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Q92667

- AKAP1_HUMAN

UniProt

Q92667 - AKAP1_HUMAN

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Protein

A-kinase anchor protein 1, mitochondrial

Gene
AKAP1, AKAP149, PRKA1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. RNA binding Source: ProtInc

GO - Biological processi

  1. blood coagulation Source: Reactome
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 1, mitochondrial
Alternative name(s):
A-kinase anchor protein 149 kDa
Short name:
AKAP 149
Dual specificity A-kinase-anchoring protein 1
Short name:
D-AKAP-1
Protein kinase A-anchoring protein 1
Short name:
PRKA1
Spermatid A-kinase anchor protein 84
Short name:
S-AKAP84
Gene namesi
Name:AKAP1
Synonyms:AKAP149, PRKA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:367. AKAP1.

Subcellular locationi

Mitochondrion outer membrane Reviewed prediction

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial outer membrane Source: UniProtKB-SubCell
  4. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24661.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929Mitochondrion Reviewed predictionAdd
BLAST
Chaini30 – 903874A-kinase anchor protein 1, mitochondrialPRO_0000016659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701Phosphothreonine1 Publication
Modified residuei105 – 1051Phosphoserine By similarity
Modified residuei107 – 1071Phosphoserine By similarity
Modified residuei169 – 1691Phosphoserine1 Publication
Modified residuei429 – 4291Phosphoserine1 Publication
Modified residuei447 – 4471Phosphothreonine1 Publication
Modified residuei533 – 5331Phosphothreonine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92667.
PaxDbiQ92667.
PRIDEiQ92667.

PTM databases

PhosphoSiteiQ92667.

Miscellaneous databases

PMAP-CutDBQ92667.

Expressioni

Tissue specificityi

AKAP149 is highly expressed in prostate and small intestine whereas S-AKAP84 is expressed in kidney, pancreas, liver, lung and brain. AKAP149 is also expressed in colon carcinoma.

Gene expression databases

ArrayExpressiQ92667.
BgeeiQ92667.
CleanExiHS_AKAP1.
GenevestigatoriQ92667.

Organism-specific databases

HPAiCAB019286.
HPA008691.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MAATS1Q7Z4T9-43EBI-2120060,EBI-2119735
MYCBPQ994172EBI-2120060,EBI-716185
PRKAR2AP138613EBI-2119593,EBI-2556122

Protein-protein interaction databases

BioGridi113818. 14 interactions.
IntActiQ92667. 10 interactions.
MINTiMINT-2411938.
STRINGi9606.ENSP00000337736.

Structurei

3D structure databases

ProteinModelPortaliQ92667.
SMRiQ92667. Positions 758-867.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini607 – 67165KHAdd
BLAST
Domaini758 – 81760TudorAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni344 – 35714PKA-RII subunit binding domainAdd
BLAST

Domaini

RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.

Sequence similaritiesi

Contains 1 KH domain.
Contains 1 Tudor domain.

Keywords - Domaini

Transit peptide, Transmembrane

Phylogenomic databases

eggNOGiNOG306785.
HOGENOMiHOG000013170.
HOVERGENiHBG057436.
InParanoidiQ92667.
KOiK16518.
OMAiDLIIWEI.
OrthoDBiEOG779NXH.
PhylomeDBiQ92667.
TreeFamiTF105401.

Family and domain databases

Gene3Di3.30.1370.10. 1 hit.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR002999. Tudor.
[Graphical view]
PfamiPF00013. KH_1. 1 hit.
PF00567. TUDOR. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 1 hit.
PS50304. TUDOR. 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: Q92667-1) [UniParc]FASTAAdd to Basket

Also known as: AKAP149

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

MAIQFRSLFP LALPGMLALL GWWWFFSRKK GHVSSHDEQQ VEAGAVQLRA    50
DPAIKEPLPV EDVCPKVVST PPSVTEPPEK ELSTVSKLPA EPPALLQTHP 100
PCRRSESSGI LPNTTDMRLR PGTRRDDSTK LELALTGGEA KSIPLECPLS 150
SPKGVLFSSK SAEVCKQDSP FSRVPRKVQP GYPVVPAEKR SSGERARETG 200
GAEGTGDAVL GEKVLEEALL SREHVLELEN SKGPSLASLE GEEDKGKSSS 250
SQVVGPVQEE EYVAEKLPSR FIESAHTELA KDDAAPAPPV ADAKAQDRGV 300
EGELGNEESL DRNEEGLDRN EEGLDRNEES LDRNEEGLDR NEEIKRAAFQ 350
IISQVISEAT EQVLATTVGK VAGRVCQASQ LQGQKEESCV PVHQKTVLGP 400
DTAEPATAEA AVAPPDAGLP LPGLPAEGSP PPKTYVSCLK SLLSSPTKDS 450
KPNISAHHIS LASCLALTTP SEELPDRAGI LVEDATCVTC MSDSSQSVPL 500
VASPGHCSDS FSTSGLEDSC TETSSSPRDK AITPPLPEST VPFSNGVLKG 550
ELSDLGAEDG WTMDAEADHS GGSDRNSMDS VDSCCSLKKT ESFQNAQAGS 600
NPKKVDLIIW EIEVPKHLVG RLIGKQGRYV SFLKQTSGAK IYISTLPYTQ 650
SVQICHIEGS QHHVDKALNL IGKKFKELNL TNIYAPPLPS LALPSLPMTS 700
WLMLPDGITV EVIVVNQVNA GHLFVQQHTH PTFHALRSLD QQMYLCYSQP 750
GIPTLPTPVE ITVICAAPGA DGAWWRAQVV ASYEETNEVE IRYVDYGGYK 800
RVKVDVLRQI RSDFVTLPFQ GAEVLLDSVM PLSDDDQFSP EADAAMSEMT 850
GNTALLAQVT SYSPTGLPLI QLWSVVGDEV VLINRSLVER GLAQWVDSYY 900
TSL 903
Length:903
Mass (Da):97,342
Last modified:February 1, 1997 - v1
Checksum:i0C906FAFFB0DBAF7
GO
Isoform 2 (identifier: Q92667-2) [UniParc]FASTAAdd to Basket

Also known as: S-AKAP84

The sequence of this isoform differs from the canonical sequence as follows:
     572-593: GSDRNSMDSVDSCCSLKKTESF → VAAPPPGKRGTLITRCPGFFEC
     594-903: 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:593
Mass (Da):62,921
Checksum:i3F2FC6A1381EFEC1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181A → V.
Corresponds to variant rs17761023 [ dbSNP | Ensembl ].
VAR_049676
Natural varianti60 – 601V → M.
Corresponds to variant rs2230770 [ dbSNP | Ensembl ].
VAR_024512
Natural varianti102 – 1021C → Y.
Corresponds to variant rs2230771 [ dbSNP | Ensembl ].
VAR_049677
Natural varianti124 – 1241R → C.
Corresponds to variant rs17833723 [ dbSNP | Ensembl ].
VAR_049678

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei572 – 59322GSDRN…KTESF → VAAPPPGKRGTLITRCPGFF EC in isoform 2. VSP_002845Add
BLAST
Alternative sequencei594 – 903310Missing in isoform 2. VSP_002846Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti795 – 7951D → H in AAH00729. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97335 mRNA. Translation: CAA66000.1.
U34074 mRNA. Translation: AAC50279.1.
AK292416 mRNA. Translation: BAF85105.1.
CH471109 Genomic DNA. Translation: EAW94515.1.
CH471109 Genomic DNA. Translation: EAW94516.1.
CH471109 Genomic DNA. Translation: EAW94518.1.
BC000729 mRNA. Translation: AAH00729.1.
CCDSiCCDS11594.1. [Q92667-1]
PIRiI39173.
RefSeqiNP_001229831.1. NM_001242902.1. [Q92667-1]
NP_001229832.1. NM_001242903.1. [Q92667-1]
NP_003479.1. NM_003488.3. [Q92667-1]
XP_005257764.1. XM_005257707.1. [Q92667-1]
XP_005257766.1. XM_005257709.1. [Q92667-1]
XP_006722189.1. XM_006722126.1. [Q92667-1]
XP_006722190.1. XM_006722127.1. [Q92667-1]
UniGeneiHs.463506.

Genome annotation databases

EnsembliENST00000314126; ENSP00000314075; ENSG00000121057. [Q92667-2]
ENST00000337714; ENSP00000337736; ENSG00000121057. [Q92667-1]
ENST00000481416; ENSP00000433212; ENSG00000121057. [Q92667-2]
ENST00000539273; ENSP00000443139; ENSG00000121057. [Q92667-1]
ENST00000571629; ENSP00000459968; ENSG00000121057. [Q92667-1]
ENST00000572557; ENSP00000459895; ENSG00000121057. [Q92667-1]
GeneIDi8165.
KEGGihsa:8165.
UCSCiuc002iux.3. human. [Q92667-1]

