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Q9Y5K3

- PCY1B_HUMAN

UniProt

Q9Y5K3 - PCY1B_HUMAN

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Protein

Choline-phosphate cytidylyltransferase B

Gene
PCYT1B, CCTB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Controls phosphatidylcholine synthesis.

Catalytic activityi

CTP + phosphocholine = diphosphate + CDP-choline.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221CTP By similarity
Binding sitei122 – 1221Substrate By similarity
Binding sitei151 – 1511Substrate By similarity
Binding sitei173 – 1731CTP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi84 – 929CTP By similarity
Nucleotide bindingi168 – 1692CTP By similarity
Nucleotide bindingi196 – 2005CTP By similarity

GO - Molecular functioni

  1. choline-phosphate cytidylyltransferase activity Source: ProtInc

GO - Biological processi

  1. CDP-choline pathway Source: GOC
  2. glycerophospholipid biosynthetic process Source: Reactome
  3. ovarian follicle development Source: Ensembl
  4. phosphatidylcholine biosynthetic process Source: Reactome
  5. phospholipid metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
  7. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_121238. Synthesis of PC.
UniPathwayiUPA00753; UER00739.

Names & Taxonomyi

Protein namesi
Recommended name:
Choline-phosphate cytidylyltransferase B (EC:2.7.7.15)
Alternative name(s):
CCT-beta
CTP:phosphocholine cytidylyltransferase B
Short name:
CCT B
Short name:
CT B
Phosphorylcholine transferase B
Gene namesi
Name:PCYT1B
Synonyms:CCTB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8755. PCYT1B.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33100.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Choline-phosphate cytidylyltransferase BPRO_0000208456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei315 – 3151Phosphoserine1 Publication
Modified residuei319 – 3191Phosphoserine1 Publication
Modified residuei362 – 3621Phosphoserine1 Publication

Post-translational modificationi

Extensively phosphorylated. The beta-1 isoform seems to be much less phosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y5K3.
PaxDbiQ9Y5K3.
PRIDEiQ9Y5K3.

PTM databases

PhosphoSiteiQ9Y5K3.

Expressioni

Tissue specificityi

Highly expressed in testis, placenta, brain, ovary and fetus.

Gene expression databases

ArrayExpressiQ9Y5K3.
BgeeiQ9Y5K3.
CleanExiHS_PCYT1B.
GenevestigatoriQ9Y5K3.

Organism-specific databases

HPAiHPA006367.

Interactioni

Protein-protein interaction databases

BioGridi114854. 7 interactions.
MINTiMINT-5006746.
STRINGi9606.ENSP00000368439.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5K3.
SMRiQ9Y5K3. Positions 41-295.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0615.
HOGENOMiHOG000230945.
HOVERGENiHBG053531.
InParanoidiQ9Y5K3.
KOiK00968.
OMAiLEHTCPH.
OrthoDBiEOG7X9G6S.
PhylomeDBiQ9Y5K3.
TreeFamiTF106336.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: Q9Y5K3-1) [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

MPVVTTDAES ETGIPKSLSN EPPSETMEEI EHTCPQPRLT LTAPAPFADE    50
TNCQCQAPHE KLTIAQARLG TPADRPVRVY ADGIFDLFHS GHARALMQAK 100
TLFPNSYLLV GVCSDDLTHK FKGFTVMNEA ERYEALRHCR YVDEVIRDAP 150
WTLTPEFLEK HKIDFVAHDD IPYSSAGSDD VYKHIKEAGM FVPTQRTEGI 200
STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKRY RFQNQVDKMK 250
EKVKNVEERS KEFVNRVEEK SHDLIQKWEE KSREFIGNFL ELFGPDGAWK 300
QMFQERSSRM LQALSPKQSP VSSPTRSRSP SRSPSPTFSW LPLKTSPPSS 350
PKAASASISS MSEGDEDEK 369
Length:369
Mass (Da):41,940
Last modified:November 1, 1999 - v1
Checksum:i87A00617DF690DD1
GO
Isoform 1 (identifier: Q9Y5K3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     321-369: VSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISSMSEGDEDEK → LKSWARCRDF

Show »
Length:330
Mass (Da):38,086
Checksum:iC1A16BC1B61906B2
GO
Isoform 3 (identifier: Q9Y5K3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     17-39: SLSNEPPSETMEEIEHTCPQPRL → MVGNQECIMEEDNRAPQLWRK

Note: No experimental confirmation available.

Show »
Length:351
Mass (Da):40,206
Checksum:i0E2BBEDD2569EAA8
GO
Isoform 4 (identifier: Q9Y5K3-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRL → MVGHQECIMEEDNRAPQLWRK

Note: No experimental confirmation available.

