modified residuei302 – 3021N6-acetyllysine1 Publication
Modified residuei319 – 3191N6-acetyllysine1 Publication
Modified residuei326 – 3261N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP50991.
PaxDbiP50991.
PeptideAtlasiP50991.
PRIDEiP50991.

2D gel databases

REPRODUCTION-2DPAGEIPI00302927.
UCD-2DPAGEP50991.

PTM databases

PhosphoSiteiP50991.

Miscellaneous databases

PMAP-CutDBP50991.

Expressioni

Gene expression databases

BgeeiP50991.
CleanExiHS_CCT4.
ExpressionAtlasiP50991. baseline and differential.
GenevestigatoriP50991.

Organism-specific databases

HPAiHPA029349.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Interacts with DYX1C1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
OLR1P783803EBI-356876,EBI-7151999

Protein-protein interaction databases

BioGridi115826. 99 interactions.
DIPiDIP-32971N.
IntActiP50991. 46 interactions.
MINTiMINT-1157924.
STRINGi9606.ENSP00000377958.

Structurei

3D structure databases

ProteinModelPortaliP50991.
SMRiP50991. Positions 18-539.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiCOG0459.
GeneTreeiENSGT00550000074956.
HOGENOMiHOG000226735.
HOVERGENiHBG106507.
InParanoidiP50991.
KOiK09496.
OMAiPCAKMLV.
OrthoDBiEOG722J8B.
PhylomeDBiP50991.
TreeFamiTF106332.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012717. Chap_CCT_delta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02342. chap_CCT_delta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P50991-1) [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
MPENVAPRSG ATAGAAGGRG KGAYQDRDKP AQIRFSNISA AKAVADAIRT
60 70 80 90 100
SLGPKGMDKM IQDGKGDVTI TNDGATILKQ MQVLHPAARM LVELSKAQDI
110 120 130 140 150
EAGDGTTSVV IIAGSLLDSC TKLLQKGIHP TIISESFQKA LEKGIEILTD
160 170 180 190 200
MSRPVELSDR ETLLNSATTS LNSKVVSQYS SLLSPMSVNA VMKVIDPATA
210 220 230 240 250
TSVDLRDIKI VKKLGGTIDD CELVEGLVLT QKVSNSGITR VEKAKIGLIQ
260 270 280 290 300
FCLSAPKTDM DNQIVVSDYA QMDRVLREER AYILNLVKQI KKTGCNVLLI
310 320 330 340 350
QKSILRDALS DLALHFLNKM KIMVIKDIER EDIEFICKTI GTKPVAHIDQ
360 370 380 390 400
FTADMLGSAE LAEEVNLNGS GKLLKITGCA SPGKTVTIVV RGSNKLVIEE
410 420 430 440 450
AERSIHDALC VIRCLVKKRA LIAGGGAPEI ELALRLTEYS RTLSGMESYC
460 470 480 490 500
VRAFADAMEV IPSTLAENAG LNPISTVTEL RNRHAQGEKT AGINVRKGGI
510 520 530
SNILEELVVQ PLLVSVSALT LATETVRSIL KIDDVVNTR
Length:539
Mass (Da):57,924
Last modified:January 23, 2007 - v4
Checksum:i39913C0D0735180D
GO
Isoform 2 (identifier: P50991-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     60-89: Missing.

Note: No experimental confirmation available.

Show »
Length:509
Mass (Da):54,720
Checksum:i53EDE4CD2799D28B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti435 – 4351R → A in AAC50384. (PubMed:8626763)Curated
Sequence conflicti531 – 5311K → R in BAH13897. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121I → V.
Corresponds to variant rs2272428 [ dbSNP | Ensembl ].
VAR_052266

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei60 – 8930Missing in isoform 2. 1 PublicationVSP_045537Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38846 mRNA. Translation: AAC50384.1.
AF026291 mRNA. Translation: AAC96010.1.
AK303082 mRNA. Translation: BAH13897.1.
AK312586 mRNA. Translation: BAG35480.1.
AC107081 Genomic DNA. Translation: AAY24140.1.
BC014676 mRNA. Translation: AAH14676.1.
BC106934 mRNA. Translation: AAI06935.1.
BC106933 mRNA. Translation: AAI06934.1.
CCDSiCCDS33206.1. [P50991-1]
CCDS58711.1. [P50991-2]
RefSeqiNP_001243650.1. NM_001256721.1. [P50991-2]
NP_006421.2. NM_006430.3. [P50991-1]
UniGeneiHs.421509.

