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Reviewed, UniProtKB/Swiss-Prot Q12904 (MCA1_HUMAN)

Last modified July 7, 2009. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Multisynthetase complex auxiliary component p43
Cleaved into the following chain:
    1- Recommended name:
            Endothelial monocyte-activating polypeptide 2
        Alternative name(s):
            EMAP-II
            Small inducible cytokine subfamily E member 1
Gene names
Name: SCYE1
Synonyms: EMAP2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Seems to have both an inflammatory cytokine activity and tRNA-binding domain. Ref.7

Subunit structure

Monomer. Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43.

Sequence similarities

Contains 1 tRNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Multisynthetase complex auxiliary component p43
PRO_0000223394
Chain147 – 312166Endothelial monocyte-activating polypeptide 2
PRO_0000019242

Regions

Domain151 – 252102tRNA-binding

Natural variations

Natural variant791P → A: dbSNP rs1134648. Ref.1
VAR_025212
Natural variant1041T → A: dbSNP rs2230254.
VAR_029156
Natural variant1171T → A: dbSNP rs2230255.
VAR_050124

Secondary structure

..................................... 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12904-1 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 5F0BF73E58810C60

FASTA31234,353
        10         20         30         40         50         60 
MANNDAVLKR LEQKGAEADQ IIEYLKQQVS LLKEKAILQA TLREEKKLRV ENAKLKKEIE 

        70         80         90        100        110        120 
ELKQELIQAE IQNGVKQIPF PSGTPLHANS MVSENVIQST AVTTVSSGTK EQIKGGTGDE 

       130        140        150        160        170        180 
KKAKEKIEKK GEKKEKKQQS IAGSADSKPI DVSRLDLRIG CIITARKHPD ADSLYVEEVD 

       190        200        210        220        230        240 
VGEIAPRTVV SGLVNHVPLE QMQNRMVILL CNLKPAKMRG VLSQAMVMCA SSPEKIEILA 

       250        260        270        280        290        300 
PPNGSVPGDR ITFDAFPGEP DKELNPKKKI WEQIQPDLHT NDECVATYKG VPFEVKGKGV 

       310 
CRAQTMSNSG IK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a novel tumor-derived cytokine. Endothelial-monocyte activating polypeptide II."
Kao J., Houck K., Fan Y., Haehnel I., Libutti S.K., Kayton M.L., Grikscheit T., Chabot J., Nowygrod R., Greenberg S., Kuang W.J., Leung D.W., Hayward J.R., Kisiel W., Heath M., Brett J., Stern D.M.
J. Biol. Chem. 269:25106-25119(1994) [PubMed: 7929199] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-79.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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. 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases."
Kim Y., Shin J., Li R., Cheong C., Kim K., Kim S.
J. Biol. Chem. 275:27062-27068(2000) [PubMed: 10852899] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 147-312.
[7]"Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry."
Renault L., Kerjan P., Pasqualato S., Menetrey J., Robinson J.-C., Kawaguchi S., Vassylyev D.G., Yokoyama S., Mirande M., Cherfils J.
EMBO J. 20:570-578(2001) [PubMed: 11157763] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 148-312, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

U10117 mRNA. Translation: AAA62202.1.
CR542281 mRNA. Translation: CAG47076.1.
AK095951 mRNA. Translation: BAG53174.1.
BC014051 mRNA. Translation: AAH14051.1.
IPIIPI00006252.
PIRB55053.
RefSeqNP_001135887.1.
NP_004748.2.
UniGeneHs.591680

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1E7ZX-ray2.05A148-312[»]
1EUJX-ray1.80A/B147-312[»]
1FL0X-ray1.50A150-312[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ12904. 5 interactions.

Proteomic databases

PRIDEQ12904.

Genome annotation databases

EnsemblENSG00000164022. Homo sapiens. [Contig view]
GeneID9255.
KEGGhsa:9255.
UCSCuc003hyg.1. human.

Organism-specific databases

GeneCardsGC04P107456.
H-InvDBHIX0004426.
HGNCHGNC:10648. SCYE1.
HPACAB017618.
HPA018476.
MIM603605. gene.
PharmGKBPA35578.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ12904.
HOVERGENQ12904.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ12904.
BgeeQ12904.
CleanExHS_SCYE1.
GermOnlineENSG00000164022. Homo sapiens.

Family and domain databases

InterProIPR012340. NA-bd_OB-fold.
IPR002547. tRNA_bd.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PfamPF01588. tRNA_bind. 1 hit.
[Graphical view]
PROSITEPS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio34695.
SOURCESearch...

Entry information

Entry nameMCA1_HUMAN
AccessionPrimary (citable) accession number: Q12904
Secondary accession number(s): B3KTR2, Q6FG28, Q96CQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 24, 2006
Last modified: July 7, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents