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Q03113

- GNA12_HUMAN

UniProt

Q03113 - GNA12_HUMAN

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Protein

Guanine nucleotide-binding protein subunit alpha-12

Gene
GNA12
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. May play a role in the control of cell migration through the TOR signaling cascade.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi71 – 711Magnesium By similarity
Metal bindingi208 – 2081Magnesium By similarity
Binding sitei353 – 3531GTP; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 718GTP By similarity
Nucleotide bindingi202 – 2087GTP By similarity
Nucleotide bindingi227 – 2315GTP By similarity
Nucleotide bindingi296 – 2994GTP By similarity

GO - Molecular functioni

  1. D5 dopamine receptor binding Source: RefGenome
  2. G-protein beta/gamma-subunit complex binding Source: RefGenome
  3. GTPase activity Source: InterPro
  4. GTP binding Source: UniProtKB-KW
  5. metal ion binding Source: UniProtKB-KW
  6. protein binding Source: UniProtKB
  7. signal transducer activity Source: InterPro

GO - Biological processi

  1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: RefGenome
  2. blood coagulation Source: Reactome
  3. cell differentiation Source: Ensembl
  4. embryonic digit morphogenesis Source: Ensembl
  5. G-protein coupled receptor signaling pathway Source: InterPro
  6. in utero embryonic development Source: Ensembl
  7. platelet activation Source: Reactome
  8. regulation of cell shape Source: Ensembl
  9. regulation of fibroblast migration Source: UniProtKB
  10. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  11. regulation of TOR signaling Source: UniProtKB
  12. response to drug Source: Ensembl
  13. Rho protein signal transduction Source: RefGenome
  14. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_18407. G alpha (12/13) signalling events.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
SignaLinkiQ03113.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein subunit alpha-12
Short name:
G alpha-12
Short name:
G-protein subunit alpha-12
Gene namesi
Name:GNA12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:4380. GNA12.

Subcellular locationi

GO - Cellular componenti

  1. brush border membrane Source: RefGenome
  2. extrinsic component of cytoplasmic side of plasma membrane Source: RefGenome
  3. heterotrimeric G-protein complex Source: RefGenome
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28765.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Guanine nucleotide-binding protein subunit alpha-12PRO_0000203770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi11 – 111S-palmitoyl cysteine By similarity

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ03113.
PaxDbiQ03113.
PRIDEiQ03113.

PTM databases

PhosphoSiteiQ03113.

Expressioni

Gene expression databases

ArrayExpressiQ03113.
BgeeiQ03113.
CleanExiHS_GNA12.
GenevestigatoriQ03113.

Organism-specific databases

HPAiCAB010046.

Interactioni

Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with UBXD5. Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane. Interacts with RGS22.2 Publications

Protein-protein interaction databases

BioGridi109030. 26 interactions.
IntActiQ03113. 4 interactions.
MINTiMINT-85969.
STRINGi9606.ENSP00000275364.

Structurei

3D structure databases

ProteinModelPortaliQ03113.
SMRiQ03113. Positions 56-373.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG279688.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiQ03113.
KOiK04346.
OMAiWQHSENE.
OrthoDBiEOG7HF1JF.
PhylomeDBiQ03113.
TreeFamiTF300673.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000469. Gprotein_alpha_12.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00440. GPROTEINA12.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: Q03113-1) [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