Genome annotation databases

EnsembliENST00000394440; ENSP00000377958; ENSG00000115484. [P50991-1]
ENST00000544079; ENSP00000443061; ENSG00000115484. [P50991-2]
GeneIDi10575.
KEGGihsa:10575.
UCSCiuc002sbo.4. human. [P50991-1]

Polymorphism databases

DMDMi52001478.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38846 mRNA. Translation: AAC50384.1 .
AF026291 mRNA. Translation: AAC96010.1 .
AK303082 mRNA. Translation: BAH13897.1 .
AK312586 mRNA. Translation: BAG35480.1 .
AC107081 Genomic DNA. Translation: AAY24140.1 .
BC014676 mRNA. Translation: AAH14676.1 .
BC106934 mRNA. Translation: AAI06935.1 .
BC106933 mRNA. Translation: AAI06934.1 .
CCDSi CCDS33206.1. [P50991-1 ]
CCDS58711.1. [P50991-2 ]
RefSeqi NP_001243650.1. NM_001256721.1. [P50991-2 ]
NP_006421.2. NM_006430.3. [P50991-1 ]
UniGenei Hs.421509.

3D structure databases

ProteinModelPortali P50991.
SMRi P50991. Positions 18-539.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115826. 99 interactions.
DIPi DIP-32971N.
IntActi P50991. 46 interactions.
MINTi MINT-1157924.
STRINGi 9606.ENSP00000377958.

PTM databases

PhosphoSitei P50991.

Polymorphism databases

DMDMi 52001478.

2D gel databases

REPRODUCTION-2DPAGE IPI00302927.
UCD-2DPAGE P50991.

Proteomic databases

MaxQBi P50991.
PaxDbi P50991.
PeptideAtlasi P50991.
PRIDEi P50991.

Protocols and materials databases

DNASUi 10575.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000394440 ; ENSP00000377958 ; ENSG00000115484 . [P50991-1 ]
ENST00000544079 ; ENSP00000443061 ; ENSG00000115484 . [P50991-2 ]
GeneIDi 10575.
KEGGi hsa:10575.
UCSCi uc002sbo.4. human. [P50991-1 ]

Organism-specific databases

CTDi 10575.
GeneCardsi GC02M062095.
HGNCi HGNC:1617. CCT4.
HPAi HPA029349.
MIMi 605142. gene.
neXtProti NX_P50991.
PharmGKBi PA26181.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0459.
GeneTreei ENSGT00550000074956.
HOGENOMi HOG000226735.
HOVERGENi HBG106507.
InParanoidi P50991.
KOi K09496.
OMAi PCAKMLV.
OrthoDBi EOG722J8B.
PhylomeDBi P50991.
TreeFami TF106332.

Enzyme and pathway databases

Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_17050. Folding of actin by CCT/TriC.

Miscellaneous databases

ChiTaRSi CCT4. human.
GeneWikii CCT4.
GenomeRNAii 10575.
NextBioi 40137.
PMAP-CutDB P50991.
PROi P50991.
SOURCEi Search...

Gene expression databases

Bgeei P50991.
CleanExi HS_CCT4.
ExpressionAtlasi P50991. baseline and differential.
Genevestigatori P50991.

Family and domain databases

Gene3Di 1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProi IPR012717. Chap_CCT_delta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view ]
PANTHERi PTHR11353. PTHR11353. 1 hit.
Pfami PF00118. Cpn60_TCP1. 1 hit.
[Graphical view ]
PRINTSi PR00304. TCOMPLEXTCP1.
SUPFAMi SSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsi TIGR02342. chap_CCT_delta. 1 hit.
PROSITEi PS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA."
    Wu-Baer F., Lane W.S., Gaynor R.B.
    J. Biol. Chem. 271:4201-4208(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  2. "Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT."
    Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.
    Mol. Cell. Biol. 18:7584-7589(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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: Brain and Thymus.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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] (ISOFORM 1).
    Tissue: Brain.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8.
    Tissue: Platelet.
  7. Bienvenut W.V., Barblan J., Quadroni M.
    Submitted (MAR-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 420-435, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  8. "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
    Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
    J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PACRG.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  10. "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 LYS-288; LYS-302; LYS-319 AND LYS-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly."
    Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., Sheffield V.C.
    Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN BBS/CCT COMPLEX.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCPD_HUMAN
AccessioniPrimary (citable) accession number: P50991
Secondary accession number(s): B2R6I3
, B7Z8B1, F5H5W3, O14870, Q53QP9, Q96C51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 141 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3