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O60641

- AP180_HUMAN

UniProt

O60641 - AP180_HUMAN

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Protein
Clathrin coat assembly protein AP180
Gene
SNAP91, KIAA0656
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats By similarity.

GO - Molecular functioni

  1. 1-phosphatidylinositol binding Source: InterPro
  2. protein binding Source: IntAct
  3. protein kinase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. clathrin coat assembly Source: InterPro
  2. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Clathrin coat assembly protein AP180
Alternative name(s):
91 kDa synaptosomal-associated protein
Clathrin coat-associated protein AP180
Phosphoprotein F1-20
Gene namesi
Name:SNAP91
Synonyms:KIAA0656
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:14986. SNAP91.

Subcellular locationi

Cell membrane By similarity. Membranecoated pit; Peripheral membrane protein; Cytoplasmic side By similarity
Note: Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane By similarity.

GO - Cellular componenti

  1. clathrin coat Source: InterPro
  2. coated pit Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37956.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 907907Clathrin coat assembly protein AP180
PRO_0000193864Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei306 – 3061Phosphoserine By similarity
Glycosylationi310 – 3101O-linked (GlcNAc) By similarity
Modified residuei313 – 3131Phosphoserine By similarity
Modified residuei602 – 6021Phosphoserine By similarity
Modified residuei623 – 6231Phosphoserine By similarity
Modified residuei629 – 6291Phosphoserine By similarity

Post-translational modificationi

Thr-310 can be modified by the addition of N-acetylglucosamine which can be further phosphorylated. There is no evidence for direct Thr-310 phosphorylation By similarity.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO60641.
PaxDbiO60641.
PRIDEiO60641.

PTM databases

PhosphoSiteiO60641.

Expressioni

Gene expression databases

ArrayExpressiO60641.
BgeeiO60641.
CleanExiHS_SNAP91.
GenevestigatoriO60641.

Organism-specific databases

HPAiCAB009745.
HPA029632.
HPA029633.

Interactioni

Subunit structurei

Binds AP2A2. Interacts with AP2B1; clathrin competes with SNAP91 By similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Necap1Q9CR952EBI-1105187,EBI-7592476From a different organism.

Protein-protein interaction databases

BioGridi115222. 5 interactions.
IntActiO60641. 2 interactions.
MINTiMINT-3000172.
STRINGi9606.ENSP00000195649.

Structurei

3D structure databases

ProteinModelPortaliO60641.
SMRiO60641. Positions 18-264.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 145132ENTH
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi361 – 583223Ala-rich
Add
BLAST
Compositional biasi536 – 55621Thr-rich
Add
BLAST
Compositional biasi809 – 89789Pro-rich
Add
BLAST

Domaini

Possesses a three domain structure: the N-terminal 300 residues harbor a clathrin binding site, an acidic middle domain 450 residues, interrupted by an Ala-rich segment, and the C-terminal domain (166 residues).

Sequence similaritiesi

Belongs to the PICALM/SNAP91 family.

Phylogenomic databases

eggNOGiNOG267212.
HOGENOMiHOG000015763.
HOVERGENiHBG049391.
InParanoidiO60641.
OMAiXRISGAP.
OrthoDBiEOG76QFM8.
PhylomeDBiO60641.
TreeFamiTF314861.

Family and domain databases

Gene3Di1.20.58.150. 1 hit.
1.25.40.90. 1 hit.
InterProiIPR011417. ANTH_dom.
IPR014712. Clathrin_Pinositid-bd_GAT-like.
IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
[Graphical view]
PfamiPF07651. ANTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60641-1) [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

