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Protein

C-type lectin domain family 12 member A

Gene

CLEC12A

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

Functioni

Cell surface receptor that modulates signaling cascades and mediates tyrosine phosphorylation of target MAP kinases.2 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
C-type lectin domain family 12 member A
Alternative name(s):
C-type lectin-like molecule 1
Short name:
CLL-1
Dendritic cell-associated lectin 2
Short name:
DCAL-2
Myeloid inhibitory C-type lectin-like receptor
Short name:
MICL
Gene namesi
Name:CLEC12A
Synonyms:CLL1, DCAL2, MICL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:31713. CLEC12A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4343CytoplasmicSequence analysisAdd
BLAST
Transmembranei44 – 6421Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini65 – 265201ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672094.

Polymorphism and mutation databases

BioMutaiCLEC12A.
DMDMi308153619.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 265265C-type lectin domain family 12 member APRO_0000313578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence analysis
Glycosylationi98 – 981N-linked (GlcNAc...)1 Publication
Disulfide bondi161 ↔ 248PROSITE-ProRule annotation
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi227 ↔ 240PROSITE-ProRule annotation

Post-translational modificationi

Highly N-glycosylated. Glycosylation varies between cell types.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ5QGZ9.
MaxQBiQ5QGZ9.
PaxDbiQ5QGZ9.
PRIDEiQ5QGZ9.

PTM databases

PhosphoSiteiQ5QGZ9.

Expressioni

Tissue specificityi

Detected in normal myeloid cells and in acute myeloid leukemia cells. Detected in neutrophils, eosinophils, monocytes and dendritic cells. Detected in spleen macrophage-rich red pulp and in lymph node (at protein level). Detected in peripheral blood leukocytes, dendritic cells, bone marrow, monocytes, mononuclear leukocytes and macrophages.4 Publications

Inductioni

Down-regulated in activated leukocytes recruited to a site of inflammation.1 Publication

Gene expression databases

BgeeiQ5QGZ9.
CleanExiHS_CLEC12A.
ExpressionAtlasiQ5QGZ9. baseline and differential.
GenevisibleiQ5QGZ9. HS.

Organism-specific databases

HPAiHPA048515.

Interactioni

Subunit structurei

Interacts with PTPN6 and PTPN11.1 Publication

Protein-protein interaction databases

BioGridi127754. 27 interactions.
STRINGi9606.ENSP00000347916.

Structurei

3D structure databases

ProteinModelPortaliQ5QGZ9.
SMRiQ5QGZ9. Positions 76-253.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini140 – 249110C-type lectinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi5 – 106ITIM motif

Domaini

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104266.
HOGENOMiHOG000111777.
HOVERGENiHBG107715.
InParanoidiQ5QGZ9.
KOiK17516.
OMAiICEKMAN.
OrthoDBiEOG7J447Q.
TreeFamiTF336674.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: Q5QGZ9-2) [UniParc]FASTAAdd to basket

Also known as: Alpha

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
MSEEVTYADL QFQNSSEMEK IPEIGKFGEK APPAPSHVWR PAALFLTLLC
60 70 80 90 100
LLLLIGLGVL ASMFHVTLKI EMKKMNKLQN ISEELQRNIS LQLMSNMNIS
110 120 130 140 150
NKIRNLSTTL QTIATKLCRE LYSKEQEHKC KPCPRRWIWH KDSCYFLSDD
160 170 180 190 200
VQTWQESKMA CAAQNASLLK INNKNALEFI KSQSRSYDYW LGLSPEEDST
210 220 230 240 250
RGMRVDNIIN SSAWVIRNAP DLNNMYCGYI NRLYVQYYHC TYKKRMICEK
260
MANPVQLGST YFREA
Length:265
Mass (Da):30,762
Last modified:October 5, 2010 - v3
Checksum:i4255FF1EA9F0D4B1
GO
Isoform 1 (identifier: Q5QGZ9-1) [UniParc]FASTAAdd to basket

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

Show »
Length:275
Mass (Da):32,040
Checksum:i71AA82DBDD039848
GO
Isoform 3 (identifier: Q5QGZ9-3) [UniParc]FASTAAdd to basket

Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     64-81: FHVTLKIEMKKMNKLQNI → CMYCPCFGQEEVSRISNI
     82-265: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:81
Mass (Da):8,965
Checksum:iF025075C173112DD
GO
Isoform 4 (identifier: Q5QGZ9-4) [UniParc]FASTAAdd to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     31-64: APPAPSHVWRPAALFLTLLCLLLLIGLGVLASMF → V

Show »
Length:232
Mass (Da):27,276
Checksum:i3BF3147C5CEB4B45
GO
Isoform 5 (identifier: Q5QGZ9-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     214-265: Missing.