MSGVVRTLSR CLLPAEAGGA RERRAGSGAR DAEREARRRS RDIDALLARE    50
RRAVRRLVKI LLLGAGESGK STFLKQMRII HGREFDQKAL LEFRDTIFDN 100
ILKGSRVLVD ARDKLGIPWQ YSENEKHGMF LMAFENKAGL PVEPATFQLY 150
VPALSALWRD SGIREAFSRR SEFQLGESVK YFLDNLDRIG QLNYFPSKQD 200
ILLARKATKG IVEHDFVIKK IPFKMVDVGG QRSQRQKWFQ CFDGITSILF 250
MVSSSEYDQV LMEDRRTNRL VESMNIFETI VNNKLFFNVS IILFLNKMDL 300
LVEKVKTVSI KKHFPDFRGD PHRLEDVQRY LVQCFDRKRR NRSKPLFHHF 350
TTAIDTENVR FVFHAVKDTI LQENLKDIML Q 381
Length:381
Mass (Da):44,279
Last modified:January 23, 2007 - v4
Checksum:i04C3F12B29255F89
GO
Isoform 2 (identifier: Q03113-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-103: MSGVVRTLSR...RDTIFDNILK → MKRRMFPRPC...HLLIAHPGSR

Show »
Length:322
Mass (Da):37,601
Checksum:iAB035356C0AACD6F
GO
Isoform 3 (identifier: Q03113-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.
     174-190: Missing.

Note: No experimental confirmation available.

Show »
Length:288
Mass (Da):34,002
Checksum:i72CABE32D6FC5D6C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681S → G.1 Publication
Corresponds to variant rs11552939 [ dbSNP | Ensembl ].
VAR_071044
Natural varianti242 – 2421F → L.
Corresponds to variant rs45606633 [ dbSNP | Ensembl ].
VAR_049359
Natural varianti330 – 3301Y → H.
Corresponds to variant rs45583847 [ dbSNP | Ensembl ].
VAR_049360

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 103103MSGVV…DNILK → MKRRMFPRPCLARMPGSRGS GSTPDGNRKCCRFEHLLIAH PGSR in isoform 2. VSP_055171Add
BLAST
Alternative sequencei1 – 7676Missing in isoform 3. VSP_055230Add
BLAST
Alternative sequencei174 – 19017Missing in isoform 3. VSP_055231Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1261K → E in AAM12615. 1 Publication
Sequence conflicti323 – 3231R → Q in AAA35867. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01694 mRNA. Translation: AAA35867.1.
AF493901 mRNA. Translation: AAM12615.1.
AK127842 mRNA. Translation: BAG54584.1.
AK295830 mRNA. Translation: BAH12193.1.
AC006028 Genomic DNA. Translation: AAP21870.1.
AC004933 Genomic DNA. Translation: AAD05026.1.
CH236953 Genomic DNA. Translation: EAL23961.1.
BC087537 mRNA. Translation: AAH87537.1.
BC111464 mRNA. Translation: AAI11465.1.
CCDSiCCDS5335.1. [Q03113-1]
PIRiA48071.
RefSeqiNP_001269370.1. NM_001282441.1.
NP_031379.2. NM_007353.2.
UniGeneiHs.487341.

Genome annotation databases

EnsembliENST00000275364; ENSP00000275364; ENSG00000146535.
ENST00000407904; ENSP00000385935; ENSG00000146535.
ENST00000544127; ENSP00000437469; ENSG00000146535.
GeneIDi2768.
KEGGihsa:2768.
UCSCiuc003smu.3. human. [Q03113-1]

Polymorphism databases

DMDMi38258934.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01694 mRNA. Translation: AAA35867.1 .
AF493901 mRNA. Translation: AAM12615.1 .
AK127842 mRNA. Translation: BAG54584.1 .
AK295830 mRNA. Translation: BAH12193.1 .
AC006028 Genomic DNA. Translation: AAP21870.1 .
AC004933 Genomic DNA. Translation: AAD05026.1 .
CH236953 Genomic DNA. Translation: EAL23961.1 .
BC087537 mRNA. Translation: AAH87537.1 .
BC111464 mRNA. Translation: AAI11465.1 .
CCDSi CCDS5335.1. [Q03113-1 ]
PIRi A48071.
RefSeqi NP_001269370.1. NM_001282441.1.
NP_031379.2. NM_007353.2.
UniGenei Hs.487341.