MSGQTLTDRI AAAQYSVTGS AVARAVCKAT THEVMGPKKK HLDYLIQATN    50
ETNVNIPQMA DTLFERATNS SWVVVFKALV TTHHLMVHGN ERFIQYLASR 100
NTLFNLSNFL DKSGSHGYDM STFIRRYSRY LNEKAFSYRQ MAFDFARVKK 150
GADGVMRTMA PEKLLKSMPI LQGQIDALLE FDVHPNELTN GVINAAFMLL 200
FKDLIKLFAC YNDGVINLLE KFFEMKKGQC KDALEIYKRF LTRMTRVSEF 250
LKVAEQVGID KGDIPDLTQA PSSLMETLEQ HLNTLEGKKP GNNEGSGAPS 300
PLSKSSPATT VTSPNSTPAK TIDTSPPVDL FATASAAVPV STSKPSSDLL 350
DLQPDFSSGG AAAAAAPAPP PPAGGATAWG DLLGEDSLAA LSSVPSEAQI 400
SDPFAPEPTP PTTTAEIATA SASASTTTTV TAVTAEVDLF GDAFAASPGE 450
APAASEGAAA PATPTPVAAA LDACSGNDPF APSEGSAEAA PELDLFAMKP 500
PETSVPVVTP TASTAPPVPA TAPSPAPAVA AAAAATTAAT AAATTTTTTS 550
AATATTAPPA LDIFGDLFES TPEVAAAPKP DAAPSIDLFS TDAFSSPPQG 600
ASPVPESSLT ADLLSVDAFA APSPATTASP AKVDSSGVID LFGDAFGSSA 650
SEPQPASQAA SSSSASADLL AGFGGSFMAP SPSPVTPAQN NLLQPNFEAA 700
FGTTPSTSSS SSFDPSVFDG LGDLLMPTMA PAGQPAPVSM VPPSPAMAAS 750
KALGSDLDSS LASLVGNLGI SGTTTKKGDL QWNAGEKKLT GGANWQPKVA 800
PATWSAGVPP SAPLQGAVPP TSSVPPVAGA PSVGQPGAGF GMPPAGTGMP 850
MMPQQPVMFA QPMMRPPFGA AAVPGTQLSP SPTPASQSPK KPPAKDPLAD 900
LNIKDFL 907
Length:907
Mass (Da):92,502
Last modified:August 1, 1999 - v2
Checksum:i23959C2B54F5EBF1
GO
Isoform 2 (identifier: O60641-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-907: 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:58
Mass (Da):6,230
Checksum:i22EBDA4093641147
GO
Isoform 3 (identifier: O60641-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     256-269: Missing.
     293-295: NEG → K
     381-671: Missing.

Show »
Length:600
Mass (Da):63,128
Checksum:i0B92B5140631B77F
GO
Isoform 4 (identifier: O60641-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     293-295: NEG → K
     616-643: Missing.

Note: Gene prediction based on EST data.

Show »
Length:877
Mass (Da):89,656
Checksum:iA9A46C044BE55582
GO

Sequence cautioni

The sequence BAA31631.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAB89292.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei59 – 907849Missing in isoform 2.
VSP_020997Add
BLAST
Alternative sequencei256 – 26914Missing in isoform 3.
VSP_020998Add
BLAST
Alternative sequencei293 – 2953NEG → K in isoform 3 and isoform 4.
VSP_020999
Alternative sequencei381 – 671291Missing in isoform 3.
VSP_021000Add
BLAST
Alternative sequencei616 – 64328Missing in isoform 4.
VSP_047049Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41Q → R in AAH60818. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB014556 mRNA. Translation: BAA31631.2. Different initiation.
AK289582 mRNA. Translation: BAF82271.1.
CR749348 mRNA. Translation: CAH18201.1. Sequence problems.
AL109915 Genomic DNA. Translation: CAB89292.1. Sequence problems.
AL109915 Genomic DNA. Translation: CAI19453.1.
AL136972 Genomic DNA. No translation available.
AF054993 mRNA. Translation: AAC09352.1.
BC060818 mRNA. Translation: AAH60818.1.
CCDSiCCDS47455.1. [O60641-1]
CCDS56437.1. [O60641-3]
CCDS56438.1. [O60641-4]
RefSeqiNP_001229721.1. NM_001242792.1. [O60641-1]
NP_001229722.1. NM_001242793.1. [O60641-4]
NP_001229723.1. NM_001242794.1. [O60641-3]
NP_001243646.1. NM_001256717.1.
NP_001243647.1. NM_001256718.1.
NP_055656.1. NM_014841.2. [O60641-1]
XP_005248827.1. XM_005248770.2. [O60641-1]
XP_006715678.1. XM_006715615.1. [O60641-1]
UniGeneiHs.368046.