Show »
Length:213
Mass (Da):24,449
Checksum:iD026446C70B23B77
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti244 – 2441K → Q.6 Publications
Corresponds to variant rs479499 [ dbSNP | Ensembl ].
VAR_037669

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MWIDFFTYSSM in isoform 1. 1 PublicationVSP_039854
Alternative sequencei31 – 6434APPAP…LASMF → V in isoform 4. 1 PublicationVSP_030030Add
BLAST
Alternative sequencei64 – 8118FHVTL…KLQNI → CMYCPCFGQEEVSRISNI in isoform 3. 1 PublicationVSP_030031Add
BLAST
Alternative sequencei82 – 265184Missing in isoform 3. 1 PublicationVSP_030032Add
BLAST
Alternative sequencei214 – 26552Missing in isoform 5. 1 PublicationVSP_030033Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY547296 mRNA. Translation: AAT11783.1.
AY498550 mRNA. Translation: AAS00605.1.
AY498551 mRNA. Translation: AAS00606.1.
AY498552 mRNA. Translation: AAS00607.1.
AY426759 mRNA. Translation: AAR84594.1.
AF247788 mRNA. Translation: AAL95693.1.
AK314001 mRNA. Translation: BAG36713.1.
AC091814 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96133.1.
BC063424 mRNA. Translation: AAH63424.1.
BC126289 mRNA. Translation: AAI26290.1.
BC126291 mRNA. Translation: AAI26292.1.
CCDSiCCDS55803.1. [Q5QGZ9-1]
CCDS73442.1. [Q5QGZ9-5]
CCDS8608.1. [Q5QGZ9-2]
CCDS8609.1. [Q5QGZ9-4]
RefSeqiNP_001193939.1. NM_001207010.1. [Q5QGZ9-1]
NP_001287659.1. NM_001300730.1. [Q5QGZ9-5]
NP_612210.4. NM_138337.5. [Q5QGZ9-2]
NP_963917.2. NM_201623.3. [Q5QGZ9-4]
XP_005253381.1. XM_005253324.2. [Q5QGZ9-2]
XP_011518872.1. XM_011520570.1. [Q5QGZ9-2]
XP_011518873.1. XM_011520571.1. [Q5QGZ9-4]
UniGeneiHs.190519.

Genome annotation databases

EnsembliENST00000304361; ENSP00000302804; ENSG00000172322. [Q5QGZ9-2]
ENST00000350667; ENSP00000345448; ENSG00000172322. [Q5QGZ9-4]
ENST00000355690; ENSP00000347916; ENSG00000172322. [Q5QGZ9-1]
ENST00000434319; ENSP00000405244; ENSG00000172322. [Q5QGZ9-5]
GeneIDi160364.
KEGGihsa:160364.
UCSCiuc001qwq.3. human. [Q5QGZ9-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY547296 mRNA. Translation: AAT11783.1.
AY498550 mRNA. Translation: AAS00605.1.
AY498551 mRNA. Translation: AAS00606.1.
AY498552 mRNA. Translation: AAS00607.1.
AY426759 mRNA. Translation: AAR84594.1.
AF247788 mRNA. Translation: AAL95693.1.
AK314001 mRNA. Translation: BAG36713.1.
AC091814 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96133.1.
BC063424 mRNA. Translation: AAH63424.1.
BC126289 mRNA. Translation: AAI26290.1.
BC126291 mRNA. Translation: AAI26292.1.
CCDSiCCDS55803.1. [Q5QGZ9-1]
CCDS73442.1. [Q5QGZ9-5]
CCDS8608.1. [Q5QGZ9-2]
CCDS8609.1. [Q5QGZ9-4]
RefSeqiNP_001193939.1. NM_001207010.1. [Q5QGZ9-1]
NP_001287659.1. NM_001300730.1. [Q5QGZ9-5]
NP_612210.4. NM_138337.5. [Q5QGZ9-2]
NP_963917.2. NM_201623.3. [Q5QGZ9-4]
XP_005253381.1. XM_005253324.2. [Q5QGZ9-2]
XP_011518872.1. XM_011520570.1. [Q5QGZ9-2]
XP_011518873.1. XM_011520571.1. [Q5QGZ9-4]
UniGeneiHs.190519.

