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Q9ULV4

- COR1C_HUMAN

UniProt

Q9ULV4 - COR1C_HUMAN

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Protein

Coronin-1C

Gene

CORO1C

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

Functioni

May be involved in cytokinesis, motility, and signal transduction.By similarity
Isoform 3: Involved in myogenic differentiation.

GO - Molecular functioni

  1. actin filament binding Source: RefGenome

GO - Biological processi

  1. actin cytoskeleton organization Source: RefGenome
  2. phagocytosis Source: ProtInc
  3. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

SignaLinkiQ9ULV4.

Names & Taxonomyi

Protein namesi
Recommended name:
Coronin-1C
Alternative name(s):
Coronin-3
hCRNN4
Gene namesi
Name:CORO1C
Synonyms:CRN2, CRNN4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:2254. CORO1C.

Subcellular locationi

Cell membrane 1 Publication. Cell projectionlamellipodium 1 Publication. Cytoplasmcytoskeleton 1 Publication
Note: All isoforms localize in a diffuse and punctate pattern in the cytosol and are highly enriched in F-actin-rich areas. Isoform 3 colocalizes with the thin filaments of the sarcomere and with the postsynaptic area and the junctional sarcoplasm of motor end plates.

GO - Cellular componenti

  1. actin cytoskeleton Source: RefGenome
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB-KW
  4. focal adhesion Source: UniProtKB
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26770.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474Coronin-1CPRO_0000050926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei446 – 4461N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9ULV4.
PaxDbiQ9ULV4.
PeptideAtlasiQ9ULV4.
PRIDEiQ9ULV4.

2D gel databases

OGPiQ9ULV4.

PTM databases

PhosphoSiteiQ9ULV4.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9ULV4.
CleanExiHS_CORO1C.
ExpressionAtlasiQ9ULV4. baseline and differential.
GenevestigatoriQ9ULV4.

Organism-specific databases

HPAiHPA041737.

Interactioni

Subunit structurei

Binds F-actin. Isoform 1 and isoform 2 appear as homotrimers, while isoform 3 seems to exist as monomers.2 Publications

Protein-protein interaction databases

BioGridi117136. 47 interactions.
IntActiQ9ULV4. 11 interactions.
MINTiMINT-1145632.
STRINGi9606.ENSP00000261401.

Structurei

3D structure databases

ProteinModelPortaliQ9ULV4.
SMRiQ9ULV4. Positions 8-391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati78 – 11841WD 11 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati128 – 16841WD 21 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati172 – 20231WD 31 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati215 – 24935WD 41 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati263 – 30341WD 51 PublicationPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili436 – 474391 PublicationAdd
BLAST

Domaini

The C-terminal coiled-coil domain is essential for cortical membrane localization and oligomerization.

Sequence similaritiesi

Belongs to the WD repeat coronin family.Curated
Contains 5 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119195.
HOGENOMiHOG000166356.
HOVERGENiHBG059978.
InParanoidiQ9ULV4.
KOiK13886.
OMAiPKISMAS.
OrthoDBiEOG7J70FB.
PhylomeDBiQ9ULV4.
TreeFamiTF314280.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR027333. CORO1C.
IPR015505. Coronin.
IPR015048. DUF1899.
IPR015049. DUF1900.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR10856. PTHR10856. 1 hit.
PTHR10856:SF10. PTHR10856:SF10. 1 hit.
PfamiPF08953. DUF1899. 1 hit.
PF08954. DUF1900. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9ULV4-1) [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
MRRVVRQSKF RHVFGQAVKN DQCYDDIRVS RVTWDSSFCA VNPRFVAIII
60 70 80 90 100
EASGGGAFLV LPLHKTGRID KSYPTVCGHT GPVLDIDWCP HNDQVIASGS
110 120 130 140 150
EDCTVMVWQI PENGLTLSLT EPVVILEGHS KRVGIVAWHP TARNVLLSAG
160 170 180 190 200
CDNAIIIWNV GTGEALINLD DMHSDMIYNV SWNRNGSLIC TASKDKKVRV
210 220 230 240 250
IDPRKQEIVA EKEKAHEGAR PMRAIFLADG NVFTTGFSRM SERQLALWNP
260 270 280 290 300
KNMQEPIALH EMDTSNGVLL PFYDPDTSII YLCGKGDSSI RYFEITDESP
310 320 330 340 350
YVHYLNTFSS KEPQRGMGYM PKRGLDVNKC EIARFFKLHE RKCEPIIMTV
360 370 380 390 400
PRKSDLFQDD LYPDTAGPEA ALEAEEWFEG KNADPILISL KHGYIPGKNR
410 420 430 440 450
DLKVVKKNIL DSKPTANKKC DLISIPKKTT DTASVQNEAK LDEILKEIKS
460 470
IKDTICNQDE RISKLEQQMA KIAA
Length:474
Mass (Da):53,249
Last modified:May 1, 2000 - v1
Checksum:iC7256797C514BB53
GO
Isoform 2 (identifier: Q9ULV4-2) [UniParc]FASTAAdd to Basket