Genome annotation databases

EnsembliENST00000369694; ENSP00000358708; ENSG00000065609. [O60641-1]
ENST00000437520; ENSP00000413277; ENSG00000065609. [O60641-3]
ENST00000439399; ENSP00000400459; ENSG00000065609. [O60641-1]
ENST00000520213; ENSP00000428026; ENSG00000065609. [O60641-3]
ENST00000520302; ENSP00000428511; ENSG00000065609. [O60641-4]
ENST00000521743; ENSP00000428215; ENSG00000065609. [O60641-1]
GeneIDi9892.
KEGGihsa:9892.
UCSCiuc003pka.3. human. [O60641-1]
uc003pkd.3. human. [O60641-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB014556 mRNA. Translation: BAA31631.2 . Different initiation.
AK289582 mRNA. Translation: BAF82271.1 .
CR749348 mRNA. Translation: CAH18201.1 . Sequence problems.
AL109915 Genomic DNA. Translation: CAB89292.1 . Sequence problems.
AL109915 Genomic DNA. Translation: CAI19453.1 .
AL136972 Genomic DNA. No translation available.
AF054993 mRNA. Translation: AAC09352.1 .
BC060818 mRNA. Translation: AAH60818.1 .
CCDSi CCDS47455.1. [O60641-1 ]
CCDS56437.1. [O60641-3 ]
CCDS56438.1. [O60641-4 ]
RefSeqi NP_001229721.1. NM_001242792.1. [O60641-1 ]
NP_001229722.1. NM_001242793.1. [O60641-4 ]
NP_001229723.1. NM_001242794.1. [O60641-3 ]
NP_001243646.1. NM_001256717.1.
NP_001243647.1. NM_001256718.1.
NP_055656.1. NM_014841.2. [O60641-1 ]
XP_005248827.1. XM_005248770.2. [O60641-1 ]
XP_006715678.1. XM_006715615.1. [O60641-1 ]
UniGenei Hs.368046.

3D structure databases

ProteinModelPortali O60641.
SMRi O60641. Positions 18-264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115222. 5 interactions.
IntActi O60641. 2 interactions.
MINTi MINT-3000172.
STRINGi 9606.ENSP00000195649.

PTM databases

PhosphoSitei O60641.

Proteomic databases

MaxQBi O60641.
PaxDbi O60641.
PRIDEi O60641.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369694 ; ENSP00000358708 ; ENSG00000065609 . [O60641-1 ]
ENST00000437520 ; ENSP00000413277 ; ENSG00000065609 . [O60641-3 ]
ENST00000439399 ; ENSP00000400459 ; ENSG00000065609 . [O60641-1 ]
ENST00000520213 ; ENSP00000428026 ; ENSG00000065609 . [O60641-3 ]
ENST00000520302 ; ENSP00000428511 ; ENSG00000065609 . [O60641-4 ]
ENST00000521743 ; ENSP00000428215 ; ENSG00000065609 . [O60641-1 ]
GeneIDi 9892.
KEGGi hsa:9892.
UCSCi uc003pka.3. human. [O60641-1 ]
uc003pkd.3. human. [O60641-3 ]

Organism-specific databases

CTDi 9892.
GeneCardsi GC06M084319.
H-InvDB HIX0006038.
HGNCi HGNC:14986. SNAP91.
HPAi CAB009745.
HPA029632.
HPA029633.
MIMi 607923. gene.
neXtProti NX_O60641.
PharmGKBi PA37956.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG267212.
HOGENOMi HOG000015763.
HOVERGENi HBG049391.
InParanoidi O60641.
OMAi XRISGAP.
OrthoDBi EOG76QFM8.
PhylomeDBi O60641.
TreeFami TF314861.

Miscellaneous databases

GeneWikii SNAP91.
GenomeRNAii 9892.
NextBioi 37299.
PROi O60641.
SOURCEi Search...

Gene expression databases

ArrayExpressi O60641.
Bgeei O60641.
CleanExi HS_SNAP91.
Genevestigatori O60641.

Family and domain databases

Gene3Di 1.20.58.150. 1 hit.
1.25.40.90. 1 hit.
InterProi IPR011417. ANTH_dom.
IPR014712. Clathrin_Pinositid-bd_GAT-like.
IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
[Graphical view ]
Pfami PF07651. ANTH. 1 hit.
[Graphical view ]
SMARTi SM00273. ENTH. 1 hit.
[Graphical view ]
SUPFAMi SSF48464. SSF48464. 1 hit.
PROSITEi PS50942. ENTH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "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: Cerebellum.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    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 3).
    Tissue: Testis.
  6. Yu W., Gibbs R.A.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 794-907.
    Tissue: Brain.
  7. "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly."
    Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T.
    PLoS Biol. 4:E262-E262(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP2B1.

Entry informationi

Entry nameiAP180_HUMAN
AccessioniPrimary (citable) accession number: O60641
Secondary accession number(s): A8K0L7
, E5RI02, Q5JX13, Q68DL9, Q6P9D3, Q9NTY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: August 1, 1999
Last modified: July 9, 2014
This is version 121 of the entry and version 2 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 6
    Human chromosome 6: 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

Similar proteinsi