3D structure databases

ProteinModelPortaliQ5QGZ9.
SMRiQ5QGZ9. Positions 76-253.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127754. 27 interactions.
STRINGi9606.ENSP00000347916.

PTM databases

PhosphoSiteiQ5QGZ9.

Polymorphism and mutation databases

BioMutaiCLEC12A.
DMDMi308153619.

Proteomic databases

EPDiQ5QGZ9.
MaxQBiQ5QGZ9.
PaxDbiQ5QGZ9.
PRIDEiQ5QGZ9.

Protocols and materials databases

DNASUi160364.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304361; ENSP00000302804; ENSG00000172322. [Q5QGZ9-2]
ENST00000350667; ENSP00000345448; ENSG00000172322. [Q5QGZ9-4]
ENST00000355690; ENSP00000347916; ENSG00000172322. [Q5QGZ9-1]
ENST00000434319; ENSP00000405244; ENSG00000172322. [Q5QGZ9-5]
GeneIDi160364.
KEGGihsa:160364.
UCSCiuc001qwq.3. human. [Q5QGZ9-2]

Organism-specific databases

CTDi160364.
GeneCardsiCLEC12A.
HGNCiHGNC:31713. CLEC12A.
HPAiHPA048515.
MIMi612088. gene.
neXtProtiNX_Q5QGZ9.
PharmGKBiPA142672094.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104266.
HOGENOMiHOG000111777.
HOVERGENiHBG107715.
InParanoidiQ5QGZ9.
KOiK17516.
OMAiICEKMAN.
OrthoDBiEOG7J447Q.
TreeFamiTF336674.

Miscellaneous databases

GeneWikiiCLEC12A.
GenomeRNAii160364.
NextBioi87949.
PROiQ5QGZ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ5QGZ9.
CleanExiHS_CLEC12A.
ExpressionAtlasiQ5QGZ9. baseline and differential.
GenevisibleiQ5QGZ9. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Bone marrow.
  2. "Identification and characterization of a novel human myeloid inhibitory C-type lectin-like receptor (MICL) that is predominantly expressed on granulocytes and monocytes."
    Marshall A.S.J., Willment J.A., Lin H.-H., Williams D.L., Gordon S., Brown G.D.
    J. Biol. Chem. 279:14792-14802(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), FUNCTION, INTERACTION WITH PTPN6 AND PTPN11, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, VARIANT GLN-244.
  3. "Dendritic-cell-associated C-type lectin 2 (DCAL-2) alters dendritic-cell maturation and cytokine production."
    Chen C.-H., Floyd H., Olson N.E., Magaletti D., Li C., Draves K., Clark E.A.
    Blood 107:1459-1467(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT GLN-244.
  4. "Novel human C-type lectin superfamily member CLL-1."
    Zhang W., Wan T., Chen T., Cao X.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLN-244.
  5. "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 2), VARIANT GLN-244.
    Tissue: Lung.
  6. "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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-244.
  8. "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 2 AND 5), VARIANT GLN-244.
    Tissue: Blood.
  9. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98.
    Tissue: Plasma.
  10. "Human MICL (CLEC12A) is differentially glycosylated and is down-regulated following cellular activation."
    Marshall A.S.J., Willment J.A., Pyz E., Dennehy K.M., Reid D.M., Dri P., Gordon S., Wong S.Y.C., Brown G.D.
    Eur. J. Immunol. 36:2159-2169(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCL12A_HUMAN
AccessioniPrimary (citable) accession number: Q5QGZ9
Secondary accession number(s): B2RA16
, Q6P4H1, Q6RH77, Q6RH78, Q8TDQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 5, 2010
Last modified: March 16, 2016
This is version 93 of the entry and version 3 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. 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

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.