Also known as: CRN2i2

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRWKDTM

Show »
Length:480
Mass (Da):54,067
Checksum:i75590C081614A540
GO
Isoform 3 (identifier: Q9ULV4-3) [UniParc]FASTAAdd to Basket

Also known as: CRN2i3

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MYGPGSQLGKSGNNSWAKERGCSIACQGSLTSARLHAPSIGERPLSHMRWKDTM

Note: Exclusively expressed in well-differentiated myoblasts as well as in mature skeletal muscle.

Show »
Length:527
Mass (Da):58,947
Checksum:i11C115B9F0B8D722
GO

Sequence cautioni

The sequence CAB82406.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRWKDTM in isoform 2. 1 PublicationVSP_047727
Alternative sequencei1 – 11M → MYGPGSQLGKSGNNSWAKER GCSIACQGSLTSARLHAPSI GERPLSHMRWKDTM in isoform 3. 1 PublicationVSP_047728

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030656 mRNA. Translation: BAA83077.1.
AM849477 mRNA. Translation: CAO94662.1.
AM849478 mRNA. Translation: CAO94663.1.
AK096363 mRNA. Translation: BAG53274.1.
AL162070 mRNA. Translation: CAB82406.1. Different initiation.
AC007569 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97826.1.
BC002342 mRNA. Translation: AAH02342.1.
CCDSiCCDS61236.1. [Q9ULV4-3]
CCDS9120.1. [Q9ULV4-1]
RefSeqiNP_001098707.1. NM_001105237.2. [Q9ULV4-3]
NP_001263400.1. NM_001276471.1. [Q9ULV4-1]
NP_055140.1. NM_014325.3. [Q9ULV4-1]
UniGeneiHs.330384.

Genome annotation databases

EnsembliENST00000261401; ENSP00000261401; ENSG00000110880. [Q9ULV4-1]
ENST00000420959; ENSP00000394496; ENSG00000110880. [Q9ULV4-3]
ENST00000541050; ENSP00000438341; ENSG00000110880. [Q9ULV4-1]
ENST00000549772; ENSP00000447534; ENSG00000110880. [Q9ULV4-2]
GeneIDi23603.
KEGGihsa:23603.
UCSCiuc001tnj.4. human. [Q9ULV4-1]
uc009zva.4. human.

Polymorphism databases

DMDMi12643898.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030656 mRNA. Translation: BAA83077.1 .
AM849477 mRNA. Translation: CAO94662.1 .
AM849478 mRNA. Translation: CAO94663.1 .
AK096363 mRNA. Translation: BAG53274.1 .
AL162070 mRNA. Translation: CAB82406.1 . Different initiation.
AC007569 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97826.1 .
BC002342 mRNA. Translation: AAH02342.1 .
CCDSi CCDS61236.1. [Q9ULV4-3 ]
CCDS9120.1. [Q9ULV4-1 ]
RefSeqi NP_001098707.1. NM_001105237.2. [Q9ULV4-3 ]
NP_001263400.1. NM_001276471.1. [Q9ULV4-1 ]
NP_055140.1. NM_014325.3. [Q9ULV4-1 ]
UniGenei Hs.330384.