Polymorphism databases

DMDMi8134304.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97335 mRNA. Translation: CAA66000.1 .
U34074 mRNA. Translation: AAC50279.1 .
AK292416 mRNA. Translation: BAF85105.1 .
CH471109 Genomic DNA. Translation: EAW94515.1 .
CH471109 Genomic DNA. Translation: EAW94516.1 .
CH471109 Genomic DNA. Translation: EAW94518.1 .
BC000729 mRNA. Translation: AAH00729.1 .
CCDSi CCDS11594.1. [Q92667-1 ]
PIRi I39173.
RefSeqi NP_001229831.1. NM_001242902.1. [Q92667-1 ]
NP_001229832.1. NM_001242903.1. [Q92667-1 ]
NP_003479.1. NM_003488.3. [Q92667-1 ]
XP_005257764.1. XM_005257707.1. [Q92667-1 ]
XP_005257766.1. XM_005257709.1. [Q92667-1 ]
XP_006722189.1. XM_006722126.1. [Q92667-1 ]
XP_006722190.1. XM_006722127.1. [Q92667-1 ]
UniGenei Hs.463506.

3D structure databases

ProteinModelPortali Q92667.
SMRi Q92667. Positions 758-867.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113818. 14 interactions.
IntActi Q92667. 10 interactions.
MINTi MINT-2411938.
STRINGi 9606.ENSP00000337736.

Chemistry

BindingDBi Q92667.

PTM databases

PhosphoSitei Q92667.

Polymorphism databases

DMDMi 8134304.

Proteomic databases

MaxQBi Q92667.
PaxDbi Q92667.
PRIDEi Q92667.

Protocols and materials databases

DNASUi 8165.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314126 ; ENSP00000314075 ; ENSG00000121057 . [Q92667-2 ]
ENST00000337714 ; ENSP00000337736 ; ENSG00000121057 . [Q92667-1 ]
ENST00000481416 ; ENSP00000433212 ; ENSG00000121057 . [Q92667-2 ]
ENST00000539273 ; ENSP00000443139 ; ENSG00000121057 . [Q92667-1 ]
ENST00000571629 ; ENSP00000459968 ; ENSG00000121057 . [Q92667-1 ]
ENST00000572557 ; ENSP00000459895 ; ENSG00000121057 . [Q92667-1 ]
GeneIDi 8165.
KEGGi hsa:8165.
UCSCi uc002iux.3. human. [Q92667-1 ]

Organism-specific databases

CTDi 8165.
GeneCardsi GC17P055162.
HGNCi HGNC:367. AKAP1.
HPAi CAB019286.
HPA008691.
MIMi 602449. gene.
neXtProti NX_Q92667.
PharmGKBi PA24661.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG306785.
HOGENOMi HOG000013170.
HOVERGENi HBG057436.
InParanoidi Q92667.
KOi K16518.
OMAi DLIIWEI.
OrthoDBi EOG779NXH.
PhylomeDBi Q92667.
TreeFami TF105401.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi AKAP1. human.
GeneWikii AKAP1.
GenomeRNAii 8165.
NextBioi 30837.
PMAP-CutDB Q92667.
PROi Q92667.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92667.
Bgeei Q92667.
CleanExi HS_AKAP1.
Genevestigatori Q92667.

Family and domain databases

Gene3Di 3.30.1370.10. 1 hit.
InterProi IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR002999. Tudor.
[Graphical view ]
Pfami PF00013. KH_1. 1 hit.
PF00567. TUDOR. 1 hit.
[Graphical view ]
SMARTi SM00322. KH. 1 hit.
SM00333. TUDOR. 1 hit.
[Graphical view ]
SUPFAMi SSF54791. SSF54791. 1 hit.
PROSITEi PS50084. KH_TYPE_1. 1 hit.
PS50304. TUDOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain."
    Trendelenburg G., Hummel M., Riecken E.-O., Hanski C.
    Biochem. Biophys. Res. Commun. 225:313-319(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon.
  2. "Characterization of S-AKAP84, a novel developmentally regulated A kinase anchor protein of male germ cells."
    Lin R.-Y., Moss S.B., Rubin C.S.
    J. Biol. Chem. 270:27804-27811(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Testis.
  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).
    Tissue: Testis.
  4. 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. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429 AND THR-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70 AND THR-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAKAP1_HUMAN
AccessioniPrimary (citable) accession number: Q92667
Secondary accession number(s): A8K8Q1
, D3DTZ0, Q13320, Q9BW14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: September 3, 2014
This is version 143 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 17
    Human chromosome 17: 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

Similar proteinsi