Show »
Length:351
Mass (Da):40,229
Checksum:i89BA4A3D7F09B353
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939MPVVT…PQPRL → MVGHQECIMEEDNRAPQLWR K in isoform 4. VSP_044659Add
BLAST
Alternative sequencei1 – 1616Missing in isoform 3. VSP_020045Add
BLAST
Alternative sequencei17 – 3923SLSNE…PQPRL → MVGNQECIMEEDNRAPQLWR K in isoform 3. VSP_020046Add
BLAST
Alternative sequencei321 – 36949VSSPT…DEDEK → LKSWARCRDF in isoform 1. VSP_001226Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541T → S in BAG59022. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF052510 mRNA. Translation: AAC39754.1.
AF148464 mRNA. Translation: AAD35088.1.
AK296333 mRNA. Translation: BAG59022.1.
AK315323 mRNA. Translation: BAG37725.1.
EU181262 Genomic DNA. Translation: ABW03924.1.
AC079168 Genomic DNA. No translation available.
CH471074 Genomic DNA. Translation: EAW99021.1.
BC045634 mRNA. Translation: AAH45634.2.
CCDSiCCDS14213.1. [Q9Y5K3-1]
CCDS55391.1. [Q9Y5K3-2]
CCDS55392.1. [Q9Y5K3-4]
RefSeqiNP_001156736.1. NM_001163264.1. [Q9Y5K3-4]
NP_001156737.1. NM_001163265.1. [Q9Y5K3-2]
NP_004836.2. NM_004845.4. [Q9Y5K3-1]
UniGeneiHs.660708.

Genome annotation databases

EnsembliENST00000356768; ENSP00000349211; ENSG00000102230. [Q9Y5K3-2]
ENST00000379144; ENSP00000368439; ENSG00000102230. [Q9Y5K3-1]
ENST00000379145; ENSP00000368440; ENSG00000102230. [Q9Y5K3-4]
GeneIDi9468.
KEGGihsa:9468.
UCSCiuc004dbi.3. human. [Q9Y5K3-1]
uc004dbk.4. human. [Q9Y5K3-2]

Polymorphism databases

DMDMi12643330.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF052510 mRNA. Translation: AAC39754.1 .
AF148464 mRNA. Translation: AAD35088.1 .
AK296333 mRNA. Translation: BAG59022.1 .
AK315323 mRNA. Translation: BAG37725.1 .
EU181262 Genomic DNA. Translation: ABW03924.1 .
AC079168 Genomic DNA. No translation available.
CH471074 Genomic DNA. Translation: EAW99021.1 .
BC045634 mRNA. Translation: AAH45634.2 .
CCDSi CCDS14213.1. [Q9Y5K3-1 ]
CCDS55391.1. [Q9Y5K3-2 ]
CCDS55392.1. [Q9Y5K3-4 ]
RefSeqi NP_001156736.1. NM_001163264.1. [Q9Y5K3-4 ]
NP_001156737.1. NM_001163265.1. [Q9Y5K3-2 ]
NP_004836.2. NM_004845.4. [Q9Y5K3-1 ]
UniGenei Hs.660708.

3D structure databases

ProteinModelPortali Q9Y5K3.
SMRi Q9Y5K3. Positions 41-295.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114854. 7 interactions.
MINTi MINT-5006746.
STRINGi 9606.ENSP00000368439.

Chemistry

DrugBanki DB00122. Choline.

PTM databases

PhosphoSitei Q9Y5K3.

Polymorphism databases

DMDMi 12643330.

Proteomic databases

MaxQBi Q9Y5K3.
PaxDbi Q9Y5K3.
PRIDEi Q9Y5K3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356768 ; ENSP00000349211 ; ENSG00000102230 . [Q9Y5K3-2 ]
ENST00000379144 ; ENSP00000368439 ; ENSG00000102230 . [Q9Y5K3-1 ]
ENST00000379145 ; ENSP00000368440 ; ENSG00000102230 . [Q9Y5K3-4 ]
GeneIDi 9468.
KEGGi hsa:9468.
UCSCi uc004dbi.3. human. [Q9Y5K3-1 ]
uc004dbk.4. human. [Q9Y5K3-2 ]

Organism-specific databases

CTDi 9468.
GeneCardsi GC0XM024576.
HGNCi HGNC:8755. PCYT1B.
HPAi HPA006367.
MIMi 604926. gene.
neXtProti NX_Q9Y5K3.
PharmGKBi PA33100.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0615.
HOGENOMi HOG000230945.
HOVERGENi HBG053531.
InParanoidi Q9Y5K3.
KOi K00968.
OMAi LEHTCPH.
OrthoDBi EOG7X9G6S.
PhylomeDBi Q9Y5K3.
TreeFami TF106336.

Enzyme and pathway databases

UniPathwayi UPA00753 ; UER00739 .
Reactomei REACT_121238. Synthesis of PC.

Miscellaneous databases

GeneWikii PCYT1B.
GenomeRNAii 9468.
NextBioi 35472668.
PROi Q9Y5K3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y5K3.
Bgeei Q9Y5K3.
CleanExi HS_PCYT1B.
Genevestigatori Q9Y5K3.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
InterProi IPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF01467. CTP_transf_2. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase."
    Lykidis A., Murti K.G., Jackowski S.
    J. Biol. Chem. 273:14022-14029(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant."
    Lykidis A., Baburina I., Jackowski S.
    J. Biol. Chem. 274:26992-27001(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION.
  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 4).
    Tissue: Hippocampus and Thalamus.
  4. SeattleSNPs variation discovery resource
    Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Brain.
  8. "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 SER-315; SER-319 AND SER-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPCY1B_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5K3
Secondary accession number(s): A8IX00
, B2RCX8, B4DK10, E9PD84, O60621, Q86XC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 119 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 X
    Human chromosome X: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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