3D structure databases

ProteinModelPortali Q9ULV4.
SMRi Q9ULV4. Positions 8-391.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117136. 47 interactions.
IntActi Q9ULV4. 11 interactions.
MINTi MINT-1145632.
STRINGi 9606.ENSP00000261401.

PTM databases

PhosphoSitei Q9ULV4.

Polymorphism databases

DMDMi 12643898.

2D gel databases

OGPi Q9ULV4.

Proteomic databases

MaxQBi Q9ULV4.
PaxDbi Q9ULV4.
PeptideAtlasi Q9ULV4.
PRIDEi Q9ULV4.

Protocols and materials databases

DNASUi 23603.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261401 ; ENSP00000261401 ; ENSG00000110880 . [Q9ULV4-1 ]
ENST00000420959 ; ENSP00000394496 ; ENSG00000110880 . [Q9ULV4-3 ]
ENST00000541050 ; ENSP00000438341 ; ENSG00000110880 . [Q9ULV4-1 ]
ENST00000549772 ; ENSP00000447534 ; ENSG00000110880 . [Q9ULV4-2 ]
GeneIDi 23603.
KEGGi hsa:23603.
UCSCi uc001tnj.4. human. [Q9ULV4-1 ]
uc009zva.4. human.

Organism-specific databases

CTDi 23603.
GeneCardsi GC12M109038.
HGNCi HGNC:2254. CORO1C.
HPAi HPA041737.
MIMi 605269. gene.
neXtProti NX_Q9ULV4.
PharmGKBi PA26770.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00760000119195.
HOGENOMi HOG000166356.
HOVERGENi HBG059978.
InParanoidi Q9ULV4.
KOi K13886.
OMAi PKISMAS.
OrthoDBi EOG7J70FB.
PhylomeDBi Q9ULV4.
TreeFami TF314280.

Enzyme and pathway databases

SignaLinki Q9ULV4.

Miscellaneous databases

ChiTaRSi CORO1C. human.
GeneWikii CORO1C.
GenomeRNAii 23603.
NextBioi 35463400.
PROi Q9ULV4.
SOURCEi Search...

Gene expression databases

Bgeei Q9ULV4.
CleanExi HS_CORO1C.
ExpressionAtlasi Q9ULV4. baseline and differential.
Genevestigatori Q9ULV4.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR027333. CORO1C.
IPR015505. Coronin.
IPR015048. DUF1899.
IPR015049. DUF1900.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
PANTHERi PTHR10856. PTHR10856. 1 hit.
PTHR10856:SF10. PTHR10856:SF10. 1 hit.
Pfami PF08953. DUF1899. 1 hit.
PF08954. DUF1900. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view ]
SMARTi SM00320. WD40. 3 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and chromosomal assignment of a novel human gene, CORO1C, homologous to coronin-like actin-binding proteins."
    Iizaka M., Han H.-J., Akashi H., Furukawa Y., Nakajima Y., Sugano S., Ogawa M., Nakamura Y.
    Cytogenet. Cell Genet. 88:221-224(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION (ISOFORM 3), ALTERNATIVE SPLICING, SUBUNIT.
  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] (ISOFORM 1).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Melanoma.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Lung.
  8. "Oligomerization, F-actin interaction, and membrane association of the ubiquitous mammalian coronin 3 are mediated by its carboxyl terminus."
    Spoerl Z., Stumpf M., Noegel A.A., Hasse A.
    J. Biol. Chem. 277:48858-48867(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, COILED-COIL REGION, WD REPEATS, INTERACTION WITH F-ACTIN, SUBCELLULAR LOCATION.
  9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCOR1C_HUMAN
AccessioniPrimary (citable) accession number: Q9ULV4
Secondary accession number(s): A7MAP0
, A7MAP1, B3KU12, Q9NSK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 133 of the entry and version 1 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3