3D structure databases

ProteinModelPortali Q03113.
SMRi Q03113. Positions 56-373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109030. 26 interactions.
IntActi Q03113. 4 interactions.
MINTi MINT-85969.
STRINGi 9606.ENSP00000275364.

PTM databases

PhosphoSitei Q03113.

Polymorphism databases

DMDMi 38258934.

Proteomic databases

MaxQBi Q03113.
PaxDbi Q03113.
PRIDEi Q03113.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000275364 ; ENSP00000275364 ; ENSG00000146535 .
ENST00000407904 ; ENSP00000385935 ; ENSG00000146535 .
ENST00000544127 ; ENSP00000437469 ; ENSG00000146535 .
GeneIDi 2768.
KEGGi hsa:2768.
UCSCi uc003smu.3. human. [Q03113-1 ]

Organism-specific databases

CTDi 2768.
GeneCardsi GC07M002767.
HGNCi HGNC:4380. GNA12.
HPAi CAB010046.
MIMi 604394. gene.
neXtProti NX_Q03113.
PharmGKBi PA28765.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG279688.
HOGENOMi HOG000038729.
HOVERGENi HBG063184.
InParanoidi Q03113.
KOi K04346.
OMAi WQHSENE.
OrthoDBi EOG7HF1JF.
PhylomeDBi Q03113.
TreeFami TF300673.

Enzyme and pathway databases

Reactomei REACT_18407. G alpha (12/13) signalling events.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
SignaLinki Q03113.

Miscellaneous databases

ChiTaRSi GNA12. human.
GeneWikii GNA12.
GenomeRNAii 2768.
NextBioi 10888.
PROi Q03113.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q03113.
Bgeei Q03113.
CleanExi HS_GNA12.
Genevestigatori Q03113.

Family and domain databases

Gene3Di 1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR000469. Gprotein_alpha_12.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR10218. PTHR10218. 1 hit.
Pfami PF00503. G-alpha. 1 hit.
[Graphical view ]
PRINTSi PR00318. GPROTEINA.
PR00440. GPROTEINA12.
SMARTi SM00275. G_alpha. 1 hit.
[Graphical view ]
SUPFAMi SSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression cDNA cloning of a transforming gene encoding the wild-type G alpha 12 gene product."
    Chan A.M.-L., Fleming T.P., McGovern E.S., Chedid M., Miki T., Aaronson S.A.
    Mol. Cell. Biol. 13:762-768(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  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 2 AND 3).
    Tissue: Hippocampus and Placenta.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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), VARIANT GLY-68.
    Tissue: Brain and Pancreas.
  7. "Socius, a novel binding partner of Galpha12/13, promotes the Galpha12-induced RhoA activation."
    Tateiwa K., Katoh H., Negishi M.
    Biochem. Biophys. Res. Commun. 337:615-620(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBXD5.
  8. "RGS22, a novel testis-specific regulator of G-protein signaling involved in human and mouse spermiogenesis along with GNA12/13 subunits."
    Hu Y., Xing J., Chen L., Guo X., Du Y., Zhao C., Zhu Y., Lin M., Zhou Z., Sha J.
    Biol. Reprod. 79:1021-1029(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RGS22.
    Tissue: Testis.
  9. "PRR5L degradation promotes mTORC2-mediated PKC-delta phosphorylation and cell migration downstream of Galpha12."
    Gan X., Wang J., Wang C., Sommer E., Kozasa T., Srinivasula S., Alessi D., Offermanns S., Simon M.I., Wu D.
    Nat. Cell Biol. 14:686-696(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TOR SIGNALING.

Entry informationi

Entry nameiGNA12_HUMAN
AccessioniPrimary (citable) accession number: Q03113
Secondary accession number(s): A4D204
, B3KXS2, B7Z3F7, Q2T9L1, Q5PPR5, Q86UM8, Q8TD71, Q9UDU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 138 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

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